Provided by: hmmer_3.1b1-3_amd64 bug

NAME

       hmmbuild - construct profile HMM(s) from multiple sequence alignment(s)

SYNOPSIS

       hmmbuild [options] <hmmfile_out> <msafile>

DESCRIPTION

       For  each  multiple  sequence  alignment  in  <msafile>  build  a  profile  HMM and save it to a new file
       <hmmfile_out>.

       <msafile> may be '-' (dash), which means reading this input from stdin rather than a file.  To  use  '-',
       you  must also specify the alignment file format with --informat <s>, as in --informat stockholm (because
       of a current limitation in our implementation, MSA file formats cannot be autodetected in a nonrewindable
       input stream.)

       <hmmfile_out>  may  not  be  '-' (stdout), because sending the HMM file to stdout would conflict with the
       other text output of the program.

OPTIONS

       -h     Help; print a brief reminder of command line usage and all available options.

       -n <s> Name the new profile <s>.  The default is to use the name of the alignment (if one is  present  in
              the  msafile,  or,  failing  that,  the  name  of  the hmmfile.  If msafile contains more than one
              alignment, -n doesn't work, and every alignment must have a name annotated in the msafile  (as  in
              Stockholm #=GF ID annotation).

       -o <f> Direct the summary output to file <f>, rather than to stdout.

       -O <f> After  each  model is constructed, resave annotated, possibly modified source alignments to a file
              <f> in Stockholm format.  The alignments are annotated with a reference annotation line indicating
              which  columns were assigned as consensus, and sequences are annotated with what relative sequence
              weights were assigned. Some residues of  the  alignment  may  have  been  shifted  to  accommodate
              restrictions  of  the  Plan7  profile architecture, which disallows transitions between insert and
              delete states.

OPTIONS FOR SPECIFYING THE ALPHABET

       The alphabet type (amino, DNA, or RNA) is autodetected by default, by looking at the composition  of  the
       msafile.   Autodetection  is normally quite reliable, but occasionally alphabet type may be ambiguous and
       autodetection can fail (for instance, on tiny toy alignments of just a few residues). To avoid  this,  or
       to increase robustness in automated analysis pipelines, you may specify the alphabet type of msafile with
       these options.

       --amino
              Specify that all sequences in msafile are proteins.

       --dna  Specify that all sequences in msafile are DNAs.

       --rna  Specify that all sequences in msafile are RNAs.

OPTIONS CONTROLLING PROFILE CONSTRUCTION

       These options control how consensus columns are defined in an alignment.

       --fast Define consensus columns as those that have a fraction >= symfrac of residues as opposed to  gaps.
              (See below for the --symfrac option.) This is the default.

       --hand Define  consensus  columns  in  next profile using reference annotation to the multiple alignment.
              This allows you to define any consensus columns you like.

       --symfrac <x>
              Define the residue fraction threshold necessary to define a consensus column when using the --fast
              option. The default is 0.5. The symbol fraction in each column is calculated after taking relative
              sequence weighting into account, and ignoring gap characters corresponding  to  ends  of  sequence
              fragments  (as  opposed  to  internal insertions/deletions).  Setting this to 0.0 means that every
              alignment column will be assigned as consensus, which may be useful in some cases. Setting  it  to
              1.0  means  that only columns that include 0 gaps (internal insertions/deletions) will be assigned
              as consensus.

       --fragthresh <x>
              We only want to count terminal gaps as deletions if the aligned sequence  is  known  to  be  full-
              length,  not if it is a fragment (for instance, because only part of it was sequenced). HMMER uses
              a simple rule to infer fragments: if the sequence length L is less than or equal to a fraction <x>
              times  the alignment length in columns, then the sequence is handled as a fragment. The default is
              0.5.  Setting --fragthresh0 will define no (nonempty) sequence as a fragment; you might want to do
              this  if  you  know  you've  got  a carefully curated alignment of full-length sequences.  Setting
              --fragthresh1 will define all sequences as fragments; you might want to do this if you  know  your
              alignment is entirely composed of fragments, such as translated short reads in metagenomic shotgun
              data.

OPTIONS CONTROLLING RELATIVE WEIGHTS

       HMMER uses an ad hoc sequence weighting algorithm to downweight closely related  sequences  and  upweight
       distantly  related  ones.  This  has  the  effect  of  making  models  less biased by uneven phylogenetic
       representation. For example, two identical sequences would typically each receive half  the  weight  that
       one sequence would.  These options control which algorithm gets used.

       --wpb  Use  the  Henikoff  position-based sequence weighting scheme [Henikoff and Henikoff, J. Mol. Biol.
              243:574, 1994].  This is the default.

       --wgsc Use the Gerstein/Sonnhammer/Chothia weighting algorithm [Gerstein et al, J. Mol.  Biol.  235:1067,
              1994].

       --wblosum
              Use  the  same  clustering  scheme  that was used to weight data in calculating BLOSUM subsitution
              matrices [Henikoff and Henikoff, Proc. Natl. Acad. Sci  89:10915,  1992].  Sequences  are  single-
              linkage  clustered at an identity threshold (default 0.62; see --wid) and within each cluster of c
              sequences, each sequence gets relative weight 1/c.

       --wnone
              No relative weights. All sequences are assigned uniform weight.

       --wid <x>
              Sets the identity threshold used by single-linkage clustering when using --wblosum.  Invalid  with
              any other weighting scheme. Default is 0.62.

OPTIONS CONTROLLING EFFECTIVE SEQUENCE NUMBER

       After  relative  weights are determined, they are normalized to sum to a total effective sequence number,
       eff_nseq.  This number may be the actual number of sequences in the alignment, but it  is  almost  always
       smaller  than  that.  The default entropy weighting method (--eent) reduces the effective sequence number
       to reduce the information content (relative entropy, or average expected  score  on  true  homologs)  per
       consensus  position. The target relative entropy is controlled by a two-parameter function, where the two
       parameters are settable with --ere and --esigma.

       --eent Adjust effective sequence number to achieve a specific relative entropy per position (see  --ere).
              This is the default.

       --eclust
              Set  effective  sequence  number  to  the number of single-linkage clusters at a specific identity
              threshold (see --eid).  This option is not recommended; it's for experiments evaluating  how  much
              better --eent is.

       --enone
              Turn  off effective sequence number determination and just use the actual number of sequences. One
              reason you might want to do this is to try to  maximize  the  relative  entropy/position  of  your
              model, which may be useful for short models.

       --eset <x>
              Explicitly set the effective sequence number for all models to <x>.

       --ere <x>
              Set the minimum relative entropy/position target to <x>.  Requires --eent.  Default depends on the
              sequence alphabet. For protein sequences, it is 0.59 bits/position; for nucleotide  sequences,  it
              is 0.45 bits/position.

       --esigma <x>
              Sets the minimum relative entropy contributed by an entire model alignment, over its whole length.
              This has the effect of making short models have higher relative entropy per  position  than  --ere
              alone would give. The default is 45.0 bits.

       --eid <x>
              Sets  the  fractional pairwise identity cutoff used by single linkage clustering with the --eclust
              option. The default is 0.62.

OPTIONS CONTROLLING PRIORS

       By default, weighted counts are converted to mean posterior probability parameter estimates using mixture
       Dirichlet  priors.   Default  mixture  Dirichlet prior parameters for protein models and for nucleic acid
       (RNA and DNA) models are built in. The following options allow you to override the default priors.

       --pnone
              Don't use any priors. Probability parameters  will  simply  be  the  observed  frequencies,  after
              relative sequence weighting.

       --plaplace
              Use a Laplace +1 prior in place of the default mixture Dirichlet prior.

OPTIONS CONTROLLING E-VALUE CALIBRATION

       The  location  parameters  for  the  expected  score  distributions for MSV filter scores, Viterbi filter
       scores, and Forward scores require three short random sequence simulations.

       --EmL <n>
              Sets the sequence length in simulation that estimates the location parameter mu for MSV filter  E-
              values. Default is 200.

       --EmN <n>
              Sets the number of sequences in simulation that estimates the location parameter mu for MSV filter
              E-values. Default is 200.

       --EvL <n>
              Sets the sequence length in simulation that estimates the location parameter mu for Viterbi filter
              E-values. Default is 200.

       --EvN <n>
              Sets  the  number  of sequences in simulation that estimates the location parameter mu for Viterbi
              filter E-values. Default is 200.

       --EfL <n>
              Sets the sequence length in simulation that estimates the location parameter tau  for  Forward  E-
              values. Default is 100.

       --EfN <n>
              Sets  the  number of sequences in simulation that estimates the location parameter tau for Forward
              E-values. Default is 200.

       --Eft <x>
              Sets the tail mass fraction to fit in the simulation that estimates the location parameter tau for
              Forward evalues. Default is 0.04.

OTHER OPTIONS

       --cpu <n>
              Set  the  number  of parallel worker threads to <n>.  By default, HMMER sets this to the number of
              CPU cores it detects in your machine - that is, it tries to maximize the  use  of  your  available
              processor  cores. Setting <n> higher than the number of available cores is of little if any value,
              but you may want to set it to something less. You can also  control  this  number  by  setting  an
              environment variable, HMMER_NCPU.

              This  option  is  only  available  if  HMMER  was compiled with POSIX threads support. This is the
              default, but it may have been turned off for your site or machine for some reason.

       --informat <s>
              Declare that the input msafile is in  format  <s>.   Currently  the  accepted  multiple  alignment
              sequence  file  formats  include Stockholm, Aligned FASTA, Clustal, NCBI PSI-BLAST, PHYLIP, Selex,
              and UCSC SAM A2M. Default is to autodetect the format of the file.

       --seed <n>
              Seed the random number generator with <n>, an integer >= 0.  If <n>  is  nonzero,  any  stochastic
              simulations  will  be reproducible; the same command will give the same results.  If <n> is 0, the
              random number generator is seeded arbitrarily, and stochastic simulations will vary  from  run  to
              run of the same command.  The default seed is 42.

       --w_beta <x>
              Window  length  tail  mass.   The upper bound, W, on the length at which nhmmer expects to find an
              instance of the model is set such that the fraction of all sequences generated by the  model  with
              length >= W is less than <x>.  The default is 1e-7.

       --w_length <n>
              Override  the model instance length upper bound, W, which is otherwise controlled by --w_beta.  It
              should be larger than the model length. The value of W is used deep in the acceleration  pipeline,
              and modest changes are not expected to impact results (though larger values of W do lead to longer
              run time).

       --mpi  Run as a parallel MPI program. Each alignment is assigned to a MPI worker node  for  construction.
              (Therefore,  the  maximum  parallelization  cannot  exceed  the  number of alignments in the input
              msafile.)  This is useful when building large profile libraries. This option is only available  if
              optional MPI capability was enabled at compile-time.

       --stall
              For  debugging MPI parallelization: arrest program execution immediately after start, and wait for
              a debugger to attach to the running process and release the arrest.

       --maxinsertlen <n>
              Restrict insert length parameterization such that the expected insert length at each  position  of
              the model is no more than <n>.

SEE ALSO

       See  hmmer(1) for a master man page with a list of all the individual man pages for programs in the HMMER
       package.

       For complete documentation, see the user guide that came with your HMMER distribution (Userguide.pdf); or
       see the HMMER web page ().

COPYRIGHT

       Copyright (C) 2013 Howard Hughes Medical Institute.
       Freely distributed under the GNU General Public License (GPLv3).

       For additional information on copyright and licensing, see the file called COPYRIGHT in your HMMER source
       distribution, or see the HMMER web page ().

AUTHOR

       Eddy/Rivas Laboratory
       Janelia Farm Research Campus
       19700 Helix Drive
       Ashburn VA 20147 USA
       http://eddylab.org