The domain within your query sequence starts at position 69 and ends at position 397; the E-value for the TTL domain shown below is 2.2e-87.

FDHTYMDEHVRISHFRNHYELTRKNYMVKNLKRFRKYLERESGKTEAAKCDFFPKTFEMP
CEYHLFVEEFRKNPGITWIMKPVARSQGKGIFLFRRLKDIMDWRKGTSGKKPTGVETQPA
RANMNPSGSHDTRSSDDQKDDLPVENYVAQRYVENPYLIGGRKFDLRVYVLVMSYIPLRA
WLYRDGFARFSNTRFTLNSIDDHYVHLTNVAVQKTSPDYHLKKGCKWMLQRFRQYLASKH
GPKAVETLFSDMDNIFIKSLQSVQKVIISDKHCFELYGYDILIDQDLKPWLLEVNASPSL
TASSQEDYELKTCLLEDTLHVVDMEARLT

TTL

TTL
PFAM accession number:PF03133
Interpro abstract (IPR004344):

Tubulins and microtubules are subjected to several post-translational modifications of the carboxy-terminal end of most major forms of tubulins has been extensively analysed. This modification cycle involves a specific carboxypeptidase and the activity of the tubulin-tyrosine ligase (TTL) and the tubulin polyglutamylase (TTLL) [(PUBMED:10685598), (PUBMED:19524510)]. Tubulin-tyrosine ligase (TTL) catalyses the ATP-dependent post-translational addition of a tyrosine to the carboxy terminal end of detyrosinated alpha-tubulin. Tubulin polyglutamylase (such as TTLL10) can modify both tubulin and non-tubulin proteins, generating side chains of glycine on the gamma-carboxyl groups of specific glutamate residues of target proteins [(PUBMED:19524510)]. Tubulin polyglutamylation may be involved in the organisation of the neuronal microtubule network, in centriole stability, axoneme motility and mitosis [(PUBMED:15890843)].

GO process:cellular protein modification process (GO:0006464)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry TTL