The domain within your query sequence starts at position 637 and ends at position 884; the E-value for the UBA_e1_thiolCys domain shown below is 9.1e-95.

PNAIEHTVQWARDEFEGLFKQSAENVNQYLTDPKFMERTLQLAGTQPLEVLEAIHCSLVL
QRPQTWADCVTWAYQHWHTQYSHNIQQLLHNFPPAQLTSSGALFWSGPKRCPHPLTFDIN
NPLHLDYVMAAANLFAQTYGLGGSQDCAVVAKLLQSLPVPKFAPKSGIRIHVSEQELQST
SATTIDDSHLEELKTALPTPDKLLGFKMYPIDFEKDDDSNFHMDFIVAASNLRAENYGIS
PADRHKSK

UBA_e1_thiolCys

UBA_e1_thiolCys
PFAM accession number:PF10585
Interpro abstract (IPR019572):

Ubiquitin-activating enzyme (E1 enzyme) activates ubiquitin by first adenylating with ATP its C-terminal glycine residue and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding an ubiquitin-E1 thiolester and free AMP. Later the ubiquitin moiety is transferred to a cysteine residue on one of the many forms of ubiquitin-conjugating enzymes (E2) [(PUBMED:1986373)]. This domain carries the last of five conserved cysteines that is part of the active site of the enzyme, responsible for ubiquitin thiolester complex formation, the active site being represented by the sequence motif PICTLKNFP [(PUBMED:11004499)]. Not all proteins in this entry contain a functional active site.

This is a PFAM domain. For full annotation and more information, please see the PFAM entry UBA_e1_thiolCys