SMART: Pfam domain ThiF

The domain within your query sequence starts at position 54 and ends at position 199; the E-value for the ThiF domain shown below is 1.5e-41.

DTCKVLVIGAGGLGCELLKNLALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDVGRPKAEV
AAEFLNDRVPNCNVVPHFNKIQDFNDTFYRQFHIIVCGLDSIIARRWINGMLISLLNYED
GVLDPSSIVPLIDGGTEGFKGNARVI

ThiF

PFAM accession number:	PF00899
Interpro abstract (IPR000594):	Ubiquitin-activating enzyme (E1 enzyme) [ (PUBMED:1647207) (PUBMED:1656558) ] 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). This domain is a NAD/FAD-binding fold found in ubiquitin activating E1 family and members of the bacterial ThiF/MoeB/HesA family. It is repeated in Ubiquitin-activating enzyme E1 [ (PUBMED:11713534) (PUBMED:15660128) (PUBMED:18662542) ].
GO function:	ubiquitin-like modifier activating enzyme activity (GO:0008641)

PFAM accession number:

PF00899

Interpro abstract (IPR000594):

Ubiquitin-activating enzyme (E1 enzyme) [ (PUBMED:1647207) (PUBMED:1656558) ] 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).

This domain is a NAD/FAD-binding fold found in ubiquitin activating E1 family and members of the bacterial ThiF/MoeB/HesA family. It is repeated in Ubiquitin-activating enzyme E1 [ (PUBMED:11713534) (PUBMED:15660128) (PUBMED:18662542) ].

GO function:

ubiquitin-like modifier activating enzyme activity (GO:0008641)

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