The domain within your query sequence starts at position 1 and ends at position 333; the E-value for the Cobalamin_bind domain shown below is 3.1e-138.

MELLKALLLLSGVFGALAEFCVIPRIDSQLVEKLGQRLLPWMDRLSSEQLNPSVFVGLRL
SSMQAGTKEDLYLHSLKIHYQQCLLRSTSSDDNSSCQPKLSGGSLALYLLALRANCEFFG
SRKGDRLISQLKWFLEDEKKAIGHNHEGHPNTNYYQYGLSILALCVHQKRLHDSVVGKLL
YAVEHDYFTYQGHVSVDTEAMAGLALTCLERFNFNSDLRPRITMAIETVREKILKSQAPE
GYFGNIYSTPLALQMLMTSPASGVGLGTACIKAGTSLLLSLQDGAFQNPLMISQLLPILN
HKTYLDLIFPDCQASRVMLVPAVEDPVHISEVI

Cobalamin_bind

Cobalamin_bind
PFAM accession number:PF01122
Interpro abstract (IPR002157):

Cobalamin (Cbl or vitamin B12) is only accessible through diet in mammals. Absorption, plasma transport and cellular uptake of Cbl in mammals involves three Cbl-transporting proteins, which are listed below in order of increasing Cbl-specificity:

  • Haptocorrin (cobalophilin), which binds Cbl and Cbl-derivatives such as cobinamide; it may play a role in preventing the absorption of cobalamin analogues produced by bacteria.
  • Transcobalamin (TC), which transport Cbl from blood to cells.
  • Intrinsic factor (IF), which promotes Cbl absorption in the ileum by specific receptor-mediated endocytosis.

The structure of TC reveals a two-domain structure, an N-terminal alpha(6)-alpha(6) barrel, and a smaller C-terminal domain [(PUBMED:16537422)]. Many interactions between Cbl and its binding site in the interface of the two domains are conserved among the other Cbl transporters. Specificity for Cbl between the different transporters may reside in a beta-hairpin motif found in the smaller C-terminal domain [(PUBMED:17274763)].

GO process:cobalamin transport (GO:0015889)
GO function:cobalamin binding (GO:0031419)

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