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Links from Protein

Items: 15

1.

Peptidase M1 N-terminal domain

This domain is found at the N-terminus of aminopeptidases from the M1 family. (from Pfam)

Date:
2023-12-12
Family Accession:
NF037667.4
Method:
HMM
2.

ERAP1-like C-terminal domain-containing protein

This large domain is composed of 16 alpha helices organized as 8 HEAT-like repeats. This domain forms a concave face that faces towards the active site of the peptidase. [1]. 21478864. Structural basis for antigenic peptide precursor processing by. the endoplasmic reticulum aminopeptidase ERAP1.. Nguyen TT, Chang SC, Evnouchidou I, York IA, Zikos C, Rock KL,. Goldberg AL, Stratikos E, Stern LJ;. Nat Struct Mol Biol. 2011;18:604-613. (from Pfam)

Date:
2024-04-03
Family Accession:
NF023266.4
Method:
HMM
3.

M1 family aminopeptidase

The M1 family metalloproteases in this family are zinc-dependent enzymes with aminopeptidase activity.

GO Terms:
Molecular Function:
metallopeptidase activity (GO:0008237)
Molecular Function:
zinc ion binding (GO:0008270)
Date:
2024-04-03
Family Accession:
NF013592.4
Method:
HMM
4.
new record, indexing in progress
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5.
new record, indexing in progress
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6.
new record, indexing in progress
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7.
new record, indexing in progress
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8.
new record, indexing in progress
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9.
new record, indexing in progress
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10.
new record, indexing in progress
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11.
new record, indexing in progress
Family Accession:
12.

M1 family metallopeptidase

M1 family metallopeptidase containing an ERAP1-like C-terminal domain with HEAT-like repeats; similar to aminopeptidase N, a broad specificity aminopeptidase, and glutamyl aminopeptidase, which releases N-terminal glutamate from a peptide

GO Terms:
Molecular Function:
aminopeptidase activity (GO:0004177)
Biological Process:
proteolysis (GO:0006508)
Molecular Function:
zinc ion binding (GO:0008270)
Molecular Function:
metallopeptidase activity (GO:0008237)
Date:
2022-10-25
Family Accession:
10176184
Method:
Sparcle
13.
new record, indexing in progress
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14.
new record, indexing in progress
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15.
new record, indexing in progress
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