ID A0A016VNC2_9BILA Unreviewed; 375 AA.
AC A0A016VNC2;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Peptidase M14 carboxypeptidase A domain-containing protein {ECO:0000259|SMART:SM00631};
GN Name=Acey_s0008.g72 {ECO:0000313|EMBL:EYC28278.1};
GN Synonyms=Acey-ZC434.9 {ECO:0000313|EMBL:EYC28278.1};
GN ORFNames=Y032_0008g72 {ECO:0000313|EMBL:EYC28278.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC28278.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M14 family.
CC {ECO:0000256|ARBA:ARBA00005988}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EYC28278.1}.
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DR EMBL; JARK01001344; EYC28278.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016VNC2; -.
DR STRING; 53326.A0A016VNC2; -.
DR MEROPS; M14.A34; -.
DR Proteomes; UP000024635; Unassembled WGS sequence.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.340; Metallocarboxypeptidase-like; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR036990; M14A-like_propep.
DR InterPro; IPR003146; M14A_act_pep.
DR InterPro; IPR000834; Peptidase_M14.
DR PANTHER; PTHR11705; PROTEASE FAMILY M14 CARBOXYPEPTIDASE A,B; 1.
DR PANTHER; PTHR11705:SF54; SHKT DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
DR Pfam; PF02244; Propep_M14; 1.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00631; Zn_pept; 1.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000024635};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 160..375
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|SMART:SM00631"
SQ SEQUENCE 375 AA; 43624 MW; 50233C52391D5B4F CRC64;
MSVLVPRERF FEEHQPAAVM KVRLRSLPSF VLCFAVITQA SLNDAGAADE KFVVVRAEPH
TLEQLKFVRE LHDNMHKYDL DFWLTPVALG HKADIMIRQE RQKWLENLFS NYSIPHNITI
KDVQQLILER EHQPKNSSSK YSKRLNDEGG NKARYGLGEY HSYEHIIHWM EDIQRYYPDK
ARVVNIGTTE EGRPIKGIKI GSNVHRNDKR IVWIDGGIHA REWAAVHTVI YVIDRLIADY
ETDPFVKRAV DQLNFYIFPV LNPDGYEYSR SGVSPMVRLW RKNRSAMLCK KDQWFRERCC
GGVDLNRNFD WFWGEIGSSS DRCSEIYQGK GPFSEAEARA VRDAMFSPEL RGKVDAFLTL
HTYSQRPASL RVETS
//
