ID A0A162PID1_9CRUS Unreviewed; 421 AA.
AC A0A162PID1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Carboxypeptidase A5 {ECO:0000313|EMBL:KZS18874.1};
GN ORFNames=APZ42_015465 {ECO:0000313|EMBL:KZS18874.1};
OS Daphnia magna.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX NCBI_TaxID=35525 {ECO:0000313|EMBL:KZS18874.1, ECO:0000313|Proteomes:UP000076858};
RN [1] {ECO:0000313|EMBL:KZS18874.1, ECO:0000313|Proteomes:UP000076858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xinb3 {ECO:0000313|EMBL:KZS18874.1,
RC ECO:0000313|Proteomes:UP000076858};
RC TISSUE=Complete organism {ECO:0000313|EMBL:KZS18874.1};
RA Gilbert D.G., Choi J.-H., Mockaitis K., Colbourne J., Pfrender M.;
RT "EvidentialGene: Evidence-directed Construction of Genes on Genomes.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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:KZS18874.1}.
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DR EMBL; LRGB01000512; KZS18874.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A162PID1; -.
DR Proteomes; UP000076858; 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 CDD; cd03860; M14_CP_A-B_like; 1.
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:SF141; PEPTIDASE M14 CARBOXYPEPTIDASE A DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR11705; PROTEASE FAMILY M14 CARBOXYPEPTIDASE A,B; 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 ECO:0000313|EMBL:KZS18874.1};
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:UP000076858};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..421
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007838194"
FT DOMAIN 128..408
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|SMART:SM00631"
SQ SEQUENCE 421 AA; 47601 MW; CED5C770326E8FC3 CRC64;
MRFCYYVGIA TLLLVNFSAS LGERIDYSGH KVVRVRAANA VQLSYLRHLQ TSDETLDFWT
DPYRVGKPVD IHVTPGKYEG LARSLSSAGI QHQIKVEDIG KAEKEERQTI EHRRELTKNQ
KAFDFENYHT YEEIVAYMEQ LALENPLVSV SSIGTTFENR SLTMATISTG SNPDKQVIVF
ECAVHAREWA APSTCLWFIN ELATKYGSDS EITQLVDGFD WKITPVTNPD GYTYSWTTDR
LWRKNRKPSS TCYGVDINRN FDTNFGGLGA SDIACVDTYH GPYSFSEEES SAVRDVLIAN
RPRVKAAISI HTYSQLWMSP YAYTHDLPLE YDEMLRVMSI GVQALQNTYG TQYQYGNHAD
TIYIASGTTV DHAYSAESIL YAYLLELRDT GEFGFQLPAS QIMETAVETW NGIKAMALEI
L
//
