ID A0A194PGK0_PAPXU Unreviewed; 411 AA.
AC A0A194PGK0;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Zinc carboxypeptidase A 1 {ECO:0000313|EMBL:KPI92158.1};
GN ORFNames=RR46_13379 {ECO:0000313|EMBL:KPI92158.1};
OS Papilio xuthus (Asian swallowtail butterfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Papilionidae; Papilioninae; Papilio.
OX NCBI_TaxID=66420 {ECO:0000313|EMBL:KPI92158.1, ECO:0000313|Proteomes:UP000053268};
RN [1] {ECO:0000313|EMBL:KPI92158.1, ECO:0000313|Proteomes:UP000053268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ya'a_city_454_Px {ECO:0000313|EMBL:KPI92158.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KPI92158.1};
RX PubMed=26354079; DOI=10.1038/ncomms9212;
RA Li X., Fan D., Zhang W., Liu G., Zhang L., Zhao L., Fang X., Chen L.,
RA Dong Y., Chen Y., Ding Y., Zhao R., Feng M., Zhu Y., Feng Y., Jiang X.,
RA Zhu D., Xiang H., Feng X., Li S., Wang J., Zhang G., Kronforst M.R.,
RA Wang W.;
RT "Outbred genome sequencing and CRISPR/Cas9 gene editing in butterflies.";
RL Nat. Commun. 6:8212-8212(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}.
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DR EMBL; KQ459604; KPI92158.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A194PGK0; -.
DR STRING; 66420.A0A194PGK0; -.
DR Proteomes; UP000053268; 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:SF142; RH39904P-RELATED; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
DR Pfam; PF02244; Propep_M14; 1.
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:KPI92158.1};
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:UP000053268};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..411
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008263261"
FT DOMAIN 116..393
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|SMART:SM00631"
SQ SEQUENCE 411 AA; 47183 MW; FEBCA8D447D87A16 CRC64;
MLKLLILCSC CVFVWSEKVR YDNFTLYNVK PLTEEHLKYL KDLYEDTDVF DFWSIPSIVE
NHVSVVSPPE TKEEFQNALK SHGIGYDVVL EDIQKAFDDQ TRNRRKRDSG MYWTNYQTID
EIYEWLHELA RTHSNFVTLI HAGKSYEGRN ITGVRISRRS GRKAFFIDGG QVGADWLSPT
VVTYLINQLV TGDDPEARSA SEDFEWHIFP IVNPDGHQFS QDSVRLWMKN RRPSRSSAIG
VDLSKNWNSQ WAVSGGSFNP SDSNYIGLGP FSEPETRYVS RYIDTIGTNL AGLLSFRAFG
QRLLIPFAHT IEPMYNYRDM LTIGRRAMGS LAVKYNTQYL VGTSKEVHDG STGTIADWVK
HRFNPPVVAT YQLRDRSWGY TLPVNQVLPS CEETYDSVMA ILREAKFMNV L
//