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Database: UniProt
Entry: A0A151MNA9_ALLMI
LinkDB: A0A151MNA9_ALLMI
Original site: A0A151MNA9_ALLMI 
ID   A0A151MNA9_ALLMI        Unreviewed;       438 AA.
AC   A0A151MNA9;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Carboxypeptidase A6 {ECO:0000313|EMBL:KYO25996.1};
GN   Name=CPA6 {ECO:0000313|EMBL:KYO25996.1};
GN   ORFNames=Y1Q_0003771 {ECO:0000313|EMBL:KYO25996.1};
OS   Alligator mississippiensis (American alligator).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC   Alligator.
OX   NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO25996.1};
RN   [1] {ECO:0000313|EMBL:KYO25996.1, ECO:0000313|Proteomes:UP000050525}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO25996.1};
RX   PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA   St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA   Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA   Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA   Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA   Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA   McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA   Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA   Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA   Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA   Ray D.A.;
RT   "Sequencing three crocodilian genomes to illuminate the evolution of
RT   archosaurs and amniotes.";
RL   Genome Biol. 13:415-415(2012).
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:KYO25996.1}.
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DR   EMBL; AKHW03005657; KYO25996.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A151MNA9; -.
DR   STRING; 8496.A0A151MNA9; -.
DR   eggNOG; KOG2650; Eukaryota.
DR   Proteomes; UP000050525; 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; cd03872; M14_CPA6; 1.
DR   Gene3D; 3.30.70.340; Metallocarboxypeptidase-like; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR033843; CPAH.
DR   InterPro; IPR036990; M14A-like_propep.
DR   InterPro; IPR003146; M14A_act_pep.
DR   InterPro; IPR000834; Peptidase_M14.
DR   PANTHER; PTHR11705:SF18; CARBOXYPEPTIDASE A6; 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.
DR   PROSITE; PS00133; CARBOXYPEPT_ZN_2; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW   ECO:0000313|EMBL:KYO25996.1};
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:UP000050525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..438
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007585334"
FT   DOMAIN          325..335
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|PROSITE:PS00133"
SQ   SEQUENCE   438 AA;  50886 MW;  12015D670310AF3D CRC64;
     MKLPGNPGSR VAALLPLCLF VLKTWVPVQA YLYNNRYAGD KVIRLVPGSD KETQALKSVF
     HQLKVDLWQP SSLSYISEGT VTDLRVPRNS SRVLLPYLQQ ANIQYTILIS DLQQVIEKQT
     GLRSSRNRRS VPGYNYEVYH SLKEIQNWMY QLNKTHSDLI HMFSIGKSYE GRPLFVLKLG
     KRSRRYKRAV WIDCGIHARE WIGPAFCQWF VKEAIKTYQS DPAMRRMLNQ LYFYIMPVFN
     VDGYHFSWTD DRFWRKTRSK NSKFRCHGVD ANRNWKVKWC DEGASFHPCD DTYCGPFPES
     EPEVKAVAHF LRKRRKQIKA YLSFHAYAQM LLYPYSYKYA TIPNFTCVES AAYKAVNALQ
     SAYGIRYRYG PASSTLYVSS GSSMDWAYKN GIPYAFAFEL RDTGHFGFLL PEALIKPTCT
     ETMLAVKNIT MHLLKKCH
//
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