ID   A0A087R7W0_APTFO        Unreviewed;       417 AA.
AC   A0A087R7W0;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Carboxypeptidase B {ECO:0000256|ARBA:ARBA00039334};
DE            EC=3.4.17.2 {ECO:0000256|ARBA:ARBA00039143};
GN   ORFNames=AS27_10148 {ECO:0000313|EMBL:KFM09564.1};
OS   Aptenodytes forsteri (Emperor penguin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC   Aptenodytes.
OX   NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM09564.1, ECO:0000313|Proteomes:UP000053286};
RN   [1] {ECO:0000313|EMBL:KFM09564.1, ECO:0000313|Proteomes:UP000053286}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM09564.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential release of a C-terminal lysine or arginine amino
CC         acid.; EC=3.4.17.2; Evidence={ECO:0000256|ARBA:ARBA00036114};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SUBCELLULAR LOCATION: Zymogen granule lumen
CC       {ECO:0000256|ARBA:ARBA00037795}.
CC   -!- SIMILARITY: Belongs to the peptidase M14 family.
CC       {ECO:0000256|ARBA:ARBA00005988}.
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DR   EMBL; KL226192; KFM09564.1; -; Genomic_DNA.
DR   RefSeq; XP_009280605.1; XM_009282330.1.
DR   AlphaFoldDB; A0A087R7W0; -.
DR   STRING; 9233.A0A087R7W0; -.
DR   MEROPS; M14.003; -.
DR   GeneID; 103901440; -.
DR   KEGG; afor:103901440; -.
DR   OrthoDB; 3540647at2759; -.
DR   Proteomes; UP000053286; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; cd03871; M14_CPB; 1.
DR   Gene3D; 3.30.70.340; Metallocarboxypeptidase-like; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR034253; CPB_M14_CPD.
DR   InterPro; IPR036990; M14A-like_propep.
DR   InterPro; IPR003146; M14A_act_pep.
DR   InterPro; IPR000834; Peptidase_M14.
DR   PANTHER; PTHR11705:SF20; CARBOXYPEPTIDASE B; 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; PS00132; CARBOXYPEPT_ZN_1; 1.
DR   PROSITE; PS00133; CARBOXYPEPT_ZN_2; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW   ECO:0000313|EMBL:KFM09564.1};
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:UP000053286};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           16..417
FT                   /note="Carboxypeptidase B"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012994763"
FT   DOMAIN          167..189
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|PROSITE:PS00132"
FT   DOMAIN          304..314
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|PROSITE:PS00133"
SQ   SEQUENCE   417 AA;  47155 MW;  53FAC39EDB8903D8 CRC64;
     MWALLVLIGA AAVSADLQDL AFDGQKVFRV FPQNDEQVEI INSLASNMQV DFWQPDSVTL
     VSPQMQVDFR VEADKSFEVE DLLKESGVEY RVLIDNLQAA LDAQFDSKAR TTGHSYEKYN
     NWETIAAWTA DIAAQNPALV SRIVIGETYE GRPMYLLKMG KRGPNKKAIF MDCGFHAREW
     ISPAFCQWFV KEALETYGKD TVMTTLLNSL DFYVLPVVNI DGYIYTWTKD RMWRKTRSKN
     AGSRCIGTDP NRNFNAGWCT VGASKNSCDS TYCGSAPESE KETKALADFI REHLPTIKAY
     LTIHSYSQML LFPYSYTYKL PSNYEELNSI ADAASKQLAS LYSTEYTYGP GATTIYPAAG
     GSDDWAYDQG IKYSFTFELR DTGRYGFVLP ESQIKPTCEE TLLAVKYIAN YVLEHLY
//