ID A0A0M8ZTC8_9HYME Unreviewed; 1184 AA.
AC A0A0M8ZTC8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Carboxypeptidase B {ECO:0000313|EMBL:KOX69233.1};
GN ORFNames=WN51_04268 {ECO:0000313|EMBL:KOX69233.1};
OS Melipona quadrifasciata.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Melipona.
OX NCBI_TaxID=166423 {ECO:0000313|EMBL:KOX69233.1, ECO:0000313|Proteomes:UP000053105};
RN [1] {ECO:0000313|EMBL:KOX69233.1, ECO:0000313|Proteomes:UP000053105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0111107301 {ECO:0000313|EMBL:KOX69233.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KOX69233.1};
RA Pan H., Kapheim K.;
RT "The genome of Melipona quadrifasciata.";
RL Submitted (JUL-2015) 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}.
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DR EMBL; KQ435896; KOX69233.1; -; Genomic_DNA.
DR STRING; 166423.A0A0M8ZTC8; -.
DR OrthoDB; 3540647at2759; -.
DR Proteomes; UP000053105; 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:SF149; FI01817P-RELATED; 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.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW ECO:0000313|EMBL:KOX69233.1};
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:UP000053105};
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..1184
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005830730"
FT DOMAIN 257..279
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00132"
FT REGION 1042..1061
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1184 AA; 134112 MW; ECCAAE8270A6E9D6 CRC64;
MRKAGGSHRG ARFVAFASLL LLVVLAFVEA SVIDRQKREF VIPDWIEIVD EPVHAENSKT
IQXNHRFVLI SVQSLGIVVQ TKCSRTFIFH SHFTLAVPSL WTRNDTTVDV MVRLEEIPRL
SRYLKQKDLE YQVVIENLQK AIDEENPSLS EQEVEELEGR KARYAWWQGV ARVPSMYSRP
RPLRYPVASV HGVGGPWQFR GHRMEWSSYH RLEDIHGYMD YLAETFPDVC SVVSIGNSVE
GRPLKVIRIS NGKANAPALW IDGGIHAREW ISPAAVTYII NHLVENSEDL EADYYILPVA
NPDGYEYTFT RDRLWRKNRK RSVGSQCTGV DLNRNFGYRW GGLGTSKDPC REIYAGSGPF
SEPETNAIRY FFEASAANFK AYLTFHSYGQ YILYPWGYDK RVPPDYADLE MVGKQVATAI
KKAGGANSVY TVGNSATTLY AASGGSDDWA KAILKIKYAY TIELRDTGKY GFVLPARYIT
PTAKEALAAV MVVTEACKSL ELVSFSPWTL LMACMKLEVL GLAPLAGISL MGVLVSQASS
PKEAIKSMML LIQLTKKYTL VYTDGAATVP QGISPQKLDE VKSVGLLTLQ ADKLSVSGPV
QMVVASTGDG PVRLSMNCLQ VWIQWPAVKM VLSFRMEPPH EWLNLTRGGS PYWMETWYGN
SPREALTPSV IRGCRLPVGT AQQTVKYFVS QIDDNSSSRK RLVSRLSVSI AKKLRYRDTI
EKSINNQNPG VQPNHLRDVG ANEEHGPVVH WFGPEFNVFG FRFLELFQIV HVFLRIRIQS
DQLMILFDNH ETMKAQTDNR CKKEKKKKKH YLNANRATQR GFLREEAGQT WVQFCHALGD
WLGEQLVLLI QKNCMRSTCD SYTNKFRERS GQILIVPIVE RRNKPWKNLL FLAISFSFLA
HRRGPLMESI VDALWVSKHH IMEKLVEITM SLVVRLRFWW TRSLRWSTAD AAVHGNCQWR
ATSTTGSTLV YHSVQGSIYG TAEDRCIVRR FSREGGECFM HRLIATKEQT TQMLSDKVEF
KLIPIYVSIK IYQKLNNKLG LDTLDPGEPG GTRKAKPPPR RPKECFAYKD TVLDGPLLRS
STIVTRCSDL PSMRRDLQRS DLVVEESPHS EPVQRLITSA ADAAVVHDIG EANIRAKSCY
GIIAASAVRR DKRSAKLREN YKLPHCSEIQ TDKSFKQNSY VNLY
//
