ID U4UJ45_DENPD Unreviewed; 529 AA.
AC U4UJ45;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Peptidase M14 carboxypeptidase A domain-containing protein {ECO:0000259|PROSITE:PS00132, ECO:0000259|PROSITE:PS00133};
GN ORFNames=D910_11376 {ECO:0000313|EMBL:ERL94094.1};
OS Dendroctonus ponderosae (Mountain pine beetle).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Curculionidae; Scolytinae; Dendroctonus.
OX NCBI_TaxID=77166 {ECO:0000313|EMBL:ERL94094.1, ECO:0000313|Proteomes:UP000030742};
RN [1] {ECO:0000313|EMBL:ERL94094.1, ECO:0000313|Proteomes:UP000030742}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23537049; DOI=10.1186/gb-2013-14-3-r27;
RA Keeling C.I., Yuen M.M., Liao N.Y., Roderick Docking T., Chan S.K.,
RA Taylor G.A., Palmquist D.L., Jackman S.D., Nguyen A., Li M., Henderson H.,
RA Janes J.K., Zhao Y., Pandoh P., Moore R., Sperling F.A., W Huber D.P.,
RA Birol I., Jones S.J., Bohlmann J.;
RT "Draft genome of the mountain pine beetle, Dendroctonus ponderosae Hopkins,
RT a major forest pest.";
RL Genome Biol. 14:R27-R27(2013).
CC -!- SIMILARITY: Belongs to the peptidase M14 family.
CC {ECO:0000256|ARBA:ARBA00005988}.
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DR EMBL; KB632379; ERL94094.1; -; Genomic_DNA.
DR AlphaFoldDB; U4UJ45; -.
DR STRING; 77166.U4UJ45; -.
DR MEROPS; M14.005; -.
DR Proteomes; UP000030742; 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:InterPro.
DR CDD; cd03858; M14_CP_N-E_like; 1.
DR CDD; cd11308; Peptidase_M14NE-CP-C_like; 1.
DR Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
DR InterPro; IPR000834; Peptidase_M14.
DR PANTHER; PTHR11532:SF94; CARBOXYPEPTIDASE D-LIKE PROTEIN; 1.
DR PANTHER; PTHR11532; PROTEASE M14 CARBOXYPEPTIDASE; 1.
DR Pfam; PF13620; CarboxypepD_reg; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00631; Zn_pept; 1.
DR SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 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 Reference proteome {ECO:0000313|Proteomes:UP000030742};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..529
FT /note="Peptidase M14 carboxypeptidase A domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004656200"
FT DOMAIN 131..153
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00132"
FT DOMAIN 270..280
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00133"
SQ SEQUENCE 529 AA; 60554 MW; F219EAACD8B116BE CRC64;
MFNVRMEGFR FSSQLFILLI AVCIGVSSGF EFKHHDNQEL FNVLRDVNIK CKNITRVYAL
NEGSVLGIPL YVIEFSTKPG RHEVCKYLIY IAMKHTTNIQ PNFNVICSFC YHFLQAIYQK
KPFKFHLLLK PEFKYIANMH GNEVLGRELL LKLADYLCDE YRTGNPHIKE LIETTRIHLM
PSMNPDGWQL ATDTGGHDYL IGRTNNNSVD LNRNFPDLDR IVFDNEYENS DKNNHLLEQL
TKLNDPLQPE TRAVIRLIMQ IPFVLSANLH GGDLVANYPY DESRSGSQSN EYAATPDDET
FRHLALAYSS RHPDMASQHR KGCVDSQFAK QGGITNGAQW YSLQGGMQDF NYLSSNDFEL
TLELGCEKYP PPEDLQLEWE RNKEALINYI WQSHIGIKGV VYDAKTKQPI SNAIIHVANV
TGVESIDIKH DITSVYGGDY YRLLTPGTYK VTVYKDGYVP HTKLVTVTNP SFTQALRVDF
PLKATASISF IESNNFIQPK IEDQYAARNR DWATWVEERE PILEPIAIA
//
