ID A0A0L0CSG6_LUCCU Unreviewed; 1672 AA.
AC A0A0L0CSG6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Peptidase M14 carboxypeptidase A domain-containing protein {ECO:0000259|PROSITE:PS00132};
GN ORFNames=FF38_05970 {ECO:0000313|EMBL:KNC34344.1};
OS Lucilia cuprina (Green bottle fly) (Australian sheep blowfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC Calliphoridae; Luciliinae; Lucilia.
OX NCBI_TaxID=7375 {ECO:0000313|EMBL:KNC34344.1, ECO:0000313|Proteomes:UP000037069};
RN [1] {ECO:0000313|EMBL:KNC34344.1, ECO:0000313|Proteomes:UP000037069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LS {ECO:0000313|EMBL:KNC34344.1,
RC ECO:0000313|Proteomes:UP000037069};
RC TISSUE=Full body {ECO:0000313|EMBL:KNC34344.1};
RX PubMed=26108605; DOI=10.1038/ncomms8344;
RA Anstead C.A., Korhonen P.K., Young N.D., Hall R.S., Jex A.R., Murali S.C.,
RA Hughes D.S., Lee S.F., Perry T., Stroehlein A.J., Ansell B.R.,
RA Breugelmans B., Hofmann A., Qu J., Dugan S., Lee S.L., Chao H., Dinh H.,
RA Han Y., Doddapaneni H.V., Worley K.C., Muzny D.M., Ioannidis P.,
RA Waterhouse R.M., Zdobnov E.M., James P.J., Bagnall N.H., Kotze A.C.,
RA Gibbs R.A., Richards S., Batterham P., Gasser R.B.;
RT "Lucilia cuprina genome unlocks parasitic fly biology to underpin future
RT interventions.";
RL Nat. Commun. 6:7344-7344(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}.
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:KNC34344.1}.
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DR EMBL; JRES01000080; KNC34344.1; -; Genomic_DNA.
DR EnsemblMetazoa; KNC34344; KNC34344; FF38_05970.
DR OMA; HCREWIA; -.
DR Proteomes; UP000037069; 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; 3.
DR Gene3D; 3.30.70.340; Metallocarboxypeptidase-like; 3.
DR Gene3D; 3.40.630.10; Zn peptidases; 4.
DR InterPro; IPR036990; M14A-like_propep.
DR InterPro; IPR003146; M14A_act_pep.
DR InterPro; IPR000834; Peptidase_M14.
DR PANTHER; PTHR11705:SF91; CARBOXYPEPTIDASE A1 (PANCREATIC)-RELATED; 1.
DR PANTHER; PTHR11705; PROTEASE FAMILY M14 CARBOXYPEPTIDASE A,B; 1.
DR Pfam; PF00246; Peptidase_M14; 4.
DR Pfam; PF02244; Propep_M14; 2.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00631; Zn_pept; 4.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 4.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 4.
DR PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
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:UP000037069};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1672
FT /note="Peptidase M14 carboxypeptidase A domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005536920"
FT DOMAIN 562..584
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00132"
SQ SEQUENCE 1672 AA; 190683 MW; C36A907E261449B5 CRC64;
MSPNGQIKMG LQIAAALALM STLTFASNLA GYEGYNKYTV FHDNDKAFEY MVELQTQDVD
LDFWLLSRNM SIVSVSPVMQ PIFEKRLAEL GVTYQAKPLM EEMMKFNETI SSDSSDCEGS
ECGHSRTRRQ ARGFFTHFPR YSEILNYMNA LAARYPQYCR YESLGRSNEG RHLAALSISL
NSRSRPRRVA YIQSGTHGRE WITPLATLYF ANELLTNIKA FTRILNDVEI YVLPLVNPDG
YEYSFTTDRF WRKNRHHYPG RSCAGVDINR NFPNNWNYRG ASQNLCSEVF SGTSPASEPE
TSAIVRYLEY NRQRIKLSLD VHSFGKFIFY PYGYSRNAHA PTRTFLHSVA SRAANQITKY
RGTHYSVGTS SSILYEASGG LDDFAYGNLG IPMSFTLELP GDNFQVASSD IIHVYKIYEI
HFNNDNQNIQ FVKKFPQITQ PLTTNRPKRD TSTRVLISPR EELKVLKYLK KKNIHFDIIN
RNVAESIRNE RKATNYSASA NTINFESYQR FDVINNYMEY LKMQYPQRLK LMSVGKSYEG
RDLKAILITN NTESEVKTAE RPLIFIDAGI HAREWIAPAT ALFIMQQLVE NNTFYERELT
MYDWLIWPVV NPDGYEYTHD IDRFWRKNRR PSNFSKCLGA DLNRNFDFNF AYSGVSKNPC
SEIYCGDEAF SESESKALRD LLISINKTCR MYLTLHSYGN YFLYPWGYDK SLPSTWPYLD
AVAYAGASAI KMASGTVYMV GGAANMLYPA AGGSDDYAFA LAKIPVVICM ELPSGGNNFD
PPSDKIQSIG TMSRVGAIVL ALAAVLALTS AEGYNGYKVF EVLPKTQEQT DFLYELSKMD
EFYDFFTLRR IPNHMARVMV NPNEEENFLN ALAEHNISFR IVIDDAGRTM EHEFQMNKMR
RSLTPFSGKG RLSTERYYSH GEINNYIEDL EKRFPSRVFL KTVGKSYEGR SIKTITITNG
DGRANKNVIF IDGGFHAREW ISPAAVLYVI EQLVENFEEN AELLLDYDFI ILPVVNPDGY
EYTQTSSSAR FWRKTRQPYQ TESKICYGAD PNRNFDFHWN EEGASSNPCS DTYAGPYGFS
EPETIIVRDL IHSLKHRGGM YLTVHSYGNY LLYPWGYTAD LPETWPDLDE VAKTGYDAIF
NATGTKYTYG SSTNVLYVAA GASDDYAFQA GFKIAMTMEL PGGGSMGFNP PASSIDRMVK
ETWVGIRAMA KKVAEKYPTE RIEFFSVKVK WTSFKMLNFR LMVVGLLWAN IYFVCINANS
YDGYKLYELL PKEEKDLNLL KNLNQQEERY DFLNSQTVIV EPNSFREFEN TLNKYNLKYK
IVDEDVGKTL KRNFEVNGLL KTLKPYKGQG RLSTERYYSH GEINAYLEYL AQSYPQRVVL
KTVGYSFEGR PMKALTITNG QGSYDKNVIL VDGGFHAREW ISPASAIYAI EQLVENYEEN
KELLESYNWV VLPVVNPDGY EYTQVSADTR MWRKTRKPLF HEGAICYGTD PNRNFDFHWN
EEGASSDPCS NTFAGPKAFS EPEAMVVRDL IHTFSVKGQM YLTLHSQGKL LLYPWGWSAD
LPDTWEDLHE VATAGAEAIY QATGTNYTVG SSTTVLYVAA GASDDYAFNA GFPISFTMEL
PGAGSTGFDP PVEMIDELVK ETWVGIKAMG LKVIEKYPFF FLINNNRKSF LI
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