ID A0A226DWP5_FOLCA Unreviewed; 651 AA.
AC A0A226DWP5;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Carboxypeptidase A2 {ECO:0000313|EMBL:OXA49892.1};
GN ORFNames=Fcan01_15526 {ECO:0000313|EMBL:OXA49892.1};
OS Folsomia candida (Springtail).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC Entomobryomorpha; Isotomoidea; Isotomidae; Proisotominae; Folsomia.
OX NCBI_TaxID=158441 {ECO:0000313|EMBL:OXA49892.1, ECO:0000313|Proteomes:UP000198287};
RN [1] {ECO:0000313|EMBL:OXA49892.1, ECO:0000313|Proteomes:UP000198287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VU population {ECO:0000313|EMBL:OXA49892.1,
RC ECO:0000313|Proteomes:UP000198287};
RC TISSUE=Whole body {ECO:0000313|EMBL:OXA49892.1};
RA Faddeeva A., Derks M.F., Anvar Y., Smit S., Van Straalen N., Roelofs D.;
RT "The genome of Folsomia candida.";
RL Submitted (DEC-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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00059}.
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:OXA49892.1}.
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DR EMBL; LNIX01000010; OXA49892.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A226DWP5; -.
DR OrthoDB; 3540647at2759; -.
DR Proteomes; UP000198287; 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; cd00041; CUB; 1.
DR CDD; cd03860; M14_CP_A-B_like; 1.
DR Gene3D; 3.30.70.340; Metallocarboxypeptidase-like; 1.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR036990; M14A-like_propep.
DR InterPro; IPR003146; M14A_act_pep.
DR InterPro; IPR000834; Peptidase_M14.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR PANTHER; PTHR11705:SF91; CARBOXYPEPTIDASE A1 (PANCREATIC)-RELATED; 1.
DR PANTHER; PTHR11705; PROTEASE FAMILY M14 CARBOXYPEPTIDASE A,B; 1.
DR Pfam; PF00431; CUB; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
DR Pfam; PF02244; Propep_M14; 1.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00042; CUB; 1.
DR SMART; SM00631; Zn_pept; 1.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
DR PROSITE; PS00133; CARBOXYPEPT_ZN_2; 1.
DR PROSITE; PS01180; CUB; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW ECO:0000313|EMBL:OXA49892.1};
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:UP000198287};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..651
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013008312"
FT DOMAIN 533..651
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
SQ SEQUENCE 651 AA; 70409 MW; 0C5719EC460435AE CRC64;
MKAAIFLVLI LVAVASGRET GLRHFKGYKV FTTLATTKEQ LDALRVLYLG SDYDFWTSPN
GLGATDIMAA PEQIPELLKM FGEHGMEYTV KFEDVETLVE AERVANAKAS TGRIDWTSYQ
TYDSIVEFLT TINSNIAAVS VIGQTTEGRD IHVVKFSNGG PPKKSILFDS NIHAREWIAG
ATGTWVINEI LTNADSYTAI LQEVDIYVIP MINADGYEYS RTNDRMWRKT RSVNAGSSCM
GCDPNRNFDF QWAGESTSSD PCSDIYYGSA PFSEPETQAI DRFVREAEAA GVQFYAYITM
HSYANLWLIP WGYTAGAYPP DFPALLSLGQ AAVAALQAVS GTVYQAGQGA DILYGAGGTS
YDWAKNHGIK YTATIEMRGN SFVLPPEQII PNALEVWAAL QVVIQRVIET VPVEEDPTPV
ETVTSCGGEI EASSAAINFQ LDADIPAGQS CIWIVKPTFD NTRARLVSSG LIGGSGIYFT
EFNAYAGTPG QHVQIANVGE DYTFNGNFFL VTLTVAVGAN TGFSLEWYSS GLAGGAPSFS
GFAALSTPTG SYSYPVGGGQ YANSENALFI VNPEVAGTRT LAFTRLDVEN DATCSYDAVS
VLTWQNNEYT QLAKFCGTSL PTPFNLPTGL ALVTFRSDSS VTGTGFTFTW A
//
