ID K5WFX0_PHACS Unreviewed; 497 AA.
AC K5WFX0;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Carboxypeptidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=PHACADRAFT_206831 {ECO:0000313|EMBL:EKM57984.1};
OS Phanerochaete carnosa (strain HHB-10118-sp) (White-rot fungus) (Peniophora
OS carnosa).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Phanerochaetaceae; Phanerochaete.
OX NCBI_TaxID=650164 {ECO:0000313|EMBL:EKM57984.1, ECO:0000313|Proteomes:UP000008370};
RN [1] {ECO:0000313|EMBL:EKM57984.1, ECO:0000313|Proteomes:UP000008370}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB-10118-sp {ECO:0000313|EMBL:EKM57984.1,
RC ECO:0000313|Proteomes:UP000008370};
RX PubMed=22937793; DOI=10.1186/1471-2164-13-444;
RA Suzuki H., MacDonald J., Syed K., Salamov A., Hori C., Aerts A.,
RA Henrissat B., Wiebenga A., vanKuyk P.A., Barry K., Lindquist E.,
RA LaButti K., Lapidus A., Lucas S., Coutinho P., Gong Y., Samejima M.,
RA Mahadevan R., Abou-Zaid M., de Vries R.P., Igarashi K., Yadav J.S.,
RA Grigoriev I.V., Master E.R.;
RT "Comparative genomics of the white-rot fungi, Phanerochaete carnosa and P.
RT chrysosporium, to elucidate the genetic basis of the distinct wood types
RT they colonize.";
RL BMC Genomics 13:444-444(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 4-O-methyl-alpha-D-glucuronosyl ester derivative + H2O = 4-
CC O-methyl-alpha-D-glucuronate derivative + an alcohol + H(+);
CC Xref=Rhea:RHEA:67452, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30879, ChEBI:CHEBI:171667, ChEBI:CHEBI:171668;
CC EC=3.1.1.117; Evidence={ECO:0000256|ARBA:ARBA00024511};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67453;
CC Evidence={ECO:0000256|ARBA:ARBA00024511};
CC -!- SIMILARITY: Belongs to the carbohydrate esterase 15 (CE15) family.
CC {ECO:0000256|ARBA:ARBA00010092}.
CC -!- SIMILARITY: Belongs to the peptidase S10 family.
CC {ECO:0000256|ARBA:ARBA00009431}.
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DR EMBL; JH930470; EKM57984.1; -; Genomic_DNA.
DR RefSeq; XP_007393316.1; XM_007393254.1.
DR AlphaFoldDB; K5WFX0; -.
DR GeneID; 18912547; -.
DR KEGG; pco:PHACADRAFT_206831; -.
DR HOGENOM; CLU_008523_10_4_1; -.
DR InParanoid; K5WFX0; -.
DR OrthoDB; 1647009at2759; -.
DR Proteomes; UP000008370; Unassembled WGS sequence.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.287.410; -; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001563; Peptidase_S10.
DR PANTHER; PTHR11802:SF113; CARBOXYPEPTIDASE Y; 1.
DR PANTHER; PTHR11802; SERINE PROTEASE FAMILY S10 SERINE CARBOXYPEPTIDASE; 1.
DR Pfam; PF00450; Peptidase_S10; 1.
DR PRINTS; PR00724; CRBOXYPTASEC.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000008370};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..497
FT /note="Carboxypeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003885649"
SQ SEQUENCE 497 AA; 55145 MW; A71FA9342071ED2C CRC64;
MFSALSQIIA PLSLAICSVA SNVQQSFALD GGRLGPSGAG LFDPVKDLLS TSDYATLGHL
AFPDYNVRVK KSDSVTGPAY TGYIDIKARH LFFYFFESRR NPNEDDLIFW TEGGPGCSSS
IGVFMELGPC KVNDIHNVSR NPYSWNEKAN IFFVDQPVGV GFSYADHGEY DYFPKSTTEE
TAKDISAFVA IFFEHFSNFK GRPFHMAGMS YGGRFIPTFA SAVYDQNAQL LAAGMTPINL
TSVIIQNGCT DLKTMIPSYY NVACQHKTVA PVLGISPCIG IKQALPRCEK WLKEACYDVT
DAISCRTALS FCWSHIGMPF LTSDHNPYDV TKRCTPDELN DSLCYPITKK ISSFLDRAGV
RKTLGIDPST QSNFSACNDD VNRRFSASLD HVFPAEYYLE ALLERGIKVL IYVGDYDWVC
NWVGNEHMTL NLDWFGKNAF VSEPLREWKI GDRAVGVTRG SGPLVFATIH GAGHMVPYDK
GEEALVLVER WLAVKEL
//
