ID K5VXU8_PHACS Unreviewed; 777 AA.
AC K5VXU8;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=WSC domain-containing protein {ECO:0000259|PROSITE:PS51212};
GN ORFNames=PHACADRAFT_263533 {ECO:0000313|EMBL:EKM51419.1};
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:EKM51419.1, ECO:0000313|Proteomes:UP000008370};
RN [1] {ECO:0000313|EMBL:EKM51419.1, ECO:0000313|Proteomes:UP000008370}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB-10118-sp {ECO:0000313|EMBL:EKM51419.1,
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).
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DR EMBL; JH930477; EKM51419.1; -; Genomic_DNA.
DR RefSeq; XP_007400560.1; XM_007400498.1.
DR AlphaFoldDB; K5VXU8; -.
DR GeneID; 18918580; -.
DR KEGG; pco:PHACADRAFT_263533; -.
DR HOGENOM; CLU_003527_1_0_1; -.
DR InParanoid; K5VXU8; -.
DR OrthoDB; 2433441at2759; -.
DR Proteomes; UP000008370; Unassembled WGS sequence.
DR CDD; cd02851; E_set_GO_C; 1.
DR Gene3D; 2.130.10.80; Galactose oxidase/kelch, beta-propeller; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR011043; Gal_Oxase/kelch_b-propeller.
DR InterPro; IPR037293; Gal_Oxidase_central_sf.
DR InterPro; IPR009880; Glyoxal_oxidase_N.
DR InterPro; IPR015202; GO-like_E_set.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002889; WSC_carb-bd.
DR PANTHER; PTHR32208:SF105; COPPER RADICAL OXIDASE; 1.
DR PANTHER; PTHR32208; SECRETED PROTEIN-RELATED; 1.
DR Pfam; PF07250; Glyoxal_oxid_N; 1.
DR Pfam; PF09118; GO-like_E_set; 1.
DR Pfam; PF01822; WSC; 2.
DR SMART; SM00321; WSC; 2.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF50965; Galactose oxidase, central domain; 1.
DR PROSITE; PS51212; WSC; 2.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000008370};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..777
FT /note="WSC domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003888798"
FT DOMAIN 50..143
FT /note="WSC"
FT /evidence="ECO:0000259|PROSITE:PS51212"
FT DOMAIN 161..258
FT /note="WSC"
FT /evidence="ECO:0000259|PROSITE:PS51212"
SQ SEQUENCE 777 AA; 83329 MW; 87B8A3326E83D2DC CRC64;
MAPYSALAFG AIVLLSAHSH ASLLPHSIRD EDYLSKRASV GPVTSGLPSG WKYGACYVDN
ANGRVFAEED PDNSALTVES CISSCTSQGF SVAGMEYSVQ CFCGNELING AVTAPDSDCN
MACGGSATEA CGGPNRLSVY STGTITTLPV PTTQTTGLPG NWQYVGCIEE GANGNRVFPY
QIINTNNNSA EACLNQCGAF GYPAAGMEYG DECWCGDISD VTSNSAGNAP ATDCNQACSG
DPIHICGAGN RLSYYTFQGG IANWNTPSNT GRYEIGGVVV PLLVTLGINN KVAFLEKFGT
SEFDNSTGAY ELDLSLVDNF DLAWRTMHVK SDVFCSAAVV LPDKAARQLN IGGWSLQSTQ
GVRLYTPDGS PGVNGTNDWE ENYEELHLQR QRWYPSALVL VNGSVLVMGG EVGSNGAPEP
SLEILPTPEG GPTWIFLDYL NRTDPNNLYP YLINLPSGKI FVGYYNEARI LDPVTFDTVQ
VLPNMPGSVT SFLAGRTYPM EGSTVMFPQH APYTDPMTVL ICGGSNFGVA LDNCVSIQPE
VENPQWTLER MPSKRVMPCI VSLPDGTFLI VNGAMQGVAG FGLATDPNFQ ALLYDPTQPV
NSRISILNTT IVARLYHSEA TLLYDGRVLI SGSDPQTPGF PEEMRIEVYY PPYLTDGRTQ
PSFTIEETDW NYGGQYSITV TLHEGTTSTM RVSLVAATSS THGNAMGSRT IFPAFSCNGN
TCTITAPPNA NISPPGWHQL FVLDGPTPSF SHWVRIGGDP GLLGEWPNFP DFTLPGE
//