ID M2RIT6_CERS8 Unreviewed; 1347 AA.
AC M2RIT6;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EMD38736.1};
GN ORFNames=CERSUDRAFT_112461 {ECO:0000313|EMBL:EMD38736.1};
OS Ceriporiopsis subvermispora (strain B) (White-rot fungus) (Gelatoporia
OS subvermispora).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Gelatoporiaceae; Gelatoporia.
OX NCBI_TaxID=914234 {ECO:0000313|EMBL:EMD38736.1, ECO:0000313|Proteomes:UP000016930};
RN [1] {ECO:0000313|EMBL:EMD38736.1, ECO:0000313|Proteomes:UP000016930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B {ECO:0000313|EMBL:EMD38736.1,
RC ECO:0000313|Proteomes:UP000016930};
RX PubMed=22434909; DOI=10.1073/pnas.1119912109;
RA Fernandez-Fueyo E., Ruiz-Duenas F.J., Ferreira P., Floudas D.,
RA Hibbett D.S., Canessa P., Larrondo L.F., James T.Y., Seelenfreund D.,
RA Lobos S., Polanco R., Tello M., Honda Y., Watanabe T., Watanabe T.,
RA Ryu J.S., Kubicek C.P., Schmoll M., Gaskell J., Hammel K.E., St John F.J.,
RA Vanden Wymelenberg A., Sabat G., Splinter BonDurant S., Syed K.,
RA Yadav J.S., Doddapaneni H., Subramanian V., Lavin J.L., Oguiza J.A.,
RA Perez G., Pisabarro A.G., Ramirez L., Santoyo F., Master E., Coutinho P.M.,
RA Henrissat B., Lombard V., Magnuson J.K., Kuees U., Hori C., Igarashi K.,
RA Samejima M., Held B.W., Barry K.W., LaButti K.M., Lapidus A.,
RA Lindquist E.A., Lucas S.M., Riley R., Salamov A.A., Hoffmeister D.,
RA Schwenk D., Hadar Y., Yarden O., de Vries R.P., Wiebenga A., Stenlid J.,
RA Eastwood D., Grigoriev I.V., Berka R.M., Blanchette R.A., Kersten P.,
RA Martinez A.T., Vicuna R., Cullen D.;
RT "Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete
RT chrysosporium provide insight into selective ligninolysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:5458-5463(2012).
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DR EMBL; KB445794; EMD38736.1; -; Genomic_DNA.
DR STRING; 914234.M2RIT6; -.
DR HOGENOM; CLU_007954_0_0_1; -.
DR OrthoDB; 119005at2759; -.
DR Proteomes; UP000016930; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032008; P:positive regulation of TOR signaling; IEA:InterPro.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR InterPro; IPR037590; WDR24.
DR PANTHER; PTHR46200; GATOR COMPLEX PROTEIN WDR24; 1.
DR PANTHER; PTHR46200:SF1; GATOR COMPLEX PROTEIN WDR24; 1.
DR Pfam; PF00400; WD40; 2.
DR SMART; SM00320; WD40; 4.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000016930};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT REPEAT 158..200
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 653..979
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 999..1020
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1189..1308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..724
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..786
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..840
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 901..919
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 929..944
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1205..1227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1241..1255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1284..1308
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1347 AA; 145078 MW; 0C509B568D2BC3C9 CRC64;
MPVTPVSTRT HSAQTLSQPS QTRISADWYS DSRSHGYQGP TRHVRFPRAM ANGGGAMAKS
GDGRRCVVAG KESLRIFRMS EPGSSASTDH KSITGRGGHR VEVSRNLWDS VGMKMDSATT
DVIWGQGLYD NKILTSARNG ELIMWDLNKS GPKCERKIRG HNRSIHALTY STHLQYYCMT
GSADGHIRVW DIRDLSKSVV QIFHPAAVRA AAFSPVGWQP HQAVVALDNG TICRWDLQMG
QRGQLDRILV AHSGPILALD WSLPASSASN AGTSSRSAPQ TTWYGAATGG SGIFDEILQG
PGGTAPGAAA GDSSGAGWLA SGGLDHCVKV WDLTAPSSKS HISHTPTYTL RTAYPIRRLL
WRPDYECELA IVSNADFSTG SEFSLAHGAG GSGSQPGLRL GVTSGPGAAV SSPKLEMLKP
STSDTMLAKD RRSSSASRHG SSDPIEIWDV RRGHIAKWML DRSAVDGGVT DLEFGDSSVI
WAQHHSGTFS QLDLRDASRP VDAIPRAALS WHAAGCLTFA ADKPKRWEIP YDDVKPEKRQ
NLQDLHIRDK AIGDAPYFPL TQSLGTFILE EAGEDLESFA SLAHRYVYEG AERQDICEHN
AKMAFNVGRH DTAQTWMLLH NLLEDILPEA PPTPPLSPLP GIVNPGLPHS MSAPAAIPTV
HTLPPPIPQP ARSMSIDADV PSSKKDSSPG SRSKRSGDRP SPSHSRSPLK TTPVSSTASS
PRRANASLPP HPAALFARRE SNVGHATKRP RLASYRRPSI STPSIHSTHS ESPSDSTRSV
SGGASSLRQV GDGALSDSDS DESDHGQGSR SASEGENGGA SEDEAPPRPP ISPYLYPRTG
IPQPSPLSQV AVQQTWTEDE KEDEDSPSPA STEESSDEAG PGSGLRRRPS KARRSLARSK
TRSRSSTVAS LSASAPKTRE EKSQPLKRQD SHSSVQTVTA GNTPVVHTKP LYGVLQRDDT
MRPSGSTKVE SIMSPRHTRV RSEALSTELV LDQEREMSAP LSVPDKAGTE RSQNAVPKQV
REAERRYREL AWEALCELFE ASADHGDVQL CTFLSLVAPK ELKVSKARTL RFVEAYLEIL
NRLRLHTAAA YIRKYVDAEE IRALTAMQTT VYTACNKCRK AIMLPPPAVQ RGAKPGGNYA
FCQGCRSATI VCTVCHLPVR ALVLACPVCA HGGHPDCLQK YYKDRPLTQI SAPSCPPSSP
RRSQPSQQPP SGLSLSLSGS GRPSASPAPS ALVTPIPEPR RLSPPRKERS ASVSVTGERR
GRAMSRGGGG SLSIPPLLRT ASHDGEGDGT RPGEDDESSA ARMSRMMEEG SVDERRLWAH
PCAAGCGHFC WAADEPFLEG ELGKEIE
//
