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Database: UniProt
Entry: M2RRM7_CERS8
LinkDB: M2RRM7_CERS8
Original site: M2RRM7_CERS8 
ID   M2RRM7_CERS8            Unreviewed;       723 AA.
AC   M2RRM7;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EMD41097.1};
GN   ORFNames=CERSUDRAFT_131629 {ECO:0000313|EMBL:EMD41097.1};
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:EMD41097.1, ECO:0000313|Proteomes:UP000016930};
RN   [1] {ECO:0000313|EMBL:EMD41097.1, ECO:0000313|Proteomes:UP000016930}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B {ECO:0000313|EMBL:EMD41097.1,
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; KB445792; EMD41097.1; -; Genomic_DNA.
DR   AlphaFoldDB; M2RRM7; -.
DR   STRING; 914234.M2RRM7; -.
DR   HOGENOM; CLU_014957_0_0_1; -.
DR   OrthoDB; 1368965at2759; -.
DR   Proteomes; UP000016930; Unassembled WGS sequence.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   CDD; cd06890; PX_Bem1p; 1.
DR   CDD; cd11878; SH3_Bem1p_1; 1.
DR   CDD; cd11879; SH3_Bem1p_2; 1.
DR   Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 2.
DR   InterPro; IPR035550; Bem1/Scd2_PX.
DR   InterPro; IPR035548; Bem1/Scd2_SH3_1.
DR   InterPro; IPR035549; Bem1/Scd2_SH3_2.
DR   InterPro; IPR001683; PX_dom.
DR   InterPro; IPR036871; PX_dom_sf.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR15706:SF2; SH3 AND PX DOMAIN-CONTAINING PROTEIN 2B; 1.
DR   PANTHER; PTHR15706; SH3 MULTIPLE DOMAIN; 1.
DR   Pfam; PF00787; PX; 1.
DR   Pfam; PF00018; SH3_1; 2.
DR   SMART; SM00312; PX; 1.
DR   SMART; SM00326; SH3; 2.
DR   SUPFAM; SSF54277; CAD & PB1 domains; 1.
DR   SUPFAM; SSF64268; PX domain; 1.
DR   SUPFAM; SSF50044; SH3-domain; 2.
DR   PROSITE; PS50195; PX; 1.
DR   PROSITE; PS50002; SH3; 2.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000016930};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          35..98
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          127..189
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          274..409
FT                   /note="PX"
FT                   /evidence="ECO:0000259|PROSITE:PS50195"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          99..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          449..469
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          485..641
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        101..122
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        487..532
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        544..641
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   723 AA;  79687 MW;  93842BC683D014BF CRC64;
     MKTLRKSLHG HKDHHISSPI VLPSSLSKPV GSIVPPKKVI KALNSHKATA PQELSFEKGD
     FFHVLKDVNE QGLWYEAHNP MTGARGLVPA YMFEEFQKGA PTPRTPTTIS PTRDSQLNGR
     PLSSPKTTTY YAVVVHDFAA ERTDELEAKA GDTIAVVAQS NREWFVAKPI GRLGRPGLIP
     VSFVEIRDPS TGQPVEDVDA LIDSGVLPRV EEWKQAMLKY KSTSIALGVL DEQSAPSILQ
     VASQDPAINV VAPTPQYQPP ANTSITRPAT PKVLPEGILL SADVKSFHYE TEEYWFRVNA
     VFQPYGASGS QPLPPARQLV LFRSYNDFYD FQVSLLDMFP HEAGRPDVST RILPYMPGPA
     EQVDNETTMT RRAELDEYLH KLCELQRYAR YILEHNLIRQ FLALKPGDAE VEIAPRIEEI
     EALSEPTYAD DQPDEAPDVD YEAERMERLR LSGRHEPSED GSDYDEGADV MGRAYDGERY
     DYGHRLSSRA STGQDIPTTA PLRTKPRSAS ASVGSPGQQT GFSHSRAESM SAYRRPSQAP
     PRAVSPQAPQ SYSRTSSPLL PSKQPGNSRT SDAARSYSSL EIDPYRQGSQ SRSSLASSHD
     PSPVSVRSSE AASIATSATS ASGGRSRSQS TAAHNPPISA NNPQTAFVKI KIFDRVSDDL
     IAIRVHPQVT HAQLMDKVQA RLGQGVLNLR YRDSLSNDLV GLEGDEDLTQ WLESTDRHVL
     YAE
//
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