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Database: UniProt
Entry: M2RR64_CERS8
LinkDB: M2RR64_CERS8
Original site: M2RR64_CERS8 
ID   M2RR64_CERS8            Unreviewed;       850 AA.
AC   M2RR64;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=CCHC-type domain-containing protein {ECO:0000259|PROSITE:PS50158};
DE   Flags: Fragment;
GN   ORFNames=CERSUDRAFT_29044 {ECO:0000313|EMBL:EMD41376.1};
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:EMD41376.1, ECO:0000313|Proteomes:UP000016930};
RN   [1] {ECO:0000313|EMBL:EMD41376.1, ECO:0000313|Proteomes:UP000016930}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B {ECO:0000313|EMBL:EMD41376.1,
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; KB445791; EMD41376.1; -; Genomic_DNA.
DR   AlphaFoldDB; M2RR64; -.
DR   STRING; 914234.M2RR64; -.
DR   HOGENOM; CLU_012455_0_0_1; -.
DR   OrthoDB; 1563424at2759; -.
DR   Proteomes; UP000016930; Unassembled WGS sequence.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd00303; retropepsin_like; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 1.
DR   Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1.
DR   InterPro; IPR032567; LDOC1-rel.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   InterPro; IPR001878; Znf_CCHC.
DR   InterPro; IPR036875; Znf_CCHC_sf.
DR   PANTHER; PTHR15503:SF22; CCHC-TYPE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR15503; LDOC1 RELATED; 1.
DR   Pfam; PF08284; RVP_2; 1.
DR   Pfam; PF00098; zf-CCHC; 1.
DR   SMART; SM00343; ZnF_C2HC; 1.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR   PROSITE; PS50158; ZF_CCHC; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016930};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT   DOMAIN          233..249
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50158"
FT   REGION          140..225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          245..271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          310..330
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          559..586
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        141..178
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        196..219
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EMD41376.1"
FT   NON_TER         850
FT                   /evidence="ECO:0000313|EMBL:EMD41376.1"
SQ   SEQUENCE   850 AA;  95958 MW;  A9B9CDE2C754A8D3 CRC64;
     GYGLPDWRQV SALSYFLKDK AYEFYVNTVS RNPRNWTLRR FFIELFNYCF PIDFRYRMRD
     KLERFRQTDK SVLDYVHQLE ALLLSAGVLS EQDKVERLWK GFKPSIQRGL YLDHLTPTSA
     TWERVVTVAQ YVEMADRAFT EPHSSGNNGG GQGGGSTPRP SGSQPSTSKF STKPGPPQAQ
     AQFRRRDGER RFPSARPSGQ GSSGGNHRND QQSGTGAPKL SDQEKARLAA EDRCYNCKEK
     GHFSRNCPKA NQVKTDRKGQ PPGVPSYSIE PSFGSAERLR DLAASTVRVD TDVVGLHSVG
     FWAADNNVPD LQSVSDSESE EDEEDILSPS QEPYYVDEDL PEFDPSDLGV PDPSLDNAIL
     EVMAMNHASA RLGDLYIQRA KRLLSRFYPY CSPSCQGPFG DLDVIDIVFS WYLRTRDDTY
     VMIQEHVPPA LSRHFVVPVE QFRSPQFNPP RWFAELVREA HDDDELDLDR YDESMGDVLS
     LEPVSVLNGM LPWPEHALRH GIDEARFVLL ERFADDVVIL DKYFALWLAV PVPLLLNERF
     NLVSWWIRQS GHARTWPPEE YLDGWDNDGP NPDNNPSDLG GDRTPPAVEL NAVATRGRQA
     EHDNLPALQR NAARPQDFKR KIPEPAVVVV EINGYPARAL LDSGSLADFM SSKLAHQLGI
     KTFELEKPLP VHLAVQGSRA KINVGCSAEI KYQAIRESRY FDIVNLLNYD LILGTPFWFQ
     HQISVGLNPT AVAVGSPIGL PIEGQQVRVL ESRAADMFEN EMERARLHIR EYAASICVST
     SDTPLPPLRV INHTIPLIDE GKVYHWRPSK CPDALRSAWN EKRDAYIKTG RWQISNARNT
     SPMLLLMKPG
//
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