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
//