ID M2R8R9_CERS8 Unreviewed; 1147 AA.
AC M2R8R9;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=CCHC-type domain-containing protein {ECO:0000259|PROSITE:PS50158};
GN ORFNames=CERSUDRAFT_97042 {ECO:0000313|EMBL:EMD35121.1};
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:EMD35121.1, ECO:0000313|Proteomes:UP000016930};
RN [1] {ECO:0000313|EMBL:EMD35121.1, ECO:0000313|Proteomes:UP000016930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B {ECO:0000313|EMBL:EMD35121.1,
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; KB445801; EMD35121.1; -; Genomic_DNA.
DR AlphaFoldDB; M2R8R9; -.
DR STRING; 914234.M2R8R9; -.
DR HOGENOM; CLU_012455_0_0_1; -.
DR OrthoDB; 1560817at2759; -.
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; IPR005162; Retrotrans_gag_dom.
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; PF03732; Retrotrans_gag; 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 Coiled coil {ECO:0000256|SAM:Coils};
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 638..654
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 37..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 103..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 320..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 755..779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 219..246
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..391
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..597
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..625
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1147 AA; 126754 MW; 8E3F72F05F926C3F CRC64;
MFTRSKARTL ASQNTEPRTP SVPGEYLATL NREPDEALDS ITNGPAVVAK PPPALGAEET
SRVEEAEEEV IRSVLLSETL SEKSDTGTSA VIEAGRNWLS HVNAETTTSH EPTGCDASGW
GRKKDAPPHL TKEAGDSEAI SKDVEPPDEQ EAAGERCAGP SSLDKGKSVD PNNWGALEID
LAELDPHVQQ RELDSYYVSR LQAPQGDRLD SKISQPVPLV DNQSEVESLK AELHELKLMF
ERALALKGAA QPMPEAIAEV PQVRETVKER GVTGEGEYDR GAANKVVEAV MKPESTRETR
PRFSSLQPIT QVEPEGFLGK AFSDLKGRRA RRSRRSMSPA PGDSCLSDES EAPSSHGYSL
EFDVGGGGST RRSKTRAEDK HPRLKPHEPE TYSGQADIEK FYKFMEQSKE YLAGYRLSKK
RYAFSLSHFT SGKAYSFYTL VVLGNPSEWS LHELFIGLFN YCFPADFHDR MRDKLDNFSQ
GNMSVREYSH ELQRMFRVVD DFTKTQKVRK LWRGFKGYII EGLISKEMSP TTESWKVVLH
AAEVLEEAAR AKERANKRAE RAPGSASKQQ DARDPKPKGH GNPKTHTDQK SRSPVGRDLR
GAAKVGSTRQ DGRKPKPPKH EHLKLTPEEC AQLAAEGKCY LCKETGHFAQ NCPRAAKVKT
HRKDRAPGIY SSNIEFGHHD TEELQELASR TVFTMELELN CVGIGPQAWY AASVLDVTSD
EAGLLKSRSV TYSWKRAMAY SPEDLYDTLP GLASVSDSSD DGWCSSDNDD GSEGDSMPIL
DPVSDSSSEE FGFSGDESEW CLSDREDSPC AQGTCPLQLP YGLREGRRPS AVGEIFAKRA
QSILLDLLLQ ALRIRLSGPV PSIQLMISIS KAVLSREEPT PCGWVTAGGS SQRFICTRDE
DTVQVWDTYL CIYLEIPLYL MYEPRFDLAN YYARMTHLRL GGQTWTTEDV DGKLVWLFDD
DVGCGALDGI ELAAVRVAAS DTYTALQRNA ATSRDFKRSV PEPVVVVVRI NGEPARTLLD
SGSLADFMSA KLAHQLGIKT FELAKPLPVH LAVQGSRAKI NLGCTADVDY QGIWEPHYFD
VVNLLNYDLI LGTPFLFQHQ VLLGLNPTKV IVGSLEALPI EGKSVRVLES RAADLFGERL
DSVRAAL
//
