ID M2SYA2_COCSN Unreviewed; 1512 AA.
AC M2SYA2;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=RING-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=COCSADRAFT_95107 {ECO:0000313|EMBL:EMD61926.1};
OS Cochliobolus sativus (strain ND90Pr / ATCC 201652) (Common root rot and
OS spot blotch fungus) (Bipolaris sorokiniana).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=665912 {ECO:0000313|EMBL:EMD61926.1, ECO:0000313|Proteomes:UP000016934};
RN [1] {ECO:0000313|EMBL:EMD61926.1, ECO:0000313|Proteomes:UP000016934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ND90Pr / ATCC 201652 {ECO:0000313|Proteomes:UP000016934};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
RN [2] {ECO:0000313|Proteomes:UP000016934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ND90Pr / ATCC 201652 {ECO:0000313|Proteomes:UP000016934};
RX PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT "Comparative genome structure, secondary metabolite, and effector coding
RT capacity across Cochliobolus pathogens.";
RL PLoS Genet. 9:E1003233-E1003233(2013).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; KB445647; EMD61926.1; -; Genomic_DNA.
DR RefSeq; XP_007702290.1; XM_007704100.1.
DR STRING; 665912.M2SYA2; -.
DR GeneID; 19141597; -.
DR KEGG; bsc:COCSADRAFT_95107; -.
DR eggNOG; KOG0298; Eukaryota.
DR HOGENOM; CLU_001592_2_0_1; -.
DR OMA; QLFEQMC; -.
DR OrthoDB; 8175at2759; -.
DR Proteomes; UP000016934; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd18070; DEXQc_SHPRH; 1.
DR CDD; cd16568; RING-HC_ScPSH1-like; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR45865:SF1; E3 UBIQUITIN-PROTEIN LIGASE SHPRH; 1.
DR PANTHER; PTHR45865; E3 UBIQUITIN-PROTEIN LIGASE SHPRH FAMILY MEMBER; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000016934};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 344..548
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1145..1183
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 49..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1205..1245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1407..1427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..75
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1512 AA; 170344 MW; C5F250916C33EDAC CRC64;
MSSFQGSARV LSASSYVPAN ARKKGEKLSS PAPDALSCIR TIHSLFPISE SCRDEEPPAK
RRKLGHDDTA PAKPPQEFSD EKSVVLVKIS LDLNMPTTSR EDEDMTYVST EPQEPIALAL
EKVRKDPSQS ALHMEVFNVV RNTGVEIVVT APASLLDSIS PHLRNAATLA TTRHGKISKS
GPRVAFCRCL LRRSAPERVT YKLEVEIRWI LGISVIEDEN IRGHCANEDL RLLSTYMRDA
VPQDNNTWTL SDFYDSIHVP PRDLKVSPRI GQALTETKLL PFQQRTVDWL LRREGVTFSP
SGALEPFVNT SPPSFKPKQD ATGRLCYVSQ LRGTIITDLA EATADTLRLL RGGILAEEMG
LGKTVELIAL MSHHKREIPQ GNVYDAYTET HVKPSGATLI IAPSSILEQW ISEMHVHAPE
LKVCHYTGLP PASARKDRHA TATVEHLMQH DVVVTTYQVL SREVHFAVPP PDRSSRHTNR
RERRSSPLMG ISWWRVCLDE AQMVETGVSQ AARVARMIPR CNAWAVSGTP LRKDVQDLRG
LLVFLRCDAY ADSKAVWGHF DKSSFKDIFH EITVRNTKDK IRDELQLPPQ KRIVITIPFT
TIEEQHYDEM IRQMCDACWL TPEGLPLEEG CQIEDAEQIE RMREWLVRLR QTCLHANVGR
KNRKALGTRH GALRTVHEVL EIMIEQNDSK WKAEAREMIL CLLKQGHIQA YAGDFANRAK
SALPYYSAAR LEAQSYIALC RTELVVEQEK LGRTSTASLR DVDEDDEENV EKMGRIPVLR
RSLRSFLELE HAAQFFTATA FHQIKEDPLQ TEPGSEDWHE KDRSETTYYE AAKVIRRELL
KESKTRAKEQ MERINAKKPF HQIAKISDLP DLGGIEARRI LDTIDNISDF LNAQTEQIQI
WRSEIVDILL TRLMDDDDDQ ETTGEEYDES LKVQDELYVY IMALRTLVAD RHAAVHGLQD
ALIEHEMNAA ERQALNKEPG ADRGHAPELV IEIANVRRRL KSMLQAGSLK GVISGIRSLI
NSVQWKAEAG DVRAASELTI LQEQFKKVQA IATDQAKAIT ELEKEQEMFR TTMNQRLEYY
RQFQQISDTV VKYKEDLDAT FDARAFNEAE ALRAQKKDSA AGFKTKCTYL KHLRSENQKE
VTAECIICRE DIEIGLLTAC GHKYCKECIN QWWRTHRSCP TCKQKLSSSD FKDISFKPSE
IKAQEETTSA SFKPQIQATS SSSSSSSSST LPSGPSSSPS SPSIYSSISN TTMREIRTIS
LTGSYGTKID MLARHLLWLR ANDPGAKSIL FSQFSDFFLV LRDAFKKWKI SAISTADRDG
IQRFKSDPSV DCLLLDAKSD SSGLTLVNAT YVFLCEPLIN AAIELQAISR VHRIGQMRGT
TVFMYLVAGT VEEAIYEISV KRRLEHMSSS SRRDNDKAKG KEDGVEGLGE QALDKANSAE
LENASLTNLL RKKGDGEVVP EHDLWHCLFG KKRRSGGEEV VRTEVERVVD RELRAGAVEA
RVAGEDEVMV DV
//
