ID R1GUT2_BOTPV Unreviewed; 1201 AA.
AC R1GUT2;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Putative chromodomain helicase protein {ECO:0000313|EMBL:EOD52071.1};
GN ORFNames=UCRNP2_1157 {ECO:0000313|EMBL:EOD52071.1};
OS Botryosphaeria parva (strain UCR-NP2) (Grapevine canker fungus)
OS (Neofusicoccum parvum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Neofusicoccum.
OX NCBI_TaxID=1287680 {ECO:0000313|EMBL:EOD52071.1, ECO:0000313|Proteomes:UP000013521};
RN [1] {ECO:0000313|Proteomes:UP000013521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR-NP2 {ECO:0000313|Proteomes:UP000013521};
RX PubMed=23766404; DOI=10.1128/genomea.00339-13;
RA Blanco-Ulate B., Rolshausen P., Cantu D.;
RT "Draft genome sequence of Neofusicoccum parvum isolate UCR-NP2, a fungal
RT vascular pathogen associated with grapevine cankers.";
RL Genome Announc. 1:E0033913-E0033913(2013).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; KB915786; EOD52071.1; -; Genomic_DNA.
DR RefSeq; XP_007580478.1; XM_007580416.1.
DR AlphaFoldDB; R1GUT2; -.
DR STRING; 1287680.R1GUT2; -.
DR KEGG; npa:UCRNP2_1157; -.
DR eggNOG; KOG0384; Eukaryota.
DR HOGENOM; CLU_000315_29_2_1; -.
DR OMA; WVQIRDD; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000013521; 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:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd18659; CD2_tandem; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.40.50.40; -; 2.
DR Gene3D; 6.10.140.1440; -; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 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 InterPro; IPR041150; Cdh1_DBD.
DR InterPro; IPR025260; CHD1-like_C.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
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 PANTHER; PTHR45623:SF14; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 1; 1.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR Pfam; PF18196; Cdh1_DBD_1; 1.
DR Pfam; PF13907; CHD1-like_C; 1.
DR Pfam; PF00385; Chromo; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01176; DUF4208; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50013; CHROMO_2; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:EOD52071.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000013521};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 15..78
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 115..175
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 213..384
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 515..673
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 781..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1051..1070
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1129..1201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 883..910
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 781..813
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1129..1194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1201 AA; 138306 MW; E7E7A587404BE224 CRC64;
MTPNYWAVAE EDDSPQIDRV ILHRRKEDTD EEMTNLSKHD FEYLVKWVGK APYHATYEDF
SLLSGYKGFR KVENYFRKIV LEEIMIMGDP EVPSEEKEKW NLDREKVEDL HADSRHVERV
IASQEGEEET EYLVKWKALP YEECTWEPAS LVGQLAQEQI DRYLDRSSKV PVSDKRESNI
QTRRKYVAIR EQPDYIKFGQ LRDFQLRGVS FLAYHWCRGE NAILADEMGL GKTVQTVSFI
NWLRHDRGQQ GPFVVVVPLS TLPAWAETFD NWAPDINYVV YNGNEASRKI IREYEMLVDG
NPKRTKFHVL LTTYEFVLAD STFLSQIKWQ FMAVDEAHRL KNRESQLYAK LMDFGAPSRL
LITGTPMQNT LGELSALMDF IMPGMIEVDE NIDLQSESAS QKIAELTNAI SPYMIRRTKQ
KVENDLPPKT EKIIRVELSD LQLEYYKNIL TRNYAALNQG GKGPKQSLLN IMMELKKASN
HPYMFPGAEE RMLAGNYRRE EQLKALVTSS GKMMLLDRLL TKLNKDNHRV LIFSQMVKML
DILGDYLQLR GYQFQRLDGT IGSGQRRQAI DHFNAFESQD FCFLLSTRAG GLGINLMTAD
TVILFDSDWN PQADLQAMAR AHRIGQKNPV TVYRLVSKDT VEEEVLERAR NKLMLEYITI
QRAVTDKGDK EAFDRAARAV AEPTSSDDIN RILKKRGQKM FEQTGNQRKL EELDIDAVLE
NAEEHKTEQP EGITTDGGED FLKSFEYTDV KLDLEWDDII PKDQLEELKA EEKRKLDEEF
LAREIEQSQP RKRKAPHEER EQRAAKKRAR QAAQEAAEAA QSGDESGPDN DPKRPLTEKE
IRNLIRAHEK FGSIEERGDE MIKEAKLTNR DREVVKATLK EVMDHCRDLL REEQAKNEAL
ARENNKVLTK KDKKAILFDW KGVKRLNAET ILERPTEMRL IKEAVEAASD WRNFRLAEAS
KPAHYSCPWG AREDGMLAVG ISKHGYGSWV AIRDDVELGM QEKFFLEEHR VDKKEERSKG
EEKNAKSPGA VHLVRRANYL ISVLKDKSSN GTNAAAKRAL DNHHRNNKKS VLLKKEFKKV
GQFISQGLKE RASPSEKARL WDFVANKYWP SKGVEGSKLN DMYQKIKISE DKAKATGGEQ
DKAKTEREQQ NKAKPERETE GKVKVEPESQ DKAKGSGREK EKEKKKDTSE KTNGETSKAT
E
//
