ID A0A0G2GXV5_9EURO Unreviewed; 1218 AA.
AC A0A0G2GXV5;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Putative swi snf family dna-dependent atpase ris1 {ECO:0000313|EMBL:KKY28003.1};
GN ORFNames=UCRPC4_g00738 {ECO:0000313|EMBL:KKY28003.1};
OS Phaeomoniella chlamydospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Phaeomoniellales; Phaeomoniellaceae; Phaeomoniella.
OX NCBI_TaxID=158046 {ECO:0000313|EMBL:KKY28003.1, ECO:0000313|Proteomes:UP000053317};
RN [1] {ECO:0000313|EMBL:KKY28003.1, ECO:0000313|Proteomes:UP000053317}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY28003.1};
RA Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT "Distinctive expansion of gene families associated with plant cell wall
RT degradation and secondary metabolism in the genomes of grapevine trunk
RT pathogens.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKY28003.1, ECO:0000313|Proteomes:UP000053317}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY28003.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKY28003.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LCWF01000018; KKY28003.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2GXV5; -.
DR OrthoDB; 200191at2759; -.
DR Proteomes; UP000053317; 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:InterPro.
DR CDD; cd18008; DEXDc_SHPRH-like; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR CDD; cd22265; UDM1_RNF168; 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; 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 InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45626:SF24; ATP-DEPENDENT HELICASE ULS1; 1.
DR PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 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; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000053317};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 466..655
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 813..864
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1046..1209
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 59..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 889..1024
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 10..44
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 91..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 891..928
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 929..980
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 981..999
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1000..1024
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1218 AA; 137144 MW; 3F9C757F8D3BBD63 CRC64;
MEPYSAALPL EHLEYELDTT LVQLETLEST DEDYESSKME LENRVRYLQY EIRHAGRERG
DMESRSVTPG RTRYSPFVDG SHDYDDNIAA LPASDSSSQG ETYNPFLTSP VSLPSRKRQR
ESLDLVSQTQ HLAKSSRPTP SSLSIASSPS ASISDDFNDE ESEMMRQLLG DTITEEYRGL
ERESRRAEHE LRKRREQERK DEELARALQE EMNQQQPGPS AMARNTSQAV FDPATRRLRT
MLPPAAPAKP SQTSFFKLSD QRHDQPSSSR TTLSDSGYSS APNLLGNESS TSFYDLSSDD
DDFQEIPSAQ FRPNMNKTPQ SYTLNNTFIP RVVPSWKHPH ADYSPSPWVG AGGSNVYSNP
AYDHLDHEIK SYPSAMGFAS GTMPGAFPSL SDLSSFSPIL PVPNVRDRLR YGIDGTTGNT
EEEIKNLLEN IRPDEEIAPE DREGDPEGMK CPLLPHQKLG LAWMKSMEEK SNKGGILADD
MGLGKTIQAL ALIMARPSED PQRKTTLIVG PVALMQQWRR EIESKICATH RLSALVLHGN
DRNIPWRDLK HYDIVLTTYG TIATEFKRKV AWDAKKKYNP NIRPSGKEDF LPVLGDECKW
YRVILDESQH IKNKATKAAL GASAIQSQYR WCMSGTPMMN NVLELYSLIH FLRIRPYNSS
EAFNRDFTRP LKNSYPEHKE RAMRALQALL KAILLRRTKK SKIDGKPILQ LPEKIVETTH
AAFSRDELNF YQALEGRAQL TFNKYLKAGS VGRNYSNMLV LLLRLRQACC HPHLIKDFAI
DTGANSEMDL KANAEAFGPD VVARLRDIEA FDCPVCIDAA ENPQIFFPCG HAVCLDCFSR
LSDPAQGLAE GREGVLQVKC PNCRAFIDPQ KVTDFNTFKA VHFTSDVDEG TAQADSDEEE
AASQAEADGE DIDTETDSGS DDESEAVDDS IKDFVVKDDD EEALKSRASN DDEDDDLNSR
QPRNVKEEPV VEGKGKEKAD GGKKKKAKKA KKKSKGKGKG KERDKLEKTQ LSLAHLRREG
QRNKASMRKY LKRLEENWIT SAKIETTMEI LEAVHNRGNR EKTIVFSAFT SLLDLLEVPV
SRKNWHYKRY DGSMTPNERN AAVNEFTDKS SCTIMLVSLK AGNAGLNLTA ANNVVIFDPF
WNPYIEEQAI DRAYRIGQMK EVHVHRVIVP DTVEDRILDL QAKKRELIEN ALDENAGRSV
ARLGVRELGF LFGVNRHI
//
