ID A0A1V8TX81_9PEZI Unreviewed; 1348 AA.
AC A0A1V8TX81;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=SWI/SNF family DNA-dependent ATPase Ris1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=B0A51_17513 {ECO:0000313|EMBL:OQO16038.1};
OS Rachicladosporium sp. CCFEE 5018.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX NCBI_TaxID=1974281 {ECO:0000313|EMBL:OQO16038.1, ECO:0000313|Proteomes:UP000192386};
RN [1] {ECO:0000313|Proteomes:UP000192386}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCFEE 5018 {ECO:0000313|Proteomes:UP000192386};
RA Coleine C., Masonjones S., Stajich J.E.;
RT "Genomes of endolithic fungi from Antarctica.";
RL Submitted (MAR-2017) 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:OQO16038.1}.
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DR EMBL; NAEU01001286; OQO16038.1; -; Genomic_DNA.
DR STRING; 1974281.A0A1V8TX81; -.
DR Proteomes; UP000192386; 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 CDD; cd18008; DEXDc_SHPRH-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; 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; 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; PF13923; zf-C3HC4_2; 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 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:UP000192386};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 569..758
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 918..972
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1161..1327
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 46..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1004..1119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..308
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1008..1027
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1048..1062
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1348 AA; 147773 MW; 198490E0FD5DC516 CRC64;
MADLTSREAI EEELAFQDYL FMTLEEASDS YEERLAEIED ARRDLNERLQ ALEQSGSQDV
GTNGYGGGPV GYGNSISSYD GVNDGPSYPA LGAPSNSRVS SGSSNSGYAG GAGLKRARPE
SGAYPDYPSK RNTPEPSSAG TPSSHGSFDW PTLDQPASAA AGNGLEAAKR RQMAAEAAIA
RQLAARRADE DFARSLSGQS GGAMASSSRG PSGVQTTLRG DGSWARPPPP AAVKQESRPV
FGQSNGYHIP PTPVNEQSSV HRPQSNSLYG APGSHLPKPN QPRGQSNGHG HHVKPESGYG
HSHHNGIKRE PSLALPPQQL PQRTRAQVVD LTGDGSDDDD GLAEIMPQHF TPNDRGLATR
NQTLPSIHRQ QLPGLSPNVS NGMYTAANLM QMPGAYPGSP SMSSGYGGQP VYNRLPPLPS
TRRAPVQQPN AGALHMMPGE TPGQFIARLS GRAMNGAANT LGSTVNQLNG LINGPYARPI
DLDDDDSDVE FAGYGARAPG YQGHDDLYNT RYNAIHDHNP EKTREEINAL LDNIRPDDDM
PEELLVKTPA SMALTLHKYQ ELGLTWMKGS EEGANKGGIL GDDMGLGKTI QMISLMVTRK
SEDPRCKTNL IVAPVALLRQ WKQEIATRIK TGRHALTVFT HHGQGKAKSF DALRKYDVVL
TTFGSLASEL KKREAFALRK KNDPTARPYP REQCALIGED NHWYRVILDE AQNIKNKSTQ
SAKAACSLQA TYRWCMTGTP MMNNVEELYS LIRFLRIRPY NVWETFRKDF TQPLKSSDDG
FRGQAMKKLQ TLCVKLMIRR TKKSEFQGKP IIVLPERTTE VDNPVFNDDE KNLYTALETK
TAVQFNRYLK AGTVGRSYTA ILVLLLRLRQ ACCHPHLIKD FSVSEAAGVT IADMEALAKE
LSEQVISRIK DTDGNFECPI CLDACTNPAI FVPCGHDTCR DCFATLADPA NATAVGEADG
EGGASVKCPH CRAKVDPKRI TDFNSFRKVH MPESFTEAER EALAVENGPE DSETESEDSE
TESEDEDQDH TLGGFIVNDE DVDSETESEG DVKPKFKKES GGELAHGPQG MFSSSKVKLK
KKKKSKEKSF TWMNGTGEGT SSGKGKGKAA MKGKGKGKKN AELTLAELKK LSTRNQGARK
KYLKKLRKEF ISSAKIDKTM ELLDTIISAP DDPTLGGEKV LIFSQWTSLL DLMEIPIDEK
GWKYRRYDGS MAASARGDAV DDFKSPRENV RIMLVSLKAG NAGLNLNVAS QVIILDPFWN
PYIEEQAIDR AHRIGQLRDV KVHRVLVTET VEDRILALQE KKRQLIETAL DEKEGKKISR
LGVQELAYLF GVTRNPNEVV RYQAQDNR
//
