ID A0A2K1QPN6_9PEZI Unreviewed; 1048 AA.
AC A0A2K1QPN6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=DNA repair protein RAD5 {ECO:0000313|EMBL:PNS17066.1};
GN ORFNames=CAC42_3636 {ECO:0000313|EMBL:PNS17066.1};
OS Sphaceloma murrayae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Myriangiales; Elsinoaceae; Sphaceloma.
OX NCBI_TaxID=2082308 {ECO:0000313|EMBL:PNS17066.1, ECO:0000313|Proteomes:UP000243797};
RN [1] {ECO:0000313|EMBL:PNS17066.1, ECO:0000313|Proteomes:UP000243797}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CQ-2017a {ECO:0000313|EMBL:PNS17066.1,
RC ECO:0000313|Proteomes:UP000243797};
RA Cheng Q.;
RT "Draft genome sequence of a variant of Elsinoe murrayae.";
RL Submitted (JUN-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:PNS17066.1}.
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DR EMBL; NKHZ01000054; PNS17066.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K1QPN6; -.
DR STRING; 2082308.A0A2K1QPN6; -.
DR InParanoid; A0A2K1QPN6; -.
DR OrthoDB; 200191at2759; -.
DR Proteomes; UP000243797; 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; 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 InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR45626:SF17; HELICASE-LIKE TRANSCRIPTION FACTOR; 1.
DR PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 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; PS00518; ZF_RING_1; 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|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000243797};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 328..526
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 746..791
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 844..1006
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 103..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 158..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1014..1048
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1048 AA; 118174 MW; BF64C1DA5125BDA3 CRC64;
MPKDSSQSIH SPLHEPPPEA SCSDSGRPST DQSTAEPLQY PTDSFTTPIK RELDNGDPNL
GHDLCTIPST LEEGPAYPRG VEPKDWDVPS IQDGVQRHIK EEKVSNQKVM SNSESHGTQE
NWPQTEEDDN NLLDLLLEEY PDWYVGDNTE EPHYLASTQA HASTEAYDLS HEDEQGDDDA
SCVEPSETVL DHLDPTDTDE HRPKRARKTQ RRAPDAGVFN EDDPTLGNID IDIFADAAEM
ENVPSQPRYG GTNIRAQALK DLTEGAKGVK RKRGIPSDAK VLNQACKAFG RSQIGPEPGG
GNQWWVRGLK VKLKPHQVIG TGFMLAQEQR ETEPRGGILA DQMGLGKTVM TLALINNKNP
QREQPRGPTL VVAPASVVRQ WADEIQKHCD TTSERYKVGK VMIFKASSEK NYLYPPLYLQ
SFTILITTYN EVAKSFPVGK PPKELTDEIQ REEWSKDHFE RNKGILHSMQ FHRVVLDEAH
VVRNPWTRNY LAVRALQSKH FWSLTGTPFI NGPADIWALL NLSGVGTDLT YGEFASKYNR
RPDPDDLALF NKWVRKCMIR RTHRSRLFDA KLISLPKTST QLLKVNFNPV ERKIYDLVES
RFRKNAEAID QECGRDQNLL TMVLRLRQLT AHPLILQDEL LNMLEREDLQ NLERVVIATH
RKHRKQTTAL LKRLRQTLAL KDPRDVNQRV VVEGPTAELL DQDSQENAFP DITTGQRYGL
RQKYDDLVRA LLEKKDQAGI EAIRQCVDCN NVAREPYFTS CKHIYCRRCI ENLQSEAAED
GLTSAACLVC DQLFSSVAPC DDSALRQAQE KTKKTAAKKS ALDVDLTEIL GVDGQIIPSA
KTIAVKAQIL QHREEEPGVK IIVFTQWLSM LRILESICKM ERWKCISYHG QMSAEARSEA
IKRFGNDDTM DVLLCSFHAG GVGLNLTMAS RVICIDHWWN NAMEQQAFSR CYRMGQTKET
SLLQICVNDT IDERMEAIKG RKQGTIDMVG GNDGKSSGKF TKDDLLKLLG ARKKKRVKEP
RVQEAATDDQ QSGIDDVESD EGEEHGVS
//
