ID A0A2S4PY31_9PEZI Unreviewed; 1113 AA.
AC A0A2S4PY31;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=DNA repair protein rad5 {ECO:0008006|Google:ProtNLM};
GN ORFNames=EPUL_002171 {ECO:0000313|EMBL:POS86907.1};
OS Erysiphe pulchra.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Erysiphe.
OX NCBI_TaxID=225359 {ECO:0000313|EMBL:POS86907.1, ECO:0000313|Proteomes:UP000237438};
RN [1] {ECO:0000313|EMBL:POS86907.1, ECO:0000313|Proteomes:UP000237438}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cflorida {ECO:0000313|EMBL:POS86907.1};
RA Wadl P.A., Mack B.M., Moore G., Beltz S.B.;
RT "Development of genomic resources for the powdery mildew, Erysiphe
RT pulchra.";
RL Submitted (OCT-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:POS86907.1}.
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DR EMBL; PEDP01000228; POS86907.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S4PY31; -.
DR STRING; 225359.A0A2S4PY31; -.
DR OrthoDB; 200191at2759; -.
DR Proteomes; UP000237438; 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:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; 2.
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; IPR014905; HIRAN.
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:SF22; DNA REPAIR PROTEIN RAD5; 1.
DR PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF08797; HIRAN; 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; SM00910; HIRAN; 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|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000237438};
KW Zinc {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 499..704
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 886..931
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 972..1113
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 345..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..377
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1113 AA; 125761 MW; 55D99090A99973C5 CRC64;
MKDFEGPPVK KRRFFSDQSD TLRNSLNSIP RNHCKNDISV STTSSTAHAV RLSSSVSYHV
PLSESNESSR EDVSASFKEA DFQYLVGKKV APNLIKKLRD ASGGQMEKAI NLYFDGFCDN
SPSSFQLKTS ELRTKGLNYV EENTKDSVEK IQILKKSTPS TDLTPESRYI GAFGCEGWVT
RSGTTLIKHG DIVRIERQKI QPHKTSVGKG KQGQITAQVV PKLNIAASRR VDVLVRFTNT
KGVEIGRIPQ NFADWISTLI DQGVCKFEGV CVYAPERLRS GDTVFLQLQC FLLRTAFGIN
TLKLQGNRNT SIFEEKESYE EKQLSQKQAS LVKLFQEINI IPSKSSETME KQKRDRILQA
TKSESVDLHD KSKNKIITGP ETDSSSSQVE EAEDGKELEQ DQLDALYEKA QSFDFNSPAA
EPSNSFTMNL RHYQKQALYW MVSKEKNLQN AHKEVSMHPL WEEYTWPTND ADDKKLPTIP
NQEKFYVNPY SGELSLKFPV QEQKCLGGIL ADEMGLGKTI EMMSLIHTHK SAGTNTLGLD
LSSYEFPTKL SVNQNEKMFA PSTTLIVAPM SLLAQWQSEA ERASKKGTLN SFVYYGNDKL
SDLKRICHER TEVPNIIITS YGVILSEFNQ VMTKNGDRSP NFGLFSLKYF RVILDEAHYI
KNRQSKTAKA CYEIEAEHRW VLTGTPIVNR LEDLFSLIRF LRVEPWSNFS FWRTFITVPF
ESKDFLRALD VVQTILEPLA LRRTKDMKTP SGEALVPLPP KTIEIVNIEL SKKEKEVYDH
ILNRAKQSFE ANVEAGTVLK AYTSIFAHVM RLRQSCCHPV LTRNPNVVAD EEEAAKVTDT
ASGLTDDMTL QSLIDRFAAE TGDSAGKNVF GAHALKQIRD DAQNECPICS EETMIERIVT
TCWHSSCKKC LLDYINHQIE KGEKPRCATC RKFLDTQNLF EVVKDEETSS DDGPPKYSLH
RLGATSSAKI VALLSHLKRL RRDAPGTKTV VFSQFTSFLS LIEPALSQAH IPFMRLDGSM
AQKIRANVLA DFASSSKGIV LLISLRAGGV GLNLTMAKRV YMMDPWWSFA VEAQAIDRVH
RMGQLDEVKV YRFIVEDSVE ERMLKIQDRK KFM
//