ID A0A061H8V9_9BASI Unreviewed; 1371 AA.
AC A0A061H8V9;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=DNA repair protein RAD5 {ECO:0008006|Google:ProtNLM};
GN ORFNames=PFL1_03328 {ECO:0000313|EMBL:EPQ29038.1};
OS Pseudozyma flocculosa PF-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX NCBI_TaxID=1277687 {ECO:0000313|EMBL:EPQ29038.1, ECO:0000313|Proteomes:UP000053664};
RN [1] {ECO:0000313|EMBL:EPQ29038.1, ECO:0000313|Proteomes:UP000053664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF-1 {ECO:0000313|EMBL:EPQ29038.1,
RC ECO:0000313|Proteomes:UP000053664};
RX PubMed=23800965; DOI=10.1105/tpc.113.113969;
RA Lefebvre F., Joly D.L., Labbe C., Teichmann B., Linning R., Belzile F.,
RA Bakkeren G., Belanger R.R.;
RT "The transition from a phytopathogenic smut ancestor to an anamorphic
RT biocontrol agent deciphered by comparative whole-genome analysis.";
RL Plant Cell 25:1946-1959(2013).
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
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DR EMBL; KE361632; EPQ29038.1; -; Genomic_DNA.
DR RefSeq; XP_007879036.1; XM_007880845.1.
DR GeneID; 19317438; -.
DR KEGG; pfp:PFL1_03328; -.
DR eggNOG; KOG1001; Eukaryota.
DR HOGENOM; CLU_000315_2_5_1; -.
DR OrthoDB; 200191at2759; -.
DR Proteomes; UP000053664; Unassembled WGS sequence.
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; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 2.
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; 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 SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00910; HIRAN; 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 Reference proteome {ECO:0000313|Proteomes:UP000053664};
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 630..867
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1073..1118
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1198..1366
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 245..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 662..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1132..1178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 675..693
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1371 AA; 148352 MW; 3214BBF2F97CD784 CRC64;
MAPSHTATGS QATAIQPSAA TTPTTSRDFF ASSPATTSQP SKGDVRDGDN AAGYTDSADA
HVAVAPASPT RSPIRRAPPR RAAAESKPLF FDIEDDDEDG DDSLGHDKSA SPSHKHKLPA
ARPQADDKDL DFRSPSSDPV LDDQDEPSTS YRPQLLSVPT AAVGALDDDL SPNFDTPSPA
GAKSVDKKRT RESALPTRSP TPAPSIHIDR DRFERRYLGT FVLSAWSMSR GTGYVQPGDL
VKIFRPRRKH PTSPAGPAAK SKSTSSGAKK AKQTTLSFGS SSGGGVGVGG AKSKGKEKED
YIVRFSNMKG FEVGRMPLEV ATWMSKLLDS EMAEFEGAVV DCPPSLTVGC DIILQVKAYI
RWEAFFLSLI TGHDPSGEFE AMRPETMETS VEKSLRERKV SLLRLYRACD LKPSLSNSIL
RAHRATNDLG SEAMLDHYGE DVPASVAASA SRAPSPSQAA RAPSLPGPLA SSGAPTASGP
GSAAAEPIDL GVGDNGDTMP AASDDEPNDG TEVTLNQLDE VYSKAQLHDI DLPEIEPPDT
FALKLRPYQK QALGWMKTME RVVGDRDDAV KADGETESPK GREPSLHPLW EEYEFPMDFD
DPEGNEALVT SNTRNFYFSP YTGDLSLDFQ KSSKGSRGGI LADEMGLGKT IMVASLIHAN
RAPEGGDVGD DESEDSSATQ QQTVKRARTA ANAPRQTSLA SAFAASMAGD QRRAMLRASV
ARGKATLVVA PMSLLSQWRD ELTRASQPGT LSAMLYYADS KADIIAQLES GKVDVVITSY
GTLTTEYKRF IDAGGALSRH AAAVAPLFAV EWLRVILDEA HHIKNRSTRN AKACCDLLAR
RRWALTGTPI VNRLTDLFSL LKFLRVEPWG DFSFFNSFIS KPFANKNPKA LDVVQVVLES
VLLRREKRMK DRDGRPIVEL PPKTVEVRNL DFSPLERQIY DNVYHRAYLQ YASMKANGTV
GKNYSVIFSV LMRLRQAVCH PLLVLRGDKA GTGLNGVAEG SLASNGAASL FDDDEGSQDL
RKLVAEFQTG SSSSGDGDAA AGDAYTQQVL EQLIKAQGGE GGGEGGQGDE EECPICFETK
IATCYLPKCM HSGCKDCILG FLQACEDREE EPCCPTCRKG PVAAEDLIEA VRTRSSRGGS
GKTGDGCKVA PSSPCEAIEV TDDDNGDGPA DEVPSSQHSQ PAVFFRRNDF RTSTKLAALL
EHLNELRVAE PGFKGVIFSQ FTSFLDLVQV ALKRNRHAFV RLDGTTSQKD REEVLKRFEG
WQKRSGSLLM LISLRAGGVG LNLTSASKVW LLDCWWNKST EDQAVDRVHR LGQTRPVTVF
RYLITDSIED RILAIQRRKT ALVSHALAGR RGADEGGKSE ALENLELLFG D
//
