ID U7PRH0_SPOS1 Unreviewed; 1229 AA.
AC U7PRH0;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=DNA repair protein RAD5 {ECO:0008006|Google:ProtNLM};
GN ORFNames=HMPREF1624_06671 {ECO:0000313|EMBL:ERS97339.1};
OS Sporothrix schenckii (strain ATCC 58251 / de Perez 2211183) (Rose-picker's
OS disease fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Sporothrix.
OX NCBI_TaxID=1391915 {ECO:0000313|EMBL:ERS97339.1, ECO:0000313|Proteomes:UP000018087};
RN [1] {ECO:0000313|Proteomes:UP000018087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58251 / de Perez 2211183
RC {ECO:0000313|Proteomes:UP000018087};
RX PubMed=24855299; DOI=10.1128/genomea.00446-14;
RA Cuomo C.A., Rodriguez-Del Valle N., Perez-Sanchez L., Abouelleil A.,
RA Goldberg J., Young S., Zeng Q., Birren B.W.;
RT "Genome sequence of the pathogenic fungus Sporothrix schenckii (ATCC
RT 58251).";
RL Genome Announc. 2:E0044614-E0044614(2014).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
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DR EMBL; KI440848; ERS97339.1; -; Genomic_DNA.
DR AlphaFoldDB; U7PRH0; -.
DR STRING; 1391915.U7PRH0; -.
DR eggNOG; KOG1001; Eukaryota.
DR HOGENOM; CLU_000315_2_5_1; -.
DR OrthoDB; 200191at2759; -.
DR Proteomes; UP000018087; 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; 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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000018087};
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 574..792
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 974..1019
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1063..1219
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1229 AA; 136809 MW; 41ECE66E3E63A21E CRC64;
MDAAEFQEPP SKRRRFSPDN GSEADHEGSK ARLDEKEKEN AQRLPQPKRR FFDDAVAIPS
LPRPQTAAQP TSSPAAMPTN GVKSTALPTN SFTPAKPSSP TPASRRPAQS SPARPGLSIT
PSSPSLSASP SPVGPVPFDS ELFAGIIGQE VGPDVLRIIR ESCGSDMERA VNMYFDGTYK
LKMQAAASRT NGVAVRPKAA SASTSASLST SSKPSISNQT STKTSPRKSV LQNRSAIPER
RYIGCFGVEG WATRSGANLL KHGDTVKIER QKIELPTIAG TKQRASKLGA SVVVRANSAA
AKRVDVIVRF TSTSGQEIGR LSKDTANWVS TLMDQRICRF EGVCVYAPER LRTNDTVVLQ
LRSFLLRSAF DQAPLKPAEN RTTGLFEEKE TAEERDLRLR QFALVRLFQE VNLLPTRVNE
AAAKRGRQDL LQAAEMAEKR EKEAAKEGLR PTQDIGSSQA PGGSDEPEDG QELEQDQLDA
LYAKAQSFDF NTPEADPPDT FALTLRTYQK QALHWMLSKE KDESVEERGE SMHPLWEEYA
WPLKDMDDND LPTVPDQASF YVNPYSGDLS LDFPAQDQHC LGGILADEMG LGKTIQMLSL
IHSHKSPIAM EAQQQKRQQA EGKLTSLVGG LRRIRTRLPN VVHAPCTTLV VAPMSLLAQW
QSEAENASVE GTLKSMVYYG SDKSANLQAL CAPDQAATAP DVVITSYGTV LSEFTQMWAK
GGGHEGHPGQ GLFSLNFFRI ILDEAHTIKN RQSKTAKACY ALLAEHRWVL TGTPVVNRLE
DLFSLIRFLR VEPWNNFSFW RTFITVPFES KDFMRALDVV QTVLEPLVMR RTKDMKTPDG
QPLVVLPTKH MEIVPVELSK VEREIYDHIY MRVKRSLTAN VEAGTVMKSF TSIFAQVLRL
RQVCCHPVLV RNMDIVADEV EAGAAADAAA GLADDMDLQS LVERFTATTD DPTDANAFGA
HVLGQIRDEA VNECPICSEE PMIQQTVTGC WHSACKACLL KYIDHETDHH RLPRCFHCRE
VINRRDLFEV VRHDDDPDTV AGQPPRISLL RVDVSESSAK VVRLIQHLRD LRRSRPTIKS
VVFSQFTSFM SLIEPALRRS NMKFLRLDGT MAQKARTAVL DEFRQSNKFT VLLLSLRAGG
VGLNLTTAKR VYMMDPWWSF SVEAQAIDRV HRMGQDEEVK VYRFIVQGSV EEKMLKIQDR
KKFIATSLGM MTDEEKKLQR VEDIKELLS
//
