ID A0A093X2M5_9PEZI Unreviewed; 1147 AA.
AC A0A093X2M5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=DNA repair protein RAD5 {ECO:0008006|Google:ProtNLM};
GN ORFNames=V490_08819 {ECO:0000313|EMBL:KFX86813.1};
OS Pseudogymnoascus sp. VKM F-3557.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1437433 {ECO:0000313|EMBL:KFX86813.1, ECO:0000313|Proteomes:UP000029320};
RN [1] {ECO:0000313|EMBL:KFX86813.1, ECO:0000313|Proteomes:UP000029320}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-3557 {ECO:0000313|EMBL:KFX86813.1,
RC ECO:0000313|Proteomes:UP000029320};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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:KFX86813.1}.
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DR EMBL; JPJS01002579; KFX86813.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093X2M5; -.
DR STRING; 1437433.A0A093X2M5; -.
DR HOGENOM; CLU_000315_2_5_1; -.
DR Proteomes; UP000029320; 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; cd16572; RING-HC_SpRad8-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; 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:UP000029320};
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 503..712
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 894..939
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 981..1137
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1147 AA; 128702 MW; 4B8E5CF28855F855 CRC64;
MNSFDSDGRP AKKRRFFTDK PEELEVDASS PAAPIPGEVE TAASEAEYGS PKETTLDDRD
TQTDVQPHAD SETPLVSDQE TFELVIGDKV DPETWRLLKQ ASGDNMERAI NMYFDGSWKR
PTVAVATSTT TSQPLTINPV KPEVSNAARS SSGPRSSKQT PRPATNIRRI PESRYIGAFG
VEGWATRSGT ALIKHGERVR IERQKIQPPK PPPVKIGKNK IAPLQVTPKP RGAAARRIDV
IVRFTNSRGE EVGRLSRETA NWVSTLIDQQ VCSFEGVCVY APDRVRTNDT IFLQLRCMLL
KSAFENKGFK PPDNRTTGLF EEKETSEEKD LRLRQVALVK LFVEVNLLPS RTSETTTRHK
RQGLLQAAEV AEQYEKEAAK KEKVAGEPDS SPSSDTEDGK ELEQDQLDTL YRKAQSFDFS
APEAEPANTF AMDLRPYQKQ ALHWMMAKEK DEKEEEKEAS MHPLWEEYVW PLKDMDDQEL
PPVEGMDNFY LNPYSGELSV EFPVQEQHCL GGILADEMGL GKTIEMMSLI HSHKSDVAMK
LQDGEPTITS VNHLPRLQTF SSVERAPCTT LVVAPMSLLA QWQSEAENAS KEGTLKSVVY
YGNEKAVNLQ SLCCAANAAS APNVIITSYG VVLSEFNQVA AKNGDRGTHG GLFSLNFFRV
ILDEAHHIKN RQSKTARACY EIEAEHRWVL TGTPIVNRLE DLFSLVRFLR VEPWSNFSFW
KTFITVPFES KDFMRALDVV QTVLEPLVLR RTKDMKTPNG EALVPLPPKT IEIVNVELSG
AEREVYEHIF FRAKRAFAEN VEAGTVMKAY TSIFAQILRL RQTCCHPILV RKQNVVADEL
EAEEAADAVS GLADDMDLQS LIERFTAETD DSADANAFGA HVLEQIRDEA DNECPICSEE
PMIEQTVTGC WHSACKKCLL DYISHQVDKG DAPRCFNCRE PLNTRDIFEV VRHEADPDAL
DSKPRIALQR LGSNSSAKIS ALMDQLKALR REHPGTKSVI FSQFTSFLSL IEPALTRAGV
AFLRLDGTMA MKARAAVLKS FRDAKGFTVI LLSLRAAGVG LNLTMARRVY MMDPWWSFAV
EAQAIDRVHR MGQTGEVEVK RFIVRESVEE RMLRIQERKK FIASSLGMMS DEEKKVQRIE
DIKELLS
//
