ID A0A1J9RSW6_9PEZI Unreviewed; 1218 AA.
AC A0A1J9RSW6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Dna repair protein rad5 {ECO:0000313|EMBL:OJD35651.1};
GN ORFNames=BKCO1_16000162 {ECO:0000313|EMBL:OJD35651.1};
OS Diplodia corticola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Diplodia.
OX NCBI_TaxID=236234 {ECO:0000313|EMBL:OJD35651.1, ECO:0000313|Proteomes:UP000183809};
RN [1] {ECO:0000313|EMBL:OJD35651.1, ECO:0000313|Proteomes:UP000183809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 112549 {ECO:0000313|EMBL:OJD35651.1,
RC ECO:0000313|Proteomes:UP000183809};
RA Fernandes I., De Jonge R., Van De Peer Y., Devreese B., Alves A.,
RA Esteves A.C.;
RT "Proteomics and genomics reveal pathogen-plant mechanisms compatible with a
RT hemibiotrophic lifestyle of Diplodia corticola.";
RL Submitted (OCT-2016) 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:OJD35651.1}.
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DR EMBL; MNUE01000016; OJD35651.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J9RSW6; -.
DR STRING; 236234.A0A1J9RSW6; -.
DR OrthoDB; 200191at2759; -.
DR Proteomes; UP000183809; 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:UP000183809};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 486..682
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 905..950
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1020..1175
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 835..864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 973..994
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..133
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..349
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1218 AA; 137499 MW; F0B215908659784F CRC64;
MSDNPIKPDP DGGPFIDPPR ASEAGASRET AIDVEQEEEP VTVKEEPRDD PDVSEAPTSK
YRDLGHDKAL PITIDDNDDD DDDGGDDHPR HDLPQDQMMA FHTGQEDQHN DPPEEPPRSP
AAPQSPLAPI SGPEAPIAPG DSIPLHLGNS LLSSPARKPK RRDLQQMRLL RKRLMSNVNN
NGYNPVYNAP PVLDPLHDAT PGPSDDAPAA EHERTPFEQA RIEYEAKKAN GTVTFEDEIM
FIRTNREEDA RTNQAAEDAR FLADGGCMDV EEDGGGPQSD SDDGLFVPQV SPPPRRRGKR
KSAWVRHAGL EDDGEDFPDV GEGPSSAMAR EMGDAEEELR EMLGEHLEGR RKKRAKRGEG
RKRKTGNGRA QSPQQEASTN VAHTLGSLMQ SNVFHDQAAN QNAPYLPEIT DTRKAEALKK
LLASVPENQR KRAVTDKKEL FKASRKFSHR AARPDGHGGW KITGMTTSLQ NHQLIGGGFM
RDRERGGVDD KPHGGICADA MGLGKTLEMI ANIINERPKK LKAGERKATL IVLPATLVSQ
WYAELNRHVD PKQRLQILVW KAGHRIETPR PVETLSRFDI VLTTYYEVQK SYPKAETPIE
LQTSEEKNRW WKEHYEAEKG PLHRVEWRRV VLDEAQAIKN FRSRTSLACR ALVSTYRWAL
SGTPILNSPL ELYPYFKFLE VPYTGSFRVF KSNYYNDGGR QEPMERLSIM VSQFMIRRTH
RDTLFGAPIV RLPKASDRVH WVHFNDLERA IYEIVHRRMV ARVNSFAREN TLQRNYRNVL
TMLLRLRQMT GNVLLVEVVM KDLLEREDHE KIRELAEVEV AGDATRRAQL IALRKVLAKP
PPPPDNEEDE SEGTPAVQVP GSLDGVPDGD ILTGGLHGLT FSFGKYLQDL RRGRDWEELK
KRTLCVMCHQ PPDSPYVTAC YHIYCHECLE MAQHDSAAKG EAHCRCSECQ CEYVWAQPCD
EFDLDSIMSD VEDGEVSTSA PPTSRWRKRK RDKGKDEENI ARSWIQKHGA VLPSAKTIAV
KAQILNWLEQ DPDAKILVYT QFISMIQIMK KVCQTEGWTF QEYTGQMAIA ARDRALDQFK
RNNTSILLAS LKCGGLGLNL TAAKHVISID PWWNSALEQQ AFCRVFRIGQ TEETSMTRFA
VAGTIDEKLI NMQVAKQEQI DRVMGDSGEP RENLTMHQMM RLFGPVKEDE QGRSFVIVED
RETLPRFNAD SEDEGDED
//
