ID A0A395NN54_TRIAR Unreviewed; 1032 AA.
AC A0A395NN54;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Dna repair rad5 {ECO:0008006|Google:ProtNLM};
GN ORFNames=TARUN_4724 {ECO:0000313|EMBL:RFU77510.1};
OS Trichoderma arundinaceum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=490622 {ECO:0000313|EMBL:RFU77510.1, ECO:0000313|Proteomes:UP000266272};
RN [1] {ECO:0000313|EMBL:RFU77510.1, ECO:0000313|Proteomes:UP000266272}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 40837 {ECO:0000313|EMBL:RFU77510.1,
RC ECO:0000313|Proteomes:UP000266272};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:RFU77510.1}.
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DR EMBL; PXOA01000278; RFU77510.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395NN54; -.
DR STRING; 490622.A0A395NN54; -.
DR Proteomes; UP000266272; 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 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; 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.
PE 4: Predicted;
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:UP000266272};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 336..531
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 848..997
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1032 AA; 117344 MW; 161CC362568799A8 CRC64;
MKPLVSPPTS PPSSLCLPSP PKSQAQHGDY QELHKPSGSS ATFEWSEVRF ADKEEQDVPV
SLREQTNSTK NNVEDSLFVE DQSLEVEEQQ GSIPQNRTAT LDTDLSEQED TTDQQVANTL
SLAISEKLEP CGMLLPEEDE DSEYENESNS SFSSDGEFEP QLQSSNASAK KKSEKPRRKI
ATNAREYVAR LHEEEDRKYE KKMQQEEGRK LSAKRPYKRK LTDVDNSPCK ILKMESIGGL
LGHNDILPNS DGKQLLPMEP IKAKTHAQQF AQLKAQIPEN CDTRRRNTQK QDLQEAVSIF
GYKKVEAQDG RWLLKGMATA LECYQITAVA WMMKRELARA KPFGGLLADA MGMGKTVMSL
ACVVGNQADE QHRRDFCNAT LVVVPNKTTG KQWEGEAHKH CKEPIKDKVF IYDPSHQELM
DKCKESFIVI TTYKELMAQY PDKSTIRMLR EQYDSDHISF SRALERLVGP IFKINWYRII
LDEAHAIKNI DSRTTHACCG LTGKYRWALS GTPLANSSAE MYPYLKFTEC ESTWSSKDFK
EMYFTKGKPN AEFEAQTSLI MYRRTMLDEF NGRKIIDLPE TKSVDLLVPL STEEQLVVDA
VTRFYEKKTI LLEQGALQQD KFKVAIEDLG DASSRSMSWM LGRASQVRKR QTISHVFCIE
PLLRHSFDPE DLKALMSSLK QVKTRETIFE QIRMETGEER GILDYDVGMQ MLLKREEAVF
GKHFDMKELF SLTLQEISLR ETTCLLCNKA TPPVDPVYAD LCGHAFCSKC LCKAVKENAR
GEDIKLAVGE DIENLQAVLD SKDEDYREPG RDSKNVSIHQ ENDRNGFFIC STLLKDAPMV
PSTKLTATMA VVLTWLHEAP DDKILIFTQF IGTAKILGFM LETLDIEFVY YYGGLPLAQK
TRALEAIRKQ AEIKVMVATL KSGGQSLNLT AANRVIIIDP WWNKTAEQQA FGRVVRLGQE
KVSHLVNIRT AENIDDHIHD LQEKKAKDVN YTLQDDGHTP RPVSEIELRK AFFRKKSKKE
EKMKKKSKNT KT
//
