ID A0A2T4C3N8_TRILO Unreviewed; 876 AA.
AC A0A2T4C3N8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Rad17-domain-containing protein {ECO:0000313|EMBL:PTB76144.1};
GN ORFNames=M440DRAFT_1401602 {ECO:0000313|EMBL:PTB76144.1};
OS Trichoderma longibrachiatum ATCC 18648.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=983965 {ECO:0000313|EMBL:PTB76144.1, ECO:0000313|Proteomes:UP000240760};
RN [1] {ECO:0000313|EMBL:PTB76144.1, ECO:0000313|Proteomes:UP000240760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18648 {ECO:0000313|EMBL:PTB76144.1,
RC ECO:0000313|Proteomes:UP000240760};
RG DOE Joint Genome Institute;
RA Aerts A., Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B.,
RA Kuo A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y., Rahimi M.J.,
RA Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT "Multiple horizontal gene transfer events from other fungi enriched the
RT ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT plant biomass.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the rad17/RAD24 family.
CC {ECO:0000256|ARBA:ARBA00006168}.
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DR EMBL; KZ679132; PTB76144.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T4C3N8; -.
DR STRING; 983965.A0A2T4C3N8; -.
DR Proteomes; UP000240760; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR004582; Checkpoint_prot_Rad17_Rad24.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR12172; CELL CYCLE CHECKPOINT PROTEIN RAD17; 1.
DR PANTHER; PTHR12172:SF0; CELL CYCLE CHECKPOINT PROTEIN RAD17; 1.
DR Pfam; PF03215; Rad17; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000240760}.
FT DOMAIN 234..416
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 533..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 725..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 820..852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..740
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..758
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 876 AA; 95499 MW; C0E01841BFFD6C6E CRC64;
MAPPAKRRRR NTVVASEDED EQPKANTLTN FLLSSPNSPA KTRAPTASPS PAKRKTANGQ
QPSSNGSPLR PSRSLKNGTT SSPRKTRAAS KADDKGKTAD LKMLFSKQAQ KATRPAADRR
TEPIDDLISD PISDDDDDEI SERQASSSSL VGQHVRKRLK GTSGAELPVL SGSLTMSQRF
LKPSRQAAID ASNDDLRPWS ERFGPRNLDE LAVHKKKVTD VRRWLEDVMG GRMRQRLLIL
KGGAGTGKTT TVRLLAKDMG CEILEWKNPA GNAVNGFVSA SSQFEDFLGR GGKFGALDLE
DAEPFSTPAS SSKPSQSQQP GSNGKKIILI EEFPNTFSRS STALSSFRRT ILQYLATQTP
SLPMFGHQRP VEPITPVVLV ISETLLTTTS ASADSLTAHR LLGPEILRHE GVGLIEFNPI
APSLLAKALE VIVQKESRKS GRRRTPGPLV LKRLGEIGDI RSAISSLEFL CLKGDQDADW
GSKVTFAKQK KGAKDGIALT RGEEESLEQI SQREASLGIF HAVGKVVYNK RDEVPSNDPA
EKLPSYLSQY SRPKPSQVSV DTLVDETGTD THTFISALHE NYVLSCEGTD PMDLSTPIDY
VNECIEYLSL ADLLSPSRDV FFGGRGGYGG TFGGDSASHV LRQDEITFQV AVRGMLFSLP
NPVKRKAWTM QKGGDAFKMF YPTSLKLWRT KEEIEGLIDV WSGKVLRGEA ELPTRSIMDG
ASIFRRNQPS GVSSSNQDQK PTTTKERECK EDARQNAEAA RDSPPVPTLG STARRELLLD
RLPYMAQIAR GRKVPGTRQK DLEKIVSFSG VNMALDEEEA DVDDDGATGE TWATDKPSEE
TSPRKKRVGI KIGGAGGGVA GMLKQKLVLS DDDIED
//