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Database: UniProt
Entry: A0A2T4C3N8_TRILO
LinkDB: A0A2T4C3N8_TRILO
Original site: A0A2T4C3N8_TRILO 
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
//
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