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Database: UniProt
Entry: A0A2T3YWH3_9HYPO
LinkDB: A0A2T3YWH3_9HYPO
Original site: A0A2T3YWH3_9HYPO 
ID   A0A2T3YWH3_9HYPO        Unreviewed;       941 AA.
AC   A0A2T3YWH3;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   08-NOV-2023, entry version 16.
DE   RecName: Full=DNA mismatch repair protein S5 domain-containing protein {ECO:0000259|SMART:SM01340};
GN   ORFNames=M441DRAFT_72973 {ECO:0000313|EMBL:PTB36909.1};
OS   Trichoderma asperellum CBS 433.97.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=1042311 {ECO:0000313|EMBL:PTB36909.1, ECO:0000313|Proteomes:UP000240493};
RN   [1] {ECO:0000313|EMBL:PTB36909.1, ECO:0000313|Proteomes:UP000240493}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 433.97 {ECO:0000313|EMBL:PTB36909.1,
RC   ECO:0000313|Proteomes:UP000240493};
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   -!- SIMILARITY: Belongs to the DNA mismatch repair MutL/HexB family.
CC       {ECO:0000256|ARBA:ARBA00006082}.
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DR   EMBL; KZ679269; PTB36909.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T3YWH3; -.
DR   STRING; 1042311.A0A2T3YWH3; -.
DR   OrthoDB; 1369806at2759; -.
DR   Proteomes; UP000240493; Unassembled WGS sequence.
DR   GO; GO:0032300; C:mismatch repair complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR   GO; GO:0030983; F:mismatched DNA binding; IEA:InterPro.
DR   GO; GO:0061982; P:meiosis I cell cycle process; IEA:UniProt.
DR   GO; GO:0006298; P:mismatch repair; IEA:InterPro.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR014762; DNA_mismatch_repair_CS.
DR   InterPro; IPR013507; DNA_mismatch_S5_2-like.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR002099; MutL/Mlh/PMS.
DR   InterPro; IPR038973; MutL/Mlh/Pms-like.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   NCBIfam; TIGR00585; mutl; 1.
DR   PANTHER; PTHR10073; DNA MISMATCH REPAIR PROTEIN MLH, PMS, MUTL; 1.
DR   PANTHER; PTHR10073:SF41; MISMATCH REPAIR PROTEIN, PUTATIVE (AFU_ORTHOLOGUE AFUA_8G05820)-RELATED; 1.
DR   Pfam; PF01119; DNA_mis_repair; 1.
DR   Pfam; PF13589; HATPase_c_3; 1.
DR   SMART; SM01340; DNA_mis_repair; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   PROSITE; PS00058; DNA_MISMATCH_REPAIR_1; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   Reference proteome {ECO:0000313|Proteomes:UP000240493}.
FT   DOMAIN          217..363
FT                   /note="DNA mismatch repair protein S5"
FT                   /evidence="ECO:0000259|SMART:SM01340"
FT   REGION          373..396
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          510..536
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          582..602
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          617..670
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        375..394
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        624..648
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   941 AA;  104079 MW;  43851F58B151AD57 CRC64;
     MPISALPQST IRSLGSSVII TTPCDVVKEL IDNAIDAGAS FIEVAVSSNY LDTIRVRDDG
     HGIDVDDFDA LGRRAHTSKL KAFNEIGSRA RESLGFRGEA LAAMNTFATI SITTRTTSDV
     VATRLQLKRA VGGSENRCPT SAPVGTTVQV TKLFDTLPAR KQYSLRNSAK YIKSTKDLFK
     AYVLARPDLR LSFKILGEAV GGWSYAPACA AEINEATLQI FGKALANSCI HVSRNSACDQ
     AAFTQASQEA TEDFILEAFM PKTGFDLPAV KGKGLYLSVD SRPLSSTCDI AKKITAIFKN
     HLNRVTGSNE SCTSVSNPFL RLNIRCPAHS YDANVTPLKD EVVFGDENKI TASFEGLCQR
     IYSERFMAEP FLSSKSSRSE EEAGDSKSHI ENSGNMHTKD LNIFSGISQG DHLTDQVTAL
     LPLPREPDSQ NGVSLTKMRT SKIVNMSRIN SNSTDEDCTI NSVDIQVPVS LMAASQISPG
     RRPQVPRISA SENIERYLLS RKNEGFKIAT DETATRKSDL QTGPPESPPG IFNRKPLQPL
     TESMLNAMNG QPDSESDVSS AEPEMLTLDD NTERTINANA REERAQQISP VPTPSSPDHE
     PLALRSPRQL RSVAEWLTPP SSGPLRNVRL SNSSFRPQQR TTARDSPTGN VAVRPWPRAP
     QSGRTIPFIL PGENRNRRRL THNETIEQEV DIPRDNPRET RAQLYFQGVQ GLNRQQDRTT
     NAFELASQLD TTRRPVSHKN FFSHEPGHHS HIIQTSLLDS QYSGDIPSSR RAQEVLNARD
     NLSATPQRDI RPSIEASVCG DSQNRAPFRN THGKLEDPRL YLIKRRRSQA RHGIARRLSS
     RRLPLEVTPI HLAMQSSSTS RRLSLRRVKT LARQTRLQGY DIVPGDWGNA ITFKSMEEAG
     KVESRLQDAV DSWKQTQNQA IEVEYKLRSA AKGKNPAFTD Q
//
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