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Database: UniProt
Entry: G9MYQ1_HYPVG
LinkDB: G9MYQ1_HYPVG
Original site: G9MYQ1_HYPVG 
ID   G9MYQ1_HYPVG            Unreviewed;       961 AA.
AC   G9MYQ1;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=DNA mismatch repair protein S5 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=TRIVIDRAFT_48473 {ECO:0000313|EMBL:EHK20231.1};
OS   Hypocrea virens (strain Gv29-8 / FGSC 10586) (Gliocladium virens)
OS   (Trichoderma virens).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=413071 {ECO:0000313|EMBL:EHK20231.1, ECO:0000313|Proteomes:UP000007115};
RN   [1] {ECO:0000313|EMBL:EHK20231.1, ECO:0000313|Proteomes:UP000007115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Gv29-8 / FGSC 10586 {ECO:0000313|Proteomes:UP000007115};
RX   PubMed=21501500; DOI=10.1186/gb-2011-12-4-r40;
RA   Kubicek C.P., Herrera-Estrella A., Seidl-Seiboth V., Martinez D.A.,
RA   Druzhinina I.S., Thon M., Zeilinger S., Casas-Flores S., Horwitz B.A.,
RA   Mukherjee P.K., Mukherjee M., Kredics L., Alcaraz L.D., Aerts A., Antal Z.,
RA   Atanasova L., Cervantes-Badillo M.G., Challacombe J., Chertkov O.,
RA   McCluskey K., Coulpier F., Deshpande N., von Doehren H., Ebbole D.J.,
RA   Esquivel-Naranjo E.U., Fekete E., Flipphi M., Glaser F.,
RA   Gomez-Rodriguez E.Y., Gruber S., Han C., Henrissat B., Hermosa R.,
RA   Hernandez-Onate M., Karaffa L., Kosti I., Le Crom S., Lindquist E.,
RA   Lucas S., Luebeck M., Luebeck P.S., Margeot A., Metz B., Misra M.,
RA   Nevalainen H., Omann M., Packer N., Perrone G., Uresti-Rivera E.E.,
RA   Salamov A., Schmoll M., Seiboth B., Shapiro H., Sukno S.,
RA   Tamayo-Ramos J.A., Tisch D., Wiest A., Wilkinson H.H., Zhang M.,
RA   Coutinho P.M., Kenerley C.M., Monte E., Baker S.E., Grigoriev I.V.;
RT   "Comparative genome sequence analysis underscores mycoparasitism as the
RT   ancestral life style of Trichoderma.";
RL   Genome Biol. 12:R40.1-R40.15(2011).
CC   -!- SIMILARITY: Belongs to the DNA mismatch repair MutL/HexB family.
CC       {ECO:0000256|ARBA:ARBA00006082}.
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:EHK20231.1}.
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DR   EMBL; ABDF02000080; EHK20231.1; -; Genomic_DNA.
DR   RefSeq; XP_013954429.1; XM_014098954.1.
DR   AlphaFoldDB; G9MYQ1; -.
DR   STRING; 413071.G9MYQ1; -.
DR   EnsemblFungi; EHK20231; EHK20231; TRIVIDRAFT_48473.
DR   GeneID; 25794783; -.
DR   VEuPathDB; FungiDB:TRIVIDRAFT_48473; -.
DR   eggNOG; KOG1978; Eukaryota.
DR   HOGENOM; CLU_004131_0_0_1; -.
DR   InParanoid; G9MYQ1; -.
DR   OMA; RMRIIGQ; -.
DR   OrthoDB; 4698638at2759; -.
DR   Proteomes; UP000007115; 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   CDD; cd16926; HATPase_MutL-MLH-PMS-like; 1.
DR   CDD; cd03484; MutL_Trans_hPMS_2_like; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.1540.20; MutL, C-terminal domain, dimerisation subdomain; 1.
DR   Gene3D; 3.30.1370.100; MutL, C-terminal domain, regulatory subdomain; 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; IPR014790; MutL_C.
DR   InterPro; IPR042120; MutL_C_dimsub.
DR   InterPro; IPR042121; MutL_C_regsub.
DR   InterPro; IPR037198; MutL_C_sf.
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:SF52; MISMATCH REPAIR ENDONUCLEASE PMS2; 1.
DR   Pfam; PF01119; DNA_mis_repair; 1.
DR   Pfam; PF13589; HATPase_c_3; 1.
DR   Pfam; PF08676; MutL_C; 1.
DR   SMART; SM01340; DNA_mis_repair; 1.
DR   SMART; SM00853; MutL_C; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF118116; DNA mismatch repair protein MutL; 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:UP000007115}.
FT   DOMAIN          217..357
FT                   /note="DNA mismatch repair protein S5"
FT                   /evidence="ECO:0000259|SMART:SM01340"
FT   DOMAIN          738..899
FT                   /note="MutL C-terminal dimerisation"
FT                   /evidence="ECO:0000259|SMART:SM00853"
FT   REGION          402..534
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          555..673
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          692..716
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        441..467
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        488..509
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        516..534
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        559..576
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        591..608
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        609..629
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        630..658
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        697..713
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   961 AA;  106566 MW;  65A8FD66B1DB9907 CRC64;
     MATIKQIDGR SVHQIQSGQV IVDLCSVVKE LVENSVDSGA TIIDVRFKNQ GLDSIEVQDN
     GSGISPANYS SVALKHYTSK LSSYSDIESL QTFGFRGEAL ASLCALSILT VTTCLEQESP
     KGSRLTFHQS GELDSTTVVA AQRGTTVTVE NLFHNLPVRR RELDRNIKRE WHKVIALLNQ
     YACIQTNVKF SVSQQPTKGK RILLFSTKGN PTTRDNIINI FGAKTLTALI PLDLHLELKP
     SGTRSDVRIG DKLGPNSHDV RIVGHISKPA HGEGRQTPDR QMFFVNGRPC SLPQLAKAFN
     EVYRSYNNSQ SPFIFADVQL DTMLYDVNVS PDKRSILLHD QNNLLDTLRS SLSQLFDTHE
     DSISIATSTQ NVKAQSSYSK FTKPGQLPRL LGESAYKSYT TTAVEHSPSY EDNKSSSTTD
     TEEPEPDDEI PQASRSMKTR PQCNTKEKLH LHNGIESVVR RDISSSPEKP APEPTHLKTV
     LVDHSPRPKA SSATSNINTV INQPQRSHGP NFKIHPEISD STSPVASDIS VEDQGSQELH
     AVVTPLREVT SLAKATDVEG KARSLEPEKL HSTLPEPGEA KELLPSEISR LDTESIIQQP
     SPTRRNRRAM DNNISRQSRD DKQSLETEPD SQHLKSTLVT TDGGSPMNTA NAGALSVESR
     IQPSKPARRK DITTGYIQSL HVEKGKLRLL HNKRPRLRTS QPGSTSHNAS SVERIDASDA
     ESRLPLIISK GDFSKMRIIG QFNLGFIIAV KPASRLGSGV EGKYDELFII DQHASDEKYN
     YEKLQNTTEI QSQRLVHPKR LQLTALEEEI ILENATALNA NGFKVNIDTT GRFSVGSRCQ
     LTSLPLSREV TFKLDDLEEL ISLLGDKSAE SSYIPRPSKV QKMFAMRACR SSIMIGKAMT
     KSQMHSLVNH MGELDKPWNC PHGRPTIRHL SRLQAWSGVG WERDLQTDSI TAWHDYMGEA
     N
//
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