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Database: UniProt
Entry: Q6MFS6_NEUCS
LinkDB: Q6MFS6_NEUCS
Original site: Q6MFS6_NEUCS 
ID   Q6MFS6_NEUCS            Unreviewed;      1157 AA.
AC   Q6MFS6;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 114.
DE   SubName: Full=Related to DNA mismatch repair protein PMS1 {ECO:0000313|EMBL:CAE85513.1};
GN   ORFNames=B2N18.120 {ECO:0000313|EMBL:CAE85513.1}, GE21DRAFT_6247
GN   {ECO:0000313|EMBL:KHE84414.1};
OS   Neurospora crassa.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=5141 {ECO:0000313|EMBL:CAE85513.1};
RN   [1] {ECO:0000313|EMBL:CAE85513.1}
RP   NUCLEOTIDE SEQUENCE.
RA   German Neurospora genome project;
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CAE85513.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Schulte U., Aign V., Hoheisel J., Brandt P., Fartmann B., Holland R.,
RA   Nyakatura G., Mewes H.W., Mannhaupt G.;
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:KHE84414.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=73 {ECO:0000313|EMBL:KHE84414.1};
RG   DOE Joint Genome Institute;
RA   Baker S.E., Grigoriev I., Haridas S., LaButti K., McCluskey K.;
RT   "Draft genome sequence of Neurospora crassa strain FGSC 73.";
RL   Submitted (NOV-2014) 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; BX897674; CAE85513.1; -; Genomic_DNA.
DR   EMBL; KN389673; KHE84414.1; -; Genomic_DNA.
DR   VEuPathDB; FungiDB:NCU08020; -.
DR   eggNOG; KOG1978; Eukaryota.
DR   HOGENOM; CLU_004131_0_0_1; -.
DR   OrthoDB; 4698638at2759; -.
DR   Proteomes; UP000053122; 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}.
FT   DOMAIN          220..360
FT                   /note="DNA mismatch repair protein S5"
FT                   /evidence="ECO:0000259|SMART:SM01340"
FT   DOMAIN          888..1062
FT                   /note="MutL C-terminal dimerisation"
FT                   /evidence="ECO:0000259|SMART:SM00853"
FT   REGION          376..463
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          478..782
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          844..864
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1131..1157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        404..425
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        439..463
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        495..521
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        530..553
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        589..628
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        662..685
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        703..722
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        727..742
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        846..860
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1137..1157
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1157 AA;  127633 MW;  AECCC4FEF9ECEE76 CRC64;
     MASDGAIKAI DPSTIHQIQS GQVIVDLCSV AKELVENALD AGATTIDVRF KNQGLDSIEV
     QDNGSGISSS NYESIALKHY TSKLSNYDDL STLQTFGFRG EALSSLCALS HFTIVTCTQK
     EAPKATKLEF ETSGKLKSTS VVSGQRGTTV SVENLFKSLP VRRRELERNI KREWGKVVNL
     LNQYACIQTS VKFTVSQQPT KGKRMVLFST KGNPTTRENI INVFGIKTMT ALIAMDLRLQ
     LKPTNTGLLA KMTAQDDDAM TEVRICGHIS RPAHGEGRQT PDRQMFYVNG RPCGLPQFAK
     VFNEVYRSYN STQSPFIFAD IQLDTHLYDV NVSPDKRTIL LHDQGQMLDN LRESLIELFE
     LQDVTIPVSH TQLLKGSTFR GPSTVPLGSL TPAREKDSRD ASEEPGSSLP SNRPENGPQG
     NRATRHAVNE DSDEAVSDED NAPNTLSTGP KTRAGPCEST PANTQASNLL ARWLERKSEA
     RKQPVSAAIN ANDSRREKSP VEKEPQSPKR ARRYDTKDAE SDAEQDTAED NEHVENNSMT
     QDVVDDKEMD RQELTMPSIP PPTQPPIPKG SLLSISRPPK RSAQEEVATI TIGGHSITSV
     IGSSNKRSRL SEGMRSVSLG SSPTKGIRTV PVPSFGGRLT QLFSASGGAS RGVSKDLEMT
     TEDVEMVDEE GKGEENEEGN ETEKGVDSDD EALFVSQTKD VPAVEYDDVD EQAEHSTREN
     SPADEEGNGP ISGQTNQSVA EGDDNGEVEL SEDAPSECCH HGDDDEEYID EDEKKAKEEK
     KVQEMIKAAE KKANEPTEEG EKRSQSFVKG RLKRKDLTFN LIQRLKTSEG DIRSRMEIWA
     KHLPRAGTAS SSTQESSDGK PTIGLDAADA EEKLSLKISK SDFAKMKIVG QFNLGFIIAV
     REASSSHSLE HSPSQQSPAA TTQEDDELFI IDQHASDEKY NFERLQSTTT VQSQRLVQPK
     PLTLTAVEEE IILEHLPALA ANGFQVRVDT SGESAVGSRC QLLSLPLSRE TTFGVADLEE
     LIFLLGDNPT SSATTAIPRP SKVRKMFAMR ACRSSIMIGR ALSRPQMEKV VRHMGEMEKP
     WNCPHGRPTM RHLCGLGSAF GEGIKEKERG WDEWEGVERE RVDWKAWVRE KREDAEEGEG
     EGQEEEEEEE EEEEMSE
//
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