ID F2RQZ2_TRIT1 Unreviewed; 1038 AA.
AC F2RQZ2;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE SubName: Full=DNA mismatch repair protein {ECO:0000313|EMBL:EGD93741.1};
GN ORFNames=TESG_01275 {ECO:0000313|EMBL:EGD93741.1};
OS Trichophyton tonsurans (strain CBS 112818) (Scalp ringworm fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=647933 {ECO:0000313|Proteomes:UP000009172};
RN [1] {ECO:0000313|Proteomes:UP000009172}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 112818 {ECO:0000313|Proteomes:UP000009172};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutL/HexB family.
CC {ECO:0000256|ARBA:ARBA00006082}.
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DR EMBL; GG698480; EGD93741.1; -; Genomic_DNA.
DR AlphaFoldDB; F2RQZ2; -.
DR HOGENOM; CLU_004131_0_0_1; -.
DR OrthoDB; 4698638at2759; -.
DR Proteomes; UP000009172; 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; 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; 2.
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; 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; 2.
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 198..333
FT /note="DNA mismatch repair protein S5"
FT /evidence="ECO:0000259|SMART:SM01340"
FT DOMAIN 767..965
FT /note="MutL C-terminal dimerisation"
FT /evidence="ECO:0000259|SMART:SM00853"
FT REGION 345..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..628
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..669
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..701
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1038 AA; 115579 MW; 6D619D6C42E3FA8B CRC64;
MATIKPIEAR SVHQIQSGQV IVDLYVRFKN NGLDLIEVQD NGHGISPNNY ESLALKHYTS
KLSTFADLTS LQTFGFRGEA LSSLCAVSNL TVVTAEAQQA PRASKLDFEF SGKLKSTQIV
AGQKGTTVSI ENLFKPLPVR RRELEKNVKR EYGKVIALLH AYACISTGVR FNVKNQMPKG
KSVVVFTTKS NPTTRENISN VYGAKTLLAL MPLDLDLEYE PSTAAKRFSS QASNKIFVHG
HISKPVFGEG RQTPDRQMFF VNSRPCGLPQ IAKAFNEVYK SFNLSQSPFI FANFEMDTSA
YDVNVSPDKR TILLHDAGAL IESLKASLTE LFENEDQTVP VSQLTFSKQS QLTPKRGQTP
PASVDAAQDK PEKPPGNADY SQELGHDDTV ERNDREPTQT PQSPMGGVLQ RFEGGDQENT
PPNTNITVEN DPVIPESSGA YDIPSNIDDE AAGGNPTQLQ SAQEQPISSS PSLGTPTHKP
GVIQNAFDRM RMNRTPVDVA TITIGNKTYQ STIGRDPVKR RLDSYPGLHL HSPSSRTRAI
TVRSKIGRSI QSFTAPGTQI EQGQIHDDPI EDDEDEEDNE IQSIGRLNGG NGPEEEPEED
PGEDSRGGEE VDGEGRTGEA HEERQVESLQ QDQPIYPEDT HSLGSDSDES YVDDDERKTR
EDAKVSELIK AAEEASAVPS EHSIERAERL IRKPRKKDST HELACAIDAS IEKIESQMKS
LQRRIQSLSN RGLHRGEDAD DDGDQQIAPE TKLSLAVSKK DFSRMRIIGQ FNLGFILATR
PGVVEDENSS SSPLAEQEQD ELFIIDQHAS DEKYNFERLQ AETTVQNQRL VKPKTLDLTA
VEEEVIIDNL AALEKNGFIV EIDTSGDEPI GRRCKLISLP LSKEVVFDTR DLEELIVLLS
EAPQQSQNNL GKRAREELES DAEYIEPSGV ASTPFSDYLV PRPSKVRKMF AMRACRSSIM
IGKNLTHRQM ETVVKHMGTI DKPWNCPHGR PTMRHLVSLG QWNEWSEWDS HKERWSRAGR
QPRSIKHIWE EFVEDYGS
//
