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Database: UniProt
Entry: A0A0F4Z5I4_TALEM
LinkDB: A0A0F4Z5I4_TALEM
Original site: A0A0F4Z5I4_TALEM 
ID   A0A0F4Z5I4_TALEM        Unreviewed;       988 AA.
AC   A0A0F4Z5I4;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=MutL C-terminal dimerisation domain-containing protein {ECO:0000259|SMART:SM00853};
GN   ORFNames=T310_0334 {ECO:0000313|EMBL:KKA25605.1};
OS   Rasamsonia emersonii CBS 393.64.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Rasamsonia.
OX   NCBI_TaxID=1408163 {ECO:0000313|EMBL:KKA25605.1, ECO:0000313|Proteomes:UP000053958};
RN   [1] {ECO:0000313|EMBL:KKA25605.1, ECO:0000313|Proteomes:UP000053958}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 393.64 {ECO:0000313|EMBL:KKA25605.1,
RC   ECO:0000313|Proteomes:UP000053958};
RA   Heijne W.H., Fedorova N.D., Nierman W.C., Vollebregt A.W., Zhao Z., Wu L.,
RA   Kumar M., Stam H., van den Berg M.A., Pel H.J.;
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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:KKA25605.1}.
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DR   EMBL; LASV01000016; KKA25605.1; -; Genomic_DNA.
DR   RefSeq; XP_013332217.1; XM_013476763.1.
DR   AlphaFoldDB; A0A0F4Z5I4; -.
DR   STRING; 1408163.A0A0F4Z5I4; -.
DR   GeneID; 25312389; -.
DR   OrthoDB; 9570at2759; -.
DR   Proteomes; UP000053958; 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:0006298; P:mismatch repair; IEA:InterPro.
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; IPR036890; HATPase_C_sf.
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   PANTHER; PTHR10073; DNA MISMATCH REPAIR PROTEIN MLH, PMS, MUTL; 1.
DR   PANTHER; PTHR10073:SF47; DNA MISMATCH REPAIR PROTEIN MLH3; 1.
DR   Pfam; PF13589; HATPase_c_3; 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.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000053958}.
FT   DOMAIN          699..912
FT                   /note="MutL C-terminal dimerisation"
FT                   /evidence="ECO:0000259|SMART:SM00853"
FT   REGION          400..471
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          494..559
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          584..609
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        409..432
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        441..457
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        526..542
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        543..559
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        584..600
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   988 AA;  109111 MW;  E85C7B9A3D44D73A CRC64;
     MSYHDASIRP LPADVAAKIK SSISITNLNG VVVELVKNSL DADAVSINIS LDYRRGGCIV
     EDDGHGIPSA EFKDGSGLGQ PHCTSKLGLG ERVYGYKGLF LASLAAMSLL TITSRHYQQA
     NANTVIFHHA KTISRLIPSP PQQSLDHEGH GTKVTVNDLF GNMPVRVKSR ALALQRPDDM
     DREWEELKRM LTALVLANDR PLKLVLSEAD KNRKVVIQAK SPSVERSDSS QVGVDLTRIG
     SILTQAGLIP LKSTESWVTV SASTPDLSIH SSISLLPSPT KQVQFISMGI NPIFAHSSAN
     VLYNEVNRIF AASDFGTTSS YQEAEERRKT AVLQTGTNVK GTSKGINRWP MFYIRIEMGE
     SWRAANEETE TFESDRSLQR ILDVLGAMVY QFLEQHHFRP RARKRLRQSP KQKSEPDRRH
     GKASRKEGDV PKCISDSAQP PVPQRPMSST EETLDSRIKL PSFQKRPSAL TTQDFGSWSR
     IKSGNGNVFD EICSGLNRRP EPAQGTSLPH RPSQADPGTK CLVERGQRGQ RCDSEKVDNG
     ESEEVTTTQS TGSDSGDGII SWTDPVTKCT VFINSRTGQC LPPRPLSSTA VNTSPLCPRP
     RSTGSLGDRR NLNVIKRPQS APSKKSSLWL EAIMDKWDNL AFPRLEKPIP SIHSDMNGEG
     CPEGKLDFRI QPDSCGLSTC TDTKSSGKLW KRGLAEADVI AQVDRKFILV RMTAAPLDSG
     DRSSGSLLVL VDQHAADERC RIEQLFDEMF TSQAGPDNSG EMMNLRTFEL SSPISFEIAA
     HETGLFKAYS EFFASWGCHY EVFEIPEQGN ATVSVSALPT LIAERCRAEP KLVVDLLRGE
     IWNREENKRG FSVRPALATS RKLPEGVDGS LPSEPIAGLP SWVGQVADCP EGIIDLLNSR
     ACRTAVMFND VLSIEECQNL ISRLSRCVFP FQCAHGRPSM IPILDLTSQM RDDDFDMLDI
     GYERTKKDLG TELGFAEAFR AWKDTHWD
//
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