ID A0A139AM15_GONPJ Unreviewed; 950 AA.
AC A0A139AM15;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 08-NOV-2023, entry version 30.
DE RecName: Full=DNA mismatch repair protein MutL {ECO:0008006|Google:ProtNLM};
GN ORFNames=M427DRAFT_54388 {ECO:0000313|EMBL:KXS17799.1};
OS Gonapodya prolifera (strain JEL478) (Monoblepharis prolifera).
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Monoblepharidomycetes; Monoblepharidales;
OC Gonapodyaceae; Gonapodya.
OX NCBI_TaxID=1344416 {ECO:0000313|EMBL:KXS17799.1, ECO:0000313|Proteomes:UP000070544};
RN [1] {ECO:0000313|EMBL:KXS17799.1, ECO:0000313|Proteomes:UP000070544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEL478 {ECO:0000313|EMBL:KXS17799.1,
RC ECO:0000313|Proteomes:UP000070544};
RX PubMed=25977457; DOI=10.1093/gbe/evv090;
RA Chang Y., Wang S., Sekimoto S., Aerts A.L., Choi C., Clum A., LaButti K.M.,
RA Lindquist E.A., Yee Ngan C., Ohm R.A., Salamov A.A., Grigoriev I.V.,
RA Spatafora J.W., Berbee M.L.;
RT "Phylogenomic Analyses Indicate that Early Fungi Evolved Digesting Cell
RT Walls of Algal Ancestors of Land Plants.";
RL Genome Biol. Evol. 7:1590-1601(2015).
CC -!- SIMILARITY: Belongs to the DNA mismatch repair MutL/HexB family.
CC {ECO:0000256|ARBA:ARBA00006082}.
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DR EMBL; KQ965745; KXS17799.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A139AM15; -.
DR STRING; 1344416.A0A139AM15; -.
DR OMA; RCSKIRS; -.
DR OrthoDB; 4698638at2759; -.
DR Proteomes; UP000070544; 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:0006298; P:mismatch repair; IEA:InterPro.
DR CDD; cd16926; HATPase_MutL-MLH-PMS-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:UP000070544}.
FT DOMAIN 289..454
FT /note="DNA mismatch repair protein S5"
FT /evidence="ECO:0000259|SMART:SM01340"
FT DOMAIN 753..914
FT /note="MutL C-terminal dimerisation"
FT /evidence="ECO:0000259|SMART:SM00853"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 34..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 613..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..542
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..561
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..650
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 950 AA; 102272 MW; D572A2E427AD74E4 CRC64;
MDNDEPDAVG QRGSGGSESA CGCRHAGCGD QNQCFEDSQT SLERTSNASG GTSASTIRET
HAPENPSTTP PAAPGRSIRP IDRSSLHRLT AAQVIVSLES AVKELVENAL DAGATSIQVV
FRDHGAVGFS VADNGHGIPK EDLPALGQKH HTSKIRSFSD LGQVSTYGFR GEALNSLCAI
ADVSIVTATK EPLGFELQLS STSTLDAPPK PAARARGTTI SVTNLFRSLP VRQQEFKRNA
RREYAKALAT VQNYAVVSTG VRLSVVNIVN SRPTPMLTTK GNAHLRDNLA DVFGAKAAID
VFDVDVSLKI PPPARGTAFT PISDALEQHQ LSDSNDDTAG AYTIRVVGVM SHPRPSAGRS
SSDTRQMYIN GRPCESPKLA KAVAEEWRAA GGAGAGGGEG SGSGTGGLPQ CFLDLKCPTD
TYDVNVTPDK RTIFLHRENE IIEELRVALR LLLERQNTHY TTSQVLRGGM GGAMVRVVGG
TVQSPANSAS ASDQRDDSEA PDVEEDVESL TGSEENEEEE GSPDEDMIVV DDDSEEDELE
ETGSADLPRR KLKRPSSPME DDGDLDEQTD HTTTGETRSD SHVDPITGPT VVAPPGIPKI
KAITSTLADF LARAGGQSST PGPPIPSLSP VKKSSGKQRP RTSFTDSAPS ATLPKRRRLD
SSPIKKQEQA NARWRTPVSM RTHTETSRMD FELKTLVARV KVYHQTRRTP RELKDTTASR
TVATSEIGAE PPAAAEEILT RIVAKNDFDR MAVIGQFNLG FILVKLSKPV EFRSRNEKGK
SELDLFIVDQ HASDEKFNFE NLKSTTPVRS QALILPQQLT LSAQDELAVA DNLEVFTRNG
FGVKVDLEAP PTQRCKLVSL PSVGGVDLNV KDFNDLLASV VEGGSGQPDL RCPRVNALFA
SRACRKSVMI GDPLSREAME KIVRHMSGMI APWNCPHGRP TMRHVLTIKN
//
