ID Q7LMB5_YEASX Unreviewed; 830 AA.
AC Q7LMB5;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 13-SEP-2023, entry version 49.
DE SubName: Full=MKT1 {ECO:0000313|EMBL:AAM00537.1};
GN Name=YNL085W {ECO:0000313|EMBL:AAM00537.1};
OS Saccharomyces cerevisiae (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=4932 {ECO:0000313|EMBL:AAM00537.1};
RN [1] {ECO:0000313|EMBL:AAM00537.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=YJM280 {ECO:0000313|EMBL:AAM00525.1}, YJM320
RC {ECO:0000313|EMBL:AAM00531.1}, and YJM326
RC {ECO:0000313|EMBL:AAM00537.1};
RX PubMed=11907579; DOI=10.1038/416326a;
RA Steinmetz L.M., Sinha H., Richards D.R., Spiegelman J.I., Oefner P.J.,
RA McCusker J.H., Davis R.W.;
RT "Dissecting the architecture of a quantitative trait locus in yeast.";
RL Nature 416:326-330(2002).
CC -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family.
CC {ECO:0000256|ARBA:ARBA00024023}.
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DR EMBL; AF458970; AAM00525.1; -; Genomic_DNA.
DR EMBL; AF458971; AAM00531.1; -; Genomic_DNA.
DR EMBL; AF458972; AAM00537.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7LMB5; -.
DR MINT; Q7LMB5; -.
DR VEuPathDB; FungiDB:YNL085W; -.
DR GO; GO:0004518; F:nuclease activity; IEA:InterPro.
DR GO; GO:0006974; P:DNA damage response; IEA:UniProt.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR CDD; cd09902; H3TH_MKT1; 1.
DR CDD; cd09858; PIN_MKT1; 1.
DR Gene3D; 3.40.50.1010; 5'-nuclease; 1.
DR InterPro; IPR022039; MKT1_C.
DR InterPro; IPR037314; MKT1_H3TH.
DR InterPro; IPR022040; MKT1_N.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR InterPro; IPR006086; XPG-I_dom.
DR InterPro; IPR006084; XPG/Rad2.
DR InterPro; IPR006085; XPG_DNA_repair_N.
DR PANTHER; PTHR11081; FLAP ENDONUCLEASE FAMILY MEMBER; 1.
DR PANTHER; PTHR11081:SF32; POST-TRANSCRIPTIONAL REGULATOR MKT1; 1.
DR Pfam; PF12246; MKT1_C; 1.
DR Pfam; PF12247; MKT1_N; 1.
DR Pfam; PF00752; XPG_N; 1.
DR SMART; SM00484; XPGI; 1.
DR SMART; SM00485; XPGN; 1.
DR SUPFAM; SSF88723; PIN domain-like; 1.
PE 3: Inferred from homology;
KW Translation regulation {ECO:0000256|ARBA:ARBA00022845}.
FT DOMAIN 1..103
FT /note="XPG N-terminal"
FT /evidence="ECO:0000259|SMART:SM00485"
FT DOMAIN 179..248
FT /note="XPG-I"
FT /evidence="ECO:0000259|SMART:SM00484"
FT REGION 345..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..400
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 830 AA; 94450 MW; DC186F942A43EE1B CRC64;
MAIKSLESFL FERGLVGSYA IEALNNCTLG IDVNHYVSRL LTNKREQYLD AIGGFPTSLK
MYLESDLKIF KDFNITPIFV FNGGLTYNQL EASGHFTAAS ASASISSTTT SSSGTNATTR
SNTESVLLQR SRGWTQWNNL ISSNQNSYID QPIQPQEPFR HNTTIDSKAY QNDLIAYFIE
HGYMYQVAPY SSWFQLAYLL NSAYIDAIYG PTDCLMLDCV DRFILGMEFP NKEFRFIDRS
RVMKDLGCTH EEFIDIAMAV GNDLQPTTLP PLQIYPVPQL FDIALEMVLN TGTNFYAYQL
STTLQNDSKE NIQNYQRGIS ALRYMPVLKD TGKVELFVQE IVVSEEDSEK NNKDGKKSNL
SSPSSASSSA SPATTVTKNA SEKLTYEKSS TKEVRKPRDI PNDVHDFIGQ MLPHEYYFYR
SIGLVTGKLF DGIVTGVYPE EPPLGGGSST SYRKLVSKSV EIFKNKEINL LTQPINRYYQ
IKQIKQVKWY AANEPTTLTN RMSPSMFETI NHLIVKTETS DEKEFSISEF ITTINGSSNM
AKDFISEKVI FPNSVPIESK LNSPFNLLST NFLRLLVLLE FFTFDFKEKL LEPTRWGEVF
LKLNELNIDS KYHESVIIFL VFLKCDVLKL DEEVQPPAPS ALSQATLRSY PEESLYVLLI
TRVLTLFQVD QKPSNYHGPI DKKTLIFRDH LSFIKENLNE LFEAVLISSL TSGEFNRLSL
DNFGWARKIV RYLPFKLDSP NTIMAMMWEF FLQKYLHNGN AKNDALSLVA TEFNTYKSTP
NLDEQFVESH RFLLEISKVM QELNAAKLID ENVFKLFTKA VEFTTTALSS
//
