ID   MKT1L_TRYB2             Reviewed;        1220 AA.
AC   Q38C92;
DT   10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=Post-transcriptional regulator MKT1L {ECO:0000305};
DE   AltName: Full=Inactive endonuclease MKT1L {ECO:0000305};
GN   Name=MKT1L {ECO:0000303|PubMed:32532821};
GN   ORFNames=Tb10.70.6480 {ECO:0000312|EMBL:EAN77578.1};
OS   Trypanosoma brucei brucei (strain 927/4 GUTat10.1).
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX   NCBI_TaxID=185431 {ECO:0000312|Proteomes:UP000008524};
RN   [1] {ECO:0000312|Proteomes:UP000008524}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=927/4 GUTat10.1 {ECO:0000312|Proteomes:UP000008524};
RX   PubMed=16020726; DOI=10.1126/science.1112642;
RA   Berriman M., Ghedin E., Hertz-Fowler C., Blandin G., Renauld H.,
RA   Bartholomeu D.C., Lennard N.J., Caler E., Hamlin N.E., Haas B., Bohme U.,
RA   Hannick L., Aslett M.A., Shallom J., Marcello L., Hou L., Wickstead B.,
RA   Alsmark U.C.M., Arrowsmith C., Atkin R.J., Barron A.J., Bringaud F.,
RA   Brooks K., Carrington M., Cherevach I., Chillingworth T.J., Churcher C.,
RA   Clark L.N., Corton C.H., Cronin A., Davies R.M., Doggett J., Djikeng A.,
RA   Feldblyum T., Field M.C., Fraser A., Goodhead I., Hance Z., Harper D.,
RA   Harris B.R., Hauser H., Hostetler J., Ivens A., Jagels K., Johnson D.,
RA   Johnson J., Jones K., Kerhornou A.X., Koo H., Larke N., Landfear S.,
RA   Larkin C., Leech V., Line A., Lord A., Macleod A., Mooney P.J., Moule S.,
RA   Martin D.M., Morgan G.W., Mungall K., Norbertczak H., Ormond D., Pai G.,
RA   Peacock C.S., Peterson J., Quail M.A., Rabbinowitsch E., Rajandream M.A.,
RA   Reitter C., Salzberg S.L., Sanders M., Schobel S., Sharp S., Simmonds M.,
RA   Simpson A.J., Tallon L., Turner C.M., Tait A., Tivey A.R., Van Aken S.,
RA   Walker D., Wanless D., Wang S., White B., White O., Whitehead S.,
RA   Woodward J., Wortman J., Adams M.D., Embley T.M., Gull K., Ullu E.,
RA   Barry J.D., Fairlamb A.H., Opperdoes F., Barrell B.G., Donelson J.E.,
RA   Hall N., Fraser C.M., Melville S.E., El-Sayed N.M.A.;
RT   "The genome of the African trypanosome Trypanosoma brucei.";
RL   Science 309:416-422(2005).
RN   [2] {ECO:0000305}
RP   FUNCTION, IDENTIFICATION IN A COMPLEX WITH PBP1; LSM12 AND XAC1,
RP   SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=427 {ECO:0000303|PubMed:32532821};
RX   PubMed=32532821; DOI=10.1074/jbc.ra120.013306;
RA   Melo do Nascimento L., Terrao M., Marucha K.K., Liu B., Egler F.,
RA   Clayton C.;
RT   "The RNA-associated proteins MKT1 and MKT1L form alternative PBP1-
RT   containing complexes in Trypanosoma brucei.";
RL   J. Biol. Chem. 295:10940-10955(2020).
CC   -!- FUNCTION: Involved in post-transcriptional regulation of gene
CC       expression. {ECO:0000269|PubMed:32532821}.
CC   -!- SUBUNIT: Forms a complex composed of at least MKT1L, PBP1, XAC1 and
CC       LSM12. {ECO:0000269|PubMed:32532821}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:32532821}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the procyclic and bloodstream forms
CC       (at protein level). {ECO:0000269|PubMed:32532821}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in both the procyclic and
CC       the bloodstream form is lethal. {ECO:0000269|PubMed:32532821}.
CC   -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. {ECO:0000305}.
CC   -!- CAUTION: Although it belongs to the XPG/RAD2 endonuclease family, only
CC       one of the seven Asp residues involved in Mg(2+) binding is conserved
CC       suggesting that it has no nuclease activity. {ECO:0000305}.
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DR   EMBL; CM000208; EAN77578.1; -; Genomic_DNA.
DR   RefSeq; XP_822406.1; XM_817313.1.
DR   AlphaFoldDB; Q38C92; -.
DR   PaxDb; Q38C92; -.
DR   GeneID; 3662740; -.
DR   KEGG; tbr:Tb10.70.6480; -.
DR   VEuPathDB; TriTrypDB:Tb927.10.1490; -.
DR   eggNOG; ENOG502R9RQ; Eukaryota.
DR   InParanoid; Q38C92; -.
DR   OMA; PGMNSNW; -.
DR   Proteomes; UP000008524; Chromosome 10.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0035061; C:interchromatin granule; IDA:GeneDB.
DR   GO; GO:0017108; F:5'-flap endonuclease activity; IBA:GO_Central.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   InterPro; IPR022039; MKT1_C.
DR   InterPro; IPR022040; MKT1_N.
DR   InterPro; IPR029060; PIN-like_dom_sf.
DR   InterPro; IPR006084; XPG/Rad2.
DR   PANTHER; PTHR11081; PTHR11081; 2.
DR   Pfam; PF12246; MKT1_C; 1.
DR   Pfam; PF12247; MKT1_N; 1.
DR   SUPFAM; SSF88723; SSF88723; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Reference proteome; Translation regulation.
FT   CHAIN           1..1220
FT                   /note="Post-transcriptional regulator MKT1L"
FT                   /id="PRO_0000451926"
FT   REGION          1..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..26
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        35..71
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..107
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1220 AA;  134815 MW;  027890055BB885D8 CRC64;
     MRKAGANRNN ERQGRNLGQQ GPQMSPPGPS MMYPHHHQHQ HHHQHQHQHQ HQHQHPHQHP
     HQHHHHHPHH NGVYGNAYDN IRQPQMPPHS FGQGVSGSPW NSPPQQTPMY NQGYNQMSPG
     TGGGYGDMGG MYRDVHGGQY PSSPSHMGGG ANIPYGRNPA MHNGLPAGAP LPGGYGALPH
     QGAHTPMGFG RGGQPLMEHM QPSGMYGAPM MRHDGYPDTR VSPPAQVGYG AGAPVGPPPP
     PPMPAGPPYG GVLPGAGVGP GGPMNASRPP AGIGGGGGGG GNAGYLEMRA RGMGPQMPAS
     NASRPPRIGT PDPGMMPPNR MNQSPMMGQG LPPQVGNFMP LPGVSPSPHA MIPTTPSMGD
     TFPGDDANMS GSTEALYDFL HDRGLVSVDN ISKFFPEGYG KDDPALKVAV DGNFCLTSLR
     DELRKRDSLW FLHSTLPEEL LMLVQQHVEW MRNMKLEPIW VFNGLSVSGD VETFLTTEAE
     LRARDAVWSK LEDGEIPDEV EIQEAFDQPL GEDVQMAVAR YLKEELGVMA VTAPFLNWAQ
     MVAFHKEGIA DLLMGPPEML LLPYDEMKVI VQIDVSNSSV NYLDRDRVLR ALFPNHVTET
     NTRVAGDRLM DLGLITATHA ALSSARVTLN LSMQEVYEEL STPTPKFRSI KDFINAHACS
     QETGKKAGLS IKHSKGRGYL RYSAVFSTKS RDTPLVYLVR VLDPDLTNAD MPTNLAGVLG
     HLVPLSLFYM QFSGLLSVRI MTAITQSYLR DECPVSDTKD YHTTLGLLMT MRSQVIGQIL
     KRIAHPPPIK RTECLSWVRW FQPILAPMDR PRDLIDLDEW EISDSDQLKK LDEDCLADYS
     IASVLSVTAD ASRPAVEESN RPAGRVPIRY NSKRETFLAI LLKSFDFLGY FSHSTAPNDA
     VDGMEMECCG MDGHDRGGSV PAAYHEKDLS SMKRSEASDI NFMADEGLKD YPSVYFPIYL
     RATIKANPLD VQASFVLLTE LVRVRIINSN PCRYINPANQ QVEISMDDQD TNSDSRVLLA
     SRIACLVKLP YRRASENLPF VWAPVYSRHL CAFTVMVRAM CRCLRELVEV ITSTVFLSGN
     SSCSLQDFAE FASILPFGDV PSTIGGLLLH YVLVFPSDYQ ANLTSREERI EYLQGKFRDI
     PDLADHLHLV MSFTLQALYL INAYMLNDKE TIVAKDQLTG TIVEDTIEMM WQKWRDHIDD
     NPPGDIHNLY PPRHQEPIPH