KTI12_SCHPO
ID KTI12_SCHPO Reviewed; 281 AA.
AC Q9P7V4;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Protein kti12;
GN Name=kti12; ORFNames=SPAC30.02c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Elongator complex-associated factor that is not a structural
CC subunit but rather transiently contacts the complex. Required for an
CC early step in synthesis of 5-methoxycarbonylmethyl (mcm5) and 5-
CC carbamoylmethyl (ncm5) groups present on uridines at the wobble
CC position in tRNA (By similarity). {ECO:0000250|UniProtKB:P34253}.
CC -!- SUBUNIT: Interacts with the elongator complex.
CC {ECO:0000250|UniProtKB:P34253}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the KTI12 family. {ECO:0000305}.
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DR EMBL; CU329670; CAB66461.1; -; Genomic_DNA.
DR PIR; T50208; T50208.
DR RefSeq; NP_594556.1; NM_001019985.2.
DR AlphaFoldDB; Q9P7V4; -.
DR SMR; Q9P7V4; -.
DR BioGRID; 278919; 22.
DR STRING; 4896.SPAC30.02c.1; -.
DR MaxQB; Q9P7V4; -.
DR PaxDb; Q9P7V4; -.
DR EnsemblFungi; SPAC30.02c.1; SPAC30.02c.1:pep; SPAC30.02c.
DR GeneID; 2542458; -.
DR KEGG; spo:SPAC30.02c; -.
DR PomBase; SPAC30.02c; kti12.
DR VEuPathDB; FungiDB:SPAC30.02c; -.
DR eggNOG; KOG3062; Eukaryota.
DR HOGENOM; CLU_027147_2_0_1; -.
DR InParanoid; Q9P7V4; -.
DR OMA; LYCEAKA; -.
DR PhylomeDB; Q9P7V4; -.
DR PRO; PR:Q9P7V4; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISM:PomBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR GO; GO:0002098; P:tRNA wobble uridine modification; ISO:PomBase.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR045106; Kti12.
DR InterPro; IPR013641; KTI12/PSTK.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR12435; PTHR12435; 1.
DR Pfam; PF08433; KTI12; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Nucleotide-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..281
FT /note="Protein kti12"
FT /id="PRO_0000339141"
FT BINDING 8..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 281 AA; 32495 MW; 4D165100842BC5CB CRC64;
MPLIIVSGYP SSGKTTRSNE LKKALEDRIH QNIDNTKDYR VIIINDESLN IEKETYRESK
NEKAARGLLY SAVQRELSKS TFVICDALNY IKGFRYQLYC ESKSMYTTHC VIHVAVPQDL
CRKFNSNKEQ PYPDDVLEQL MFRYEEPNGM TRWDSPLFTV LHDDASCPID DIWSVLIHNK
NVKPNQATMV KPPAEVNYLY ELDKTTQDVI MLILDNSNDT SLITVPGSKL QIALPSVTVS
LPLLQRLRRQ FIQINRQQSY NTNVLKEMFV EFLNGQFETL D