ID D3ZBQ4_RAT Unreviewed; 345 AA.
AC D3ZBQ4;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE RecName: Full=Queuine tRNA-ribosyltransferase accessory subunit 2 {ECO:0000256|HAMAP-Rule:MF_03043};
DE AltName: Full=Queuine tRNA-ribosyltransferase domain-containing protein 1 {ECO:0000256|HAMAP-Rule:MF_03043};
GN Name=Qtrt2 {ECO:0000313|Ensembl:ENSRNOP00000076283.1,
GN ECO:0000313|RGD:1310054};
GN Synonyms=QTRT2 {ECO:0000256|HAMAP-Rule:MF_03043};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000076283.1, ECO:0000313|Proteomes:UP000002494};
RN [1] {ECO:0000313|Ensembl:ENSRNOP00000076283.1, ECO:0000313|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000076283.1,
RC ECO:0000313|Proteomes:UP000002494};
RX PubMed=15057822; DOI=10.1038/nature02426;
RG Rat Genome Sequencing Project Consortium;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0000313|Ensembl:ENSRNOP00000076283.1}
RP IDENTIFICATION.
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000076283.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Non-catalytic subunit of the queuine tRNA-ribosyltransferase
CC (TGT) that catalyzes the base-exchange of a guanine (G) residue with
CC queuine (Q) at position 34 (anticodon wobble position) in tRNAs with
CC GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the
CC hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-
CC cyclopenten-1-yl)amino)methyl)-7-deazaguanosine). {ECO:0000256|HAMAP-
CC Rule:MF_03043}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03043};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_03043};
CC -!- SUBUNIT: Heterodimer of a catalytic subunit QTRT1 and an accessory
CC subunit QTRT2. {ECO:0000256|HAMAP-Rule:MF_03043}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03043}.
CC Mitochondrion outer membrane {ECO:0000256|HAMAP-Rule:MF_03043};
CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_03043};
CC Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_03043}. Note=May associate
CC with the mitochondrion outer membrane. {ECO:0000256|HAMAP-
CC Rule:MF_03043}.
CC -!- SIMILARITY: Belongs to the queuine tRNA-ribosyltransferase family.
CC QTRT2 subfamily. {ECO:0000256|HAMAP-Rule:MF_03043}.
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DR RefSeq; XP_008766983.1; XM_008768761.2.
DR AlphaFoldDB; D3ZBQ4; -.
DR SMR; D3ZBQ4; -.
DR PeptideAtlas; D3ZBQ4; -.
DR Ensembl; ENSRNOT00000093552.2; ENSRNOP00000076283.1; ENSRNOG00000060729.3.
DR GeneID; 288364; -.
DR UCSC; RGD:1310054; rat.
DR AGR; RGD:1310054; -.
DR CTD; 79691; -.
DR RGD; 1310054; Qtrt2.
DR GeneTree; ENSGT00530000063679; -.
DR HOGENOM; CLU_037350_0_0_1; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000060729; Expressed in ovary and 19 other cell types or tissues.
DR ExpressionAtlas; D3ZBQ4; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:1990234; C:transferase complex; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0008479; F:tRNA-guanosine(34) queuine transglycosylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0101030; P:tRNA-guanine transglycosylation; ISO:RGD.
DR Gene3D; 3.20.20.105; Queuine tRNA-ribosyltransferase-like; 2.
DR HAMAP; MF_03043; QTRT2; 1.
DR InterPro; IPR028592; QTRTD1.
DR InterPro; IPR036511; TGT-like_sf.
DR InterPro; IPR002616; tRNA_ribo_trans-like.
DR NCBIfam; TIGR00449; tgt_general; 1.
DR PANTHER; PTHR46064; QUEUINE TRNA-RIBOSYLTRANSFERASE ACCESSORY SUBUNIT 2; 1.
DR PANTHER; PTHR46064:SF1; QUEUINE TRNA-RIBOSYLTRANSFERASE ACCESSORY SUBUNIT 2; 1.
DR Pfam; PF01702; TGT; 1.
DR SUPFAM; SSF51713; tRNA-guanine transglycosylase; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03043};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_03043};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_03043};
KW Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03043};
KW Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00022787,
KW ECO:0000256|HAMAP-Rule:MF_03043};
KW Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_03043}; Zinc {ECO:0000256|HAMAP-Rule:MF_03043}.
FT DOMAIN 116..343
FT /note="tRNA-guanine(15) transglycosylase-like"
FT /evidence="ECO:0000259|Pfam:PF01702"
FT BINDING 281
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03043"
FT BINDING 283
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03043"
FT BINDING 286
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03043"
FT BINDING 312
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03043"
SQ SEQUENCE 345 AA; 38596 MW; D4EFBDB9470665E5 CRC64;
MMKLNLTKVV NGCRLGKIQN LGKAGDCTVD IPGCLLYTRT GSAPHLTHQT LHNIHGVPAM
AQLTLSSLAE HHEVLAEYKK GIGSFIGMPD SLFYCSLHDP VSPGPPGYVT NKVLQKSVII
GVIEGGDVTE ERLRSARETA KRPVGGFLLD GFQGGPAVTE TRLHLLSSVT AELPEDKPRL
ICGVSRPDEV LECIERGVDL FESFFPYQVT ERGCALTFTF DCQLNPEETL LQQNGIQEEI
KCLDQIKKME ATGCNQEMTS FEINLKEKKY QEDFQPLVRG CSCYCCTNHT RAYVHHLLVT
NELLASVLLM MHNFEHYFRF FCSIREALKS DTLAQLKELI RRQMS
//
