ARCH_DANRE
ID ARCH_DANRE Reviewed; 162 AA.
AC Q566V0; A2CE72;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Protein archease;
DE AltName: Full=Protein zbtb8os;
GN Name=zbtb8os; ORFNames=si:dkeyp-2e4.1, zgc:112460;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Olfactory epithelium;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the tRNA-splicing ligase complex required to
CC facilitate the enzymatic turnover of catalytic subunit RTCB. Together
CC with ddx1, acts by facilitating the guanylylation of RTCB, a key
CC intermediate step in tRNA ligation (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the tRNA-splicing ligase complex. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the archease family. {ECO:0000305}.
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DR EMBL; CR376783; CAM12942.1; -; Genomic_DNA.
DR EMBL; CR786566; CAM12942.1; JOINED; Genomic_DNA.
DR EMBL; CR786566; CAM12945.1; -; Genomic_DNA.
DR EMBL; CR376783; CAM12945.1; JOINED; Genomic_DNA.
DR EMBL; BC093322; AAH93322.1; -; mRNA.
DR RefSeq; NP_001017687.1; NM_001017687.1.
DR AlphaFoldDB; Q566V0; -.
DR SMR; Q566V0; -.
DR STRING; 7955.ENSDARP00000020953; -.
DR PaxDb; Q566V0; -.
DR Ensembl; ENSDART00000017770; ENSDARP00000020953; ENSDARG00000016368.
DR GeneID; 550382; -.
DR KEGG; dre:550382; -.
DR CTD; 339487; -.
DR ZFIN; ZDB-GENE-050417-176; zbtb8os.
DR eggNOG; KOG4528; Eukaryota.
DR GeneTree; ENSGT00390000003245; -.
DR HOGENOM; CLU_111362_0_0_1; -.
DR InParanoid; Q566V0; -.
DR OMA; WLSELLY; -.
DR OrthoDB; 1360804at2759; -.
DR PhylomeDB; Q566V0; -.
DR TreeFam; TF105957; -.
DR PRO; PR:Q566V0; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 13.
DR Bgee; ENSDARG00000016368; Expressed in swim bladder and 28 other tissues.
DR GO; GO:0072669; C:tRNA-splicing ligase complex; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006388; P:tRNA splicing, via endonucleolytic cleavage and ligation; ISS:UniProtKB.
DR Gene3D; 3.55.10.10; -; 1.
DR InterPro; IPR002804; Archease.
DR InterPro; IPR023572; Archease_dom.
DR InterPro; IPR036820; Archease_dom_sf.
DR PANTHER; PTHR12682; PTHR12682; 1.
DR Pfam; PF01951; Archease; 1.
DR SUPFAM; SSF69819; SSF69819; 1.
PE 2: Evidence at transcript level;
KW Calcium; Metal-binding; Reference proteome; tRNA processing.
FT CHAIN 1..162
FT /note="Protein archease"
FT /id="PRO_0000285952"
FT BINDING 34
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 161
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 162
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CONFLICT 55
FT /note="M -> V (in Ref. 2; AAH93322)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 162 AA; 19020 MW; 91771170C0C1A846 CRC64;
MNDRELDLTE EQKALKAKYP PITKKYEYLD HTADVQIHSW GNSLEEAFEQ CAMGMFGYMT
DTETVEPIDT VEVESEGDDM ESLLYHFLDD WLFKFSADIF FIPREVKVLH IDRMRYKIRS
IGWGEEFSIN KHPQGTEVKA ITYSAMQIHE TEQPEIFVII DI
