ARCH_AERPE
ID ARCH_AERPE Reviewed; 144 AA.
AC Q9YFV2;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2002, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Protein archease {ECO:0000255|HAMAP-Rule:MF_01222};
GN OrderedLocusNames=APE_0148.1;
OS Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS K1).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Aeropyrum.
OX NCBI_TaxID=272557;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT Aeropyrum pernix K1.";
RL DNA Res. 6:83-101(1999).
CC -!- FUNCTION: Activates the tRNA-splicing ligase complex by facilitating
CC the enzymatic turnover of catalytic subunit RtcB. Acts by promoting the
CC guanylylation of RtcB, a key intermediate step in tRNA ligation. Can
CC also alter the NTP specificity of RtcB such that ATP, dGTP or ITP is
CC used efficiently (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the archease family. {ECO:0000255|HAMAP-
CC Rule:MF_01222}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000002; BAA79059.2; -; Genomic_DNA.
DR PIR; A72770; A72770.
DR AlphaFoldDB; Q9YFV2; -.
DR SMR; Q9YFV2; -.
DR STRING; 272557.APE_0148.1; -.
DR EnsemblBacteria; BAA79059; BAA79059; APE_0148.1.
DR KEGG; ape:APE_0148.1; -.
DR PATRIC; fig|272557.25.peg.103; -.
DR eggNOG; arCOG04055; Archaea.
DR OMA; WLSELLY; -.
DR Proteomes; UP000002518; Chromosome.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006388; P:tRNA splicing, via endonucleolytic cleavage and ligation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.55.10.10; -; 1.
DR HAMAP; MF_01222; Archease_arch; 1.
DR InterPro; IPR002804; Archease.
DR InterPro; IPR022952; Archease_arc.
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 3: Inferred from homology;
KW Calcium; Metal-binding; Reference proteome; tRNA processing.
FT CHAIN 1..144
FT /note="Protein archease"
FT /id="PRO_0000068840"
FT BINDING 14
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
SQ SEQUENCE 144 AA; 16457 MW; 75CF97D7CA11AC44 CRC64;
MQCGGWMHEE HTADVLVIAY GRTLEEAFEN AARGVYEVVT DTSRVEPRRR VDASIEGIDL
ENLLYRFIEN LIAYTDSEGL VFGLFRVCKI ECNGESCSIV ASAWGEEFDP SRHEHRTIVK
AMTYADMEIK EENGCWRVQF VVDI