ARCH_PYRHO
ID ARCH_PYRHO Reviewed; 142 AA.
AC O59205;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Protein archease {ECO:0000255|HAMAP-Rule:MF_01222};
GN OrderedLocusNames=PH1536;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.44 ANGSTROMS) OF 2-142 IN COMPLEX WITH CALCIUM,
RP FUNCTION, AND MUTAGENESIS OF GLU-8; HIS-9; ASP-12; LYS-117; ASP-141 AND
RP ILE-142.
RX PubMed=24435797; DOI=10.1093/nar/gkt1375;
RA Desai K.K., Cheng C.L., Bingman C.A., Phillips G.N. Jr., Raines R.T.;
RT "A tRNA splicing operon: Archease endows RtcB with dual GTP/ATP cofactor
RT specificity and accelerates RNA ligation.";
RL Nucleic Acids Res. 42:3931-3942(2014).
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. {ECO:0000269|PubMed:24435797}.
CC -!- SIMILARITY: Belongs to the archease family. {ECO:0000255|HAMAP-
CC Rule:MF_01222}.
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DR EMBL; BA000001; BAA30646.1; -; Genomic_DNA.
DR PIR; F71030; F71030.
DR RefSeq; WP_010885612.1; NC_000961.1.
DR PDB; 4N2P; X-ray; 1.44 A; A/B/C/D=2-142.
DR PDBsum; 4N2P; -.
DR AlphaFoldDB; O59205; -.
DR SMR; O59205; -.
DR STRING; 70601.3257963; -.
DR EnsemblBacteria; BAA30646; BAA30646; BAA30646.
DR GeneID; 1443852; -.
DR KEGG; pho:PH1536; -.
DR eggNOG; arCOG04055; Archaea.
DR OMA; WLSELLY; -.
DR OrthoDB; 125788at2157; -.
DR Proteomes; UP000000752; Chromosome.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0006388; P:tRNA splicing, via endonucleolytic cleavage and ligation; IDA:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Calcium; Metal-binding; tRNA processing.
FT CHAIN 1..142
FT /note="Protein archease"
FT /id="PRO_0000068850"
FT BINDING 12
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:24435797"
FT BINDING 141
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:24435797"
FT BINDING 142
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:24435797"
FT MUTAGEN 8
FT /note="E->A: Does not affect ability to stimulate RtcB
FT ligase activity but has an effect on ATP utilization by
FT RtcB."
FT /evidence="ECO:0000269|PubMed:24435797"
FT MUTAGEN 9
FT /note="H->A: Impaired ability to stimulate RtcB ligase
FT activity."
FT /evidence="ECO:0000269|PubMed:24435797"
FT MUTAGEN 12
FT /note="D->A: Impaired ability to stimulate RtcB ligase
FT activity."
FT /evidence="ECO:0000269|PubMed:24435797"
FT MUTAGEN 117
FT /note="K->A: Impaired ability to stimulate RtcB ligase
FT activity."
FT /evidence="ECO:0000269|PubMed:24435797"
FT MUTAGEN 141
FT /note="D->A: Impaired ability to stimulate RtcB ligase
FT activity."
FT /evidence="ECO:0000269|PubMed:24435797"
FT MUTAGEN 142
FT /note="Missing: Impaired ability to stimulate RtcB ligase
FT activity."
FT /evidence="ECO:0000269|PubMed:24435797"
FT STRAND 3..10
FT /evidence="ECO:0007829|PDB:4N2P"
FT STRAND 14..21
FT /evidence="ECO:0007829|PDB:4N2P"
FT HELIX 22..37
FT /evidence="ECO:0007829|PDB:4N2P"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:4N2P"
FT STRAND 47..57
FT /evidence="ECO:0007829|PDB:4N2P"
FT HELIX 58..76
FT /evidence="ECO:0007829|PDB:4N2P"
FT STRAND 78..90
FT /evidence="ECO:0007829|PDB:4N2P"
FT STRAND 93..104
FT /evidence="ECO:0007829|PDB:4N2P"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:4N2P"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:4N2P"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:4N2P"
SQ SEQUENCE 142 AA; 16646 MW; 6400ACCABF5B9189 CRC64;
MKKWEHYEHT ADIGIRGYGD SLEEAFEAVA IALFDVMVNV NKVEKKEVRE IEVEAEDLEA
LLYSFLEELL VIHDIEGLVF RDFEVKIERV NGKYRLRAKA YGEKLDLKKH EPKEEVKAIT
YHDMKIERLP NGKWMAQLVP DI
