ID   ARCH_METTH              Reviewed;         140 AA.
AC   O27635;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 131.
DE   RecName: Full=Protein archease {ECO:0000255|HAMAP-Rule:MF_01222};
GN   OrderedLocusNames=MTH_1598;
OS   Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS   10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=187420;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA   Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA   Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA   Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA   Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA   Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA   Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA   Reeve J.N.;
RT   "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT   functional analysis and comparative genomics.";
RL   J. Bacteriol. 179:7135-7155(1997).
RN   [2]
RP   PRELIMINARY FUNCTION.
RX   PubMed=15162483; DOI=10.1002/prot.20141;
RA   Canaves J.M.;
RT   "Predicted role for the archease protein family based on structural and
RT   sequence analysis of TM1083 and MTH1598, two proteins structurally
RT   characterized through structural genomics efforts.";
RL   Proteins 56:19-27(2004).
RN   [3]
RP   STRUCTURE BY NMR.
RX   PubMed=11854485; DOI=10.1073/pnas.042684599;
RA   Yee A., Chang X., Pineda-Lucena A., Wu B., Semesi A., Le B., Ramelot T.,
RA   Lee G.M., Bhattacharyya S., Gutierrez P., Denisov A., Lee C.-H., Cort J.R.,
RA   Kozlov G., Liao J., Finak G., Chen L., Wishart D., Lee W., McIntosh L.P.,
RA   Gehring K., Kennedy M.A., Edwards A.M., Arrowsmith C.H.;
RT   "An NMR approach to structural proteomics.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:1825-1830(2002).
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). May also act as a chaperone or
CC       modulator of proteins involved in DNA or RNA processing. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the archease family. {ECO:0000255|HAMAP-
CC       Rule:MF_01222}.
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DR   EMBL; AE000666; AAB86071.1; -; Genomic_DNA.
DR   PIR; C69080; C69080.
DR   RefSeq; WP_010877206.1; NC_000916.1.
DR   PDB; 1JW3; NMR; -; A=1-140.
DR   PDBsum; 1JW3; -.
DR   AlphaFoldDB; O27635; -.
DR   BMRB; O27635; -.
DR   SMR; O27635; -.
DR   STRING; 187420.MTH_1598; -.
DR   PaxDb; 187420-MTH_1598; -.
DR   EnsemblBacteria; AAB86071; AAB86071; MTH_1598.
DR   GeneID; 77402119; -.
DR   KEGG; mth:MTH_1598; -.
DR   PATRIC; fig|187420.15.peg.1561; -.
DR   HOGENOM; CLU_111362_3_0_2; -.
DR   InParanoid; O27635; -.
DR   EvolutionaryTrace; O27635; -.
DR   Proteomes; UP000005223; 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; Archease domain; 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; ARCHEASE; 1.
DR   PANTHER; PTHR12682:SF11; PROTEIN ARCHEASE; 1.
DR   Pfam; PF01951; Archease; 1.
DR   SUPFAM; SSF69819; MTH1598-like; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Calcium; Metal-binding; Reference proteome; tRNA processing.
FT   CHAIN           1..140
FT                   /note="Protein archease"
FT                   /id="PRO_0000068846"
FT   BINDING         12
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         139
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         140
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   STRAND          4..6
FT                   /evidence="ECO:0007829|PDB:1JW3"
FT   STRAND          10..18
FT                   /evidence="ECO:0007829|PDB:1JW3"
FT   STRAND          20..22
FT                   /evidence="ECO:0007829|PDB:1JW3"
FT   HELIX           23..37
FT                   /evidence="ECO:0007829|PDB:1JW3"
FT   STRAND          48..58
FT                   /evidence="ECO:0007829|PDB:1JW3"
FT   HELIX           59..75
FT                   /evidence="ECO:0007829|PDB:1JW3"
FT   STRAND          84..89
FT                   /evidence="ECO:0007829|PDB:1JW3"
FT   STRAND          91..101
FT                   /evidence="ECO:0007829|PDB:1JW3"
FT   STRAND          124..128
FT                   /evidence="ECO:0007829|PDB:1JW3"
FT   STRAND          131..139
FT                   /evidence="ECO:0007829|PDB:1JW3"
SQ   SEQUENCE   140 AA;  16183 MW;  1F82F57056E55AFC CRC64;
     MKGFEFFDVT ADAGFWAYGH DLEEVFENAA LAMFEVMTDT SLVEAAEERR VEITSEDRVS
     LLYDWLDELL FIHDTEFILF SKFKVKIDEK DDGLHLTGTA MGEEIKEGHE RRDEVKAVTF
     HMMEILDEDG LIKARVILDL
//