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Database: UniProt
Entry: A0A117ME40_9EURY
LinkDB: A0A117ME40_9EURY
Original site: A0A117ME40_9EURY 
ID   A0A117ME40_9EURY        Unreviewed;       633 AA.
AC   A0A117ME40;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Methyltransferase type 11 {ECO:0000313|EMBL:KUK98917.1};
GN   ORFNames=XE11_2829 {ECO:0000313|EMBL:KUK98917.1};
OS   Methanomicrobiales archaeon 53_19.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales.
OX   NCBI_TaxID=1641394 {ECO:0000313|EMBL:KUK98917.1, ECO:0000313|Proteomes:UP000054757};
RN   [1] {ECO:0000313|Proteomes:UP000054757}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA   Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA   Andersen G.L., Banfield J.F.;
RT   "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT   Other Microbial Community Members in Biogeochemical Transformations in Oil
RT   Reservoirs.";
RL   MBio 7:e01669-15(2015).
CC   -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC       {ECO:0000256|ARBA:ARBA00010871}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KUK98917.1}.
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DR   EMBL; LGHF01000276; KUK98917.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A117ME40; -.
DR   PATRIC; fig|1641394.3.peg.133; -.
DR   Proteomes; UP000054757; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   Gene3D; 2.20.25.110; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR011095; Dala_Dala_lig_C.
DR   InterPro; IPR041698; Methyltransf_25.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR23132; D-ALANINE--D-ALANINE LIGASE; 1.
DR   PANTHER; PTHR23132:SF25; D-ALANINE--D-ALANINE LIGASE A; 1.
DR   Pfam; PF07478; Dala_Dala_lig_C; 1.
DR   Pfam; PF13649; Methyltransf_25; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Methyltransferase {ECO:0000313|EMBL:KUK98917.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Transferase {ECO:0000313|EMBL:KUK98917.1}.
FT   DOMAIN          389..602
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          611..633
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..25
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        611..625
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   633 AA;  72385 MW;  0C11D5125184B162 CRC64;
     MTDDIQTDEP PDSRTKGKHR DRRTIGPVPN LEEYVKPDWW RGIFNRLYLK TDGDVVDDQH
     ITESEIDRIV QVLNLQSDAK ILDLCCGQGR HTLELMRRGY NAEGLDQSHY LIQRARSTAK
     KEGLSVRFRE GDARRLPYRT DTYDVVLVLG NSFGYFDSVE EDLRILTELR RILKPWGRVL
     LDVADGDYLK EHFQARSWEW IDDAMFVCRE RSLSLDEQRL ISREVITDVE KGVVADQFYA
     ERLYTPEALR RLLEKAGFSG ITFHKIDTES QRNQDLGMME RRHIVTAVLK KEWSTTKTRG
     QERAKHVAVM LGDPAKPDAL KPSCTFDDDD FYTIDQMKVD YVFNLCDEGF NNDPRKELHV
     PALLEIFEIP YTGSGPQSLA FCYDKSLVRG VAKEMGIPVP DACFITPGDR TYDVGMKLPA
     IVKPNAGDSS YGITQESIAR TIEELSDVIN ALRTKLGYDR SLLVEEFLTG KDISVGIIGN
     PSGYCTVLPI IEEDYSALPP ELPRICGYEA KWLPDSPYWK IVSKPAELPE EIEKVIVRCC
     LALFKRLECR DYCRFDWRLD EHGSPKLLEV NPNPGWCWDG HLAKMAKYAG LSYPEMLGRI
     LKAAEERFGM EPETGAREGE KDPLPFDLTR QTA
//
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