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
//