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Database: UniProt
Entry: A0A1S9ZFX8_9GAMM
LinkDB: A0A1S9ZFX8_9GAMM
Original site: A0A1S9ZFX8_9GAMM 
ID   A0A1S9ZFX8_9GAMM        Unreviewed;       936 AA.
AC   A0A1S9ZFX8;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Ribosomal RNA large subunit methyltransferase K/L {ECO:0000256|HAMAP-Rule:MF_01858};
DE   Includes:
DE     RecName: Full=23S rRNA m2G2445 methyltransferase {ECO:0000256|HAMAP-Rule:MF_01858};
DE              EC=2.1.1.173 {ECO:0000256|HAMAP-Rule:MF_01858};
DE     AltName: Full=rRNA (guanine-N(2)-)-methyltransferase RlmL {ECO:0000256|HAMAP-Rule:MF_01858};
DE   Includes:
DE     RecName: Full=23S rRNA m7G2069 methyltransferase {ECO:0000256|HAMAP-Rule:MF_01858};
DE              EC=2.1.1.264 {ECO:0000256|HAMAP-Rule:MF_01858};
DE     AltName: Full=rRNA (guanine-N(7)-)-methyltransferase RlmK {ECO:0000256|HAMAP-Rule:MF_01858};
GN   Name=rlmL {ECO:0000256|HAMAP-Rule:MF_01858};
GN   ORFNames=B0180_09825 {ECO:0000313|EMBL:OOR82257.1};
OS   Moraxella canis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Moraxella.
OX   NCBI_TaxID=90239 {ECO:0000313|EMBL:OOR82257.1, ECO:0000313|Proteomes:UP000190322};
RN   [1] {ECO:0000313|EMBL:OOR82257.1, ECO:0000313|Proteomes:UP000190322}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 8415A {ECO:0000313|EMBL:OOR82257.1,
RC   ECO:0000313|Proteomes:UP000190322};
RA   Engstrom-Jakobsson H., Salva-Serra F., Thorell K., Gonzales-Siles L.,
RA   Karlsson R., Boulund F., Engstrand L., Moore E.;
RT   "Draft genome sequence of Moraxella canis CCUG 8415A type strain.";
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Specifically methylates the guanine in position 2445
CC       (m2G2445) and the guanine in position 2069 (m7G2069) of 23S rRNA.
CC       {ECO:0000256|HAMAP-Rule:MF_01858}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanosine(2069) in 23S rRNA + S-adenosyl-L-methionine = H(+) +
CC         N(2)-methylguanosine(2069) in 23S rRNA + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:43772, Rhea:RHEA-COMP:10688, Rhea:RHEA-COMP:10689,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74269, ChEBI:CHEBI:74481; EC=2.1.1.264;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01858};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanosine(2445) in 23S rRNA + S-adenosyl-L-methionine = H(+) +
CC         N(2)-methylguanosine(2445) in 23S rRNA + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:42740, Rhea:RHEA-COMP:10215, Rhea:RHEA-COMP:10216,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74269, ChEBI:CHEBI:74481; EC=2.1.1.173;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01858};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01858}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. RlmKL family.
CC       {ECO:0000256|HAMAP-Rule:MF_01858}.
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:OOR82257.1}.
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DR   EMBL; MUXT01000014; OOR82257.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1S9ZFX8; -.
DR   Proteomes; UP000190322; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0052915; F:23S rRNA (guanine(2445)-N(2))-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0070043; F:rRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   CDD; cd11715; THUMP_AdoMetMT; 1.
DR   Gene3D; 3.30.2130.30; -; 1.
DR   Gene3D; 3.30.750.80; RNA methyltransferase domain (HRMD) like; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 2.
DR   HAMAP; MF_01858; 23SrRNA_methyltr_KL; 1.
DR   InterPro; IPR017244; 23SrRNA_methyltr_KL.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR000241; RlmKL-like_Mtase.
DR   InterPro; IPR019614; SAM-dep_methyl-trfase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR004114; THUMP_dom.
DR   PANTHER; PTHR47313; RIBOSOMAL RNA LARGE SUBUNIT METHYLTRANSFERASE K/L; 1.
DR   PANTHER; PTHR47313:SF1; RIBOSOMAL RNA LARGE SUBUNIT METHYLTRANSFERASE K_L; 1.
DR   Pfam; PF10672; Methyltrans_SAM; 1.
DR   Pfam; PF02926; THUMP; 1.
DR   Pfam; PF01170; UPF0020; 1.
DR   PIRSF; PIRSF037618; RNA_Mtase_bacteria_prd; 1.
DR   SMART; SM00981; THUMP; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 2.
DR   PROSITE; PS00092; N6_MTASE; 1.
DR   PROSITE; PS51165; THUMP; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01858};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW   Rule:MF_01858}; RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00529};
KW   rRNA processing {ECO:0000256|HAMAP-Rule:MF_01858};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW   Rule:MF_01858};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01858}.
FT   DOMAIN          88..217
FT                   /note="THUMP"
FT                   /evidence="ECO:0000259|PROSITE:PS51165"
FT   REGION          818..905
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          917..936
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        831..886
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   936 AA;  105992 MW;  7F2385A7728E1B73 CRC64;
     MGGSYFLNSY HGLCYNTLFF KTQIWTLMTQ HKPSYFADLK NFDVNEFTIV VTCADGLEAA
     LQIELGSFGL SSDVLRAGRV AVITDLAKLY HICLYSRVAS RVLLPLGEYH FKQKLSQTAP
     SQSVEVLDED VPEALYQFAS RIDWTDLFGL EHRFAIRLST DKRLSVNQQF ATLRIKDAIA
     DVFNRAFGAR PDVDAKQPDF QIFAAANHKF AEIFLDLSGT SLHRRGYRVA NTAAPLKENL
     AAALLYECGW HEGTYDTIID PMCGSGTFIT EALLMRADYP VGLEKSADEF GFYCWQHHDD
     EMWDEMVSDA TQRFHARLAQ MQAKPLTVIA CDADAYAVQA CHKNLMAAGL SPILDQVTLA
     QRALYQLPKL LSTLTCSKPL IITNPPYGER LGDTDFIKPL YHGLGLHVAA GMRSVAANTG
     QAIDATMAVL ASHIEHADTL PIIEPQTLRC HNGALTVYFR HGELNLSESS ALIFEWQKQE
     ITHPEAQDFI NRLQKNLSNL KKQAIKVGVT NLRVYDADLP NFNVAIDVYG DKIHVQEYAP
     PKQIPADVAK ARFNLVLQAV REVFGVPRES IFIKTRAKQS GNEQYTKNDN AAKRRKMWVM
     RELDAYFYVN FTEYLDTGLF IDHRNMRAKV GAASRAKRVL NLFSYTCTAS VHAALSGAKS
     VTSVDLSANY LDWGKQNFAL NGLVLDAMTE DGEKYQFIAH DVFEWIKGHT EQYDVIFIDP
     PTFSNSKKFK GTFDVQRDHV ALINRAMNRL TADGVLYFSN NYMRFEFDES LMARYDVKDI
     THETIGFDFD LKKPIHRSYE IRHKNAVKSE AVFLDDAVDQ KPQPKTPKSF DQPKRFAKKF
     NQTTDKKPNH KPGKDGKKSH ADRFNNFDHR AKRSAPDSRR FNDSDHKPNQ ATNQPSIKRV
     YVNPKLADEN LAQRLTDKLA EASPQGEKRY KIKKKS
//
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