ID E1VUR9_GLUAR Unreviewed; 262 AA.
AC E1VUR9;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Putative haemolysin {ECO:0000313|EMBL:CBT75372.1};
GN OrderedLocusNames=AARI_11600 {ECO:0000313|EMBL:CBT75372.1};
OS Glutamicibacter arilaitensis (strain DSM 16368 / CIP 108037 / IAM 15318 /
OS JCM 13566 / NCIMB 14258 / Re117) (Arthrobacter arilaitensis).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Glutamicibacter.
OX NCBI_TaxID=861360 {ECO:0000313|Proteomes:UP000006878};
RN [1] {ECO:0000313|EMBL:CBT75372.1, ECO:0000313|Proteomes:UP000006878}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 16368 / CIP 108037 / IAM 15318 / JCM 13566 / Re117
RC {ECO:0000313|Proteomes:UP000006878};
RX PubMed=21124797; DOI=10.1371/journal.pone.0015489;
RA Monnet C., Loux V., Gibrat J.F., Spinnler E., Barbe V., Vacherie B.,
RA Gavory F., Gourbeyre E., Siguier P., Chandler M., Elleuch R., Irlinger F.,
RA Vallaeys T.;
RT "The Arthrobacter arilaitensis Re117 genome sequence reveals its genetic
RT adaptation to the surface of cheese.";
RL PLoS ONE 5:E15489-E15489(2010).
RN [2] {ECO:0000313|Proteomes:UP000006878}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16368 / CIP 108037 / IAM 15318 / JCM 13566 / Re117
RC {ECO:0000313|Proteomes:UP000006878};
RA Genoscope.;
RT "Complete genome sequence of Arthrobacter arilaitensis (strain DSM 16368 /
RT CIP 108037 / JCM 13566 / Re117).";
RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TlyA family.
CC {ECO:0000256|ARBA:ARBA00029460}.
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DR EMBL; FQ311875; CBT75372.1; -; Genomic_DNA.
DR RefSeq; WP_013348516.1; NC_014550.1.
DR AlphaFoldDB; E1VUR9; -.
DR STRING; 861360.AARI_11600; -.
DR KEGG; aai:AARI_11600; -.
DR eggNOG; COG1189; Bacteria.
DR HOGENOM; CLU_058015_1_0_11; -.
DR OrthoDB; 9784736at2; -.
DR Proteomes; UP000006878; Chromosome.
DR GO; GO:0008168; F:methyltransferase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd00165; S4; 1.
DR Gene3D; 3.10.290.10; RNA-binding S4 domain; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR004538; Hemolysin_A/TlyA.
DR InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR InterPro; IPR002942; S4_RNA-bd.
DR InterPro; IPR036986; S4_RNA-bd_sf.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR047048; TlyA.
DR NCBIfam; TIGR00478; tly; 1.
DR PANTHER; PTHR32319; BACTERIAL HEMOLYSIN-LIKE PROTEIN; 1.
DR PANTHER; PTHR32319:SF0; BACTERIAL HEMOLYSIN-LIKE PROTEIN; 1.
DR Pfam; PF01728; FtsJ; 1.
DR Pfam; PF01479; S4; 1.
DR PIRSF; PIRSF005578; TlyA; 1.
DR SMART; SM00363; S4; 1.
DR SUPFAM; SSF55174; Alpha-L RNA-binding motif; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS50889; S4; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000006878};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182}.
FT DOMAIN 2..68
FT /note="RNA-binding S4"
FT /evidence="ECO:0000259|SMART:SM00363"
SQ SEQUENCE 262 AA; 27857 MW; 040BBF4BE878C993 CRC64;
MNRLDQELVV RDLARSRTEA AKLVEAERVL LNGQVAAKAS KKIAEGDDLA LIPSEGEEYV
SRAGHKLAGA LDVFTTINPE GLRCLDAGAS TGGFTDVLLR RGAKSVVAAD VGHGQLVDVI
RNDPRVQVHE GLNVRYLTPE DIGGVVDLVV ADLSFISLRL VIDALAGAAK DSGSLVLMVK
PQFEVGREHL NRTGVVTNPE LRRSSVEAVI ASANAAGLHL RGLARSPLPG QDGNAEFFLW
LASGENPQSA DVPLIEQNVD YS
//
