ID Q5QVG4_IDILO Unreviewed; 486 AA.
AC Q5QVG4;
DT 04-JAN-2005, integrated into UniProtKB/TrEMBL.
DT 04-JAN-2005, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE SubName: Full=RimK-like domain (C-terminal) fused to uncharacterized conserved domain {ECO:0000313|EMBL:AAV82992.1};
GN OrderedLocusNames=IL2160 {ECO:0000313|EMBL:AAV82992.1};
OS Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Idiomarina.
OX NCBI_TaxID=283942 {ECO:0000313|EMBL:AAV82992.1, ECO:0000313|Proteomes:UP000001171};
RN [1] {ECO:0000313|EMBL:AAV82992.1, ECO:0000313|Proteomes:UP000001171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-735 / DSM 15497 / L2-TR
RC {ECO:0000313|Proteomes:UP000001171};
RX PubMed=15596722; DOI=10.1073/pnas.0407638102;
RA Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y.,
RA Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S.,
RA Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S.,
RA Denery J., Aizawa S., Shibata S., Malahoff A., Alam M.;
RT "Genome sequence of the deep-sea gamma-proteobacterium Idiomarina
RT loihiensis reveals amino acid fermentation as a source of carbon and
RT energy.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004).
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DR EMBL; AE017340; AAV82992.1; -; Genomic_DNA.
DR RefSeq; WP_011235388.1; NC_006512.1.
DR AlphaFoldDB; Q5QVG4; -.
DR STRING; 283942.IL2160; -.
DR KEGG; ilo:IL2160; -.
DR eggNOG; COG0189; Bacteria.
DR HOGENOM; CLU_016765_0_0_6; -.
DR OrthoDB; 9800957at2; -.
DR Proteomes; UP000001171; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013651; ATP-grasp_RimK-type.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR025839; RLAN_dom.
DR PANTHER; PTHR21621:SF0; BETA-CITRYLGLUTAMATE SYNTHASE B-RELATED; 1.
DR PANTHER; PTHR21621; RIBOSOMAL PROTEIN S6 MODIFICATION PROTEIN; 1.
DR Pfam; PF08443; RimK; 1.
DR Pfam; PF14401; RLAN; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000001171}.
FT DOMAIN 286..480
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 486 AA; 55672 MW; DA351E375560D2D1 CRC64;
MQQHVHLIID NAADWQPYYP SQSLLTASEY LQSAHLQSRY HVLNLCNDLS YLSTGYYVSL
LAEARGQRVM PSVATINDLT NFSHYQLLIN TADRSLTKYL QNRDEKSLSL LICFGLCEQP
ELASFARQIF ERYPCPILKV ELEFNGRWHI NKLTSGALNQ LTDEQQSFFG NSLDHFSKRV
WRKARTRKEY RFDLAILYNP DEAIPTSDKK ALSLFIKAAK EADIEAELIT ANDFNRLLEF
DALFIRETTR INHYTYHFAK KAEANGMVVI DHPDSIVKCA NKVFLKELLD KHKVATPKTE
LLLSQSDIDY EAIGERLGYP VVLKIPDGSF SIGVEKAEDL AQFKQVATEL FKQSTILLAQ
EYMRTDYDWR IGVLNNRPIY ACQYFMARNH WQIYNHSESS SRGKSGSFAT LGVHQAPKDV
VRLALQATRL IGDGLYGVDI KQTPQGPVVI EINDNPSIES GVEDKHLGYE LYRLIMADFG
RRLDEY
//
