ID A0A0R2RVP1_9FLAO Unreviewed; 734 AA.
AC A0A0R2RVP1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=MFS transporter {ECO:0000313|EMBL:KRO66647.1};
GN ORFNames=ABR84_03315 {ECO:0000313|EMBL:KRO66647.1};
OS Cryomorphaceae bacterium BACL21 MAG-121220-bin10.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Cryomorphaceae.
OX NCBI_TaxID=1655592 {ECO:0000313|EMBL:KRO66647.1, ECO:0000313|Proteomes:UP000051758};
RN [1] {ECO:0000313|EMBL:KRO66647.1, ECO:0000313|Proteomes:UP000051758}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BACL21 MAG-121220-bin10 {ECO:0000313|EMBL:KRO66647.1};
RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA Andersson A.F.;
RT "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: In eubacteria ppGpp (guanosine 3'-diphosphate 5'-diphosphate)
CC is a mediator of the stringent response that coordinates a variety of
CC cellular activities in response to changes in nutritional abundance.
CC {ECO:0000256|RuleBase:RU003847}.
CC -!- SIMILARITY: Belongs to the relA/spoT family.
CC {ECO:0000256|RuleBase:RU003847}.
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:KRO66647.1}.
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DR EMBL; LICC01000040; KRO66647.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2RVP1; -.
DR STRING; 1655592.ABR84_03315; -.
DR Proteomes; UP000051758; Unassembled WGS sequence.
DR GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
DR CDD; cd00077; HDc; 1.
DR CDD; cd05399; NT_Rel-Spo_like; 1.
DR CDD; cd01668; TGS_RSH; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.30.70.260; -; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR006674; HD_domain.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR004811; RelA/Spo_fam.
DR InterPro; IPR045600; RelA/SpoT_AH_RIS.
DR InterPro; IPR007685; RelA_SpoT.
DR InterPro; IPR004095; TGS.
DR InterPro; IPR012676; TGS-like.
DR InterPro; IPR033655; TGS_RelA/SpoT.
DR NCBIfam; TIGR00691; spoT_relA; 1.
DR PANTHER; PTHR21262:SF31; BIFUNCTIONAL (P)PPGPP SYNTHASE_HYDROLASE SPOT; 1.
DR PANTHER; PTHR21262; GUANOSINE-3',5'-BIS DIPHOSPHATE 3'-PYROPHOSPHOHYDROLASE; 1.
DR Pfam; PF13291; ACT_4; 1.
DR Pfam; PF13328; HD_4; 1.
DR Pfam; PF19296; RelA_AH_RIS; 1.
DR Pfam; PF04607; RelA_SpoT; 1.
DR Pfam; PF02824; TGS; 1.
DR SMART; SM00471; HDc; 1.
DR SMART; SM00954; RelA_SpoT; 1.
DR SUPFAM; SSF55021; ACT-like; 1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81271; TGS-like; 1.
DR PROSITE; PS51831; HD; 1.
DR PROSITE; PS51880; TGS; 1.
PE 3: Inferred from homology;
FT DOMAIN 58..158
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 402..463
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
SQ SEQUENCE 734 AA; 84161 MW; 8CBB0235F3D939A7 CRC64;
MTPDVLEIEN KEIAKQYKQL LKISYQTLSK DDKKLIRMAF DIAVDAHKEQ RRKSGEAYIF
HPIAVAKIVA AEIGLDATSI AAALLHDVVE DTAYNLADIE QLFGPTVTRI VHGLTKISHL
EYQSDVSLQA ENFRKMLLTL NEDIRVIIIK IADRMHNMQT MDSMSPEKQL KIASETLYIY
APLAHRIGLY NIKSELEDLG LKYTEPAVYR DIVDKIKESK QEQDHFITSF TQVIRDRLND
ENIKFDIKGR PKSIFSIRRK MVVQNVSFDE VYDKFAIRII YNTTSENEKF LAWKIYSIVT
DHFRPNPIRL RDWISAPKST GYEALHITVM GPDGRWVEVQ IRSQRMNEIA EKGYAAHYKY
KNGDSQDEGL DLWLNKLQET LETAQRDAVD FVEDFKLNLY TKEIFVFSPK GDLYSLAKGA
TALDFAFHVH TEIGKHTRGA KVNGKLVPLS FALNNGDQVE IITSEKTKPS ANWLNYVITG
RAIAKIKSTL KEEEKQIAEE GKVILMRKLK SQKITLDDKV TQRLVVYFKL KTSLDLFYRI
GAGMIDNKML KEFVAANNNA FVNFFKNRIR RPKDNDYVHK EELTVKYDQL VFGKEEEKLD
YKVSPCCNPI PGDDVFGFLT IHEGIKVHKT NCPNALQMQS NYNYRIIKAF WIDATQSDFK
ATLKITGMDT FGMVNSVTKV VSSNHHIDMK SVHFDTNDGT FIGNIVVKVK NKAILDNLVK
NIQKINGIDK VTRL
//
