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Database: UniProt
Entry: A0A0C1VBD0_9CYAN
LinkDB: A0A0C1VBD0_9CYAN
Original site: A0A0C1VBD0_9CYAN 
ID   A0A0C1VBD0_9CYAN        Unreviewed;       357 AA.
AC   A0A0C1VBD0;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-SEP-2017, entry version 23.
DE   RecName: Full=Small ribosomal subunit biogenesis GTPase RsgA {ECO:0000256|HAMAP-Rule:MF_01820};
DE            EC=3.6.1.- {ECO:0000256|HAMAP-Rule:MF_01820};
GN   Name=rsgA {ECO:0000256|HAMAP-Rule:MF_01820};
GN   ORFNames=QQ91_35210 {ECO:0000313|EMBL:KIF41517.1};
OS   Lyngbya confervoides BDU141951.
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC   Oscillatoriaceae; Lyngbya.
OX   NCBI_TaxID=1574623 {ECO:0000313|EMBL:KIF41517.1, ECO:0000313|Proteomes:UP000031561};
RN   [1] {ECO:0000313|EMBL:KIF41517.1, ECO:0000313|Proteomes:UP000031561}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BDU141951 {ECO:0000313|EMBL:KIF41517.1,
RC   ECO:0000313|Proteomes:UP000031561};
RA   Malar M.C., Sen D., Tripathy S.;
RT   "Draft genome sequence of Lyngbya confervoides BDU141951.";
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: One of several proteins that assist in the late
CC       maturation steps of the functional core of the 30S ribosomal
CC       subunit. Helps release RbfA from mature subunits. May play a role
CC       in the assembly of ribosomal proteins into the subunit. Circularly
CC       permuted GTPase that catalyzes slow GTP hydrolysis, GTPase
CC       activity is stimulated by the 30S ribosomal subunit.
CC       {ECO:0000256|HAMAP-Rule:MF_01820, ECO:0000256|SAAS:SAAS00828801}.
CC   -!- SUBUNIT: Monomer. Associates with 30S ribosomal subunit, binds 16S
CC       rRNA. {ECO:0000256|HAMAP-Rule:MF_01820,
CC       ECO:0000256|SAAS:SAAS00828796}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01820,
CC       ECO:0000256|SAAS:SAAS00820346}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family.
CC       RsgA subfamily. {ECO:0000256|SAAS:SAAS00720088}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KIF41517.1}.
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DR   EMBL; JTHE01000274; KIF41517.1; -; Genomic_DNA.
DR   RefSeq; WP_039729165.1; NZ_JTHE01000274.1.
DR   EnsemblBacteria; KIF41517; KIF41517; QQ91_35210.
DR   Proteomes; UP000031561; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0042274; P:ribosomal small subunit biogenesis; IEA:UniProtKB-UniRule.
DR   CDD; cd01854; YjeQ_EngC; 1.
DR   HAMAP; MF_01820; GTPase_RsgA; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR030378; G_CP_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR004881; Ribosome_biogen_GTPase_RsgA.
DR   InterPro; IPR010914; RsgA_GTPase_dom.
DR   PANTHER; PTHR32120; PTHR32120; 1.
DR   Pfam; PF03193; RsgA_GTPase; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00157; TIGR00157; 1.
DR   PROSITE; PS50936; ENGC_GTPASE; 1.
DR   PROSITE; PS51721; G_CP; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000031561};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01820,
KW   ECO:0000256|SAAS:SAAS00820338};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_01820,
KW   ECO:0000256|SAAS:SAAS00698892};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01820,
KW   ECO:0000256|SAAS:SAAS00720101};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01820,
KW   ECO:0000256|SAAS:SAAS00720208};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01820,
KW   ECO:0000256|SAAS:SAAS00698882};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031561};
KW   Ribosome biogenesis {ECO:0000256|HAMAP-Rule:MF_01820,
KW   ECO:0000256|SAAS:SAAS00720213};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01820,
KW   ECO:0000256|SAAS:SAAS00720223};
KW   rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01820,
KW   ECO:0000256|SAAS:SAAS00720235};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01820, ECO:0000256|SAAS:SAAS00720226}.
FT   DOMAIN       94    261       CP-type G. {ECO:0000259|PROSITE:PS51721}.
FT   DOMAIN      112    259       EngC GTPase. {ECO:0000259|PROSITE:
FT                                PS50936}.
FT   NP_BIND     151    154       GTP. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   NP_BIND     203    211       GTP. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       284    284       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       289    289       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       291    291       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       297    297       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
SQ   SEQUENCE   357 AA;  38919 MW;  3283A9E5FC82A46F CRC64;
     MNLEQFGWCA NSTSALAFAS FEQAAWVAAR VIAEQRGAYR VHTGTVAYPA QITGQLQHRT
     VDPLMLPAVG DWVVVEPHAT QNTATIHQVL PRTSQFVRKV AGTTTAGQVV AANVDTVFLM
     SGLDGDFNLR RIERYLVTAW DSGASPVIVL NKVDVCTDVA ATIAQVAAIA IGVPIHAVSA
     ELGRGLSQLD PYLQPGKTVA LIGSSGVGKS TLTNYLLGDA QQSTQAVRAD DSRGRHTTTH
     RQLIRLPSGA LLIDTPGMRE LQLWQVGAGL SETFADIEAL AADCKFRDCQ HDQEPGCAVQ
     AAIAAGQLTA QRLQSYQKLQ REQQWIEQRR EGHAHQNTKR RWKQITKTMR QRQQPLS
//
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