ID A0A0D6KG61_9CYAN Unreviewed; 388 AA.
AC A0A0D6KG61;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=CobW/P47K family protein {ECO:0000313|EMBL:EKE98445.1};
GN ORFNames=FDUTEX481_03979 {ECO:0000313|EMBL:EKE98445.1};
OS Tolypothrix sp. PCC 7601.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC Tolypothrix.
OX NCBI_TaxID=1188 {ECO:0000313|EMBL:EKE98445.1, ECO:0000313|Proteomes:UP000032761};
RN [1] {ECO:0000313|EMBL:EKE98445.1, ECO:0000313|Proteomes:UP000032761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7601 / UTEX B 481 {ECO:0000313|Proteomes:UP000032761};
RX PubMed=25953173;
RA Yerrapragada S., Shukla A., Hallsworth-Pepin K., Choi K., Wollam A.,
RA Clifton S., Qin X., Muzny D., Raghuraman S., Ashki H., Uzman A.,
RA Highlander S.K., Fryszczyn B.G., Fox G.E., Tirumalai M.R., Liu Y., Kim S.,
RA Kehoe D.M., Weinstock G.M.;
RT "Extreme Sensory Complexity Encoded in the 10-Megabase Draft Genome
RT Sequence of the Chromatically Acclimating Cyanobacterium Tolypothrix sp.
RT PCC 7601.";
RL Genome Announc. 3:0-0(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000256|ARBA:ARBA00001702};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000256|ARBA:ARBA00001702};
CC -!- SIMILARITY: Belongs to the SIMIBI class G3E GTPase family. ZNG1
CC subfamily. {ECO:0000256|ARBA:ARBA00034320}.
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:EKE98445.1}.
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DR EMBL; AGCR01000090; EKE98445.1; -; Genomic_DNA.
DR RefSeq; WP_045873354.1; NZ_JH930369.1.
DR AlphaFoldDB; A0A0D6KG61; -.
DR STRING; 1188.FDUTEX481_03979; -.
DR PATRIC; fig|1188.3.peg.8005; -.
DR HOGENOM; CLU_017452_0_1_3; -.
DR OrthoDB; 504781at2; -.
DR Proteomes; UP000032761; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd03112; CobW-like; 1.
DR Gene3D; 3.30.1220.10; CobW-like, C-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR036627; CobW-likC_sf.
DR InterPro; IPR011629; CobW-like_C.
DR InterPro; IPR003495; CobW/HypB/UreG_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR13748:SF65; 47 KD PROTEIN; 1.
DR PANTHER; PTHR13748; COBW-RELATED; 1.
DR Pfam; PF02492; cobW; 1.
DR Pfam; PF07683; CobW_C; 1.
DR SMART; SM00833; CobW_C; 1.
DR SUPFAM; SSF90002; Hypothetical protein YjiA, C-terminal domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT DOMAIN 287..375
FT /note="CobW C-terminal"
FT /evidence="ECO:0000259|SMART:SM00833"
FT REGION 224..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 388 AA; 43812 MW; E0C327A89F2EADF0 CRC64;
MQSAVTPESQ AMDAPKQGIP VTIITGFLGS GKTTLLNHIL TNQQGLKTAV LVNEFGEIGI
DNELIVSTEE NMVELSNGCI CCTINSDLVD AVYKVLEREE KLDYLVVETT GLADPLPVAL
TFLGTELRDL TRLDSIITVV DAANYSLDLF NSQAAYSQIA YGDVIILNKA DLVDETALNE
LERKIGEVRE GARILRTTRS EVPLPLILSV GLFESDKYFD TVEDEHDHHD HEHHDHDHDH
DHDHSTCGHD HHDHDHDHST CGHDHHDHDH EHEHHHHHSD HLENDGFSSI SFQSDKPLSI
RKFQYFLDNQ LPTNVFRAKG IMWFEESPKR HIFHLCGKRF TMDDDEWKGQ PKNQLVLIGQ
NLDTDTLLSQ LEKCLCIPSV SRGKGFGK
//
