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Database: UniProt
Entry: A0A176VYN0_MARPO
LinkDB: A0A176VYN0_MARPO
Original site: A0A176VYN0_MARPO 
ID   A0A176VYN0_MARPO        Unreviewed;       343 AA.
AC   A0A176VYN0;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=CobW/HypB/UreG nucleotide-binding domain-containing protein {ECO:0000259|Pfam:PF02492};
GN   ORFNames=AXG93_2145s1800 {ECO:0000313|EMBL:OAE25880.1};
OS   Marchantia polymorpha subsp. ruderalis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC   Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX   NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE25880.1, ECO:0000313|Proteomes:UP000077202};
RN   [1] {ECO:0000313|EMBL:OAE25880.1, ECO:0000313|Proteomes:UP000077202}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Tak-1 and cv. Tak-2 {ECO:0000313|Proteomes:UP000077202};
RC   TISSUE=Whole gametophyte {ECO:0000313|EMBL:OAE25880.1};
RA   Honkanen S., Jones V.A., Morieri G., Champion C., Hetherington A.J.,
RA   Kelly S., Saint-Marcoux D., Proust H., Prescott H., Dolan L.;
RT   "Mechanisms controlling the formation of the plant cell surface in tip-
RT   growing cells are functionally conserved among land plants.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the SIMIBI class G3E GTPase family. UreG
CC       subfamily. {ECO:0000256|ARBA:ARBA00005732}.
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:OAE25880.1}.
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DR   EMBL; LVLJ01002289; OAE25880.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A176VYN0; -.
DR   OrthoDB; 5484572at2759; -.
DR   Proteomes; UP000077202; Unassembled WGS sequence.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0016151; F:nickel cation binding; IEA:InterPro.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR   CDD; cd05540; UreG; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_01389; UreG; 1.
DR   InterPro; IPR003495; CobW/HypB/UreG_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR004400; UreG.
DR   NCBIfam; TIGR00101; ureG; 1.
DR   PANTHER; PTHR31715; UREASE ACCESSORY PROTEIN G; 1.
DR   PANTHER; PTHR31715:SF0; UREASE ACCESSORY PROTEIN G; 1.
DR   Pfam; PF02492; cobW; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nickel insertion {ECO:0000256|ARBA:ARBA00022988};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077202}.
FT   DOMAIN          87..257
FT                   /note="CobW/HypB/UreG nucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02492"
FT   REGION          1..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..59
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   343 AA;  38147 MW;  30B69D81147B1024 CRC64;
     MADHGAPHFH SHDTDMHPHE HTHDEQEHHH HEHDHSSKDE WKGADGKIYH SHDGLAPHTH
     EPLESPGFFS RRARPITSRD FKERAFTIGI GGPVGTGKTA LMLALCRELR DKYSIAAVTN
     DIFTKEDGEF LVKNGALPPE RIRAVETGGC PHAAIREDIS INLGPLEELS HLFSAEILLC
     ESGGDNLAAN FSRELADYII YIIDVSGGDK IPRKGGPGIT QADLLVINKT DLAEAVGANL
     KVMEQDSLRM RDGGPFVFAQ IEQKALELYL LGLVFTSLLK ADSTRTRMPS NYTKTKIVDL
     FLLNFRSYLT PSSLSEVKHN IGVSEIVNHI LSAWEEATHH KRR
//
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