ID A0A8H6F5Y3_CANAX Unreviewed; 860 AA.
AC A0A8H6F5Y3;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 16.
DE SubName: Full=CobW/HypB/UreG, nucleotide-binding domain family protein {ECO:0000313|EMBL:KAF6070512.1};
GN ORFNames=FOB64_002177 {ECO:0000313|EMBL:KAF6070512.1};
OS Candida albicans (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Pichiomycetes;
OC Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5476 {ECO:0000313|EMBL:KAF6070512.1, ECO:0000313|Proteomes:UP000536275};
RN [1] {ECO:0000313|EMBL:KAF6070512.1, ECO:0000313|Proteomes:UP000536275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FDAARGOS_656 {ECO:0000313|EMBL:KAF6070512.1,
RC ECO:0000313|Proteomes:UP000536275};
RA Campos J., Goldberg B., Tallon L., Sadzewicz L., Vavikolanu K., Mehta A.,
RA Aluvathingal J., Nadendla S., Nandy P., Geyer C., Yan Y., Sichtig H.;
RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT Supporting development and validation of Infectious Disease Dx tests.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + phosphate + H(+); 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:ARBA00049117};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000256|ARBA:ARBA00049117};
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:KAF6070512.1}.
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DR EMBL; JABWAD010000025; KAF6070512.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A8H6F5Y3; -.
DR Proteomes; UP000536275; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-ARBA.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR CDD; cd03112; CobW-like; 1.
DR FunFam; 6.10.250.3410:FF:000001; Protein DBF4 homolog A; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 1.
DR Gene3D; 3.30.1220.10; CobW-like, C-terminal domain; 1.
DR Gene3D; 6.10.250.3410; DBF zinc finger; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR036627; CobW-likC_sf.
DR InterPro; IPR011629; CobW-like_C.
DR InterPro; IPR003495; CobW/HypB/UreG_nucleotide-bd.
DR InterPro; IPR055116; DBF4_BRCT.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013939; Regulatory_Dfp1/Him1.
DR InterPro; IPR051316; Zinc-reg_GTPase_activator.
DR InterPro; IPR006572; Znf_DBF.
DR InterPro; IPR038545; Znf_DBF_sf.
DR PANTHER; PTHR13748; COBW-RELATED; 1.
DR PANTHER; PTHR13748:SF31; ZINC-REGULATED GTPASE METALLOPROTEIN ACTIVATOR 1A-RELATED; 1.
DR Pfam; PF02492; cobW; 1.
DR Pfam; PF07683; CobW_C; 1.
DR Pfam; PF22437; DBF4_BRCT; 1.
DR Pfam; PF08630; Dfp1_Him1_M; 1.
DR Pfam; PF07535; zf-DBF; 1.
DR SMART; SM00586; ZnF_DBF; 1.
DR SUPFAM; SSF90002; Hypothetical protein YjiA, C-terminal domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51265; ZF_DBF4; 1.
PE 3: Inferred from homology;
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00600}.
FT DOMAIN 798..847
FT /note="DBF4-type"
FT /evidence="ECO:0000259|PROSITE:PS51265"
FT REGION 378..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 689..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..466
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..714
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 860 AA; 97144 MW; 9AB6009B9AE7BA43 CRC64;
MDEIPELVTE LPENGVIKTE KVPAAPFVPS SSTPTALAKK IPITIVTGYL GSGKSTLLQN
IGKTANKRLA IILNEFGDSS VIEKSVTIQD QGDSVQEWLD IGNGCLCCTV KDNGVTAIEN
LIENSKDKID YILLETTGVA DPAPIAKMFW LDEGLASNIY IDGVVTVVDA EHITKCLDDV
GGHWHKESLG EDVEFEDGIT TAHLQLALAD VILLNKIDKV SDTQPMTQRI RQINQTSPIH
TTSFGDIEIS KILDLHAFDV DAKLTTSETS FHDDRISTVT ITFPFLENEE GFSKVENFLQ
HVLWDNFVNG KNVEVHRMKG LLVHGNDVRV VQGVRDTYEI IENGKLLEEV KENKLVFIGK
NLHRPDLQEE LRMSKVEEHE SVNNLKRKFP SLAKPRQPLK ETNSNIPSPH KRAKIESPGK
QQSTQQPQQQ PQPQPQPQPQ QEKATHKPKK SSHQSKNNDK LAGDEMHEWQ QSWRRIMKSS
IVYFEGDQQS LEYRKAHKLL RLVGCKVTPF YDNNVTIIIS KRPYDSKTEY SPHDIFSNVS
KASIKVWNYD KVFRFLKHLG INIQTGVDEL AVNTHTILPP SLTNNNEKPD LYNLLKEEKI
YGSTDRDPNA KRDDLHYLGK NYLYVYDLTQ TVRPIAIREW KDPTDQNSER KRLKRLRKFE
ANQAHREALR LATYKMINGI SMSVHGFTAT STSTDKVDEE EDSTVKEPSE DPRFRQPLNR
NSSCMQSKAF EAMASGYNGA SNAVQPSMDS NLNSAAAMAG GNGLGPALSQ VPSKQLNNLK
RRILMKKKTT NTTEKKDKEH ASGYCENCRV KYTNFDEHIM TNRHRNFACD DRNFQDIDEL
IASLRERKSL GNVISNGDYV
//
