KAD6_CANAL
ID KAD6_CANAL Reviewed; 248 AA.
AC Q8TG40; A0A1D8PC69; Q5AB96;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Adenylate kinase isoenzyme 6 homolog HBR1 {ECO:0000255|HAMAP-Rule:MF_03173};
DE Short=AK6 {ECO:0000255|HAMAP-Rule:MF_03173};
DE EC=2.7.4.3 {ECO:0000255|HAMAP-Rule:MF_03173};
DE AltName: Full=Dual activity adenylate kinase/ATPase {ECO:0000255|HAMAP-Rule:MF_03173};
DE Short=AK/ATPase {ECO:0000255|HAMAP-Rule:MF_03173};
DE AltName: Full=Hemoglobin and proliferation-regulated protein 1;
DE Short=Hb-regulated protein 1;
GN Name=HBR1; Synonyms=FAP7; OrderedLocusNames=CAALFM_C100340WA;
GN ORFNames=CaO19.13495, CaO19.6074;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RX PubMed=15189997; DOI=10.1128/ec.3.3.764-775.2004;
RA Pendrak M.L., Yan S.S., Roberts D.D.;
RT "Hemoglobin regulates expression of an activator of mating-type locus alpha
RT genes in Candida albicans.";
RL Eukaryot. Cell 3:764-775(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [5]
RP FUNCTION.
RX PubMed=17365652; DOI=10.1080/13693780601164314;
RA Pendrak M.L., Rodrigues R.G., Roberts D.D.;
RT "Induction of a high affinity fibronectin receptor in Candida albicans by
RT caspofungin: requirements for beta (1,6) glucans and the developmental
RT regulator Hbr1p.";
RL Med. Mycol. 45:157-168(2007).
RN [6]
RP INDUCTION.
RX PubMed=17614954; DOI=10.1111/j.1365-2958.2007.05788.x;
RA Wilson D., Tutulan-Cunita A., Jung W., Hauser N.C., Hernandez R.,
RA Williamson T., Piekarska K., Rupp S., Young T., Stateva L.;
RT "Deletion of the high-affinity cAMP phosphodiesterase encoded by PDE2
RT affects stress responses and virulence in Candida albicans.";
RL Mol. Microbiol. 65:841-856(2007).
CC -!- FUNCTION: Broad-specificity nucleoside monophosphate (NMP) kinase that
CC catalyzes the reversible transfer of the terminal phosphate group
CC between nucleoside triphosphates and monophosphates. Has also ATPase
CC activity. May be involved in rRNA maturation and transcription
CC regulation (By similarity). Induces transcription of mating-type
CC proteins ALPHA1 and ALPHA2 and moderately represses transcription of
CC mating-type protein A1 in response to hemoglobin and growth signals.
CC Involved in the induction of a high affinity fibronectin receptor by
CC sub-inhibitory dosages of caspofungin. {ECO:0000255|HAMAP-
CC Rule:MF_03173, ECO:0000269|PubMed:15189997,
CC ECO:0000269|PubMed:17365652}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03173};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03173}.
CC Nucleus {ECO:0000255|HAMAP-Rule:MF_03173}.
CC -!- INDUCTION: Induced in the presence of exogenous hemoglobin and during
CC the exponential growth phase and by cold-stress.
CC {ECO:0000269|PubMed:15189997, ECO:0000269|PubMed:17614954}.
CC -!- SIMILARITY: Belongs to the adenylate kinase family. AK6 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03173}.
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DR EMBL; AF466197; AAM10638.1; -; Genomic_DNA.
DR EMBL; CP017623; AOW25732.1; -; Genomic_DNA.
DR RefSeq; XP_719036.1; XM_713943.1.
DR AlphaFoldDB; Q8TG40; -.
DR SMR; Q8TG40; -.
DR STRING; 237561.Q8TG40; -.
DR PRIDE; Q8TG40; -.
DR GeneID; 3639295; -.
DR KEGG; cal:CAALFM_C100340WA; -.
DR CGD; CAL0000197369; HBR1.
DR VEuPathDB; FungiDB:C1_00340W_A; -.
DR eggNOG; KOG3347; Eukaryota.
DR HOGENOM; CLU_079096_3_0_1; -.
DR InParanoid; Q8TG40; -.
DR OMA; QCEIFGT; -.
DR OrthoDB; 1488235at2759; -.
DR PHI-base; PHI:4925; -.
DR PRO; PR:Q8TG40; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004017; F:adenylate kinase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IDA:CGD.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR GO; GO:0036166; P:phenotypic switching; IMP:CGD.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0010468; P:regulation of gene expression; IMP:CGD.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00039; Adenylate_kinase_AK6; 1.
DR InterPro; IPR020618; Adenyl_kinase_AK6.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR12595; PTHR12595; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Nucleus;
KW Reference proteome; Ribosome biogenesis; rRNA processing; Transcription;
KW Transcription regulation; Transferase.
FT CHAIN 1..248
FT /note="Adenylate kinase isoenzyme 6 homolog HBR1"
FT /id="PRO_0000153901"
FT REGION 49..72
FT /note="NMP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03173"
FT REGION 124..134
FT /note="LID"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03173"
FT REGION 188..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..241
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 19..24
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03173"
FT BINDING 55
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03173"
FT BINDING 95
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03173"
FT BINDING 121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03173"
FT BINDING 125
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03173"
SQ SEQUENCE 248 AA; 28668 MW; E147D1B7354958D5 CRC64;
MTTMSRRYTP NIIITGTPGC GKSSHSSSLV SQLNQTLGKE TTIHFKHFNI SEIAKERDCI
ESYDAKLDTS IVDEDKLLDS LEPDLEKGGV VVDWHCCDIF PERLIDLVVV LRTDNSNLFD
RLKTRNYNDL KLQENLDCEI MEVILQEAKD SYIPDIVIEL RSDTAEEMDE NVDRISSWVE
TWIEDHPDGV SNELNKQYNP DDSSDEGDDN SDSDEYELEE DEQEEEEERE EYDEETNEEM
EHTEDIAQ
