ID Q0RNY1_FRAAA Unreviewed; 642 AA.
AC Q0RNY1;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE SubName: Full=Adenosine 5'-phosphosulfate kinase (Partial match) {ECO:0000313|EMBL:CAJ60755.1};
DE EC=2.7.1.25 {ECO:0000313|EMBL:CAJ60755.1};
GN Name=cysC {ECO:0000313|EMBL:CAJ60755.1};
GN OrderedLocusNames=FRAAL2106 {ECO:0000313|EMBL:CAJ60755.1};
OS Frankia alni (strain DSM 45986 / CECT 9034 / ACN14a).
OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX NCBI_TaxID=326424 {ECO:0000313|EMBL:CAJ60755.1, ECO:0000313|Proteomes:UP000000657};
RN [1] {ECO:0000313|EMBL:CAJ60755.1, ECO:0000313|Proteomes:UP000000657}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACN14a {ECO:0000313|Proteomes:UP000000657};
RX PubMed=17151343; DOI=10.1101/gr.5798407;
RA Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., Couloux A.,
RA Cournoyer B., Cruveiller S., Daubin V., Demange N., Francino M.P.,
RA Goltsman E., Huang Y., Kopp O.R., Labarre L., Lapidus A., Lavire C.,
RA Marechal J., Martinez M., Mastronunzio J.E., Mullin B.C., Niemann J.,
RA Pujic P., Rawnsley T., Rouy Z., Schenowitz C., Sellstedt A., Tavares F.,
RA Tomkins J.P., Vallenet D., Valverde C., Wall L.G., Wang Y., Medigue C.,
RA Benson D.R.;
RT "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT reflect host range and host plant biogeography.";
RL Genome Res. 17:7-15(2007).
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DR EMBL; CT573213; CAJ60755.1; -; Genomic_DNA.
DR RefSeq; WP_011603271.1; NC_008278.1.
DR AlphaFoldDB; Q0RNY1; -.
DR STRING; 326424.FRAAL2106; -.
DR KEGG; fal:FRAAL2106; -.
DR eggNOG; COG0529; Bacteria.
DR eggNOG; COG2046; Bacteria.
DR HOGENOM; CLU_022950_0_1_11; -.
DR OrthoDB; 9804504at2; -.
DR Proteomes; UP000000657; Chromosome.
DR GO; GO:0004020; F:adenylylsulfate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0000103; P:sulfate assimilation; IEA:InterPro.
DR CDD; cd02027; APSK; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.10.400.10; Sulfate adenylyltransferase; 1.
DR InterPro; IPR002891; APS_kinase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015947; PUA-like_sf.
DR NCBIfam; TIGR00455; apsK; 1.
DR PANTHER; PTHR42700; SULFATE ADENYLYLTRANSFERASE; 1.
DR PANTHER; PTHR42700:SF1; SULFATE ADENYLYLTRANSFERASE; 1.
DR Pfam; PF01583; APS_kinase; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:CAJ60755.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000657};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CAJ60755.1}.
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 320..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..287
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 642 AA; 65352 MW; AF3873D1253A2F6E CRC64;
MSATSHPDPD PDRLPKPGAT GATDPSHGPA ADDRLLRLVT PDRAAELTTA SLGWPSLTLT
PVQLAELELL LVGAFGPNPG YPAAQELAGV PVPILAVPAA DAEPLAAGDT VALRDPEGVM
IAALHVRTLL PAPAGSTVRL VGTLDGVRLP HHPDHPALRL TPDQLRAELR ARGWTGPQVG
AGAAWAVWAD GLLHTADVGR IRALTRQGKR CVVLAPVGGA DPADAGHHLR VRCLQAALDA
VDAPLRPSEA TLASEAVASD AIAAGAAGRR HEPGPDPYRR PGTGDHPPRH RSLLVLVPAV
PSALLATPRE PGMSATVLPP AGGTRHPLAP GPAGFEPAGF EPSGLEPSGF EPSGLEPAAL
SSAGPAPAGV APAAIPLEPD GGAAGATPSA NADAEVLARL TAQRAHLASS YGLSGSLIGP
AIGAPGRQEL ASLLDAGGPI PAELTPPAVA AELARAIPPR SQRGLTIFFT GLSGSGKSTL
AGLLVCRLLE QGGRRITLLD GDVVRAHLSQ GLGFSRADRD LNVRRIGFVA AQVAGAGGTA
VCAPIAPYAR VRTQVREMVQ AAGGGFVLVH VSTPLEVCEA RDRKGLYAKA RAGVIPAFTG
VSDPYEQPTD ADVTVDTAQL SGDEAVDRIL DHLRVAGWLT PA
//