ID U6H4R4_9EIME Unreviewed; 657 AA.
AC U6H4R4;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Sulfate adenylyltransferas-adenylylsulfate kinase, putative {ECO:0000313|EMBL:CDI86877.1};
GN ORFNames=EPH_0022340 {ECO:0000313|EMBL:CDI86877.1};
OS Eimeria praecox.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX NCBI_TaxID=51316 {ECO:0000313|EMBL:CDI86877.1};
RN [1] {ECO:0000313|EMBL:CDI86877.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDI86877.1};
RA Reid A.J., Blake D., Billington K., Browne H., Dunn M., Hung S.,
RA Kawahara F., Miranda-Saavedra D., Mourier T., Nagra H., Otto T.D.,
RA Rawlings N., Sanchez A., Sanders M., Subramaniam C., Tay Y., Dear P.,
RA Doerig C., Gruber A., Parkinson J., Shirley M., Wan K.L., Berriman M.,
RA Tomley F., Pain A.;
RT "Genomic analysis of the causative agents of coccidiosis in chickens.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDI86877.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDI86877.1};
RA Aslett M.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; HG696218; CDI86877.1; -; Genomic_DNA.
DR AlphaFoldDB; U6H4R4; -.
DR EnsemblProtists; CDI86877; CDI86877; EPH_0022340.
DR VEuPathDB; ToxoDB:EPH_0022340; -.
DR OrthoDB; 22780at2759; -.
DR GO; GO:0004020; F:adenylylsulfate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004781; F:sulfate adenylyltransferase (ATP) activity; 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; 3.40.50.620; HUPs; 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; IPR025980; ATP-Sase_PUA-like_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR024951; Sulfurylase_cat_dom.
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 Pfam; PF01747; ATP-sulfurylase; 1.
DR Pfam; PF14306; PUA_2; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000313|EMBL:CDI86877.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 24..168
FT /note="ATP-sulfurylase PUA-like"
FT /evidence="ECO:0000259|Pfam:PF14306"
FT DOMAIN 179..451
FT /note="Sulphate adenylyltransferase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01747"
FT REGION 277..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 657 AA; 73329 MW; AD725E97DFC8F017 CRC64;
MPSSADNAAP RKGAVSVAVA LPSDWTVNER QMCDLEMIIS GAFAPLQGFM GLSDYQSVLD
SMTLANGEVF SLPVVLAIPK SCCGDTAATN VYWMSSAQSV STNQGRMMLR DVVGTVIAQL
DVESVFLPDL EEEMQKVLGT TDYNHPYVKY LRDNHSDCYY VGGKISPVNP IVHFNFELYR
MTPAVCKQKI KARNYEVVVG FQTRNPLHRS HYELIKHALQ TAAGTEKKQP MLFLSPVIGP
TQPGDVPYYL RTRCYEHVIR YFEQDEECKF SHLCDTTAST PNRSPPRSQQ HSTGLSASGE
AATGEEDSSS NAMLVLIPLA MRMAGPRECV LHARIRKNYG CTHFIVGRDH AGPSTRKQDG
TPFYGPYDAH KLLGSVAEKL GIKPIFGEEM LYVGEEHGGY IPAGRLEEVK RQKPNVEVNS
ISGTEFRKRL TTRMPIPEWF SFPSVIDELQ QFYKQNHERG LCVYFTGLPC SGKSTLANAL
EAAILENRSE RRKVTLLDAD VVRQHLSKGL GFSREDRRKV GRNGYGRVGT NVRRIGYIAS
EITKHGGICI VANIAPYTCD REFNRKLIEQ EGGVYVEVYV CTPLSVCEER DIKHLYKKAR
QGIIKQFTGV SDPYEAPQHP ELTIDSSSDI KDKVAQVHQY LKDQGYVLEA PPLSKCC
//
