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Database: UniProt
Entry: A0A0N4W602_HAEPC
LinkDB: A0A0N4W602_HAEPC
Original site: A0A0N4W602_HAEPC 
ID   A0A0N4W602_HAEPC        Unreviewed;       611 AA.
AC   A0A0N4W602;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 2.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=APS kinase {ECO:0000313|WBParaSite:HPLM_0000543901-mRNA-1};
GN   ORFNames=HPLM_LOCUS5431 {ECO:0000313|EMBL:VDO25979.1};
OS   Haemonchus placei (Barber's pole worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Trichostrongylidae; Haemonchus.
OX   NCBI_TaxID=6290 {ECO:0000313|Proteomes:UP000038042, ECO:0000313|WBParaSite:HPLM_0000543901-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:HPLM_0000543901-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (APR-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDO25979.1, ECO:0000313|Proteomes:UP000268014}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHpl1 {ECO:0000313|EMBL:VDO25979.1,
RC   ECO:0000313|Proteomes:UP000268014};
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Sulfur metabolism; sulfate assimilation.
CC       {ECO:0000256|ARBA:ARBA00005050}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the sulfate
CC       adenylyltransferase family. {ECO:0000256|ARBA:ARBA00009290}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the APS kinase
CC       family. {ECO:0000256|ARBA:ARBA00007268}.
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DR   EMBL; UZAF01016337; VDO25979.1; -; Genomic_DNA.
DR   STRING; 6290.A0A0N4W602; -.
DR   WBParaSite; HPLM_0000543901-mRNA-1; HPLM_0000543901-mRNA-1; HPLM_0000543901.
DR   OMA; TENCTPE; -.
DR   UniPathway; UPA00097; -.
DR   Proteomes; UP000038042; Unplaced.
DR   Proteomes; UP000268014; Unassembled WGS sequence.
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:UniProtKB-EC.
DR   GO; GO:0000103; P:sulfate assimilation; IEA:UniProtKB-UniPathway.
DR   CDD; cd02027; APSK; 1.
DR   CDD; cd00517; ATPS; 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   HAMAP; MF_00065; Adenylyl_sulf_kinase; 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   InterPro; IPR002650; Sulphate_adenylyltransferase.
DR   NCBIfam; TIGR00455; apsK; 1.
DR   PANTHER; PTHR11055; BIFUNCTIONAL 3'-PHOSPHOADENOSINE 5'-PHOSPHOSULFATE SYNTHASE; 1.
DR   PANTHER; PTHR11055:SF1; PAPS SYNTHETASE, ISOFORM D; 1.
DR   Pfam; PF01583; APS_kinase; 1.
DR   Pfam; PF01747; ATP-sulfurylase; 1.
DR   Pfam; PF14306; PUA_2; 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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Reference proteome {ECO:0000313|Proteomes:UP000268014};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          199..374
FT                   /note="ATP-sulfurylase PUA-like"
FT                   /evidence="ECO:0000259|Pfam:PF14306"
FT   DOMAIN          383..603
FT                   /note="Sulphate adenylyltransferase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01747"
SQ   SEQUENCE   611 AA;  68324 MW;  2CC829D4CB6EE5B7 CRC64;
     YSTGATNVTY QQHKTGREER AAVLGKHDGF RGCTIWFTGL SGAGKTTIAF AVEKILTQMG
     IPCCGLDGDN VRHGLCKNLG FSKEERSENI RRVAEVSKLF ADQGLVCLAS FISPFRVDRE
     EARRIHEKVR FFEVYVSTSL QECEKRDPKK LYSKARAGEI SGFTGIDSAY EPPEDAELAY
     LFDVFLIVAF QAMRQLSGPP LRELFVESEE EKLALLEAAK NMPTIELGPV EVQWLQVLSE
     GWATPLPGFM RERQYLQALH FGQLLDLKKK TVFPGEKDDG AEDPWPMDEP VNQSVPIVLP
     ITDDFIGDKV SPSVALTRHG VVLAVLNDGE IFAHRREERV ARQFAFSDPR HPAVEQVLSS
     GPWCLGGDLK VLERITFDDG LNSFRKTPSE LRKIFEEKGA DAVFVFQLRN PIHNGHALLM
     RDTREKLLKK YRNPMLLLHP LGGWTKDDDV PLSVRMRQHE AVIAEGVLDP SWTVLSIFPS
     PMLYAGPTEV QWHARARIAA GVHTYIVGRD PAGIQHPDTG DFLYEPTHGA KVLSMAPGLS
     QLHILPFRVA AYDKKAGKMA FFDPSRKEDF DFISGTRMRG LARSGATPPD GFMAPSAWQI
     LADYYKSIAK K
//
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