ID A0A1D3D816_9EIME Unreviewed; 1622 AA.
AC A0A1D3D816;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Ubiquitin-activating enzyme {ECO:0000313|EMBL:OEH79587.1};
GN ORFNames=cyc_09102 {ECO:0000313|EMBL:OEH79587.1};
OS Cyclospora cayetanensis.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Cyclospora.
OX NCBI_TaxID=88456 {ECO:0000313|EMBL:OEH79587.1, ECO:0000313|Proteomes:UP000095192};
RN [1] {ECO:0000313|EMBL:OEH79587.1, ECO:0000313|Proteomes:UP000095192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHN_HEN01 {ECO:0000313|EMBL:OEH79587.1,
RC ECO:0000313|Proteomes:UP000095192};
RX PubMed=27129308; DOI=10.1186/s12864-016-2632-3;
RA Liu S., Wang L., Zheng H., Xu Z., Roellig D.M., Li N., Frace M.A., Tang K.,
RA Arrowood M.J., Moss D.M., Zhang L., Feng Y., Xiao L.;
RT "Comparative genomics reveals Cyclospora cayetanensis possesses coccidia-
RT like metabolism and invasion components but unique surface antigens.";
RL BMC Genomics 17:316-316(2016).
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:OEH79587.1}.
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DR EMBL; JROU02000343; OEH79587.1; -; Genomic_DNA.
DR VEuPathDB; ToxoDB:cyc_09102; -.
DR VEuPathDB; ToxoDB:LOC34624595; -.
DR InParanoid; A0A1D3D816; -.
DR Proteomes; UP000095192; Unassembled WGS sequence.
DR GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR Gene3D; 1.10.10.2660; Ubiquitin-activating enzyme E1, SCCH domain; 1.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR042063; Ubi_acti_E1_SCCH.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR PANTHER; PTHR10953:SF162; SUMO-ACTIVATING ENZYME SUBUNIT 1; 1.
DR PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR Pfam; PF00899; ThiF; 2.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 4.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000095192};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1622
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008914228"
FT DOMAIN 803..840
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
FT DOMAIN 926..1416
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
FT REGION 101..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 294..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 845..871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1106..1148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1186..1219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1131..1148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1202..1219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1622 AA; 170579 MW; D569FE74D6E4CC64 CRC64;
MYRPQGDTWM SDTTMLILPL LLGVLQARGL IRSLAGGSGS ESTLGCPASQ DHLKVHLRPS
QSCSILSNAP WYLQAQKILK FHGWKCGEDF LEGQELQYRH GAREGDREFR GPNSSLKRRK
RGASGEQAEG LVRISMLSLE GAPSEIAAEA AADASTGRGR AKCAAIEYLE GFKGGVGYLR
RTGGIMEGRR RSRVVAADSA VISVCFAVFL LVGGCCRLRK RRHCEPAHTR ASTRGPTAVV
VTPRSMRSCL APALPPPPLE GGQKTPPGEA GESAERLAPA ATAALRAIID RSHDVRPVQA
GEGGPSRGIS REPLGAATSS ADVVACCPTS EDSGTLATQG GGEEDLSLRS FLSRQLLVWG
PEQQALLPDS CVLLIGAGGA AVEAAKCLLQ SGVGRVLLAD PEPPSPAERA ANFAVAEHSA
AACEKQSAAL PLDADATAAS SQCSEEPAIQ LAKHPELPRE PLKGQLPPKR DTLTRAAVAC
GALRRVAAPY ARVSEVSLQQ QAGEAAPAWR MRVLQLLEQV DVLLLCDRPL QQKLFFASLA
RELRISKRRL PQGSLDRQQR SAGPLVVAVC TAGLTGRIAV DFGDFCFSGV NEEAALAALL
QKHAQSQEQQ REQLQKPHAA EATSVSFPPL SEALSLQGEG LCASQQSERA VIGEEQQCLT
AAFEALDAEE AGTLPENNDA ERVSDGIGAQ AALDLESPEA PSDVGSLRSW NASRAAKAGE
LAVLMAKGSR GHLAPIAAAM GAFAAQETLK GLTRRYPPLQ RPFPTEGFAE HGAPADSPVA
SAGADDAAID ATVLPSPWAG QQQLLGEELQ RHLNHMRVLL VGAGAIGCEV LKNFALMGIS
TQCPGRKTGT RDSNSTARSH SCNSRCSATS SSSARGGLIA ALRKAYRDLR RRRELSGSEA
AARASGTSAA AAGGLCEAKH CPGGLLSVMD GDVVEVSNLS RQVLFSFSSL QQPKASAAAA
AAARLSSCMQ LQAFPLMLTP ETLRKLPSMF FQQQDLIVAA LDSVEARLYV DALCLLHARP
WVEAGTLGLR GHSQSLVPHL TEPYGAAAAT AGAPSLAAVP LCSVRGTPTA PLHAVHWASA
VLHQTFRGDL AAAHLLLQQL VEQHTHPSVD RPEGVSALDG PPFAASPDAS EASSDALQHP
KWQQGQSQQH RCRLGAGVVP LSPAHLLLVS WALSLFDVLF DNGGQQQGDL HGSPSTVEDA
WGAREASSSQ KQQPLSADPT DTDVLDFIAA AGQLLATALH LEQAALPGGV AASASAEAAA
AALRQQQAEE LLLRGGGVGP WSRQSVSNAL KQLLQARHER TAGATVGTTL ASGKAARGIA
DLYSAAEALT RAVSAAAKRP DSPPLRPPGL PSLSADEAVP LRFLTAAARL RCRAFGLSPL
PDPEETQQLL GRIVPATATA TTLAAALACL EVYRLAALRL AGSHGMPFLA EAPPLRPPTL
RFRGGRWGGQ PLSPWNFFRL RLRGSTEEST RSNVSNGVDV GAVVGETEAA SALTIAELVR
LIETDAGVRV QSLTCEDTLL YSALEEGSAL KQHYGTLTPQ IAELFDTQPQ PQLLPLPDPK
TLLSEALQQV ISMKGRSKGQ QEQNRQKQQE KEQLVWAVVV ISALDSAGAD APLPPLKALI
KA
//
