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Database: UniProt
Entry: A0A1I8H3P3_9PLAT
LinkDB: A0A1I8H3P3_9PLAT
Original site: A0A1I8H3P3_9PLAT 
ID   A0A1I8H3P3_9PLAT        Unreviewed;      1086 AA.
AC   A0A1I8H3P3;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=ThiF domain-containing protein {ECO:0000313|WBParaSite:maker-uti_cns_0004299-snap-gene-0.10-mRNA-1};
OS   Macrostomum lignano.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC   Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX   NCBI_TaxID=282301 {ECO:0000313|Proteomes:UP000095280, ECO:0000313|WBParaSite:maker-uti_cns_0004299-snap-gene-0.10-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:maker-uti_cns_0004299-snap-gene-0.10-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2016) to UniProtKB.
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DR   AlphaFoldDB; A0A1I8H3P3; -.
DR   WBParaSite; maker-uti_cns_0004299-snap-gene-0.10-mRNA-1; maker-uti_cns_0004299-snap-gene-0.10-mRNA-1; maker-uti_cns_0004299-snap-gene-0.10.
DR   Proteomes; UP000095280; Unplaced.
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; 3.
DR   InterPro; IPR045886; ThiF/MoeB/HesA.
DR   InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR   InterPro; IPR035985; Ubiquitin-activating_enz.
DR   PANTHER; PTHR10953:SF29; NEDD8-ACTIVATING ENZYME E1 REGULATORY SUBUNIT; 1.
DR   PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR   Pfam; PF00899; ThiF; 1.
DR   SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 2.
PE   4: Predicted;
FT   DOMAIN          545..697
FT                   /note="THIF-type NAD/FAD binding fold"
FT                   /evidence="ECO:0000259|Pfam:PF00899"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          502..545
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        505..534
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1086 AA;  121806 MW;  61D5257850C1512F CRC64;
     NVLNKQQQQQ QQEQHQQSPS WSVAQSVANP KAKKYDRQLR LWGDHGQQAI EQARVLLIGA
     NAVGTETLKN MEDCGSNFFV ELARIGEPRA KVCAELLREL NEDVIGDFLE DRLDVLLQRD
     PGFFTGFSLV IASGVRHSDL LVLSDLLYDR DVPLIVCQQH GMLATCQLVA REHFVWEAHP
     DNPLPDLRLE NPLPEFVAFC DAQDLSAMDS QRHSHTPWLV ILYKFLSKWR QANAGKFPSN
     YAERQAVRQL IRSGERGESD LHGDEENWRQ AQSAVTTALL PSKLPSNVNE LFKLADQFWL
     RRQQLSDSSA PSEDRQAAVP PSNWLLLCRT LAEFYRQRGC LPLCGTLPDM VSDSDRYVAL
     LNIYRRAADA DLVEFSRLLR VVCLDIGLSA DSVPASQIAL FCKNARHLRL VKTASYREPA
     TAATVARCLE ETAEAGPTCC PRLRPVPHRI RSLPRRHRRC EFSGRRWPVE AEMPTASSGL
     AGSLATTSAA CPIGARGSAA RAVQIRSSRE MSSTNNNNNN NKSNINSHPV GRSRSQLPTP
     KAKKYDRQLR LWGDHGQQAI EQARVLLIGA NAVGTETLKN MVLPGVGSFT IMDHRRVTEE
     DCGSNFFVEL ARIGEPRAKV CAELLRELNE DVIGDFLEDR LDVLLQRDPG FFTGFSLVIA
     SGVRHSDLLV LSDLLYDRDV PLIVCQQHGM LATCQLVARE HFVWEAHPDN PLPDLRLENP
     LPEFVAFCDA QDLSAMDSQR HSHTPWLVIL YKFLSKWRQA NAGKFPSNYA ERQAVRQLIR
     SGERGESDLH GDEENWRQAQ SAVTTALLPS KLPSNVNELF KLADQFWLRR QQLSDSSAPS
     EDRQAAVPPS NWLLLCRTLA EFYRQRGCLP LCGTLPDMVS DSDRYVALLN IYRRAADADL
     VEFSRLLRVV CLDIGLSADS VPASQIALFC KNARHLRLVK TASYRELSRP LPQTVARCLE
     ETAEAGPSPF WWYLLFHACD RFHTEFGRFP GDTDDVNFLA DAGQLKLKCQ QLAQDWLASL
     ATTSAACPTS APEDLLHELC RFGRAEVHSV AAWMGGEGIK LITGQFVPET RTMLYDAVSQ
     TFLPVF
//
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