ID F9WCF5_TRYCI Unreviewed; 1099 AA.
AC F9WCF5;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Ubiquitin-like 1-activating enzyme E1A {ECO:0000256|ARBA:ARBA00044354};
GN ORFNames=TCIL3000_0_55160 {ECO:0000313|EMBL:CCD14948.1};
OS Trypanosoma congolense (strain IL3000).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Nannomonas.
OX NCBI_TaxID=1068625 {ECO:0000313|EMBL:CCD14948.1, ECO:0000313|Proteomes:UP000000702};
RN [1] {ECO:0000313|Proteomes:UP000000702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL3000 {ECO:0000313|Proteomes:UP000000702};
RA Jackson A.P., Berry A., Allison H.C., Burton P., Anderson J., Aslett M.,
RA Brown R., Corton N., Harris D., Hauser H., Gamble J., Gilderthorp R.,
RA McQuillan J., Quail M.A., Sanders M., Van Tonder A., Ginger M.L.,
RA Donelson J.E., Field M.C., Barry J.D., Berriman M., Hertz-Fowler C.;
RT "Divergent evolution of antigenic variation in African trypanosomes.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CCD14948.1, ECO:0000313|Proteomes:UP000000702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL3000 {ECO:0000313|EMBL:CCD14948.1,
RC ECO:0000313|Proteomes:UP000000702};
RX PubMed=22331916; DOI=10.1073/pnas.1117313109;
RA Jackson A.P., Berry A., Aslett M., Allison H.C., Burton P.,
RA Vavrova-Anderson J., Brown R., Browne H., Corton N., Hauser H., Gamble J.,
RA Gilderthorp R., Marcello L., McQuillan J., Otto T.D., Quail M.A.,
RA Sanders M.J., van Tonder A., Ginger M.L., Field M.C., Barry J.D.,
RA Hertz-Fowler C., Berriman M.;
RT "Antigenic diversity is generated by distinct evolutionary mechanisms in
RT African trypanosome species.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:3416-3421(2012).
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC {ECO:0000256|ARBA:ARBA00004718}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC {ECO:0000256|ARBA:ARBA00005673}.
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:CCD14948.1}.
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DR EMBL; CAEQ01001715; CCD14948.1; -; Genomic_DNA.
DR AlphaFoldDB; F9WCF5; -.
DR VEuPathDB; TriTrypDB:TcIL3000_0_55160; -.
DR OMA; FWSGHRK; -.
DR OrthoDB; 168734at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000000702; Unassembled WGS sequence.
DR GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 2.40.30.180; Ubiquitin-activating enzyme E1, FCCH domain; 1.
DR Gene3D; 3.50.50.80; Ubiquitin-activating enzyme E1, inactive adenylation domain, subdomain 1; 1.
DR Gene3D; 3.40.50.12550; Ubiquitin-activating enzyme E1, inactive adenylation domain, subdomain 2; 1.
DR Gene3D; 1.10.10.2660; Ubiquitin-activating enzyme E1, SCCH domain; 1.
DR InterPro; IPR032420; E1_4HB.
DR InterPro; IPR042302; E1_FCCH_sf.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR042449; Ub-E1_IAD_1.
DR InterPro; IPR019572; UBA_E1_SCCH.
DR InterPro; IPR042063; Ubi_acti_E1_SCCH.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR InterPro; IPR033127; UBQ-activ_enz_E1_Cys_AS.
DR InterPro; IPR000011; UBQ/SUMO-activ_enz_E1-like.
DR PANTHER; PTHR10953:SF162; SUMO-ACTIVATING ENZYME SUBUNIT 1; 1.
DR PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR Pfam; PF16191; E1_4HB; 1.
DR Pfam; PF00899; ThiF; 2.
DR Pfam; PF10585; UBA_E1_SCCH; 1.
DR PRINTS; PR01849; UBIQUITINACT.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 2.
DR PROSITE; PS00865; UBIQUITIN_ACTIVAT_2; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000000702};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 28..447
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
FT DOMAIN 296..364
FT /note="Ubiquitin-activating enzyme E1 four-helix bundle"
FT /evidence="ECO:0000259|Pfam:PF16191"
FT DOMAIN 485..999
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
FT DOMAIN 669..956
FT /note="Ubiquitin-activating enzyme SCCH"
FT /evidence="ECO:0000259|Pfam:PF10585"
FT REGION 871..893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 663
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 1099 AA; 122392 MW; 245A07CDCC658CEE CRC64;
MVNQGDVSVA KGTASAIDSR FLDQQSRTIG TYGLETMAKL ISFKVLIVGC GGVGIETAKN
LALAGVHTII LCDPKKCEEK DMGVNFAITH SSLSARLSRA EASQRLVAEL NPNVRVRTVD
ALSETVVSEV HSVVFTSAAA DWSSKTLLKW DQFCRSKTPS ISFIFAYQGG SLASIFADHA
PNFTVKDLDG RPMLQKLITE VVTKKDKSGS EYTRIRYETP EGQTPGALRD YTEVKFSEVK
GMCKSNGESI NGKIFKGVVC TGDPHNTVRI YPSLQSQGYS AYETSGFIHE MKENCQLQFR
GFSEALLRPG QFVAVSPMMD NSEESQSHIA FNALLRFFDK HGRLPQLHDG TEAEEVVSFA
KAVNAENKAA GAALKQEDGP MFIQHENKEF PSRIAPPPPP KPLFVETLDE DFVRTQALVA
AAELQPLCAV WGAVLAQEIV KITGKYTPIC QWFHISYPSI LARSELYTKS LHEYKVGDHR
YHHLVSMFGK TFVDRLNNLK MFMAGCGALG CENIKNFALC GITCGPRGSF VVTDNDRIEV
SNLSRQFLFR EENVGQPKSS VAVSRMKSIN ADARADARQD YIGTATEHIY HDNFWSELDV
VVNALDNMET RLYIDQKCVN FHKILVEAGT MGTGGNVDIV VPGKTTSYSD GGAADSTGGI
PMCTLRNFPY TSDHCTEWAR AQFDDLFVSP MQTVRQLLEN PQAFTERIKN EINNAQSAGE
RLSLVEKNLG ILQGVQKTMS VLTAGVTLEK CVQCAWETMF HLFRDRILDL QRSFPKDAKK
KNGEKFWSGH RKYPTPLEVK MQSITSDPDV ANFLISASNL FACMYGVHPQ KHEPRFNDPK
NRWMEQYRSL DWLNKIMKNY AMPAYKPGAV EGLDDDTRQS MEKHEEAPDQ RSREETLNTL
LANVVAAAQK CSNMKTMPLD FEKDDDDNFH IDFVAATSNL RARNYDIATQ ERFKVKLVAG
KIIPAIATTT AAVTGLALIE YFKALQGNDV SCLRNGMIDI GTNNYVLFER DAPLKHRTRV
EKTYLPEQDY TYKKKIICLP EGYTKYDMIE IPVNKRTTVQ EFATELMSKV NSLLPAGGSN
PCEVSAIGVG KGDFMERIA
//
