ID A0A0M0J714_9EUKA Unreviewed; 1618 AA.
AC A0A0M0J714;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Ubiquitin-like 1-activating enzyme E1A {ECO:0000256|ARBA:ARBA00044354};
GN ORFNames=Ctob_005939 {ECO:0000313|EMBL:KOO22127.1};
OS Chrysochromulina tobinii.
OC Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Prymnesiales;
OC Chrysochromulinaceae; Chrysochromulina.
OX NCBI_TaxID=1460289 {ECO:0000313|EMBL:KOO22127.1, ECO:0000313|Proteomes:UP000037460};
RN [1] {ECO:0000313|Proteomes:UP000037460}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP291 {ECO:0000313|Proteomes:UP000037460};
RX PubMed=26397803; DOI=10.1371/journal.pgen.1005469;
RA Hovde B.T., Deodato C.R., Hunsperger H.M., Ryken S.A., Yost W., Jha R.K.,
RA Patterson J., Monnat R.J. Jr., Barlow S.B., Starkenburg S.R.,
RA Cattolico R.A.;
RT "Genome Sequence and Transcriptome Analyses of Chrysochromulina tobin:
RT Metabolic Tools for Enhanced Algal Fitness in the Prominent Order
RT Prymnesiales (Haptophyceae).";
RL PLoS Genet. 11:e1005469-e1005469(2015).
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:KOO22127.1}.
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DR EMBL; JWZX01003308; KOO22127.1; -; Genomic_DNA.
DR OrthoDB; 168734at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000037460; 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; 3.80.10.10; Ribonuclease Inhibitor; 2.
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; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_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; PF13516; LRR_6; 2.
DR Pfam; PF00899; ThiF; 2.
DR Pfam; PF10585; UBA_E1_SCCH; 1.
DR PRINTS; PR01849; UBIQUITINACT.
DR SMART; SM00368; LRR_RI; 4.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 2.
DR SUPFAM; SSF52047; RNI-like; 1.
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:UP000037460};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 153..557
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
FT DOMAIN 422..499
FT /note="Ubiquitin-activating enzyme E1 four-helix bundle"
FT /evidence="ECO:0000259|Pfam:PF16191"
FT DOMAIN 587..1097
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
FT DOMAIN 771..1047
FT /note="Ubiquitin-activating enzyme SCCH"
FT /evidence="ECO:0000259|Pfam:PF10585"
FT REGION 97..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 765
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 1618 AA; 176180 MW; E3E0EBDEC410138B CRC64;
MDRRFRANGK IDYLADPRLS KLTFASIQKH IEATCVSRGF PAVELKKKLF GCATKFALVS
VADEFNVELE TLLNELGPIK TFTPVMRSMN DVKYMEKHAA EKAERERSNA ASAPADVADT
SHAQSPPPRR KAAPANVTDL EGDLKFMDRN SRMIGAFGLD VIAKMVGMKV LIVGCKGIGI
EVAKNTVLAG VHTLTIFDPA PTSVRDLGTN FFLTEADVGK PRATVCAPRV AELNSNVLVQ
AAEGGELTEA LVAQHTIAVF TRGSRTELTR WNEFCRSQKH PISFLCCYGG GAWGGLFVDH
GDSFTIRDAT GRAPLIKLVK SIEVKEDHVL VRYDTPDGQP PEGLPDGGLV EFDEVKGLIS
AGAWAEAGNP SGGSLNNAGP VRTSHASEDP VKTFRISLPT DLSGPPTAWM GGGVITEKKE
ATTVHFRSFA ECVHKPGGVV MAGDGTQGFL MTDMTFSMVE LQLHVAQQGV FAFEEASGRL
PNINDAADAA QVVVLAKEFE AATGVLGGMG LEVDESITAR VAMHCRIELQ PMSAFWGGVV
AQELVKVAGK YTPIQQFLHL QSFAALPDTA PSAEDAAPLG CRYDDMIAVY GRAFQERLGE
LRVFMVGCGA LGCEFMKNFA LLGVCCGPTG SLVVTDNDRI EVSNLNRQFL FREDNVGKPK
SEAAAARALT MNPSLNIEAK QDLVATTTEH LFDSDFWNGL DLVCNALDNM KARLYVDAQC
IFYEKPLLES GTMGTGANVD IVVPHLTRSY ADGGAADEGG GVPMCTLRNF PHLIDHCIEW
ARAKFEDLFA DPAQKAAKVL EDVNSFVKKT RSETLQATDG RSSKISKEIP KLKKLISTLE
MGTKGPTMSD AVALAWAAFH ELFRDILLDL TEQFPDGSKD KKGEPFWSGH KRFPKAAHYD
ASNPEHVAFM LATSNLFAAM LGIPGKKPPS ELNQPGPMRW QAPYRSAEWL AGMLAKIGGP
PERVKGAVEI DGEEKKEGAD DMAREEAELE QLLKRIADMG AGAKGHFEPA DFEKDDDDNF
HIDFITACSN LRAANYHIPT TSRHKCKMIA GRIIPAIATT TASVTGLVML EMLKVLQNKP
TAQLRNGNYD LGSNQYMLFE AEPPAQLATK VMASACMCWP AIASDCLPHQ VEITMPDPKD
HPDAYDAKGN LVDMYKDPDM MLGFAERVRC YPDPHTKYDK MWVGPVAPTA TVQQLREAID
ACFAEAGLKA AMINGPTQRI ECEKDEHNAS GIKAGSRSLW NPLLSSTRAN LEKPWGPLLK
ELTTRDEIKW QTVDDPVDVS GKRLCTDLTI QLQNDDGDDV KTPTIIIKLA PFEFVSYKER
KAREVTPWLE SFAKKGKLCF LCTDTAEREF NAEDAKVLAD AMIAQGPCEV EYIFFQNSKI
GDQGLEAVAK AMAAGATPKL LTMDLSNILA TDAGFMHLIG AIKHCPNLRD LVFKQNSLTD
AAFSALHEVI KRGEWPAMER LNLAGTQSER HTISDASFVP FGHDLADGVI KTTRLEEIEL
SDTDISDAGL ASIALAIQRG HLRKLRSLYM QACRITDEGA RALADALRAN KRTQLFDIRL
GYQNSHDAMA PRVTPEGGKA AIEAAGESLG RRVFCVLDAL EEHSSREVQE SHGPGVNG
//
