ID A0A085M584_9BILA Unreviewed; 1168 AA.
AC A0A085M584;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=SUMO-activating enzyme subunit 1 {ECO:0000256|ARBA:ARBA00044187};
DE AltName: Full=Ubiquitin-like 1-activating enzyme E1A {ECO:0000256|ARBA:ARBA00044354};
GN ORFNames=M513_06761 {ECO:0000313|EMBL:KFD52380.1}, M514_06761
GN {ECO:0000313|EMBL:KFD69961.1};
OS Trichuris suis (pig whipworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichuridae; Trichuris.
OX NCBI_TaxID=68888 {ECO:0000313|EMBL:KFD52380.1, ECO:0000313|Proteomes:UP000030764};
RN [1] {ECO:0000313|EMBL:KFD52380.1, ECO:0000313|Proteomes:UP000030764}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DCEP-RM93F {ECO:0000313|EMBL:KFD69961.1}, and DCEP-RM93M
RC {ECO:0000313|EMBL:KFD52380.1};
RX PubMed=24929829; DOI=10.1038/ng.3012;
RA Jex A.R., Nejsum P., Schwarz E.M., Hu L., Young N.D., Hall R.S.,
RA Korhonen P.K., Liao S., Thamsborg S., Xia J., Xu P., Wang S.,
RA Scheerlinck J.P., Hofmann A., Sternberg P.W., Wang J., Gasser R.B.;
RT "Genome and transcriptome of the porcine whipworm Trichuris suis.";
RL Nat. Genet. 46:701-706(2014).
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC {ECO:0000256|ARBA:ARBA00004718}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBUNIT: Heterodimer of SAE1 and UBA2/SAE2. The heterodimer corresponds
CC to the two domains that are encoded on a single polypeptide chain in
CC ubiquitin-activating enzyme E1. Interacts with UBE2I.
CC {ECO:0000256|ARBA:ARBA00026003}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC {ECO:0000256|ARBA:ARBA00005673, ECO:0000256|RuleBase:RU000519}.
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DR EMBL; KL363228; KFD52380.1; -; Genomic_DNA.
DR EMBL; KL367491; KFD69961.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A085M584; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000030758; Unassembled WGS sequence.
DR Proteomes; UP000030764; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd01490; Ube1_repeat2; 1.
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 Gene3D; 3.10.290.60; Ubiquitin-activating enzyme E1, UFD domain; 1.
DR InterPro; IPR032420; E1_4HB.
DR InterPro; IPR032418; E1_FCCH.
DR InterPro; IPR042302; E1_FCCH_sf.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR018965; Ub-activating_enz_E1_C.
DR InterPro; IPR042449; Ub-E1_IAD_1.
DR InterPro; IPR038252; UBA_E1_C_sf.
DR InterPro; IPR019572; UBA_E1_SCCH.
DR InterPro; IPR042063; Ubi_acti_E1_SCCH.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR InterPro; IPR018075; UBQ-activ_enz_E1.
DR InterPro; IPR033127; UBQ-activ_enz_E1_Cys_AS.
DR InterPro; IPR000011; UBQ/SUMO-activ_enz_E1-like.
DR NCBIfam; TIGR01408; Ube1; 1.
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; PF16190; E1_FCCH; 1.
DR Pfam; PF09358; E1_UFD; 1.
DR Pfam; PF00899; ThiF; 2.
DR Pfam; PF10585; UBA_E1_SCCH; 1.
DR PRINTS; PR01849; UBIQUITINACT.
DR SMART; SM00985; UBA_e1_C; 1.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 2.
DR PROSITE; PS00865; UBIQUITIN_ACTIVAT_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU000519};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU000519};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU000519};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 1033..1158
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT ACT_SITE 738
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 1168 AA; 131484 MW; 58623BDFC6B57BF2 CRC64;
MLIPMKSAFL KRTPWWERHF NAHYWSPCKR VLVTHFVTTG RHLCSKARFS ARVTIGVVCP
SFGLVVPLRM ATSMSVINNG TSSLSKREAS PLTGCAYSTK RAKADIVDHT ASEDLAEGQS
PPLREMNAST FGFAPGQTIN GDVRNGAASA QGSFDPQLYS RQIYVLGEQA MRRLRISSAL
ISGIGGAGVE IAKNLILGGV RQVTIHDCKN AQWRDLSAQY YLDESSIGKN RAVQSLGLLE
ELNDSVTVNY SIRPLSEDII REHDLIIVTE MSFDEQCKVN EMTRREGKKF MSVDCRGLFG
YVFNDFGPNH VINDSNGEPC TEVLLEHIDR ATGEVTTLES AKHGLEDGDY VVFSEVKGMV
ELNNCEPKKV RVIKPFKFAV DGLSNFSEYV EGGKAKQVKV PTKMEFKPLN ESIREPEFLI
SDFGKMDRPN QMHLMWQALY KFCHAHGRMP RVQNLADAEQ IVSIVEELNA SASDSLRVEK
VDARLAKLLS FQALGNLAPI TGFIGGLAAQ EAMKALTSIF TPAKQWFYFD AIECLSEPGH
PYGLRDERSC AARQNRYDGQ TAVFGHDFQE ALAKQKWFIV GAGAIGCELL KYFSMMGVAS
SQKGCLYVTD MDTIEVSNLN RQFLFRKHDV GKKKSDVAVG AAKEFNPSLN LKSMCERVCG
ETENIFDDDF FENLNGVANA LDNVEARTYM DRRCVYYRLP LLESGTQGPK GNVQVVYPHL
TESYSSSQDP PERSIPICTL KNFPNAIEHT IQWARDLFEG AFTNPAEMAN QFLEDPRAFF
ERVKKMHAGQ MIEMLDNVYR VLSVERPETA EDCVVWARNY WEKCFNYSIR QLLHNFPPDQ
TTSLGAKFWS GSKRCPHPLQ FDVANTEHLR FVFAAAYLRS LMYGLKPVED MSSVADIAKR
VSVPTFEPKA GVKIAVTEEE ATRMNNEDGD EQQFQELHLL LAKLKPEKSK RLFPIDFEKD
DDSNHHMEFI TTASNLRAEN YDIEKADLLK TKQIAGRIIP AIATTTAAVA GLACLEFYKV
VLAAANDPVL ERFKNSFINL ALPYFGFAEP VKAAVKKYYD TPWTLWDRFE IQGDITLQQL
VDYMKEKHQL EVTMLSQGVT MLFSFFLTPA KQKERMGMKI SELVQMISNR PIPEGVKAIV
LELMCTDEQG EDVEVPYVKY YLPSMEQC
//
