ID A0A016SU59_9BILA Unreviewed; 1051 AA.
AC A0A016SU59;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
GN Name=Acey_s0173.g391 {ECO:0000313|EMBL:EYB94263.1};
GN Synonyms=Acey-uba-1 {ECO:0000313|EMBL:EYB94263.1};
GN ORFNames=Y032_0173g391 {ECO:0000313|EMBL:EYB94263.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYB94263.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine
CC = AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-
CC L-cysteine.; EC=6.2.1.45; Evidence={ECO:0000256|ARBA:ARBA00000488};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC {ECO:0000256|ARBA:ARBA00005673, ECO:0000256|RuleBase:RU000519}.
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:EYB94263.1}.
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DR EMBL; JARK01001509; EYB94263.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016SU59; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000024635; 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; cd01491; Ube1_repeat1; 1.
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:SF4; UBA_E1_C DOMAIN-CONTAINING PROTEIN; 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 Reference proteome {ECO:0000313|Proteomes:UP000024635};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 921..1047
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT ACT_SITE 623
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 1051 AA; 117552 MW; F3E71D5652F734A3 CRC64;
MYRAFLMFLS QESAITLKNS SANSDSKRMT AAKNGQEAMD TDAAGLDTNL YSRQIYALGE
SAMINLRKAS VLISGLGGVG VEIAKNLILG GVRSVTLHDT KNARWIDLSA QYYLTEEDIG
KNRAAASFER LAELNDSVNC QLVVDQLTED FVKQFDLVVL TDAPRSEQLK VAGWTRAHNR
CLLVADARGL YSYIFADFSN SFRVDDPNGE QIKEFLIEYI DAETGDVTTL ENQMHGLEDG
DHVTFSEVKG MTQLNGCSPI KVTVKKPHVF NIGDAAKNLS PYEEGGRVKQ VKVPTTVSHK
ALADSLAEPE FVYWDFAKFD YPSQLHLLWN ALYKFEAKHG RHPNPRSDSD VQLLKAELPS
GAEVDEKLLK RFSYQASGNL VTIASVVGGI AAQEAMKAVT HHMTPLKQWL YLDSDDALPG
DWSEFDNAKL TEEDCKPRGC RYDGQAAVFG WKYQNALFNQ KWFVVGAGAI GCELLKNLAM
MGVACGEGGL IKITDMDQIE ISNLNRQFLF RMNDVGSKKS TVAGRAVKVF NKDVRIQALS
ERVGADTEHI FNDDFFAELD GVANALDNID ARRYMDRRCV FYRLPLLESG TMGTKGNTQV
VYPYLTESYG SSVDPPEKDI PICTLKNFPN EIQHTIQWAR DLFEGLFTGP AETANQFLSD
ERSFLERLEQ MNVSQRTQLL SQVKDVLIDS KPSNAEDCVK WARLLFQEHY HDNIAQMLHS
FPPDQVTDQG AKFWSGTKRC PHVLEFDPTQ EEHRNFVYAA SILRAQIYGI KPILDVDLVM
KIASSVQPPP FKPRAGVKIA VTEAEAKENA ESEDANADGV LEQLKVKLAR LNTKSIQKLN
PIDFEKDDDT NHHMEMITAA SNLRAENYSI QPADRMKTKQ IAGRIIPAIA TTTATVAGLV
CIELYKMVGS NGLPKTPMTR FKNGFINLAL PFFGFSEPIA APVKKYNETS FTLWDRLEIK
GPKTLQEAVD WIQNETGLEV TMLSSGVSLI YSFFMDAKKR AHRMPMDVKA VVEDVSKREV
PRHQRSLVLE VMATDPNTDE DVEVPYIRYV L
//
