ID A0A0C2H424_9BILA Unreviewed; 316 AA.
AC A0A0C2H424;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
DE Flags: Fragment;
GN ORFNames=ANCDUO_05524 {ECO:0000313|EMBL:KIH64166.1};
OS Ancylostoma duodenale.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=51022 {ECO:0000313|EMBL:KIH64166.1, ECO:0000313|Proteomes:UP000054047};
RN [1] {ECO:0000313|EMBL:KIH64166.1, ECO:0000313|Proteomes:UP000054047}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zhejiang {ECO:0000313|EMBL:KIH64166.1,
RC ECO:0000313|Proteomes:UP000054047};
RA Mitreva M.;
RT "Draft genome of the parsitic nematode Ancylostoma duodenale.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; KN728204; KIH64166.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C2H424; -.
DR Proteomes; UP000054047; Unassembled WGS sequence.
DR GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR Gene3D; 1.10.10.2660; Ubiquitin-activating enzyme E1, SCCH domain; 2.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
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 PANTHER; PTHR10953:SF4; UBA_E1_C DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR Pfam; PF10585; UBA_E1_SCCH; 2.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
DR PROSITE; PS00865; UBIQUITIN_ACTIVAT_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000054047};
KW Signal {ECO:0000256|SAM:SignalP};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..316
FT /note="E1 ubiquitin-activating enzyme"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002149531"
FT DOMAIN 35..86
FT /note="Ubiquitin-activating enzyme SCCH"
FT /evidence="ECO:0000259|Pfam:PF10585"
FT DOMAIN 88..260
FT /note="Ubiquitin-activating enzyme SCCH"
FT /evidence="ECO:0000259|Pfam:PF10585"
FT ACT_SITE 29
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KIH64166.1"
SQ SEQUENCE 316 AA; 35929 MW; DEF62D3E9A85D426 CRC64;
FFVICIILTI IIHHYRSSVD PPEKDIPICT LKNFPNEIQH TIQWARDLFE GLFTGPAETA
NQFLSDERSF LERLEQMNVS QRTQLLSQEH YHDNIAQMLH SFPPDQVTDQ GAKFWSGTKR
CPHVLEFDPS QEEHRNFVYA ASILRAQIYG LKPILDVDLV MKIASSVQPP PFKPRAGVKI
AVTEAEAKEN AESEDANADG VLEQLKVKLA RLNTKSIQKL NPIDFEKDDD TNHHMEMITA
ASNLRAENYS IQPADRMKTK QIAGRIIPAI ATTTATVAGL VCIELYKYNE TSFTLWDRLE
IKGPKTLQEA VDWIQE
//
