ID A0A0D1ZYP7_9PEZI Unreviewed; 439 AA.
AC A0A0D1ZYP7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=NEDD8-activating enzyme E1 catalytic subunit {ECO:0000256|ARBA:ARBA00015203, ECO:0000256|RuleBase:RU368009};
DE EC=6.2.1.64 {ECO:0000256|ARBA:ARBA00023624, ECO:0000256|RuleBase:RU368009};
GN ORFNames=PV09_08834 {ECO:0000313|EMBL:KIV99532.1};
OS Verruconis gallopava.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Venturiales; Sympoventuriaceae; Verruconis.
OX NCBI_TaxID=253628 {ECO:0000313|EMBL:KIV99532.1, ECO:0000313|Proteomes:UP000053259};
RN [1] {ECO:0000313|EMBL:KIV99532.1, ECO:0000313|Proteomes:UP000053259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 43764 {ECO:0000313|EMBL:KIV99532.1,
RC ECO:0000313|Proteomes:UP000053259};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Ochroconis gallopava CBS43764.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalytic subunit of the dimeric E1 enzyme, which activates
CC NEDD8. {ECO:0000256|RuleBase:RU368009}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + [NEDD8 protein] + [E1 NEDD8-activating enzyme]-L-
CC cysteine = AMP + diphosphate + [E1 NEDD8-activating enzyme]-S-[NEDD8
CC protein]-yl-L-cysteine.; EC=6.2.1.64;
CC Evidence={ECO:0000256|ARBA:ARBA00024626,
CC ECO:0000256|RuleBase:RU368009};
CC -!- PATHWAY: Protein modification; protein neddylation.
CC {ECO:0000256|ARBA:ARBA00005032, ECO:0000256|RuleBase:RU368009}.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family. UBA3
CC subfamily. {ECO:0000256|ARBA:ARBA00006310,
CC ECO:0000256|RuleBase:RU368009}.
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DR EMBL; KN847576; KIV99532.1; -; Genomic_DNA.
DR RefSeq; XP_016209402.1; XM_016362794.1.
DR AlphaFoldDB; A0A0D1ZYP7; -.
DR STRING; 253628.A0A0D1ZYP7; -.
DR GeneID; 27316807; -.
DR VEuPathDB; FungiDB:PV09_08834; -.
DR HOGENOM; CLU_013325_13_1_1; -.
DR InParanoid; A0A0D1ZYP7; -.
DR OrthoDB; 20494at2759; -.
DR UniPathway; UPA00885; -.
DR Proteomes; UP000053259; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019781; F:NEDD8 activating enzyme activity; IEA:UniProtKB-UniRule.
DR GO; GO:0045116; P:protein neddylation; IEA:UniProtKB-UniRule.
DR CDD; cd01488; Uba3_RUB; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 1.10.10.520; Ubiquitin activating enzymes (Uba3). Chain: B, domain 2; 1.
DR Gene3D; 3.10.290.20; Ubiquitin-like 2 activating enzyme e1b. Chain: B, domain 3; 1.
DR InterPro; IPR014929; E2-binding.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR023318; Ub_act_enz_dom_a_sf.
DR InterPro; IPR030468; Uba3_N.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR PANTHER; PTHR10953:SF6; NEDD8-ACTIVATING ENZYME E1 CATALYTIC SUBUNIT; 1.
DR PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR Pfam; PF08825; E2_bind; 1.
DR Pfam; PF00899; ThiF; 1.
DR SMART; SM01181; E2_bind; 1.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU368009};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU368009};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU368009};
KW Reference proteome {ECO:0000313|Proteomes:UP000053259};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU368009}.
FT DOMAIN 356..439
FT /note="E2 binding"
FT /evidence="ECO:0000259|SMART:SM01181"
SQ SEQUENCE 439 AA; 48733 MW; 9CD70D0E9E541A73 CRC64;
MAAAAVAGES ALISGVDGAR KRWKYLDNIL LRRGPFVDEE ATLGQGSVDM LSTQKVLVIG
AGGLGCEILK NLALSGFKDI HVIDMDTIDV SNLNRQFLFR QADVGRPKAE VAAEFVQKRV
KGVTITPYCG KIQDKDEDYY MQFNMVICGL DSIEARRWIN ATLVGMVDME NPESLKPLID
GGTEGFKGQA RVILPTMTSC IECQLDMHAP RAAVPLCTLA TIPRQPQHCI EWAHIIAWDE
ERKDMTLDTD DPEHITWLYQ KALKRAEEYN IQGVTYSMTQ GVVKNIIPAI ASTNAIIAAS
CCNEAFKLAT ATNPFLGTPG TNNYMMYTGD DSVYTYTFEH LKKDDCPVCG NLAKPLEVDA
NMTLGDLVDS FAERPEAQLK RPSVRSEAKT LYMQFPPGLE ESTRPNLKKK LSELVTNKEE
IIVTDPAFTT SFRFIVHFK
//
