ID M2V6D4_COCH5 Unreviewed; 1030 AA.
AC M2V6D4;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
GN ORFNames=COCHEDRAFT_1165813 {ECO:0000313|EMBL:EMD95582.1};
OS Cochliobolus heterostrophus (strain C5 / ATCC 48332 / race O) (Southern
OS corn leaf blight fungus) (Bipolaris maydis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=701091 {ECO:0000313|EMBL:EMD95582.1, ECO:0000313|Proteomes:UP000016936};
RN [1] {ECO:0000313|EMBL:EMD95582.1, ECO:0000313|Proteomes:UP000016936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C5 / ATCC 48332 / race O {ECO:0000313|Proteomes:UP000016936};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
RN [2] {ECO:0000313|Proteomes:UP000016936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C5 / ATCC 48332 / race O {ECO:0000313|Proteomes:UP000016936};
RX PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT "Comparative genome structure, secondary metabolite, and effector coding
RT capacity across Cochliobolus pathogens.";
RL PLoS Genet. 9:E1003233-E1003233(2013).
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}.
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DR EMBL; KB445570; EMD95582.1; -; Genomic_DNA.
DR AlphaFoldDB; M2V6D4; -.
DR STRING; 701091.M2V6D4; -.
DR eggNOG; KOG2012; Eukaryota.
DR HOGENOM; CLU_002556_0_0_1; -.
DR OMA; GANLHAF; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000016936; 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:UP000016936};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 897..1025
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT ACT_SITE 605
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 1030 AA; 114609 MW; 7F40932D8B96C71E CRC64;
MQVDSPATAV EQLKEASGNN GDIDESLYSR QLYVLGHEAM KRMGSSNVLV AGLRGLGVEI
AKNVALAGVK SLTLYDPKPA ALADLSSQFF LTPDDVGKPR ASVTVPRVSE LNPYTPVQEF
SGKDLTSDLS QLKQFQVVVL TDTPLDDQIK IADYCHNNGI YIVITDTFGL FGTIFTDFGK
NFTVGDPTGE NVTNGIIAGI DEEGIVSALD ETRHGLEDGD WVTFSEVEGM EALNGCAPRK
IEVKGPYTFS IGDVSGLGEY KRGGQFIQVK MPKILNFEPF SKQLKKPELL ISDFAKFDRP
QQLHVGIQAL HKFAKLHKGE FPRPHHEADA TELFKIAQEI ADEGEEKVEL DEKLIKELSY
QARGDLSPVA AFFGGMAAQE VLKSVSGKFH PIVQFLYFDS LESLPTSTTR SEEQCAPIGS
RYDGQIAVLG QEYQKKLSNV KQFLVGAGAI GCEMLKNWAM MGLATGPEGK ITVTDNDQIE
KSNLNRQFLF RPADVGKLKS DAAAKAVQVM NPDLKGKIVT LQDKVGPETE HIFNEDFWNS
LDGVTNALDN VEARTYVDRR CVFFRKPLLD SGTLGTKGNT QVVLPFITES YSSSQDPPEK
SFPMCTLRSF PNRIEHTIAW ARESFDSLFV KGPEIVNLYL TQPDYLGASL KQSGNEKQTL
ETLRDFLVTE KPLTFDDCII WARHQFEKNY NHAIAQLLYN FPKDSKTGSG QPFWSGPKRA
PDPTKFDPSN PTHFTYVEAA ATLHAFNYGI KPNASREHYV EVLNDMIVPD FQPDPTVKIQ
ADEKEPDPNA NQAGGDDNDV LNKIISQLPD PKSLAGFRLE PVEFEKDDDT NHHIDFITAA
SNLRAENYKI EQADRHKTKF IAGKIIPAIA TTTALVTGLV NLELYKIIDG KKDIEQYKNG
FINLALPFFG FSEPIASPKG TYQGHDGEVT IDKLWDRFEV EDITLKEFVD HFEKKGLSIQ
MISSGVSLLY ASFYPPSKLK DRMPLKMSKL VEHVSKKPIP DHQKNVIFEI TAEDQKEEDV
EIPYVMVKLQ
//
