ID A0A498MPV8_LABRO Unreviewed; 1047 AA.
AC A0A498MPV8;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Ubiquitin-like modifier-activating enzyme 1 {ECO:0000313|EMBL:RXN22380.1};
GN ORFNames=ROHU_023509 {ECO:0000313|EMBL:RXN22380.1}, ROHU_034838
GN {ECO:0000313|EMBL:RXN02662.1};
OS Labeo rohita (Indian major carp) (Cyprinus rohita).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Labeoninae; Labeonini; Labeo.
OX NCBI_TaxID=84645 {ECO:0000313|EMBL:RXN22380.1, ECO:0000313|Proteomes:UP000290572};
RN [1] {ECO:0000313|EMBL:RXN22380.1, ECO:0000313|Proteomes:UP000290572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN22380.1};
RC TISSUE=Testis {ECO:0000313|EMBL:RXN22380.1};
RA Das P., Kushwaha B., Joshi C.G., Kumar D., Nagpure N.S., Sahoo L.,
RA Das S.P., Bit A., Patnaik S., Meher P.K., Jayasankar P., Koringa P.G.,
RA Patel N.V., Hinsu A.T., Kumar R., Pandey M., Agarwal S., Srivastava S.,
RA Singh M., Iquebal M.A., Jaiswal S., Angadi U.B., Kumar N., Raza M.,
RA Shah T.M., Rai A., Jena J.K.;
RT "Draft genome sequence of Rohu Carp (Labeo rohita).";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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:RXN22380.1}.
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DR EMBL; QBIY01013496; RXN02662.1; -; Genomic_DNA.
DR EMBL; QBIY01012595; RXN22380.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498MPV8; -.
DR STRING; 84645.A0A498MPV8; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000290572; 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; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR PANTHER; PTHR10953:SF195; UBIQUITIN-LIKE MODIFIER-ACTIVATING ENZYME 1; 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 1: Evidence at protein level;
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 Proteomics identification {ECO:0007829|PeptideAtlas:A0A498MPV8};
KW Reference proteome {ECO:0000313|Proteomes:UP000290572};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 911..1042
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 621
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 1047 AA; 116820 MW; 12F3566FA7D8DF41 CRC64;
MSSSPLSKKR RVSGSETKTG SHCSSSNSVR TELSHTPANG MAKNGNDAEI DEGLYSRQLY
VLGHDAMKRM QSSNVLISGL RGLGVEIAKN VILGGVKSVT LHDQGVAEWK DLSSQFYLRE
EDLGKNRADV SQPRLAELNS YVPVTSYTGA LTNEYLTKFQ VVVLTNSSLD EQIRMGDFCH
SNGIKLIVAD TRGLFGQLFC DFGEDMTVFD TNGEQPLSAM ISMITKDSAG VVTCLDEARH
GFESGDFVTF TEVQGMTELN GCEPIEIKSL GPYTFSICDT SSFSDYVRGG IVTQVKMPKT
VAFKSLSSSM AEPEFMLTDF AKFDRPGQLH VGFQALHAFE KKHSRLPKPW SQSDADELMA
LAEEVNAAQT GSAKQEQLDQ AVIKKLSCVA AGDLAPINAF IGGLAAQEVM KWLYFDAVEC
LSEAEDAVLT EEECAPRNCR YDGQIAVFGS KLQELLAKQR YFLVGAGAIG CELLKNFAMM
GLASGEGEVI VTDMDTIEKS NLNRQFLFRP WDVTKMKSET AAAAVKQMNP SVRITGHQNR
VGPDTEKVYD DDFFESLHGV ANALDNVDAR MYMDRRCVYY RKPLLESGTL GTKGNVQVVI
PFLTESYSSS QDPPEKSIPI CTLKNFPNAI EHTLQWARDE FEGLFKQPAE NALQYLTDQK
FMERTLKLPG AQPLEVVEAV YKSLVTDYPR SWEDCVAWAR NHWQCQYNNN IRQLLHNFPP
DQLTSSGAPF WSGPKRCPHP LEFSTNNDLH MDYIMAAANL YAQSYGLPGS TDRSALTKLL
QDIKVPEFTP KSGVKIHVSD QELQSANASI DDSRLEELKT QLPSTEASSQ FKLCPIDFEK
DDDTNFHMDF IVAASNLRAE NYDIPPADRH KSKLIAGKII PAIATTTAAV VGLVCLELLK
IVQGHKKLES YKNGFMNLAL PFFAFSEPIA APKHKYYEID WTLWDRFEVK GIQSNGEEMT
LRQFLDYFKN EHKLEITMLS QGVSMLYSFF MPAAKLKERL DLPMTEIVTK VSKKKLGKHV
KALVFELCCN DETEEDVEVP YVRYTIR
//
