ID E6ZG69_DICLA Unreviewed; 895 AA.
AC E6ZG69;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Ubiquitin-like modifier-activating enzyme 1 {ECO:0000313|EMBL:CBN80586.1};
GN Name=UBA1 {ECO:0000313|EMBL:CBN80586.1};
GN ORFNames=DLA_It00110 {ECO:0000313|EMBL:CBN80586.1};
OS Dicentrarchus labrax (European seabass) (Morone labrax).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Moronidae; Dicentrarchus.
OX NCBI_TaxID=13489 {ECO:0000313|EMBL:CBN80586.1};
RN [1] {ECO:0000313|EMBL:CBN80586.1}
RP NUCLEOTIDE SEQUENCE.
RA Kuhl H., Tine M., Hecht J., Knaust F., Reinhardt R.;
RT "Analysis of single nucleotide polymorphisms in three chromosomes of
RT European sea bass Dicentrarchus labrax.";
RL Comp. Biochem. Physiol. Part D Genomics Proteomics 6:70-75(2011).
RN [2] {ECO:0000313|EMBL:CBN80586.1}
RP NUCLEOTIDE SEQUENCE.
RX DOI=10.1016/j.ygeno.2011.06.004;
RA Kuhl H., Tine M., Beck A., Timmermann B., Kodira C., Reinhardt R.;
RT "Directed sequencing and annotation of three Dicentrarchus labrax L.
RT chromosomes by applying Sanger- and pyrosequencing technologies on pooled
RT DNA of comparatively mapped BAC clones.";
RL Genomics 0:0-0(2011).
RN [3] {ECO:0000313|EMBL:CBN80586.1}
RP NUCLEOTIDE SEQUENCE.
RA Tine M., Kuhl H., Beck A., Bargelloni L., Reinhardt R.;
RT "Comparative analysis of intronless genes in teleost fish genomes: Insights
RT into their evolution and molecular function.";
RL Mar. Genomics 4:109-119(2011).
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; FQ310506; CBN80586.1; -; Genomic_DNA.
DR AlphaFoldDB; E6ZG69; -.
DR UniPathway; UPA00143; -.
DR GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
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 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; IPR042449; Ub-E1_IAD_1.
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 InterPro; IPR000011; UBQ/SUMO-activ_enz_E1-like.
DR PANTHER; PTHR10953:SF198; E1 UBIQUITIN-ACTIVATING ENZYME; 1.
DR PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR Pfam; PF16191; E1_4HB; 1.
DR Pfam; PF16190; E1_FCCH; 1.
DR Pfam; PF00899; ThiF; 2.
DR Pfam; PF10585; UBA_E1_SCCH; 1.
DR PRINTS; PR01849; UBIQUITINACT.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 2.
DR PROSITE; PS00865; UBIQUITIN_ACTIVAT_2; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 12..365
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
FT DOMAIN 185..253
FT /note="Ubiquitin-activating enzyme E1 FCCH"
FT /evidence="ECO:0000259|Pfam:PF16190"
FT DOMAIN 254..324
FT /note="Ubiquitin-activating enzyme E1 four-helix bundle"
FT /evidence="ECO:0000259|Pfam:PF16191"
FT DOMAIN 414..864
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
FT DOMAIN 568..824
FT /note="Ubiquitin-activating enzyme SCCH"
FT /evidence="ECO:0000259|Pfam:PF10585"
FT ACT_SITE 562
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 895 AA; 99976 MW; 7F7821983C96BB2F CRC64;
MSEIGEIDEG FYSRQLYVLG HDAMHRMGTA SVLIAGMRGL GIEIAKNVIL SGVKSVTIQD
EGQTVWTDLS SQFFLKEAHL GQNRATCSIQ QLSALNPRVR VFAHTGPLDD TLLLQFQVVV
LTDSSLDDQK RFGELCHLHG IKFIVADTKG LCGQLFCDFG EEFEVLDRDG EAPESATIQS
ISKADPGVVL CTDEQSHKFS DGCKVSFSEV QGMTELNSIG PVEIKYRGEY SFSIGDTSAF
SEYKRGGIVT EVKQPLRLHF KPLSEALLDT KLLVMNDFGK ISRHKTLHLA FQALHSFVKK
EQRLPGLWSQ PDADALLDMV RELNTVAKLK QLDEAAVQKL SYTARGDLAP MNAFIGGLVA
QEVIKGTRYD GQIAVFGSAF QKKLERQKYF LLILSFVSRH FSRLELVLLA VSFLKNFALI
GLGAGEEGHI TVTDMDFIEK SNLNRQFLFR SQDIGKPKSE VAAKAVQEMN PQMKITAHQN
RLDPDSEAVF DYNFFMGLDG VAAALDNVEA RIYLDQRCIQ HQKPMLEGGT QGSKGHTLVV
VPHLTESYGQ PKTNANNAIP LCTLKNFPHR IEHTLQWARD QFEGQFKQTP ENVNLFLSDE
GFVERTLGHG DAEALEVLGG VWNSLEDIKD GGQHPTSWED CVSWARCKWE TVYNNDIRQL
LHCLPPEKVT ATGLPFWSGS KRCPHPLTFD LKNTTHMEYV VAAANLYGQI YGIKGTRDCT
SIREILEKVH VPPFTPKSSV KIHVTDKEMK EAKERDSDDA EKARLEELKG KLASPSMKSS
AKQMYPIDFE KDDDSNFHMD YIVAASNLRA ENYDIPAADR HKSKGIAGRI IPAIATTTAA
VAGLMCLELY KLVQGHQNIS SYRTSYFILA VQHYVWCQPG RPRSFECMSH IDVEL
//
