ID H3ARY3_LATCH Unreviewed; 915 AA.
AC H3ARY3;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Ubiquitin-activating enzyme E1 C-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN Name=UBA7 {ECO:0000313|Ensembl:ENSLACP00000012404.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000012404.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000012404.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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; AFYH01133206; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01133207; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01133208; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01133209; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01133210; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01133211; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01133212; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01133213; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01133214; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01133215; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H3ARY3; -.
DR STRING; 7897.ENSLACP00000012404; -.
DR Ensembl; ENSLACT00000012497.1; ENSLACP00000012404.1; ENSLACG00000010924.1.
DR eggNOG; KOG2012; Eukaryota.
DR GeneTree; ENSGT00940000158975; -.
DR HOGENOM; CLU_002556_0_0_1; -.
DR InParanoid; H3ARY3; -.
DR TreeFam; TF300586; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008672; 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 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; 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: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 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:UP000008672};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 15..387
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
FT DOMAIN 187..254
FT /note="Ubiquitin-activating enzyme E1 FCCH"
FT /evidence="ECO:0000259|Pfam:PF16190"
FT DOMAIN 255..324
FT /note="Ubiquitin-activating enzyme E1 four-helix bundle"
FT /evidence="ECO:0000259|Pfam:PF16191"
FT DOMAIN 411..892
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
FT DOMAIN 597..844
FT /note="Ubiquitin-activating enzyme SCCH"
FT /evidence="ECO:0000259|Pfam:PF10585"
FT REGION 765..784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 591
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 915 AA; 102952 MW; A319A3390644574A CRC64;
MASTENTEDI DESLYSRQLY VLGHEAMRRM KASNILISGM KGLGVEIAKN VILAGVNSVT
LHDEGDTQWS DLSSQFYLSE EDIGKNRALA SERQLAELNS YVHVMAYTKG LSQDFLSKFQ
VVVLTNSPLD EQLQLGHFCH SNNIKFIVAD TKGLFGQLFC DFGEEFEVTD LNGVQPASAV
VENISKDCPG VVTCSDENGL ENGDFVTFSH IQGMTELNGC EPIQIKYLDT YSFSICDTTG
FSDYQRGGVV TEVKVPKKFN FKPLREAMID PQFIDMDYVK IQQQGTLHIG FQALHKFYQE
NNRLPKPRGQ TDAEKLVAIA RVLNREAPPT VKQDPLDEDL VRKMAFVAAG DLSPINTFIG
GVAAQEVMKA CTGKFTPLPK WLYFDALECL PEENEEVVLT EEECAPRDCR YDGQIAVFGA
AFQRKLAKQK YFMVGAGAIG CELLKIFAMI GLATEEGGNI TVTDMDSIER SNLNRQFLFR
DKDIMKLKSE VAAAAVRKMN PNVRVVSHQN RVGPDTEHFY TDEFYEGLDG LANALDNVET
RVYMDGRCVC YRKPLLESGT LGTKGNTQII VPFLTKSYGS FHDPEKSIPL CTLRYFPSSI
EHTLQWARDE FEGLFKQPAE TVNQFLQDPP CNYQTLRTLN RDPGFLEQPE TLYKSLVSEK
PASWFKCVTW ARNHWQNLYN NNIRQLLHSF PPDQVTKSGF PFWAGPKRCP HPLEFSVNNP
THMDYIVAAA NLFAETYGIQ GSQDRATIAD LLKIVHLPEF TPKSGVKIPT NDQDMEDSSE
QLDDENLKET REKLTALKSS FHMMQPINFE KDDDTNFHMD FIVAASNLRA ENYDIPPADR
HKSKLIAGKI IPAIATTTAA VVGLVCLELY KVIQGHQRIT SYRNSFINMA LPLFCFPQPS
PAETTKVNNE VWSVW
//
