ID G5BZX5_HETGA Unreviewed; 977 AA.
AC G5BZX5;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Ubiquitin-like modifier-activating enzyme 7 {ECO:0000313|EMBL:EHB14817.1};
GN ORFNames=GW7_19930 {ECO:0000313|EMBL:EHB14817.1};
OS Heterocephalus glaber (Naked mole rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Heterocephalus.
OX NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB14817.1, ECO:0000313|Proteomes:UP000006813};
RN [1] {ECO:0000313|EMBL:EHB14817.1, ECO:0000313|Proteomes:UP000006813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993625; DOI=10.1038/nature10533;
RA Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT "Genome sequencing reveals insights into physiology and longevity of the
RT naked mole rat.";
RL Nature 479:223-227(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, ECO:0000256|RuleBase:RU000519}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JH172617; EHB14817.1; -; Genomic_DNA.
DR AlphaFoldDB; G5BZX5; -.
DR STRING; 10181.G5BZX5; -.
DR eggNOG; KOG2012; Eukaryota.
DR InParanoid; G5BZX5; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000006813; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004839; F:ubiquitin activating enzyme activity; IEA:UniProtKB-EC.
DR CDD; cd01491; Ube1_repeat1; 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:SF143; UBIQUITIN-LIKE MODIFIER-ACTIVATING ENZYME 7; 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:UP000006813};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 868..976
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT ACT_SITE 595
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 977 AA; 107887 MW; 10C0C7080FAEC64B CRC64;
MAVLEPSEWL DKELYSRQLP VLGPPAMQRI REAKVLLSGL QGLGAEVAKN LVLMGVGSLT
LHDPHPTCWS DLAAQVFLSE RDLGKSRAEA SQEHLAQLNE AVQVFVHPSD ITEDLLLKFQ
VVVLTASKLE EQLMVGALCH KHGICFLVAD TRGLVGQLFC DFGDEFIVHD PTEAEPLTAA
IQHITQGFPG VLTLRGEDKE HSFCDGDLVT FSGIKGMVEL NSCSPRPIRV QKDRSLEIGD
TSTFSPYLHG GIVTEVKRPE TVRHKPLDRA LIQPCVVAPS AQEAHRAHCL HQAFRALHKF
QNLHGRLPQP WDPVDAEIMV TLAQNLGPLK GAEEEPLNEA LLRTVALSSA GVLSPMASIL
GAVTAQEVLK AISRKFIPLD QWLYFDALDC LPEDEELFPN PEDCALRDSR YDGQIAVFGA
GFQETLSHQH YLLVGAGAIG CELLKGFALV GLGAGASGGV TVVDMDHIEY SNLSRQFLFR
PWDIDKPKAE VAAAATQDLN PDLEVIAHVQ VLDHTTEHIY GDNFFSHVDG VVAAVDSFEA
RHYVAARCIH YLKPLLEAGT QGTKGSASVF VPYVTEVYKG PASAEASEDA PTPVCTMRRF
PSTYEHTLEW ARNEFEGLFR LSAETISCYQ QACTSLADVD GPQMLTSLQR VLGVLRVRPQ
TWRDCVMWAL GHWQLCFHDD IIQLLSLLPP DKVHEDGTPF WSGPKRCPQP LKFDISQDMH
LLYILAAANL FAQMHGLPGS SDQIALRELL NLLLQTDPPH PAPVLAESGP EQLKELQEAL
EVWSKGPPLK SLVFEKDEDG NFHMDFVRAA ASLQSQNYGI SEPVDHAQSM RMVSQIIPAI
ATTTAAVAGL LGLELYKMVG RPRPVGAFRH TYLHLAENRL QRSVPSTPAI QKFHHLEWTR
WDRLKVPAGQ PERTLESLLA HLQEQHGLNV RMLLRGQALL YSARWSPESQ AQYLPLSPLP
GDPKLPASCL PHQLLLK
//