ID A0A384DNB4_URSMA Unreviewed; 898 AA.
AC A0A384DNB4;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 03-AUG-2022, sequence version 2.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Ubiquitin-like modifier-activating enzyme 1 {ECO:0000256|ARBA:ARBA00044109};
DE EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
DE AltName: Full=Ubiquitin-activating enzyme E1 {ECO:0000256|ARBA:ARBA00030371};
GN Name=LOC103680817 {ECO:0000313|RefSeq:XP_008708516.2};
OS Ursus maritimus (Polar bear) (Thalarctos maritimus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=29073 {ECO:0000313|Proteomes:UP000261680, ECO:0000313|RefSeq:XP_008708516.2};
RN [1] {ECO:0000313|RefSeq:XP_008708516.2}
RP IDENTIFICATION.
RC TISSUE=Whole blood {ECO:0000313|RefSeq:XP_008708516.2};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC {ECO:0000256|ARBA:ARBA00005673, ECO:0000256|RuleBase:RU000519}.
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DR RefSeq; XP_008708516.2; XM_008710294.2.
DR AlphaFoldDB; A0A384DNB4; -.
DR STRING; 29073.ENSUMAP00000002599; -.
DR KEGG; umr:103680817; -.
DR OrthoDB; 20494at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000261680; Chromosome Y.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004839; F:ubiquitin activating enzyme activity; IEA:UniProtKB-EC.
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; 3.40.50.12550; 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; 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; IPR018074; UBQ-activ_enz_E1_CS.
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:SF155; 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; 1.
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; PS00536; UBIQUITIN_ACTIVAT_1; 1.
DR PROSITE; PS00865; UBIQUITIN_ACTIVAT_2; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW ATP-binding {ECO:0000256|RuleBase:RU000519};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU000519};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU000519};
KW Reference proteome {ECO:0000313|Proteomes:UP000261680};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 762..893
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT ACT_SITE 472
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
FT NON_TER 1
FT /evidence="ECO:0000313|RefSeq:XP_008708516.2"
SQ SEQUENCE 898 AA; 100897 MW; 69A6B3E232219FB4 CRC64;
VVVLTNSPLE DQLQVGEFCH SRGIKLVVAD TRGLFGQLFC DFGEEMILTD SNGEQPLSAM
VSMVTKDSPG VVTCLDEARH GFESGDFVSF TEVQGMHELN GTYPIEIKVL GPYTFSICDT
SSFSEYIRGG IVSQVKVPKK ISFKSLPASL AEPDFVITDF AKYSRPGQLH IGFQALHHFC
AQHGRAPRPH NEEDATELVT LAQAVNARAL PAVQQDILDE DLIRKLSYVA AGDLAPINAF
IGGLAAQEVM KACSGKFMPV MQWLYFDALE CLPEDKQALT EDKCLPCQNR YDGQVAVFGS
DLQEKLGKQK YFLVGAGAIG CELLKNFAMI GLGCGEDGAV TVTDMDTIEK SNLNRQFLFR
PWDVTKLKSD TAAAAVRHIN PYIRVMSHQN CVGPDTEHIY DDSFFQNLDG VANALDNVDT
RMYMDRHCVY YRKPLLESGT LGTKGNVQVV IPFLTESYSS SQDPPEKSIP ICTLKNFPNA
IEHTLQWARD EFEGLFKQPA ENVNQYLTDS NFVERTLCLA GTQPLEMLEA VQRSLVLQRP
HTWADCVTWA YHHWHTQYSN NIRQLLHNFP PDQLTSSGAL FWSGPKRCPH PLIFDVNNPL
HLDYVMAAAN LFAQTYGLMG SQDRAAVAIL LQSVHIPEFT PRSDVKIHVS DQELQNSSAS
VDDSCIQELK AMLPSPEKLP GFKMYPINFE KDDNTNFHMD FIVAASNLRA ENYNIPPADR
HKSKMIAGKI IPAIATTTAA IVGLVCLELY KVVQGHRQLE SYKNSFMNLA LPFFSFSEPL
APPRHQYYNQ EWTLWDRFEV QGLQPNGEEM TLKQFLDYFK TEHKLEITML SQGVSMLYSF
FMPATKLRER LDQPVTEIVS RVSKRKLGRH VRALVLELCC NDESGEDVEV PYVRYTIR
//
