ID A0A452R673_URSAM Unreviewed; 1001 AA.
AC A0A452R673;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
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};
OS Ursus americanus (American black bear) (Euarctos americanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000013842.1, ECO:0000313|Proteomes:UP000291022};
RN [1] {ECO:0000313|Proteomes:UP000291022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT in black bear kidneys.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSUAMP00000013842.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A452R673; -.
DR STRING; 9643.ENSUAMP00000013842; -.
DR Ensembl; ENSUAMT00000015535.1; ENSUAMP00000013842.1; ENSUAMG00000011120.1.
DR GeneTree; ENSGT00940000158975; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000291022; 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; 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:UP000291022};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 909..1000
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 619
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 1001 AA; 112226 MW; 0E043BFE80509A31 CRC64;
MTRALPSGLT SPPSSTFGKR TSVKTGLRYH SPTLLSSTAM CLSAPILGPS LRTSFVVSRW
WSSPILPWRT SCRWVSSVIA VESSWSWQTH EAYLGECLPL TFSQALARPR QDPFAPTEFI
LFPANPSLSF DSVHLAFPIW HDCHLIASSK GLSLLSSYSL HLEGHIEYLH AWVLGSSPVV
SYRQLFCDFG EEMILTDSNG EQPLSAMVSM VTKDSPGVVT CLDEARHGFE SGDFVSFTEV
QGMHELNGTY PIEIKVLGPY TFSICDTSSF SEYIRGGIVS QVKVPKKISF KSLPASLAEP
DFVITDFAKY SRPGQLHIGF QALHHFCAQH GRAPRPHNEE DATELVTLAQ AVNARALPAV
QQDILDEDLI RKLSYVAAGD LAPINAFIGG LAAQEVMKAC SGKFMPVMQW LYFDALECLP
EDKQALTEDK CLPCQNRYDG QVAVFGSDLQ EKLGKQKYFL VGAGAIGCEL LKNFAMIGLG
CGEDGAVTVT DMDTIEKSNL NRQFLFRPWD VTKLKSDTAA AAVRHINPYI RVMSHQNRVG
PDTEHIYDDS FFQNLDGVAN ALDNVDTRMY MDRRCVYYRK PLLESGTLGT KGNVQVVIPF
LTESYSSSQD PPEKSIPICT LKNFPNAIEH TLQWARDEFE GLFKQPAENV NQYLTDSNFV
ERTLCLAGTQ PLEMLEAVQR SLVLQRPHTW ADCVTWAYHH WHTQYSNNIR QLLHNFPPDQ
LTSSGALFWS GPKRCPHPLI FDVNNPLHLD YVMAAANLFA QTYGLMGSQD RAAVAILLQS
VHIPEFTPRS DVKIHVSDQE LQNSSASVDD SCIQELKAML PSPEKLPGFK MYPINFEKDD
NTNFHMDFIV AASNLRAENY NIPPADRHKS KMIAGKIIPA IATTTAAIVG LVCLELYKVV
QGHRQLESYK NSFMNLALPF FSFSEPLAPP RHQYCNQEWT LWDRFEVQGL QPNGEEMTLK
QFLNYFKTEH KLEITMLSQG VSMLYSFFMP ATKLRERLDQ P
//
