ID G0PHQ2_CAEBE Unreviewed; 441 AA.
AC G0PHQ2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Ubiquitin-like modifier-activating enzyme 5 {ECO:0000256|ARBA:ARBA00016279};
GN ORFNames=CAEBREN_22526 {ECO:0000313|EMBL:EGT56895.1};
OS Caenorhabditis brenneri (Nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=135651 {ECO:0000313|Proteomes:UP000008068};
RN [1] {ECO:0000313|Proteomes:UP000008068}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB2801 {ECO:0000313|Proteomes:UP000008068};
RG Caenorhabditis brenneri Sequencing and Analysis Consortium;
RA Wilson R.K.;
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family. UBA5
CC subfamily. {ECO:0000256|ARBA:ARBA00005339}.
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DR EMBL; GL380499; EGT56895.1; -; Genomic_DNA.
DR AlphaFoldDB; G0PHQ2; -.
DR STRING; 135651.G0PHQ2; -.
DR EnsemblMetazoa; CBN22526.1; CBN22526.1; WBGene00161251.
DR eggNOG; KOG2336; Eukaryota.
DR HOGENOM; CLU_013325_0_1_1; -.
DR InParanoid; G0PHQ2; -.
DR OMA; MHSENTP; -.
DR Proteomes; UP000008068; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR CDD; cd00757; ThiF_MoeB_HesA_family; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR PANTHER; PTHR10953:SF9; UBIQUITIN-LIKE MODIFIER-ACTIVATING ENZYME 5; 1.
DR Pfam; PF00899; ThiF; 1.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008068};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 68..318
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
FT REGION 24..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 441 AA; 49445 MW; 78E4C470BE899335 CRC64;
MTEQPVDKYV EDLTSRLEKA IDNLSGQKHD DSIDNHIRDS QRSVKNKPVP YREKISKLSA
EVVDSNPYSR LMALQRMGIV QDYEKIREKT VAVVGVGGVG SVVAEMLTRC GIGKLILFDY
DKVEIANMNR LFYQPDQAGL SKVDAARDTL IHVNPDVQIE VHNFNITTMD NFDTFVGRIR
NGSLTNGKID LVLSCVDNFE ARMAVNMACN EENQIWMESG VSENAVSGHI QYIEPGKTAC
FACVPPLVVA SNIDERTLKR EGVCAASLPT TMAVVAGFLV MNTLKFLLHF GEVSHYVGYN
ALADFFPRHS IKPNPTCEDS HCLIRQKEYQ NKKSSETIDI DFQTTEEEPI VHEDNEWGIE
LVDESEPATT TDEKTSSDVA EGLKFAYEPV KKEVESKEAG NTDRETAENA KNDALLKLKD
ILLEADMMKK MEEKNQLTKK H
//