ID   A0A2K6A953_MANLE        Unreviewed;       342 AA.
AC   A0A2K6A953;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Ubiquitin-like modifier-activating enzyme 5 {ECO:0000256|ARBA:ARBA00016279};
DE   AltName: Full=UFM1-activating enzyme {ECO:0000256|ARBA:ARBA00030506};
GN   Name=UBA5 {ECO:0000313|Ensembl:ENSMLEP00000036604.1};
OS   Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Mandrillus.
OX   NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000036604.1, ECO:0000313|Proteomes:UP000233140};
RN   [1] {ECO:0000313|Ensembl:ENSMLEP00000036604.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000256|ARBA:ARBA00004555}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family. UBA5
CC       subfamily. {ECO:0000256|ARBA:ARBA00005339}.
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DR   AlphaFoldDB; A0A2K6A953; -.
DR   Ensembl; ENSMLET00000060207.1; ENSMLEP00000036604.1; ENSMLEG00000042373.1.
DR   GeneTree; ENSGT00940000156177; -.
DR   Proteomes; UP000233140; Unplaced.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
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   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:UP000233140};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          53..269
FT                   /note="THIF-type NAD/FAD binding fold"
FT                   /evidence="ECO:0000259|Pfam:PF00899"
SQ   SEQUENCE   342 AA;  38190 MW;  636BB49A063130E7 CRC64;
     MAESVERLQQ RVQELERELA QERNRRVPGS GEGGGGRIRI EKMSSEVVDS NPYSRLMALK
     RMGIVSDYEK IRTFAVAIVG VGGVGSVTAE MLTRCGIGKL LLFDYDKVEL ANMNRLFFQP
     HQAGLSKVQA AEHTLRNINP DVLFEVHNYN ITTVENFQHF MDRISNGGLE EGKPVDLVLS
     CVDNFEARMT INTCAPPLVV AANIDEKTLK REGVCAASLP TTMGVVAGIL VQNVLKFLLN
     FGTVSFYLGY NAMQDFFPTM SMKPNPQCDD RNCRKQQEEY KKKVAALPKQ EVMQEEEEII
     HEDNDWGIEL VSEVSEEELK NSSGPVPDLP EGITVAYTIP KK
//