ID   A0A667WQT3_9TELE        Unreviewed;      1035 AA.
AC   A0A667WQT3;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Ubiquitin-like modifier-activating enzyme 1 {ECO:0000313|Ensembl:ENSMMDP00005007980.1};
GN   Name=LOC115359979 {ECO:0000313|Ensembl:ENSMMDP00005007980.1};
OS   Myripristis murdjan (pinecone soldierfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Holocentriformes; Holocentridae; Myripristis.
OX   NCBI_TaxID=586833 {ECO:0000313|Ensembl:ENSMMDP00005007980.1, ECO:0000313|Proteomes:UP000472263};
RN   [1] {ECO:0000313|Ensembl:ENSMMDP00005007980.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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}.
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DR   AlphaFoldDB; A0A667WQT3; -.
DR   Ensembl; ENSMMDT00005008220.1; ENSMMDP00005007980.1; ENSMMDG00005004397.1.
DR   GeneTree; ENSGT00940000166002; -.
DR   InParanoid; A0A667WQT3; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000472263; Unplaced.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
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   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; IPR042449; Ub-E1_IAD_1.
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:SF198; E1 UBIQUITIN-ACTIVATING ENZYME; 1.
DR   PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR   Pfam; PF16191; E1_4HB; 1.
DR   Pfam; PF16190; E1_FCCH; 1.
DR   Pfam; PF00899; ThiF; 2.
DR   Pfam; PF10585; UBA_E1_SCCH; 1.
DR   PRINTS; PR01849; UBIQUITINACT.
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:UP000472263};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|RuleBase:RU000519}.
FT   DOMAIN          37..395
FT                   /note="THIF-type NAD/FAD binding fold"
FT                   /evidence="ECO:0000259|Pfam:PF00899"
FT   DOMAIN          210..278
FT                   /note="Ubiquitin-activating enzyme E1 FCCH"
FT                   /evidence="ECO:0000259|Pfam:PF16190"
FT   DOMAIN          282..349
FT                   /note="Ubiquitin-activating enzyme E1 four-helix bundle"
FT                   /evidence="ECO:0000259|Pfam:PF16191"
FT   DOMAIN          433..920
FT                   /note="THIF-type NAD/FAD binding fold"
FT                   /evidence="ECO:0000259|Pfam:PF00899"
FT   DOMAIN          620..874
FT                   /note="Ubiquitin-activating enzyme SCCH"
FT                   /evidence="ECO:0000259|Pfam:PF10585"
FT   ACT_SITE        614
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ   SEQUENCE   1035 AA;  115109 MW;  724CA50A4F5B62A3 CRC64;
     MLDVCHSRSS VKQIYTPLSA GQLHNMTEMG EIDEGFYSRQ LYVLGREAMQ RMGAARVLIA
     GMRGLGVEIA KNVILSGVNS VTVQDEGVAS WTDLTSQFFL NESHIGQNRA TSSLPQLSAL
     NPHVHVSVHT GPLDENLLLQ FQVVVLTDSS LDDQKRFGRH CHLNGIKFIV ADTKGLCGQL
     FSDFGEEFEV LDADGETPVS AMIEHITKGN PGMVTCTYNQ KLHFRDGCEV SFSEVQGMTE
     LNSMSPMKIT VCSPDCFSIV DTSGFSEYKR GGIVTEVKQR HVLKFKSLDE ALLDRELLVN
     TDFGKTARHE TLHLAFQALH SFVKKEGRLP KPRSQSDADV LAVMVRELNA AAQLEQLDEA
     VVRRLSYTAQ GDLAPLNAFI GALAAQEVIK ACGRKFMPLQ QWLYFDALEC LPEDDEDEDQ
     LTEDCFSPKG VRYDGQIAVF GSAFQEKLGR QKHFLVGAGA IGCELFKNFA LIGLGAGEGG
     HITVTDMDSI ERSNLHRQFL FRSKDIGKQK SEVAAKAVKA MNPEMNITAH QNRLGSDSEH
     VYDYHFFMGL DGVFAALDNV ETRVYLDERC VRHKKPMLEG GTRGGQGHTL VVVPHLTESY
     GPHGLSSDEA IPLCTLKNFP YRIEHTLQWA RDQFEGLFKQ TPDNVNLYLR EPGFVERTLG
     LGEGEALDVL QGVCSNLEGI EAGGQRPTCW EDCVGWARCK WETLYNNDIL QLLHCFPPEQ
     VTSSGLPFWS GAKRCPHPLT FDPNNTTHMD YVVAAANLYG QIYGIKGTKD RASIKKVLEE
     VRVPPFSPKS SVKIYVTDEE MDAEKQRGND DAARLDELTE KLASLSLSGL ALQMHPIDFE
     KDVDDNFHVD YIVAASNLRA ENYDIPAADR LQSKRIAGRI MPAIATTTAA VAGLMCLELY
     KLVQGHRKIS SYRSAFLNLA LPLPALSFEA LNLRQTRVIG DRRVREWGNS VSWDMGLQQQ
     GAVRQYSSGF SYGYKQKHCC YIRGCRDDRG SCDFVLDAEA PASKPPATQN SRRAFKLILR
     FSLSLLISVY QPWAN
//