ID   A0A383Z0X4_BALAS        Unreviewed;       913 AA.
AC   A0A383Z0X4;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Ubiquitin-like modifier-activating enzyme 7 isoform X3 {ECO:0000313|RefSeq:XP_007168777.1};
GN   Name=UBA7 {ECO:0000313|RefSeq:XP_007168777.1};
OS   Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS   (Balaenoptera davidsoni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC   Balaenopteridae; Balaenoptera.
OX   NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_007168777.1};
RN   [1] {ECO:0000313|RefSeq:XP_007168777.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_007168777.1};
RG   RefSeq;
RL   Submitted (JAN-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   RefSeq; XP_007168777.1; XM_007168715.2.
DR   AlphaFoldDB; A0A383Z0X4; -.
DR   GeneID; 103014692; -.
DR   CTD; 7318; -.
DR   OrthoDB; 20494at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000261681; 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   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; 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:SF143; UBIQUITIN-LIKE MODIFIER-ACTIVATING ENZYME 7; 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; 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:UP000261681};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|RuleBase:RU000519}.
FT   DOMAIN          782..909
FT                   /note="Ubiquitin-activating enzyme E1 C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00985"
FT   ACT_SITE        502
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ   SEQUENCE   913 AA;  101270 MW;  0E2379EE0023786B CRC64;
     MIPTLPAGLT CLPSFSSLSR TWEGAGLRHL KNFWLSSMEL FRCASTQVTS LRTCCWTSRQ
     LFCDFGEDFT VQDPTEAEPL MAAIQHISQG SPGILTLREE ADAHRFNSGD LVTFSGIEGM
     VELNGCAPRP LHVQRDGTLE IGDTTTFSRY LRGGAVTEVK RPKTVSHEPL DTALLQPRVV
     AQSPQEVHRA HCLHQAFHAL HKFQQLHGRP PKPWDPVDAE MVVDLAQALE SLKGTEGEPL
     EEQLDKALVR TVALSSAGGL SPMAAVLGAV AAQEVLKAVS KKFMPLDQWL YFDALDCLPE
     DEEPFPNPED YAPRDCRYDG QIAVFGAGFQ EKLSHQHYLL VGAGAIGCEL LKGFALVGLG
     AGGSGGVTVA DMDHVERSNL SRQFLFRPQD FGRPKAEVAA EAAHRLNSDL QVTPLTYQLD
     LTTEHIYGDN FFSSVDGVAA ALDSFQARRY VAARCTHYLK PLLEAGTKGT LGSACVFIPH
     VTEDYRAPAS AAASEDASYP VCTVRHFPST TEHTLQWARD EFEGLFRLSA ETINCHQQAF
     TSLAHLDESQ VLTLQQVVLG VLRERPQTWQ DCVLWALGQW QLCFHYGITQ LLSRFPPDKV
     LEDGTLFWSG PKQCPRPLEF DASQDTHLLY VLAAASLYAQ MHGLPGSRDQ TAFRRLLKLL
     PLPDPQDLAP IFASDLELAS AYAEFGPEQS KKLHEALEIW TVGPPLEPLT FEKDDDFHVD
     FVAAAASLRA QNYGIPPADR TKTKQIVGRI TPAIATTTAA VAGLVGLELY KVVGSPRPRS
     AFRHSYLNLA ENYFSRWVPH APAIQEFHHW KWTCWDRLEV PAGQPERTLE SLLAHVQKLN
     GLRVRMLLHG KALLYSAGWS PEKQDQHLSR RVTDLVLEVT RQVPEPGQRV LVLELSYEGE
     KEDVTFPPLH YKL
//