ID A0A484GV47_SOUCH Unreviewed; 1064 AA.
AC A0A484GV47;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=SUMO-activating enzyme subunit 1 {ECO:0000256|ARBA:ARBA00044187};
DE AltName: Full=Ubiquitin-like 1-activating enzyme E1A {ECO:0000256|ARBA:ARBA00044354};
DE Flags: Fragment;
GN ORFNames=DBR06_SOUSAS2110257 {ECO:0000313|EMBL:TEA39473.1};
OS Sousa chinensis (Indo-pacific humpbacked dolphin) (Steno chinensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Delphinidae; Sousa.
OX NCBI_TaxID=103600 {ECO:0000313|EMBL:TEA39473.1, ECO:0000313|Proteomes:UP000295264};
RN [1] {ECO:0000313|EMBL:TEA39473.1, ECO:0000313|Proteomes:UP000295264}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MY-2018 {ECO:0000313|EMBL:TEA39473.1};
RC TISSUE=Skin {ECO:0000313|EMBL:TEA39473.1};
RX PubMed=30031902;
RA Ming Y., Jian J., Yu F., Yu X., Wang J., Liu W.;
RT "Molecular footprints of inshore aquatic adaptation in Indo-Pacific
RT humpback dolphin (Sousa chinensis).";
RL Genomics 0:0-0(2018).
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC {ECO:0000256|ARBA:ARBA00004718}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBUNIT: Heterodimer of SAE1 and UBA2/SAE2. The heterodimer corresponds
CC to the two domains that are encoded on a single polypeptide chain in
CC ubiquitin-activating enzyme E1. Interacts with UBE2I.
CC {ECO:0000256|ARBA:ARBA00026003}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC {ECO:0000256|ARBA:ARBA00005673}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TEA39473.1}.
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DR EMBL; QWLN02004155; TEA39473.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A484GV47; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000295264; Unassembled WGS sequence.
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 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; IPR042449; Ub-E1_IAD_1.
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; IPR033127; UBQ-activ_enz_E1_Cys_AS.
DR InterPro; IPR000011; UBQ/SUMO-activ_enz_E1-like.
DR PANTHER; PTHR10953:SF162; SUMO-ACTIVATING ENZYME SUBUNIT 1; 1.
DR PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR Pfam; PF16191; E1_4HB; 1.
DR Pfam; PF16190; E1_FCCH; 1.
DR Pfam; PF09358; E1_UFD; 1.
DR Pfam; PF00899; ThiF; 3.
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 Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000295264};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 933..1060
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT ACT_SITE 653
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:TEA39473.1"
SQ SEQUENCE 1064 AA; 116843 MW; 660148CD480F3C27 CRC64;
GLLTSDLQSP ALLLPTHRYV LGLPAMQRIQ RAKVLLSGLQ GVGAEVAKNL VLMGVGSLTL
HDPHPTCWSD LSAQFFLSEQ DLGRSRAEAS QELLAKLNGA VQVCIHTGDI TEDLLLDFQV
PSQPYSPGQP SVPLQPLAAG STQVVVLTAS ELQEQLKVGT ICHKHGVCFL VADTRGLVGQ
LFCDFGEDFT VQDPTEAEPL VAAIQHISQG SPGIVTLREE ADAHRFNNGD LVTFSGIEGM
VELNGCAPRP LHVQRDGTLE IGDTTTFSHY LRGGAVTEVK RPKTVSHEPL DTALFQPRVV
AQSPQEVHRA HCLHQAFHAL HKFQQLHGRP PKPWDPVDAE MVVDLAQALE SLKGTEGEPL
EEQLDKALVR TVALSSAGGL SPMAAVLGAV AAQEVLKAVS KKFMPLDQWL YFDALDCLPE
DEEPFPNPED YAPRDCRYDG QIAVFGAGFQ EKLSHQRYLL VGAGAIGCEL LKGFALVGLG
AGGSGGVTVA DMDHVERSNL SRQFLFRPQD FGVSADLAPH PCPGLSSHNA TLPPPNVFLL
SSQRPKAEVA AEAARRLNSD LQVTPLTYQL DLTTEHIYGD NFFSSVDGVA AALDSFQARR
YVAARCTHYL KPLLEAGTKG TLGSACVFIP HVTEDYRAPA SAAASEDASY PVCTVRHFPS
TTEHTLQWAR DEFEGLFHLS AETVNCHQQA LTSLAHLDES QVLTVQQVVL GVLRQRPQTW
RDCVLWALGQ WQLCFHYGIT QLLSRFPPDK VLENGTLFWS GPKRCPRPLE FDASQDTHLL
YVLAAANLYA QMHGLPGSRD QTALRRLLKL LPLPDPQDLA PIFSSDLELP SAYAEFGPEQ
SKQLHEALEI WTVGPPLEPL TFEKDNDFHV DFVAAAASLR AQNYGIPPAD RTKTKRIVGQ
ITPAIATTTA AVAGLVGLEL YKVVGSPRPR SAFRHSYLNL AENYFSRWVP HAPAIQKFHH
WKWTCWDRLE VPAGQPERTL ESLLAHVQKL NGLRVRMLLH GKALLYSAGW SPEKQDQHLS
RRVTDLVLEV TRQVPKPGQR VLVLELSYEG EKEDVTFPPL HYKL
//
