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Database: UniProt
Entry: A0A2Y9RNR3_TRIMA
LinkDB: A0A2Y9RNR3_TRIMA
Original site: A0A2Y9RNR3_TRIMA 
ID   A0A2Y9RNR3_TRIMA        Unreviewed;      1013 AA.
AC   A0A2Y9RNR3;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Ubiquitin-like modifier-activating enzyme 6 isoform X2 {ECO:0000313|RefSeq:XP_023593564.1};
GN   Name=LOC101354602 {ECO:0000313|RefSeq:XP_023593564.1};
OS   Trichechus manatus latirostris (Florida manatee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX   NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_023593564.1};
RN   [1] {ECO:0000313|RefSeq:XP_023593564.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-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}.
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DR   RefSeq; XP_023593564.1; XM_023737796.1.
DR   AlphaFoldDB; A0A2Y9RNR3; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000248480; 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; cd01490; Ube1_repeat2; 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; IPR018075; UBQ-activ_enz_E1.
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:SF186; UBIQUITIN-LIKE MODIFIER-ACTIVATING ENZYME 6; 1.
DR   Pfam; PF16191; E1_4HB; 1.
DR   Pfam; PF16190; E1_FCCH; 1.
DR   Pfam; PF09358; E1_UFD; 1.
DR   Pfam; PF00899; ThiF; 2.
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.
PE   3: Inferred from homology;
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248480}.
FT   DOMAIN          882..1004
FT                   /note="Ubiquitin-activating enzyme E1 C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00985"
SQ   SEQUENCE   1013 AA;  114287 MW;  F62ADABB5F10EC05 CRC64;
     MFSNHTCSYK FVCLFSVQIQ ICPLCRQNLW RLMMHYTAKN IVLAGIKALT IHDTENCQPW
     DLGTNFFICE DDVANMRNRA EAVLQHIAEL NPYVHVTSSS LPLNETTDLS FLDEYQCVVL
     TEIRLPLQKK INDFCRSQCP PIKFISADVH GIWSRLFCDF GDEFEVLDTT GEEPKEIFIS
     SITQANPGIV TCLENHPHKL ETGQFVTFRE INGMTGLNGS TQQITVVSPF SFSIRDTTEL
     EPYLHGGIAV QVKTPKIFYF ESLEKQIKHA KCLIADFSKP EAPLQIHTAM LALDQFRENY
     SRKPNVGCQQ DSEELLKLAT SISETLEEKP EVNADIVNWL SWTAQGFLAP LAAAVGGVAS
     QEVLKAVTGK FSPLCQWLYI EATDIVESLG KPECEEFLPR GDRYDALRAC IGDSLCKTLQ
     NLNIFLVGCG AIGCEMLKNL ALLGVGTGKE KGMVTITDPD LIEKSNLNRQ FLFRPHHIQK
     PKSYTAADAT LKINPQLKID AHLNKVCPAT ETIYNDAFYT KQDIIITALD NVEARRYVDS
     RCLANLRPLL DSGTMGTKGH TEVIVPHLTE SYNSHRDPPE EEIPFCTLKS FPAIIEHTIQ
     WARDKFESSF SHKPSLFNKF WQTYHSAEEV LQKIQTGHSL EGCFQVTKLL SRRPRNWSQC
     VELARLKFEK YFNHKALQLL HCFPLDTRLK DGSLFWQSPK RPPSPIKFDL NEPLHLSFIQ
     NAAKLYAMVY CIPFTEKDLS ADALLDILSD VKIQEFKPSN KVVQTDETAR KPDHVPISGE
     DERNAIFQLE KAISSNEATK SDLQMAVLSF EKDDDRNGHI DFITAVSNLR AKMYGIEPAN
     RFKTKRIAGK IIPAIATSTA AVSGLVALEM LKVAGGCPFE AYKNCFLNLA IPIIVFTETS
     EVRKTEIRNG ISFTIWDRWT VHGKEDFTLL DFINAVKEKY GIEPAMVVQG VKMLYVPIMP
     GHAKRLKLTM HKLVKPSTEK KYVDLTVSFA PDTDGDEDLP GPPVRYYFSH DTD
//
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