ID A0A6G0IQF9_LARCR Unreviewed; 1871 AA.
AC A0A6G0IQF9;
DT 12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT 12-AUG-2020, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=Ubiquitin-like modifier-activating enzyme 1 {ECO:0000313|EMBL:KAE8293523.1};
GN ORFNames=D5F01_LYC08635 {ECO:0000313|EMBL:KAE8293523.1};
OS Larimichthys crocea (Large yellow croaker) (Pseudosciaena crocea).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Sciaenidae; Larimichthys.
OX NCBI_TaxID=215358 {ECO:0000313|EMBL:KAE8293523.1, ECO:0000313|Proteomes:UP000424527};
RN [1] {ECO:0000313|EMBL:KAE8293523.1, ECO:0000313|Proteomes:UP000424527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JMULYC20181020 {ECO:0000313|EMBL:KAE8293523.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAE8293523.1};
RA Xiao S.;
RT "Chromosome genome assembly for large yellow croaker.";
RL Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
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}.
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:KAE8293523.1}.
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DR EMBL; REGW02000008; KAE8293523.1; -; Genomic_DNA.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000424527; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
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 CDD; cd01490; Ube1_repeat2; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
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; 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:SF195; UBIQUITIN-LIKE MODIFIER-ACTIVATING ENZYME 1; 1.
DR Pfam; PF16191; E1_4HB; 1.
DR Pfam; PF16190; E1_FCCH; 1.
DR Pfam; PF09358; E1_UFD; 1.
DR Pfam; PF00069; Pkinase; 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.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
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:UP000424527};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU000519}.
FT DOMAIN 24..286
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 331..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 715..861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..745
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 746..779
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 831..855
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1446
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 1871 AA; 205701 MW; A3F8ECCFF249AAFE CRC64;
MPFGCLALRD GRTYDSMSDV TDKYEIGQVL RAKEFCELCL AKDRQTDKVF VCKKFLKKDG
RKVRKAAKNE IMILKLVNHP NILQLIDTFE TRKEYFIIQE LATGGDVFDW ILDQGNYTER
DASNVIRQVL EAVAYLHSLN IVHRNLKLEN LMYYTENNHN KVVLRDFYLS RFENGPITEP
CGTPEYLAPE VVARHRYGRP VDCWAVGVIM FILLSGNPPF YDETEEENTD LHNRIIFCRI
VAGDFEFDSP YWDDISPAAK ELVCRLMEVD QMLRITAQDA LWHEWIAGNG ASEKNLKDGV
CAQFEKNFAK AKWRKAIRVT TFMQRLKNSE ALTDSSAEVQ GSEEAGDGEG GVSQGTSDEG
DKGTSDGGVT SSSVSLEVTV ESTPPGMDQD EERGKDEENW PIGPSVGISP SDMQEPLCQQ
SQSITDPKIT QEQPDKVGAK KAASDGTRKM AANLGQNKAV PESKLSPMMM PGPSMLSEGS
SSTTLDKKHT SASPDPSSKR KMAATLHGPP PTGSTAATGS PGKRPAMPRE QKDETDGSWC
QTQVPEAVAE RSVVAAATVT PAILPGAGVD VGLGVTLRGD ASPMGRQDRD VRRTDRHSAE
FSIARAGPAA GQGCYSVGSS ASLGRHATPY NPDVGSAGLG MAGSYGSPYS SLYTSGGGVG
MYGTGLQHGG GGSCATTDWQ MDSVIEQIEK QMAAVLEKIE GDMPSLLEQI SDCPAEAPRA
RSTHASPATS RARSTQHSST ATSATPPPLP TSPRPALPSL PRLTIPPPSY PPPSPPTQSS
PKAVGEQEDR DGQRDAARSG QSPRAGMGRV ISDVMSSSPL SKKRRLSGSE TKTGSHCSSS
NSVRTDLSHT PANGMAKNGN DAEIDEGLYS RQLYVLGHDA MKRMQNSNVL ISGMRGLGVE
IAKNVILGGV RSVTVHDQGV AEWRDLSSQF YLREEDLGKN RAEVSQPRLA ELNNYVPVTA
YTGTLADEYL TKFQVVVLTN STLEEQQQVG EFCHSKGIKL IIADTRGLFG QLFCDFGEEM
MVYDTNGEQP LSAMISMITK DNSGVVTCLD EARHGFESGD FVTFTEVQGM TELNGCQPVE
IKVLGPYTFS ICDTAGFTDY VRGGIVSQVK MPKKIAFKSI SSSMAEPEFM MTDFAKFDRP
GQLHVGFQAI HAFQKKHNQL PVPWSQADGD ELLTLAKEVN SAQTGSAKVE ELDEALLKKL
SYVAAGDLAP VNAFIGGLAA QEVMKACTGK FMPIMQWLYF DALECLAEEE GVLLTEEECA
PRNCRYDGQI AVFGSKLQDL LGKQRYFLVG AGAIGCELLK NFAMIGLAGG EGEVIVTDMD
TIEKSNLNRQ FLFRPHDVTK MKSDTAAAAV KQMNPSIRIT GHQNRVGPDT ERVYDDDFFE
SLDGVANALD NVDARMYMDR RCVYYRKPLL ESGTLGTKGN VQVVIPFLTE SYSSSQDPPE
KSIPICTLKN FPNAIEHTLQ WARDEFEGLF KQPPENAMQY LTDPKFMERT LKLPGAQPVE
VLEAVYKSLV TDCPHSWADC VAWARNHWQC QYSNNIRQLL HNFPPEQLTS SGAPFWSGPK
RCPHALEFST SNDLHMDYVM AAANLYAQTY GVQGSTDRAG VIKILQDVKV PPFTPRSGVK
IHVSDQDLQN SNSSVDDSRL EELKVQLPSS DSSKFKLSPI DFEKDDDTNF HMDFIVAASN
LRAENYDIPP TDRHKSKLIA GKIIPAIATT TAAVVGLVCL ELIKIVQGHK KLESFKNGFM
NLALPFFAFS EPIAAPRHKY YEIDWSLWDR FEVTGLQPNG EEMTLRQFLD YFKNEHKLEI
TMLSQGVSML YSFFMPAAKL KERLDLPMTE IVTKVSKKKL GKHVKALVFE LCCNDLSDED
VEVPYVRYTI R
//
