ID A0A1Q9DYX5_SYMMI Unreviewed; 1804 AA.
AC A0A1Q9DYX5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=E1 ubiquitin-activating enzyme {ECO:0000256|ARBA:ARBA00012990};
DE EC=6.2.1.45 {ECO:0000256|ARBA:ARBA00012990};
GN Name=UBA1 {ECO:0000313|EMBL:OLQ00381.1};
GN ORFNames=AK812_SmicGene16967 {ECO:0000313|EMBL:OLQ00381.1};
OS Symbiodinium microadriaticum (Dinoflagellate) (Zooxanthella
OS microadriatica).
OC Eukaryota; Sar; Alveolata; Dinophyceae; Suessiales; Symbiodiniaceae;
OC Symbiodinium.
OX NCBI_TaxID=2951 {ECO:0000313|EMBL:OLQ00381.1, ECO:0000313|Proteomes:UP000186817};
RN [1] {ECO:0000313|EMBL:OLQ00381.1, ECO:0000313|Proteomes:UP000186817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP2467 {ECO:0000313|EMBL:OLQ00381.1,
RC ECO:0000313|Proteomes:UP000186817};
RA Aranda M., Li Y., Liew Y.J., Baumgarten S., Simakov O., Wilson M., Piel J.,
RA Ashoor H., Bougouffa S., Bajic V.B., Ryu T., Ravasi T., Bayer T.,
RA Micklem G., Kim H., Bhak J., Lajeunesse T.C., Voolstra C.R.;
RT "Genome analysis of coral dinoflagellate symbionts highlights evolutionary
RT adaptations to a symbiotic lifestyle.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine
CC = AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-
CC L-cysteine.; EC=6.2.1.45; Evidence={ECO:0000256|ARBA:ARBA00000488};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:OLQ00381.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LSRX01000330; OLQ00381.1; -; Genomic_DNA.
DR OrthoDB; 20494at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000186817; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter 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; cd06257; DnaJ; 1.
DR CDD; cd17319; MFS_ExuT_GudP_like; 1.
DR Gene3D; 1.10.287.110; DnaJ domain; 1.
DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 2.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
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; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR032420; E1_4HB.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_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; IPR033127; UBQ-activ_enz_E1_Cys_AS.
DR PANTHER; PTHR10953:SF4; UBA_E1_C DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF16191; E1_4HB; 1.
DR Pfam; PF09358; E1_UFD; 1.
DR Pfam; PF07690; MFS_1; 1.
DR Pfam; PF00899; ThiF; 2.
DR Pfam; PF10585; UBA_E1_SCCH; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SMART; SM00985; UBA_e1_C; 1.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 3.
DR SUPFAM; SSF46565; Chaperone J-domain; 1.
DR SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS50850; MFS; 1.
DR PROSITE; PS00865; UBIQUITIN_ACTIVAT_2; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000186817};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT TRANSMEM 21..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 59..78
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 90..109
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 115..137
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 149..174
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 301..321
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 328..349
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 355..373
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 421..442
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 25..446
FT /note="Major facilitator superfamily (MFS) profile"
FT /evidence="ECO:0000259|PROSITE:PS50850"
FT DOMAIN 923..984
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT REGION 738..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 785..915
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1241..1267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 788..807
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..827
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 891..912
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1368
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10132"
SQ SEQUENCE 1804 AA; 199492 MW; 14529DDE787FB914 CRC64;
MRKAAPAESL SMLATQAAWK IKKRLLPIFV LVTVANYLDR GNISYAAEGL KQRLGLDDVG
YGAASSALFY TYVCFQWPHA WIAKRLGVRL WLAVVIALWG CATLLTAWVD SATELVLSRL
LIGFAEAGSF PLIYMHLDSY LPAEEVSRSW SVIVAASQVA SIVSGPLAAG LIQLPVNRMV
SAHWEWLFVV EGFFALVVAA VVYCCLLDDE GNGDMLHLTT EEKLALANAR GNSVHQAALP
KQTAAGSKCR LLSGGLLDWK AWYLGIVSLL IATPVYAFMF FSPELIHTIL GASASPWMVD
MLNGLPYLCG ALMMISVGQT INFFAERFYH GSVSMILAAV LAIGFPMVYE RSSPIVALVN
VCLLYGVAAA VYIPMDTMPS AYCSESAESY SILNSIKSIS GIIGPPLFGA VREAVDGPTA
IAVLGLSEVL GLTLFLIFFM LIGELKASVR CTELPTEQIE HSKSFDNEAS SDSDLQSAYR
CATALESQLL AKTSWKEGRA LPGFHLSAGS FQSKVPDMAK FGRSEQLHFA VQAVMAYREK
HGQLPPVRDA AAADECVQLA KDMNSARTSE GEPSVFVEEV EADVVKNVAM FARCMISPMA
AFLGGVVAQE VVKFTGKYTP LHQFLYLDMF ELCPASEPPD WKPLGSRYDD QIAIFGSAIQ
QAISNMKLFL VGAGALGCEF LKSFAMIGAS CGSGKVLVTD MDRIEISNLN RQFLFGQYCT
RASPRRLLPP ESKDCFRAAM GRGGGRGGGP KKGEVQANPA EANAVDPKVI SEILERLAKL
EKWKAKWKER KERKRQKKDK ADKKKQKRSL RKNEEEERTK KRAKKDVSSS PAPVSNAPPP
EVDAAVKKPT AAKSKPKAKA KNLAALPAPV KGEPSQGSHE QLARNAPKEA AKPVEAAKGE
QAKTEPEDAA NKVVPSDPRA AHCCYDMLQI DRTATVEQVK RAYRSLAIKM HPDKGGSHKA
FCALQLAFDV LQDEVERQAY DRELRESRSR DGQVGQAVDS APVVQPAAVS PVMLRDALMG
TPPRHWPEML KELLTVNLKL LQEFLNMSQQ QQNEVAKEHQ ESHPQHSKAG VPGICRSGNF
YYAKASRAHI SINSKPATLV EAIDANIALK QIWNIVKKYP DDLEGGLRRA VKERREIDQD
TIFFMRFRLD FRWESIRITT PQSSDVESML RDRRTLLQLA ERRASKEEFQ KAQQAMKENA
QEELVAQRNY ASVRQQLVAE VAREVLWRHA ADSRSLLSLK NRADEAASDP ESSDSDTTDV
GSSKSQVAAR AAKAMNADLK VDAMEVRVGP DTEDTFDDAF WDSLDCVVNA LDNIQARMYV
DSRCVWFSKP LLESGTLGTK ANVQVVLPKM TQSYGDSQDP PEESIPLCTV KHFPNAIEHT
IEWAREAFEQ LFVETPREGN SFLEDPESYL RKLPTTGSGT SQVQRLRSLQ YMLEKRTMPF
DACAEYAVME FQEKFHDSIV QLLHTFPLDH VTSEGTKFWS GPKRPPAPIK FDANDALHVD
FLLAAANLYA ASLGVPENRD RTAVARMAAA VKVPDFRPRE MKIKVDDKDT SGEACIDDDA
LARKLTVEMS EKVKSLKVTP DLRPAEFEKD DDSNFHIQFI AAAANLRARN YKIQEVDFLK
VKMTAGKIIP AIATTTAMVT GLVSAELLKI ATLRNRKVED FKNAFVTLAL PLWVLSEPLP
PLKTVSKEHD PIVMGPVKAR PEGFTTWDKV ECKLGDVTLK EFLDWLTAEV SIEVMIMSSG
NTCLYNSYIP AHKKRLQEKI TTLWETITKQ KLSQKKTYLT LEVSASDLDE GIDVVIPTVK
FQFR
//
