ID A0A068Y639_ECHMU Unreviewed; 1290 AA.
AC A0A068Y639;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Ubiquitin modifier activating enzyme 6 {ECO:0000313|EMBL:CDS37646.1};
GN ORFNames=EmuJ_000491100 {ECO:0000313|EMBL:CDS37646.1};
OS Echinococcus multilocularis (Fox tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus.
OX NCBI_TaxID=6211 {ECO:0000313|EMBL:CDS37646.1};
RN [1] {ECO:0000313|EMBL:CDS37646.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23485966; DOI=10.1038/nature12031;
RA Tsai I.J., Zarowiecki M., Holroyd N., Garciarrubio A., Sanchez-Flores A.,
RA Brooks K.L., Tracey A., Bobes R.J., Fragoso G., Sciutto E., Aslett M.,
RA Beasley H., Bennett H.M., Cai J., Camicia F., Clark R., Cucher M.,
RA De Silva N., Day T.A., Deplazes P., Estrada K., Fernandez C., Holland P.W.,
RA Hou J., Hu S., Huckvale T., Hung S.S., Kamenetzky L., Keane J.A., Kiss F.,
RA Koziol U., Lambert O., Liu K., Luo X., Luo Y., Macchiaroli N., Nichol S.,
RA Paps J., Parkinson J., Pouchkina-Stantcheva N., Riddiford N., Rosenzvit M.,
RA Salinas G., Wasmuth J.D., Zamanian M., Zheng Y., Cai X., Soberon X.,
RA Olson P.D., Laclette J.P., Brehm K., Berriman M., Garciarrubio A.,
RA Bobes R.J., Fragoso G., Sanchez-Flores A., Estrada K., Cevallos M.A.,
RA Morett E., Gonzalez V., Portillo T., Ochoa-Leyva A., Jose M.V., Sciutto E.,
RA Landa A., Jimenez L., Valdes V., Carrero J.C., Larralde C.,
RA Morales-Montor J., Limon-Lason J., Soberon X., Laclette J.P.;
RT "The genomes of four tapeworm species reveal adaptations to parasitism.";
RL Nature 496:57-63(2013).
RN [2] {ECO:0000313|EMBL:CDS37646.1}
RP NUCLEOTIDE SEQUENCE.
RA Zhang Y., Guo Z.;
RL Submitted (NOV-2015) 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}.
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DR EMBL; LN902843; CDS37646.1; -; Genomic_DNA.
DR STRING; 6211.A0A068Y639; -.
DR eggNOG; KOG2012; Eukaryota.
DR OMA; WSHCVEL; -.
DR UniPathway; UPA00143; -.
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; 3.50.50.80; 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 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; IPR019572; UBA_E1_SCCH.
DR InterPro; IPR042063; Ubi_acti_E1_SCCH.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR InterPro; IPR000011; UBQ/SUMO-activ_enz_E1-like.
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; 3.
PE 3: Inferred from homology;
KW Ligase {ECO:0000256|ARBA:ARBA00022598}.
FT DOMAIN 1161..1283
FT /note="Ubiquitin-activating enzyme E1 C-terminal"
FT /evidence="ECO:0000259|SMART:SM00985"
FT REGION 592..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1290 AA; 142579 MW; 4BE531E0E4F335E6 CRC64;
MFPSFEEQRP QEIDDSFYSR QRYVIGDDAM RRLSDSCVLI CGLGGVGVEI AKNLVLAGVR
ELILDDSTVC SAEDLATQFY VHPEDVAQGR TRAEASQKAL AALNPYVHVS IKTRTRANEG
VDIDQEINTL PACKIHCMVI TDSHLFFAAL LNNYCRQHHV KFVYANTIGT FGNVFCDFGP
NIKFSPPDEE PPSTFFIESI ENAEKPKLVI RAFEQHKISD GGFITFNEVT GMVELNGKIV
QVKEISPRVL ELDIDTRTFG KFTGNGLATE VKQAPNVTHL PLAKQLEDPK LSIVDLVNPD
SAAQMHVAFI ALMAFIYTKK QLPKAWFKKD ATLFLKLAER FRLRNMKIDT TLLERICFTS
RGQLPPLCSF FGGVAAQEVI KAVTCRFTPL NQWMYFGADS VIPSEIPRNS GLSVEPRYRP
LVRCIGPQNM RKVAMASTFM VGCGAIGCEL LKNLALLGLA SGAPQAAAAE LSSNLSNSAT
SPSPDDETSA ISSEIVEDDD NEELMPLIIR DFHHMVIELS HLGMELDVFR PYQLDHGDTF
PVADGDLQST PVASLEMPTM GTTHSPSATR STMTALLTDA STGAVTAVAG PKGESATELP
EDENFAPLGS PATSSSTSFY RIDERELLRL PMITRVSSQS DYDADVESMA QQTFSCPQPT
TTTATVATNT DANTNANTCD GPCITITDMD HIEKSNLNRQ FLFHSEHVGL AKSNVAAESI
RQINPALKVV ALQEKLDSNT EGGVFTDDFL QIAASGKDKS GPPIVLAALD NIKGRRYLDT
RCVANRLVMF DSGTQGTKGH TQVILPGITE SYSSQKDPPE EEGASDVVPY CTLKSFPAKA
SDCVEWAREK FFTQFTLKPQ GMDRFLRAFG YSCKELQDAL QTILAKGPSD WWPNDATPRN
VFLRCLNMPQ LTFFNSRPRT WKECICLGRE KFEKYFTHKA LHLLYKFPAD KVLKGGEPFW
QLPRRKPRPL TFDVSNKLHV DFVWSFARLL GKQAGIHIPS MSVPAMAASF VKEALIDFTP
KPYVPSDKEV IVDTSVSRPT PLDGPSSCPT ADDEFHAQLE IAIARLSDPD CRLTCQSIEF
DKDNEKDGHI DFISAATNLR AAMYGLPETG RYEVKRIAGR IIPAIATTTA AVAGLVSLEV
LKYICFSGTA SETECLTSHS RNNFVNLSLP SVISVLPGLC VAKNLPNNTH FTVWDRWEMK
LPTKKSTLKE FIDLLELKYG LNVSLITQNC RPIYMTLLPN FECNLPKPML SLLTYTPKDT
YVDLVIVYEG KGDDDDDVEG PPFRLILPTD
//
