ID A0A0V1LR36_9BILA Unreviewed; 1945 AA.
AC A0A0V1LR36;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Cullin-4A {ECO:0000313|EMBL:KRZ61957.1};
GN Name=CUL4A {ECO:0000313|EMBL:KRZ61957.1};
GN ORFNames=T02_8348 {ECO:0000313|EMBL:KRZ61957.1};
OS Trichinella nativa.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ61957.1, ECO:0000313|Proteomes:UP000054721};
RN [1] {ECO:0000313|EMBL:KRZ61957.1, ECO:0000313|Proteomes:UP000054721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS10 {ECO:0000313|EMBL:KRZ61957.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|ARBA:ARBA00034078};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor Fz/Smo family.
CC {ECO:0000256|ARBA:ARBA00008077}.
CC -!- SIMILARITY: Belongs to the complex I 24 kDa subunit family.
CC {ECO:0000256|ARBA:ARBA00010643}.
CC -!- SIMILARITY: Belongs to the cullin family.
CC {ECO:0000256|ARBA:ARBA00006019, ECO:0000256|PROSITE-ProRule:PRU00330,
CC ECO:0000256|RuleBase:RU003829}.
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:KRZ61957.1}.
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DR EMBL; JYDW01000013; KRZ61957.1; -; Genomic_DNA.
DR Proteomes; UP000054721; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:InterPro.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd03064; TRX_Fd_NuoE; 1.
DR Gene3D; 1.20.1310.10; Cullin Repeats; 4.
DR Gene3D; 1.10.2000.10; Frizzled cysteine-rich domain; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 1.10.10.1590; NADH-quinone oxidoreductase subunit E; 1.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR045093; Cullin.
DR InterPro; IPR016158; Cullin_homology.
DR InterPro; IPR036317; Cullin_homology_sf.
DR InterPro; IPR001373; Cullin_N.
DR InterPro; IPR019559; Cullin_neddylation_domain.
DR InterPro; IPR016159; Cullin_repeat-like_dom_sf.
DR InterPro; IPR000539; Frizzled/Smoothened_7TM.
DR InterPro; IPR036790; Frizzled_dom_sf.
DR InterPro; IPR017981; GPCR_2-like_7TM.
DR InterPro; IPR002023; NuoE-like.
DR InterPro; IPR042128; NuoE_dom.
DR InterPro; IPR041921; NuoE_N.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR NCBIfam; TIGR01958; nuoE_fam; 1.
DR PANTHER; PTHR11932; CULLIN; 1.
DR PANTHER; PTHR11932:SF123; CULLIN 4, ISOFORM A; 1.
DR Pfam; PF01257; 2Fe-2S_thioredx; 1.
DR Pfam; PF00888; Cullin; 1.
DR Pfam; PF10557; Cullin_Nedd8; 1.
DR Pfam; PF01534; Frizzled; 1.
DR SMART; SM00182; CULLIN; 1.
DR SMART; SM00884; Cullin_Nedd8; 1.
DR SMART; SM01330; Frizzled; 1.
DR SUPFAM; SSF75632; Cullin homology domain; 1.
DR SUPFAM; SSF74788; Cullin repeat-like; 1.
DR SUPFAM; SSF63501; Frizzled cysteine-rich domain; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS01099; COMPLEX1_24K; 1.
DR PROSITE; PS50069; CULLIN_2; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000054721};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 216..237
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 289..318
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 338..363
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 383..403
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 424..445
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 214..405
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT DOMAIN 1582..1818
FT /note="Cullin family profile"
FT /evidence="ECO:0000259|PROSITE:PS50069"
FT REGION 749..775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 804..831
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 813..831
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1945 AA; 221802 MW; 3864971B619C07F3 CRC64;
MRMQTYLSIA LLHLQKRLFP VDIVQQYKGG GQRFFFTNSW LNDPLCWRST TEKCLTHDKE
LKCFGETLAT KEVYPLSIIT NANTSGYENF YRLSHCWPYL KEMLCSAMMA PCKNSRVRLI
SESLCIETRD QCQFLIKHGR WPKILSNCRD SKLYSRDCKQ SLQPLFRHEN ISTNRASCLL
PLVYSEHRDQ LHFPNCAFNC TSHWLKPQEH EELDSVVLFL SPIICTFLIL TLIATVTGVR
RIPKDFYPLA WKIFCHAVIA LVIAFRFKFK YLVSCNSDGS LRSKDQKHFR SSICTLQFVC
LYLSTLASSG WLTVFFAFQL AETLPSSSDF SHSVYDKLIN NVHFALWGPC LLLVITVISS
MSYGPDGING MCYFGVDDPM NNFYLVYLPT GIALIMTTTF FVITVARRHH ISRAANTVAS
QRRLWYGFST AKLGILFATN LLLYVTDLGF HIYDMSMFYK RNTALVDFFL CQLDHPYPSL
HCKLMHTLNI ALVKVGFLVQ FLFPGLIDCA FLWLQSRYEL DREAWLQLFR EKIGMIRNRS
KMHGNRKGNL NNDCKDECEL HSLQSAMDVQ ITTNRYARTT PLNSASGSAV DVGTQSDSEL
LTRHRSKREF IERFRKRSDM RYLRKHEAPS SSLSRTPSSL RSCLLPTPLR VLSAPGMPFS
TSSLQSLPAE GAAVPDAGAC AATWNPYYPY LQFYPAPFNN SVWTNVMQAG CQFTVPQPAA
HGLPHFTYPV CVNPAWFNGV AAVASGAKST EPGVACPTES APPAPSASAA SGTTKTDVPV
QAASCRVAES STCDQKKMEK SRQISAAAAA AASADDDEDE EPWDDSDFDS EEEEFVERQL
LAMKAQQQQS PSALKEQNYL FLHFQQMLSA MVLCRSWLVG RLQWAAVRRS HDQLFVHRDT
PDNNADVPFE FSEENMKRVE AIKALYPVGY TSAAILPVLD LAQRQHGWLP ISAMNKVADV
IGVPKMRIYE VATFYTMYNR QKVGKYHVQV CTTTPCMLRG ADQILKHVKK ECLGSDAVGE
TSQDFMFTVS EVECLGACAN APMMQINDDY YEDLTYDDVT RIFGEIRAGK KPKMGPQSGR
LAAEPISGLT SLTSTPYGPD KFGDSGEKKN TLIIPMETYV ILENYFYKKS RNCIWGRVIV
SSVVVSGIHL GDILKLSAYF SLKMSSLISI NRETRSDGSR SAKQSKFLTP PNRSETVRWT
DNVRHHQPGN IPLTFQSDCC KWLNTNQSIC LMEEQLECKW KKLEEPVWAI LMQKSYKNST
EDLFSTVDEI VRFIGKSKWL YEKLFTFCEV CVSKRSAVLM EGNLDALSFS KLVMKIWQEH
CSQMKSIRLI FSQLDRSAAL QEMPMMSIWE MGLTIFRSCA IMRSSIQTKL VDSLLFLIHQ
ERSGEDVDHL LIRNLLHMFA TLNIYREILE VRLLEETKTF YLEEGMRRIE VDDVPHYLAY
VTKQLKLESE RTEFYLDKNS GKSLISVVED GLISPHVEDI LNKGFDCMLY NSQLDDLKLL
YQLISYDPAN IDELKMRFSN YISVNVMSFL KGDEIDCEAL RSLLKYRDFV SNVVSYCFSD
SAGIDLAARS VFSSIVNKKS AKVNELLAKF IDMKLRTGRK QYPEEELDQE TVKALSLFRI
VDGKDLFEMF YQKFLAKRLL FGKSASFDAE KAVLSELKRE CGSDFTSKLE VMFRDFETSK
EFASGFKNYL TASNCLNSVV EMNVSVLTIG NWPSYPKMDI IYPQVLLSSM SQFEHFYMEK
HAGRKLSWQS YVGQCLVAAR FKPGVRCTLF VEKELQVSLF QGIVLLLFND SDQLSFKSIQ
QQTNIETVEL RRTLQSLACG KFRVIQKVPK GKDVNENDTF IFNANFTSPM LRIKINQIQS
KETNEENFMT VEQVNSNRVF SIDAAIVRIL KTRKTISHSE LMSEIVRQLQ FSVQASDVKK
RIENLIERRF ISRDVKNSSN YNYIS
//