ID A0A0V1H027_9BILA Unreviewed; 1903 AA.
AC A0A0V1H027;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Cullin-4B {ECO:0000313|EMBL:KRZ03750.1};
DE Flags: Fragment;
GN Name=CUL4B {ECO:0000313|EMBL:KRZ03750.1};
GN ORFNames=T11_3509 {ECO:0000313|EMBL:KRZ03750.1};
OS Trichinella zimbabwensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ03750.1, ECO:0000313|Proteomes:UP000055024};
RN [1] {ECO:0000313|EMBL:KRZ03750.1, ECO:0000313|Proteomes:UP000055024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ03750.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-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:KRZ03750.1}.
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DR EMBL; JYDP01000183; KRZ03750.1; -; Genomic_DNA.
DR Proteomes; UP000055024; 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:SF126; 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000055024};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 240..261
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 273..293
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 314..339
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 359..384
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 405..425
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 445..466
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 238..426
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT DOMAIN 1546..1776
FT /note="Cullin family profile"
FT /evidence="ECO:0000259|PROSITE:PS50069"
FT REGION 774..859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..811
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 830..858
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRZ03750.1"
FT NON_TER 1903
FT /evidence="ECO:0000313|EMBL:KRZ03750.1"
SQ SEQUENCE 1903 AA; 216326 MW; 773D3CFEA4F8A3F2 CRC64;
LSYCSYAMLY DYCFLFLFLL NGISVVLNKN LTHDPSHFQK RLFPVDIVQQ YKGGGQRFFF
TNNWLNDPLC WRSTTEKCLT HDKELKCFGE TLATKEIYPL SVSTNANISG YENFYRLSHC
WPYLKEMLCS AMMAPCKNSR VRLISESLCI ETRDQCQFLI KHGRWPKILS NCQDSKLYSR
ECKQSLQPLF RHENTSTNRA SCLIPLVYSE HRDQLHFPNC AFNCTSHWLK PQEHEELDSV
VLFLAPIICT FLILTLIATV TGVRRIPKVF YPLAWKVFCH AVIALVVAFR FKFKYLVSCN
SDGSLRSKDQ KSSICTLQFV CLYLSTLASS GWLTVFFAFQ LAETLPSSSD FSHSVYDKLI
NNVHFALWGP CLLLVITVIS SMSYGPDGIN GMCYFGVDDP MNNFYLVYLP TGIALIMTTT
FFIITVARRH HISRAANAVA SQRRLWYGFS TAKLGILFST NLLLYVTDLG LHIYDMSMFY
KRNTALVDFF LCQLDHPYPS IHCKLMHTLN IALVKVGFLV QFLFPGLIDC AFLWLQSRYE
LDREAWLQLF RDKIGMIRNR SKMHGNRKGN INNDCKDECE LHSLQSAMDD DITTRYARTT
PLNSASASAV DVGTQSDSEL LTRHRSKREF IERFRKRSDM RYLRKHEAPS SSLSRTPSSL
RSCLLPTPLR VLSAPGMPFS TSSLQSLPAE GATVPGAGAG AGACAATWNP YYPYLQFYPA
PFNSSVWTSV MQAGCQFSVP QPAAPGLPQF TYPVCVNPAW FNGVAVASGA KSTEPYTACP
TESAPPAPST SSATGTKTDV PIQATSIVES STCDEKKTEM SRQISAEAAA AEEEDDDDDE
EEEEEPWDDS DFDSEEEEFV ERQLLAMKAQ QQQSCSTHTA NTLKEQNMLS TLVLCRSLVG
RLQWAAVRRS HDQLFVHRDT PDNNADVPFE FSEENMKRIE AIKAIYPVGY TSAAILPVLD
LAQRQHGWLP ISALNKVADV IGVPKMRIYE VATFYTMYNR QKVGKYHVQV CTTTPCMLRG
ADQILKHAKK ECLGNDAVGE SSDDFMFTVS EVECLGACAN APMMQINDDY YEDLTCDDVS
RILNEIRAGK KPKMGPQSGR LAAEPISGLT SLTSTPYGPG KFGDSSEKKN TSIIQVEAYV
VSGIHLGDIL KLSAMSSLMS ISCETPSDGS RCAKQSKFFT PPNRSETVRW TDNVRHHRPG
NIPLTFQSAN QSVCLVEEQL ECKWKKLEEP VWAILMQKSY KNSTEDLFST VDEIVRFIGK
SKWLYEKLFT FCEECVSKRS AVLMEGNLDA LSFSKLVMKI WKEHCSQMKS IRQIFSQLDR
SAALQEMPMM EMGLTIFRSH AIMRSSIQTK LVDSLLFLIH QERSGEDIYH EILEDRLLEE
TKTFYLEEGK RRIEVEDVPQ YLAYVTNQLK LESERTEFYL DKNSGKSLIS MVENGLISPH
VEDILNKGFD RMLYNSQLDD LKLLYQLISY DPANIEELKT RFVNYISVNV VSLLKGDEID
CEALRSLLNY RDFVSNVVTY CFSDSAVIDL AARSVFSSIV NKKSAKVNEL LAKFIDMKLR
TGRKQYPEEE LDQDTIKALS LFRIVDGKDL FEMFYQKFLA KRLLFGKSAS FDAEKAVLSE
LKRECGSDFT SKLEVMFRDF ETSKEFASGF KNYLIASNCL NSVVEMNVNV LTIGNWPSYP
KMDIIYPQVL LSSMSHFEHF YMDKHAGRKL SWQSYVGQCL LAARFKPGVE KELQVSLFQG
IILLLFNDSD QLSFKLIQQK TNIETMELRR TLQSLACGKF RVIQKVPKGK DVNENDTFVF
NANFNSPMLR IRINQIQSKE TNEENCMTVE QVNSNRVFSI DAAIVRILKT RKTISHSELM
SEMVRQLQFS VQASDVKKRI ENLIERRFIS RDIKNSSSYN YIS
//
