GenomeNet

Database: UniProt
Entry: B0WMP8_CULQU
LinkDB: B0WMP8_CULQU
Original site: B0WMP8_CULQU 
ID   B0WMP8_CULQU            Unreviewed;      1141 AA.
AC   B0WMP8;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   24-JAN-2024, entry version 84.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   Name=6040606 {ECO:0000313|EnsemblMetazoa:CPIJ008431-PA};
GN   ORFNames=CpipJ_CPIJ008431 {ECO:0000313|EMBL:EDS31133.1};
OS   Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Culicinae; Culicini; Culex; Culex.
OX   NCBI_TaxID=7176;
RN   [1] {ECO:0000313|EMBL:EDS31133.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JHB {ECO:0000313|EMBL:EDS31133.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.,
RA   Hannick L., Megy K., O'Leary S., Pearson M., Haas B.J., Mauceli E.,
RA   Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA   Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA   Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA   Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA   Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA   Fraser-Liggett C., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT   "Annotation of Culex pipiens quinquefasciatus.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:CPIJ008431-PA}
RP   IDENTIFICATION.
RC   STRAIN=JHB {ECO:0000313|EnsemblMetazoa:CPIJ008431-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
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; DS232000; EDS31133.1; -; Genomic_DNA.
DR   RefSeq; XP_001849975.1; XM_001849923.1.
DR   AlphaFoldDB; B0WMP8; -.
DR   STRING; 7176.B0WMP8; -.
DR   EnsemblMetazoa; CPIJ008431-RA; CPIJ008431-PA; CPIJ008431.
DR   KEGG; cqu:CpipJ_CPIJ008431; -.
DR   VEuPathDB; VectorBase:CPIJ008431; -.
DR   VEuPathDB; VectorBase:CQUJHB007506; -.
DR   eggNOG; KOG3161; Eukaryota.
DR   HOGENOM; CLU_291380_0_0_1; -.
DR   InParanoid; B0WMP8; -.
DR   OMA; WRECSTA; -.
DR   OrthoDB; 2909513at2759; -.
DR   Proteomes; UP000002320; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.120.1790; -; 1.
DR   Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 1.
DR   InterPro; IPR041523; ROQ_II.
DR   InterPro; IPR048575; Roquin_1_2-like_ROQ.
DR   InterPro; IPR000571; Znf_CCCH.
DR   InterPro; IPR036855; Znf_CCCH_sf.
DR   PANTHER; PTHR13139; RING FINGER AND CCCH-TYPE ZINC FINGER DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR13139:SF54; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR   Pfam; PF18386; ROQ_II; 1.
DR   Pfam; PF21206; Roquin_1_2-like_ROQ; 1.
DR   Pfam; PF00642; zf-CCCH; 1.
DR   SMART; SM00356; ZnF_C3H1; 1.
DR   SUPFAM; SSF90229; CCCH zinc finger; 1.
DR   PROSITE; PS50103; ZF_C3H1; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00723}; Reference proteome {ECO:0000313|Proteomes:UP000002320};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00723}.
FT   DOMAIN          387..415
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   ZN_FING         387..415
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT   REGION          32..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          429..833
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          955..1003
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1018..1052
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1059..1078
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        485..507
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        508..534
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        535..550
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        555..574
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        610..643
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        647..672
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        695..741
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        765..779
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        789..833
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1018..1049
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1062..1078
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1141 AA;  124881 MW;  2ECC8CE8D74569D7 CRC64;
     MSVPALTIIT TDLDNLPVNN ALLQLVSTSN TAVSSPGNNG NGGSSSSASS SLGSSADPDL
     CSPSVQNLCP DDLQCYKIAR GCIEELALYL KPYPNGNAGG LLSRPMQRKL VTLVNCQLIE
     DEGRARSLRA ARSLGERTVT ELILQHQNPQ QLSTNLWAAV RARGCQFLGP AMQEEVLKLV
     LLALEDGSAL SRKVLVMFVV QRLEPHFPQA SKTSIGHVVQ LLYRASCFKV SKREGDSSLM
     QLKEEFRTYE ALRREHDAQI VQIATEAGLR IAPDQWSSLL YGDTAHKSHM QSIIDKLQTP
     QSFVQSVQEL IIALQRTGDP ANLSGLRMHL KHLAGIDSNA ENHVPTWREC STALEAVKRV
     VIGLVDFVQH HGNRKLQEPG HLAHNSKYKI SLCRDLNLRG TCPRGPNCTF AHSEEELEKY
     RTKLRTKNIR TPNGKDHVGV GEYMGDLGMP SGSQHGGYHS SGEEASPLRY PKSTPPMRYL
     DKSPMSSHSH ASHGSSSNSN SSHNSHLAPI PAPPPPHIQP HHPSSYPNVP PQPSPLQQQH
     GANGGRSFNF NPSMPYGARP PPPPMQPPPS VRGNFIRPPN GNYNMGHHPP LPPMPHNGPM
     QNHHTYPGSG GQPVPPPQLE QMHPPPPPPP MMNAPPPPYL GQGYPNEYPN TADNNNKMDQ
     RRQFNPWDTQ QPPPQQSGHP APPPVNMMGH QTPKSYHPQP PPPSMMGKVG HMPPPQHHPL
     PQQQQQPPPP SLAPPPPQQH QQQSHPNAGK FYPTAGNGPL HHHVAAAAKQ RDYREKHHNG
     GRHMPPHGGG SHSQQQHPVA AYGNGNRSSM HTPLPQNPTQ ATPSSQTSNG GTMMNGYHGG
     SAFPFNRSEA QELFKILGSS NAAELAQFAT MAGAVQDKFV RSDSLLADDD LVIPENDYSS
     AGSVTGAKFG PISRMTNNLL GSGAGKQRGE FPFASSLLDA DWLQNLQHHL YNDSLGEQSS
     SNCSSTSSSF YQNSHPNQQQ QQLPVSAAHT NSKQHEPNNN TLDLDLFQVD RKLADFGTGA
     DNQSNVTSQL LHHHQQQQQQ QQQSQHHPHH TMAAAAAALL SSHHHHQQQQ QQQQFAQQHA
     AALQQQQQQH VMQKLQSVLA DPVQRFSDLM VNGGGGGVQS ELKIHSLKDV KVRGHYRYYD
     T
//
DBGET integrated database retrieval system