ID A0A6P9A880_THRPL Unreviewed; 2604 AA.
AC A0A6P9A880;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 18-JUN-2025, entry version 21.
DE RecName: Full=RanBP-type and C3HC4-type zinc finger-containing protein 1 {ECO:0000256|ARBA:ARBA00017887};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN Name=LOC117651989 {ECO:0000313|RefSeq:XP_034252506.1};
OS Thrips palmi (Melon thrips).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Thysanoptera; Terebrantia; Thripoidea; Thripidae;
OC Thrips.
OX NCBI_TaxID=161013 {ECO:0000313|RefSeq:XP_034252506.1};
RN [1] {ECO:0000313|RefSeq:XP_034252506.1}
RP IDENTIFICATION.
RC TISSUE=Total insect {ECO:0000313|RefSeq:XP_034252506.1};
RG RefSeq;
RL Submitted (MAR-2025) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC EC=2.3.2.31; Evidence={ECO:0000256|ARBA:ARBA00001798};
CC -!- SIMILARITY: Belongs to the RBR family. {ECO:0000256|ARBA:ARBA00008278}.
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DR RefSeq; XP_034252506.1; XM_034396615.1.
DR FunCoup; A0A6P9A880; 9.
DR EnsemblMetazoa; XM_034396615.1; XP_034252506.1; LOC117651989.
DR GeneID; 117651989; -.
DR KEGG; tpal:117651989; -.
DR InParanoid; A0A6P9A880; -.
DR OrthoDB; 9978677at2759; -.
DR Proteomes; UP000515158; Unplaced.
DR GO; GO:0071797; C:LUBAC complex; IEA:InterPro.
DR GO; GO:0036435; F:K48-linked polyubiquitin modification-dependent protein binding; IEA:TreeGrafter.
DR GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; IEA:TreeGrafter.
DR GO; GO:1990450; F:linear polyubiquitin binding; IEA:TreeGrafter.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:TreeGrafter.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0097039; P:protein linear polyubiquitination; IEA:TreeGrafter.
DR GO; GO:0060255; P:regulation of macromolecule metabolic process; IEA:UniProtKB-ARBA.
DR CDD; cd19815; Bbox1_HOIP; 1.
DR CDD; cd20337; BRcat_RBR_HOIP; 1.
DR CDD; cd20351; Rcat_RBR_HOIP; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 6.10.140.1100; -; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR Gene3D; 2.30.30.380; Zn-finger domain of Sec23/24; 1.
DR InterPro; IPR047543; Bbox1_RNF31-like.
DR InterPro; IPR047540; BRcat_RBR_RNF31-like.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR047542; Rcat_RBR_RNF31-like.
DR InterPro; IPR026254; RNF31-like.
DR InterPro; IPR032065; RNF31-UBA.
DR InterPro; IPR041031; RNF31_C.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR16004:SF2; E3 UBIQUITIN-PROTEIN LIGASE LUBEL; 1.
DR PANTHER; PTHR16004; RING FINGER PROTEIN 31-RELATED; 1.
DR Pfam; PF18091; E3_UbLigase_RBR; 1.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF22191; IBR_1; 1.
DR Pfam; PF16678; UBA_HOIP; 1.
DR SMART; SM00647; IBR; 1.
DR SMART; SM00547; ZnF_RBZ; 1.
DR SUPFAM; SSF90209; Ran binding protein zinc finger-like; 1.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000515158};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 2095..2337
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 2099..2148
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 760..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 808..828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1098..1312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1391..1510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1571..2012
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..10
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..53
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..70
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..148
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..170
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..281
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..442
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..522
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..594
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..681
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..702
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 760..771
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1108..1157
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1172..1186
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1194..1224
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1233..1272
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1273..1297
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1411..1428
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1455..1468
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1482..1493
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1581..1594
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1601..1616
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1627..1638
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1657..1672
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1674..1690
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1699..1746
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1750..1764
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1782..1793
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1794..1809
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1810..1822
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1840..1873
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1876..1897
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1905..1955
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1965..2009
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2604 AA; 287845 MW; 35576E109DC64158 CRC64;
MQNHGADRWR AGSMGPTTGT LPAANTKFRS ARPMPAWVHQ QQQAQARLLN ARLPPHEPPP
PPTSEPPPLD PDYEVIEFPS QQYINTQPSQ AKTNGSAGGR RGDGKHCDLC GSSTPAVRCD
QCASQIFCYS CDDMYHRHPK RTTHRRKPLQ QAVRPPLPPK GEAPAAPVPP PRRKGRSSRM
GTPSPLDGQR SMLAGPSPSL PCLPEDCMPS RFRGRDDWSP LDARVRAHQI AMGRASPSLS
GHFPSSRDSG YPDWDSEQQQ GWSRQRSSSI SGSDGYRSGS GLAPGRFTDG MAGGLATMRR
GATPQRGIGI MSSASVSNLH QQHAMQQQPP FGMMQAQSMA HLGGCPSCAC HPGGPGAPPG
MVWMDGMGTP MGAPMGAWDG GTLHRHNSMG MLPSVKSRLS VRSRTRHAPE PVRAPTPISV
TDSDEEDADE DVDEEADDVD DAEHERAQAP AAAPPAGLPK TQWECEHCTF INKPGTRICT
VCCKTSDNPR PAGPAQPQGP AMQRRLSQSS ADRVAPARTA AARRMKTEAL PKPARNQIQQ
EEEDDDEEEE EEDVEEAQEE VEDDEDEEVD EEAEGESAQE ESVEDEEEEV EEEVAPQKRR
AHSKQLQQQQ LMQQQLQQQP KNAKAMKQAQ NKGIQKTAAA AKPLATKASA AQQTTASTAS
KPAQAPAAAP APAKQTNKAP KVSTGVGPSP PRDIPDKDHN QGREAAPASQ KKGTKMMTSK
GTSPPPQNMS TQRDPRRLRR AQSVGLADDI HWAQLQRSLS RQSLNSDSQS LPMSPRELSP
ARSYAGGLSN RFLEDDMPDV AYPVRPGRGL QRWDRRPSAS DYSTTSTFQR DRLENRSLTF
QPLERALERS RRSMSRAGSQ PPDYFHTIED MMHMQTRAES MKTQGLELVR LLREAEVLGF
TAEDLQAALA HCGDRPPIAW LQENWRNMMD TVVTLATNYG HERRENTVGT ISVDEARDAL
RAHKGNVWSA VTECVEQRQK KYAELLSRGN FTREDIVTSL TANHGNLEAA YVELSRTQLK
PFLMRIWGPP SVGTDNEAGN MAVVGAEDGV EAARHGAEAA ASRKSSLLSA PHDGDEDDSA
ADFVDARSDV ELDAAVSPRP EMADATSAPP VQQKAVQQVQ QEQRTQAEQP AKPQAEPPQQ
KGAAKAKADK APQTQAKVPT TKQAKPTEKT KPPQAVRPPQ QVQSAQLVQR IQMVQAPQQV
QPPKQVQKQV PPQQVQPPLQ VLPPQQVPPP QQVQPQQVQP QQQVQPPQQV QPPQQVQPSQ
QEQPPEQVQP PQQVLPPQPV QPPQPPQQVH PPQPPQQVQP APQVPGTQPF SLGGLVMNAA
ASAAALTLAG VAADPVESAA GPSVGQGNDG HLDQTIDRLE KEISQLKLLT GQTAGPENNI
ESLIERVKEV RRSQSEVGGG GQEATPAAEP GAKDAAQDGV KEANDNDKGT TTVAVHAKLH
IDQAGVATPK LERRPSRREH RKKDRKSHIS VQEAKGPQIT LAKEKQDEKK EADAVVPPVA
PPRRPERHER RLVAAAAPAV LRPVVSRIPM PVRAVLGVVE EAPHAQDLLH GVPESEKQAL
SLYAKRIQNA IAAEKARPEP EPADEDSDDD DADSLENNAS TREDLVRQDT VVEVKRPARA
PQPDAANAKD AKDAKEGPRG MQQQLELFKQ KRLQQQQHKD AVKRQQSEEK PKPQSKQSPK
QQQPKPAEQP KQPPKPQEQP RQQQVKPQEQ PKQQQAKPQE QPRQQQAKPQ EQPRQQQAKP
QEQPRQQHVK PQEKPDQHRA KPPELPKQPL TKLQEQPKQA VTKPAQQTKQ RQQTKQEDLT
KQTHAKQEPP KQQQVKQEQP AKPLDRLKQQ AVQKPPSKLP QPTQSKVQQQ QPPSKQQQTV
QQPPVVAKPA APQIVLDEED SDEYETEEEY EDGDEEPRDN KLAEADVDVD DEEYEDEEEA
DEEEEAEEEE VEEEVEDEEE VDEDVEEDDE SDDDELKTAW DGIEVEVKEK DIVIEKEKDN
AKDNLREKGK DSEKEKEKDD EKEKDKEKSA STATVEIVPI IKERVVLQPA AELPKEVKER
LEREREARRF LAEGLVTSYD EAELAAQLLQ LDFSREDALS AATECTTLQQ ALAFLQQECE
LCTGKYPMKQ MVSMLKCVHR CCRDCAKNYF TIQVTDRTIA DANCPFCKEP NLDGQASDDD
VLEYFSNLDI MLKTILDAPV HELFQRKLRD RTLIMDPNFR WCVKCDSGFI ANPRQRRLVC
PDCRSVTCAS CRRTWEKQHE NISCEKFAEW KEKNDPETQA AGLAKHLAEH GITCPKCQTK
FSLSRGGCMH CTCSQCKHEF CSGCAKPFTM GAKCGQTPYC AKLGLHAHHP RNCLFYLRDK
EPVQLKQLLK DHGVEFNEEL PAWMVAGTEA PDKKAEAGKE AQVAGDAQAA EVKVNGNAEA
NVDAETKVEG SAAPAKPAAK PMKCPMQLQR ETPEGLIDAV CGVEAPPGHA GLCRSHYIEL
LAREVRRLAL DTLGILTADD LETVVRRSDK RLPPNPYGTP PSAYRQALAQ QNGNSAEAPR
FWREVPVWPR QPTRHALLTG STVEYLVALI GRHRLDPVVL FDLGEAVLEL TRRGMPPPER
QPGMSDEDFR IVCVKVVEEQ IPLD
//
