ID A0A3B0KCA2_DROGU Unreviewed; 2809 AA.
AC A0A3B0KCA2;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Blast:E3 SUMO-protein ligase RanBP2 {ECO:0000313|EMBL:SPP83819.1};
GN ORFNames=DGUA_6G016296 {ECO:0000313|EMBL:SPP83819.1};
OS Drosophila guanche (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7266 {ECO:0000313|EMBL:SPP83819.1, ECO:0000313|Proteomes:UP000268350};
RN [1] {ECO:0000313|Proteomes:UP000268350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Alioto T., Alioto T.;
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
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; OUUW01000008; SPP83819.1; -; Genomic_DNA.
DR OMA; ACETPKD; -.
DR Proteomes; UP000268350; Unassembled WGS sequence.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046907; P:intracellular transport; IEA:InterPro.
DR CDD; cd13171; RanBD1_RanBP2_insect-like; 1.
DR CDD; cd13172; RanBD2_RanBP2_insect-like; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 4.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR Gene3D; 4.10.1060.10; Zinc finger, RanBP2-type; 2.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR000156; Ran_bind_dom.
DR InterPro; IPR045255; RanBP1-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR001876; Znf_RanBP2.
DR PANTHER; PTHR23138:SF169; E3 SUMO-PROTEIN LIGASE RANBP2; 1.
DR PANTHER; PTHR23138; RAN BINDING PROTEIN; 1.
DR Pfam; PF00638; Ran_BP1; 4.
DR Pfam; PF00641; zf-RanBP; 2.
DR SMART; SM00160; RanBD; 4.
DR SMART; SM00547; ZnF_RBZ; 2.
DR SUPFAM; SSF50729; PH domain-like; 4.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50196; RANBD1; 4.
DR PROSITE; PS01358; ZF_RANBP2_1; 2.
DR PROSITE; PS50199; ZF_RANBP2_2; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Ligase {ECO:0000313|EMBL:SPP83819.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00322};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00322}.
FT DOMAIN 1328..1464
FT /note="RanBD1"
FT /evidence="ECO:0000259|PROSITE:PS50196"
FT DOMAIN 1664..1801
FT /note="RanBD1"
FT /evidence="ECO:0000259|PROSITE:PS50196"
FT DOMAIN 1838..1867
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 1957..1986
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 2098..2223
FT /note="RanBD1"
FT /evidence="ECO:0000259|PROSITE:PS50196"
FT DOMAIN 2653..2796
FT /note="RanBD1"
FT /evidence="ECO:0000259|PROSITE:PS50196"
FT REGION 826..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1066..1100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1552..1575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1634..1663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1800..1819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2061..2110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2510..2543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2553..2572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2611..2650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 889..916
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1552..1571
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1800..1817
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2061..2085
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2611..2630
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2809 AA; 304957 MW; 5DB15F9955BAFC3E CRC64;
MSVARMYYKI QEYPKAIEYL NSYLKVKDEA NAHKLIAACY TLRKQPDPKL ALEHYQRCIQ
LNPKQPEVIN DACQLLLDEN SSSKGLFSVE CAKFWLDKAG GIQLNESELM FQLRMKIKLH
ESTNGGDGGV GSGYGALSDI TAANSEMNAL EEIMHRELQA RPQDVKLRVR LMRCYLEKKK
LEEAFTYAFR VELDEKSGTS QCADWYDIIW TTLTKLEQGK DLKKWGPRFW QLALLTLDRL
AQLSLESGKT MLDCSSHLFR LDQYLHRFSM EKSSSADQLQ PELQQSCIDH YSGQLLLHAV
ALVFKRELVS NHNKWVKSLK SALPLLLLGY QTKPLPENCT QPWMKHCDED QKKLLQLWRL
QGAFRCAQLG RTLFGCLEPA NAHDMDQKEN IQTGGQNNQP MIGLFENSDK LLACARLQWQ
DKNWRRQLFP VLFSHPEHKL KENSSHLVRN PKLEEPLYEW PEEADIESYE RQALLLQPQS
LAQHVYLALG AIEALGSAPR VAFYEGLRRD VKQDLSFCGQ ESLSQLDIDV FLYATVIHTH
SRLASQRESY DSCNLGNFSA SARPHMLPYA NVLSQLATPE QSGWWDLVLR SHKNQVPDCS
RGEQRAQMQM GLEAVRGVNG AKADTIILFK LGAILCSRQD RDVLEHRIDT LYKQGFNMMR
REQQQGGGGH EHYPRFFKIV SDSSREAFQE RLRLAEEAVS YFSSKMFKAH QYQQFIDEVR
GLNLPMATYL QAEAYRMLEY SSQINRDAKA RYWEQRRDYL QQTQQLLRNQ VKHPLYGMIR
SEVGRCEEDR CETNYDVYGS PENHNNSSSY EDAEDADFYA GASLTLNRSR RHGEPPVASR
DTPVRGTPAT PVTAATPLAS NAKFNQLEET VNQMSKSLCQ LKDDVSTGIT DMRQEIKNLT
EKFTGIEDLI KKLKITHRET PTRDVDPATA LGLDDLLIIE ELDAQQQQHQ QSQAAAAAAV
AQQQQHQQLL STNYGAPNAN PGGFFNGVPG IQSPQDRFLQ GAYGSPLFNQ NQLYNYYAAQ
AQQYMRTPPA AGTLPPLNIF GAQNPNFAGI PGIFPPAPAV APPRSYLEPA GSFGQTPASL
IPPQSAVPAA AAPPQQPPGP APAIAALLPV EPPKPPTAAV GGPGFFNSSA PVFMPSPIQA
PQAKPPLVAA APVVAPPPTA AVAPTPAIPS LFNRALNNQP VEKEPPANVV ITSSDPLPKP
ATVAGVQPTL SVTIPAQHIK PSLVQNTEQQ PQLQQQPAAL PVTVPTAAVT ATSSGAFNFS
FGTSNAESPF SFKTQVAKAA AEKQKEQEAE QAQALLLNES AKSAASEPNK SAVAADASLE
LDYDPRPDFQ PIIALPDEIE VRTGEEDEEV KFCFRAKLFR LVSHEWKERG IGNIKILKNQ
ATGVSRILMR REQTHKVCAN HKINSEMSLA TPQGDTEQKS FIWAANDFAD EEVVPETFLV
RFKSPDTAKQ FHIAYTVARQ EASKAATTTT DTAAAAVPEV PKAPAAAPAP ATAVPKSFVT
STPATSFGKP FEPSNMKLSE SLAALAAPAF STNQTSSTTV AKSLFGGQQP AAAAATTTPT
STAVSSTPTA SAAPPTVPPF ASFSFGQQGA GPTASPFGNL SFGSMSFGSV SAVNSNTSGN
NNTLFTTAVL QDSTLQGQQQ QQRSKSTGKE ETESDAEEYE STAQFNPVIP LPEVVKVVTG
EEDEDVLFEN RAKLLRYFKE TSEWKERGLG SMKLLRNRKD PSQVRLVMRR EQVHKTCCNQ
RLLPETTFKY LVNSTTALTW AAQDFADQEL EQTTLCVRFK KPETCKEFYD AVLKAQKEMK
EVESSSTKTD GKQLAAKEEK SGAAATASKG FGDAFKPKAG SWNCEACYTS NGQDQLYCLS
CEGPKDATVP PKQPAGLDLS NALNLSTSSA SKFSFGFAPA TTEAAPATAA TTLPSGFIFG
AKPQSTEKPA ASVAATSSAP AALPDKASGF GDAFKPKAGS WSCRSCYLSN TGDALYCSAC
EAPKDDTVPK KESNALGSTS GLILPATTKF NFGFGEPAAP PTVAGEVKDG EATKSVFGSA
SFSFVPKTSA AAPVSLESGT FSFTMPKPAQ QQPKSPGGSG NDNGENNDSD PEEENNTHFA
PVIPLPEKVD VKTGEEDEEV LYVQRAKLYR LTDEWRERGV GNVKILRHKQ TGKLRVLMRR
EPIFKVCLNH ALTASVAYKP KDERSWLFVV HDYSGGESVN ERFTLRFKNK DIADNFLKVV
KSALDGTAPA IVEEPHTSAA PPAADITEAS RDSASLISQE KKSLADEHDL SFGSGCTGCV
GCDPEKFDWT NHQTSTAPIA DEVYPPLPMH LPALKLPPAA DLLAQSQQQQ PAAAQLSGGS
SIFRASSLAS ANSGGFSGFG QAVSANSTEA LASTPASKPE ENKPSTAFVF GSAASDKPTF
GKSLFGGGKP QQQQQQSIFS SSQGNVLGSI FGSGIAETKD QSAKSIFGGV GGGANPELTK
SIFGGVAKVD PVTAAAPKTI FGGTNTSVFG GGSSGFVFAS EVPAFGQKTQ GITFGDLAKP
PTPPKDKETG ESNEQTKDNN IPKSVFSLAF GDTKETSSPA AGGAGGGAVG SSSLADLASK
AGSDDFASLS AKNQGTPMGF NKSGSGGGFY NLTHQNDFKN FQSPKGNNTT GGGGDADGEG
DGDATNDDNY DPYYAPIVDL PDEIVVKTGE EDETKLFGER SRLYRFDTKT KEWKERGTGE
LKILEHPQLQ SFRMLMRQEL VPKVLLNMKI AGDLKLVPMN GQKKSFSWYG LNYAADAEGK
TSMEGVVEQL ACRFGKQDVA DQFLDRVNQC IKRASEASAQ AQENSETED
//