ID F4WCN2_ACREC Unreviewed; 3735 AA.
AC F4WCN2;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 18-JUN-2025, entry version 67.
DE SubName: Full=RING finger protein 31 {ECO:0000313|EMBL:EGI68212.1};
GN ORFNames=G5I_03308 {ECO:0000313|EMBL:EGI68212.1};
OS Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS echinatior).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Acromyrmex.
OX NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN [1] {ECO:0000313|EMBL:EGI68212.1}
RP NUCLEOTIDE SEQUENCE.
RA Nygaard S., Zhang G.;
RT "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT adaptations to social evolution and fungus farming.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the RBR family. {ECO:0000256|ARBA:ARBA00008278}.
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DR EMBL; GL888070; EGI68212.1; -; Genomic_DNA.
DR FunCoup; F4WCN2; 10.
DR STRING; 103372.F4WCN2; -.
DR EnsemblMetazoa; XM_011052055.1; XP_011050357.1; LOC105143613.
DR eggNOG; KOG1812; Eukaryota.
DR InParanoid; F4WCN2; -.
DR OrthoDB; 9978677at2759; -.
DR Proteomes; UP000007755; Unassembled WGS sequence.
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 CDD; cd19815; Bbox1_HOIP; 1.
DR CDD; cd20337; BRcat_RBR_HOIP; 1.
DR CDD; cd20351; Rcat_RBR_HOIP; 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; IPR000315; Znf_B-box.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
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; 2.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 1.
DR PROSITE; PS50199; ZF_RANBP2_2; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000007755};
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:PRU00322}.
FT DOMAIN 73..119
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 784..813
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 3287..3528
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 3291..3340
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 831..882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 899..942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 951..970
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1028..1066
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1231..1256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1288..1311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1342..1365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1477..1526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1726..1792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1921..1944
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2026..2046
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2330..2357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2489..2509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2789..2919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2944..2995
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 3110..3137
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 35..44
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..205
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..269
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..392
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..403
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..432
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..459
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..478
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..511
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..534
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..545
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..591
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..614
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..663
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..689
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..706
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..731
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..752
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..762
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..931
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 953..970
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1028..1039
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1054..1066
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1245..1256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1288..1297
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1493..1521
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1736..1772
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1933..1944
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2037..2046
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2335..2357
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2790..2799
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2824..2841
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2861..2873
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2944..2954
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3735 AA; 415781 MW; C377EB708E4CA003 CRC64;
MAISNPSTKL RMARSMPHWV MAQQQQAEQQ HRRPPTPPKI PPPSLSGDCG DPDYEIIEFP
TRPQAQKPSM PQSNAGKCAL CGTENVFARC DTCNENFCEA CDDMNHKHPK RKGHVRRRIL
TANASRSKPP LPPKGENLLN PPPVPPPRRN RKTSQTKSAL IKGSAQLSLL DKVGSLKRNF
SNAKPSLDSS ARVSKSTNTL NTSSNDASVS GTDKMTTLQE RYRKYQEVMR AQDANRRRHP
SADTKDTLSG RPLSVGSPKP APPLPPPPPP RTMIQSASVC DLTAAHMWNS GMHQAQSMAH
LGPGGMPMMW YPPVNSWDVS MGGSNLSLHH PTMWGYPMGY PSTQMLPSHY PGSLSRGHSP
VRSVKSRRSR PASPSPSLKS RKSYASRSRS RRSPGSPSDA SSENSDESDI DDRLSRGSRS
RRGSVPRSIR QRSYHDEDTR SLVSRGRRER LMTEEKVMNA EDQWSESPST KRYSTSSRSY
DEFQKSNTIS SGRRYDHDDR SVSKMDPRLD RVQNGTYRDR RRRSTDDESS DRKVNTPNRA
RVTSSSDDHF ERVENALKRA SSLRRDIMLD DLERSSHRDS RRSSFDSDSQ IKKMPSREVT
SPKRIPREKT RLLERQSSQG GHSDHANKDE VESHLTRKEQ QRHDISRERE FVTKRELFRQ
KDFDDLDQTS NKRSSGKSSF ESDNQSIRKT PSKEIPIRKE KDKEDSALPE TIGNLQVTDR
QSKNSIRTAE AQQKRQDSTE TKQQQTRTSQ SQKEPKTEKR DTVGSTNASS KKIVPDETVM
MEIPKEEWAC EHCTFINKIN DRVCVVCCKT KSSALPPSIL NDDPVAEPIE LRAPKNEISN
NIGDPNHDPE KRTKKISNSE ESGDNGSVKN KEAIAPDNDS LENSETTITA IVSQAKEASL
KSVNTTSPVD GNLSSEASSS VLTSSSVANT SKADNTNTMS DEEKIRGKLL KSHSVSTGTS
PPPQSISTQT YDYLPAKGTL RRSASIATSK SYSYYDDSDG EEQAGFVNSP DLYPRALQEQ
YLQQLITDHR SRERTRRNSI DSSHLYYRSR EPSQSRYTEA GSSTSQAVST LTRQGLEIVE
LLREAEKQGF TTDDVQVALA QGASNPLEWL QTQWPHLVET VQVLVIAQGK ELKQNSIGVL
SPAEAKEALR SVKGDMWNAV AIAIQRRQQK CEQIMAKGNF TLTDVIRALD NNAGIEDATL
LELQKNQLKP FLMRIWGPPV GVENEEAAPH EDATGAVGGG TGIGSTEQVS NVSDTEAQKQ
VMSPIVDHFV ALQADFQKQL AALRELTDNW RHEKDPPNKL GNNKSDNLYD HSDEPTVLID
ANLVPRAVQA LDVAEPSNLT ITRQEQTTVD SRDDSKYSLN TTKPTEGLDQ VDAALPIEIP
ASTVDDLAKT SAMNSSHTLK YPSKIDHADD STGESSTIDA DKSVVQITKS NLLKFDGQKN
YEVKQIVQLH EETRETHADT SPTSIDETAV ATEVTNLPEE QERLLPNNAG VEVSSSHRTS
SLDTTNNTEP GQSSSTRQET LSGPEIPSDI ARQSTAMGNS ESLVEVGKSV ELSGALRTPS
PNSSVPQGAD ILPQHASRDE SSIADTANVT EKVHASASER DLSAREQSDQ RVIKEIPTQN
DDEPHNVTVE ALLSAVKSLP EQFLTPFITA MQMLSPGKGD VNETSDVQLM NQLNTLHSMK
IDDHKVDVSE AEITDRTKIN ALQKSMVTDV PPKIDAEQKS VSAAVLENKT GSQSLSEKDQ
EGKHLEKSSE KLKSNKIIDK EIARSKVPES RMVKSRSSVP DIKQQHQDVR SVGTDIDESN
ISQTNIATDL TFSDSVDVMD KDTPEESRIM NDAVTSNIGI AGASQTDVVG EIYSCKNSLE
IVDVSARSNN QGESIGDETV SKARSAEEIH SGELSSFHVQ PLIISSTHHQ SIVQKSLELT
SDNCSTDAPS SSKEVESPSE KTSHEKLLVN TDIDSLLKNN LLRDESSLAS INNFNVEKSA
AQSITEINVL PEESIVHNSN ADHSTVSHEV IMNVTNMANK QDINKSDERQ LNDSSHAHVS
STSSTLSLAK VNSSSDHSLD IKSPLIEIFD DQETTLRHDK NDTKPIVSKN AVHVSEKVEQ
TISVTYHTPA SDDKNETTLK ENVPVEQNTT NNLSITQSRT IESIVPPLTH SHASMEMNLN
NLRNQEKEIT FVLAKSDNLM IEQTSDVQSL TDSQDIINQD QLFNSTKNQE IITLPHNHIT
HTKIISPSLS KDNLDINTYP KNISYLEISN SFSDLKTSKD IKIPENSTTV SIPEISKSID
NNSVANSNKL PDENVHSQLN ELSNSNNDIP DNTSPQLSVE HVLSLESKKS ISHPINRDEE
LHLRDEVSQS HDDKRQDIKM SNSTTRNILH ALKNFNIFFT TPPEGRNIAS TVNEDSSDSI
IANVNDATPG IPDTFEIKVS ESPVTTVNDC APIKNIANIV QRETVQIEDV DTMENAKNVD
SPGNEISVIA SNEQVEPSKL SNNESLIEKN TEQVNQSRKS VIAKPVVSRR SRSPLKKIVR
RKSPVKIVKK STSVPRKNLA RKSASPYSTT VTKAKATVNE ITKRSNRAMQ SDKSRIKELL
KPTYIANNKT DNKNKLVAKK PDKTVKQSLN SAQKTAANIK VNDNKKVSMS GLEKISIVNH
ATNLEPQTKI PIVKKYNGNK LENFKKRTEY PKNKIIEDIQ NKNPESSKNI KAETFENRAI
KKINHKIEIS NDGKVLIKME KCNLKSKSFL TSKIPILMRR KMTQLTDSAS SNFSKINLND
TSLLKSASTK LPIMLPAISK LSLKIPEKAN VSNSSSMQKI DSKDSNKLKR NQIKSNNRAI
EITENVKDKQ ILEGNHAKES TVENEETEEP PKVKSIESEL NENSQVSNST HNDPSADLGK
QLEVENAIEE SSDAFSFDSE CSEEDEDTGT AKYISDHNSE YNSVEEFTDA ELLLEKTLNE
IRSEISESDE RTSESEESEA VTYSYETESH DHDSTSSEDS VDEQEIKSSG LKDSVEDVYE
ELSSEGEEMN EQVKTLQQVE VLDKETDVII HNEINDNEAI ISNRMESNSQ VTQKDKENKL
KAPTATTIVE LPRSEINSEI NEKILEISQN LKADSNIAVI NSATASSANI KQDTNSKENI
QSQMNDLKKD ETKLEVASKI EQRDQSTMQT DAIKTLRITS RESRDKRVKV GRRVSTGSKE
VKIEKDDTLK GVDRARAPKK RFSLVASFIR RFEGEENTER ESIRRKRQGS PKTERERIAR
RLLAEGRAAN YDEAEVAASL LTLKFGDTEA LQAAKECSSI ESALAFLQQE CELCTGRFAM
SQIVSMLKCV HRCCNECAKN YFTIQISDRN ITDAVCPYCK EPNLKDASED EVLEYFSNLD
IQLKTLLDPP IHELFQRKLR DRTLMQDPNF KWCIQCSSGF YADPDHKRLI CPDCRSVTCA
FCRRPWEKQH EGISCEKFAA WKDENDPDNQ AAGLAKHLAD NGIDCPKCKF RYSLSRGGCM
HFTCSQCKYE FCCGCGKAFM MGAKCAVSPY CAKLGLHAHH PRNCLFYLRD KEPAQLQQLL
KENGINYDIE GPVGQRKCKV QLQKETPTGV VDAVCNSDVV EGHAGLCRIH YVEYLVRKIR
LTQLEPLPLL NVDDLETCVR RAGLKLPANW YGRDPEHYRN DLVKHYIEYL AGLVLKGRLD
PVAIFDLNDA KQELRRRGKV PPAKDQEMSE RDYLEACIQV TNTIPPCLLG PPLPPPPLLP
VCSSSSFGSS SHLLP
//
