ID A0A195CVA4_9HYME Unreviewed; 3495 AA.
AC A0A195CVA4;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 28-JUN-2023, entry version 39.
DE SubName: Full=RING finger protein 31 {ECO:0000313|EMBL:KYN04608.1};
GN ORFNames=ALC62_04600 {ECO:0000313|EMBL:KYN04608.1};
OS Cyphomyrmex costatus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Cyphomyrmex.
OX NCBI_TaxID=456900 {ECO:0000313|EMBL:KYN04608.1, ECO:0000313|Proteomes:UP000078542};
RN [1] {ECO:0000313|EMBL:KYN04608.1, ECO:0000313|Proteomes:UP000078542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS0001 {ECO:0000313|EMBL:KYN04608.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYN04608.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Cyphomyrmex costatus WGS genome.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the RBR family. {ECO:0000256|ARBA:ARBA00008278}.
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DR EMBL; KQ977259; KYN04608.1; -; Genomic_DNA.
DR STRING; 456900.A0A195CVA4; -.
DR Proteomes; UP000078542; Unassembled WGS sequence.
DR GO; GO:0071797; C:LUBAC complex; IEA:InterPro.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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 RNF31; 1.
DR PANTHER; PTHR16004; RING FINGER PROTEIN 31-RELATED; 1.
DR Pfam; PF18091; E3_UbLigase_RBR; 1.
DR Pfam; PF16678; HOIP-UBA; 1.
DR Pfam; PF01485; IBR; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000078542};
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 691..720
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 3046..3287
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 3050..3099
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 106..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 571..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 732..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 849..873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 930..971
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1191..1214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1245..1266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1332..1366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1392..1430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1464..1510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1678..1698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1827..1846
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2231..2264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2660..2752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2770..2845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2881..2907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2975..2994
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..149
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..245
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..417
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..445
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..532
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..602
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..647
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..762
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..790
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 854..873
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 930..947
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 948..971
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1339..1362
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1464..1488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1492..1510
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2231..2262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2660..2685
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2686..2708
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2793..2823
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2888..2907
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3495 AA; 389561 MW; 93FD4816391917CE CRC64;
MAISNPSTKL RMARSMPHWV MVQQQQAEQQ HRRPPTPPKI PPPSLSGDCG DPDYEIIEFP
TRPQAQKPSM PQSNIGKCAL CGTENVFAHC DMCNENFCEA CDDMNHKHPK RKGHVRRRIL
TANASRSKPP LPPKGENLLN PPPVPPPRRN RKTTQAKSAL IKGSAQLSLL DKVASLKRNF
SNEKPSLDSS TTVSKSTNTL NTSSNDAAGS GTDKMTTLQE RYRKYQEVMR AQDANRRRHP
SADTRDTLSA KPLSVGSPKP APPLPPPPPR TMIQSASVCD LTAAHMWNTG MHQAQSMAHL
GPGGMPMMWY PPVNWDVSMG GSNLSLHHPS MWGYPMGYPS AQMLPPHYPG SLSRGHSPAR
SVKSRRSRPA SPSPSLKSRK SYASRSRSRR SPGSPSDASS EKSDESDIDD RLSRGSKSRR
GSVSRSIRQR NYHDEDTRSL VSRGRRERLM MEEKVINAED QWSESPSSKR YSTSSRSYDE
FQKSNTISSG RRYNDDRLVS KMDPRLDRIQ NGTYRDRRRR STDDESSDRK VNTSNRARVT
SSSDDHFERV ENALKRASSL RRDIMLDDLE RSSTRRDSRR SSFDSDGQIK KTPSREVTSP
KRTSGEKTPL PETIRNLQVT DRQRSVDKDQ QSKDPIRTAE AQQKRQDSTK QKTQMSQSQK
EPKAEKKNTV ESTSALSKKI TSDETVMIEI PKEEWACEHC TFINKINDRV CVVCCKTRSS
ALPPSILNND SVTGPIEPRA PKNEISNIIG DPEKRTKKIS NSEESGDSGS VKNKETIAPD
NDSLVESSET TVTAIASQAK EESLESVNAT LSVDESLSLE ASSSTLTSLV ANTSKIDNTS
TMVNEEKIRG KLSKSHSVST GTSPPPQSIS TQTYDYFPAK GTLRRSASTA TSKSYSYYDD
SDGEEQAAFV NSPDLYPRAL QEQYLQQLIT DHRSRERTRR NSIDSSHLYY RSREPSQSRY
MEAGPSTSQT VSTLTRQGLE IVELLREAEK QGFTTDDVQV ALAQGAPNPI EWLQTQWPHL
VETVQVLVTA QGKELNENSI GVLSPVEAKE ALRSVKGDMW NAVAIAIQRR QQKCDHIMAK
GNFALMDVIR ALDNNAGIED ATLLELQKNQ LKPFLMRIWG PPVGVENEEA APHEDTAGAV
GGGMGVDSME QVSNVSDTEA QRQVMSPIVD HFVALQADFQ KQLTALRELT DNWRHEKDPP
NKLGNNKSDN LYDHSDEPTV LIDANLVPRA VQALDVAEPS NLTITRQEQT TVDSRDDSKY
SLNTKKPTEG LDQIDAALST NISVSKVDDL AKTSAMDSSD TLEYSSKIND ADDSTGELST
INESVVRIIE SNPPKFDGQK NNEVKHTAQT NEETRERADT STTSIDETTV AMEVTNLPEG
QERLLPNNAG VEVSSSHVTS ALDTTNNTEP GQSSSTRQET SSGPELPSDI ARQSTAMGNS
ESLVEVGKSV ELSEALRFSF PNSSVPQRAD ILPQHTSRDE SSIADTANMT EKVHVDASER
DLSTREQSDQ RVIKEIPTQN DEPHVVAVEA LLSAVKSLPE QFLTPFITAM RAMQMLSPGK
GDVNVTSDVQ LMNQLNTLHS MKIDDHKADI SEAKITDRMN IGAFQKSMIT DVSPRIDAEK
SVFAAVLENE TGSQSLSEKG QEGKHLEKGY VKLNTDKIID KVIASKVPEF RMVKSRSSVP
DIKQQHQDVR SVRTDTNESN ISQTNIATDL TFSDSVDVMD KDTLEKSRAV NEAATSNVGV
AEVSQTDVIG EICSRKNSLE IVDMPARSDD QGESVGDKIV SKAKSAEEIH SGELTNSHVQ
LLTISSMHDK SVVQKSLELT FDNCSTDVTS SSKEVENPSE KTSHDKLLVD NTDIDSLFKN
DSSRDKSSLT SINDFNVEKS ASQSITEINI SQEDSIVHNS NAAHSIVSHE VIMNVTNMAN
KQDINKPDER QLNDSSHAHV STSALSLSST LSLTKVNSSS DHSLDIKSPL VEIFDNQETT
LRHDKNDTKP IVSKNAVHVS EKVEQTISVT YHTPASDDKN ETTLKENVPV EQNTANNLSI
TQSRTIESIL PSLTPSHAVM EMNSNNLRNQ EKEITFDLAK SDSLMIGQTS NIQFLTDSQD
INQDRLFDPT NNQEIIELPH NHLTHTKVMS SSFSKNNFNV NTYPKNISHL EISNSDLKTS
KDIKILEDSK TVSISETSKS IDNNSVTYIN KLPDENVHSQ LSELSNNNNN TPDDTSSRLS
VEHVLSLEPK KSISHPINHD EKLHLGDKVS QSHDDKRQDI KTSNSTTRNI LHALKNFNIF
FTTPTEERNI ASTVNEDSFP DSIIANVNDA TPGIPDTFEI KVSESPVTTV NDCAPIKNIA
NIVECETGQI EGIDTIENAK NVDSSGNEIL IVTSNEQVEP SKLSTNESSI EQVNQSRKNV
IAKPVKYRSK SPLKKIVRRK SPVKIIKKSA NVSKKNLARK SANPYSTTVT KAKITASEIT
KRSNRTMQPD ESRIKEVLKP TYVANETGNK NKLVVREPDY PKNKNIQNIQ NKNPGDSKNV
KAETFENQTI KKINHKIETS NDDKILKIEK DNFKFKMSLP SKIPILMRRK NTQLTDSASS
NFSKINLNDT SLLKNASKLP VMSPVISKLS LKISEKVNVS NSPIMQKIDS KDINKLKRIQ
IKSSNDRAIE ITENVKDKQI LEENHAKESA VENEETEEPP KVKSIESELN ENSQASNSTH
NDPSADLSKQ LEVENAIEES SDAFSSDSEC SGEDEDTGTA KYISDHNSEY NSVEEFTDAE
LLLEKTLNEI RSEISESEEE STNESEESEA VTYSYETESH DHDSTSSEDS VDEQEIKSNE
LEDSVEDVYE ELLSEGEERE TTEQVETLQQ FEVLDSNITV IDSATASSAN IEHTNSKENI
QSQMNNPKKE TKLKDTSEIE ERDQSTKQTD AIKTLRVTSH ESRDKRLKVG RRASTGSKEI
KIEKDDTLKG VDQARTPKKR FSLVASFIRR FEGEENAERE SIRHKRQGSP KTERERIARR
LLAEGRAANY DEAEVAASLL TLKFGDTEAL QAAKECSSIE SALAFLQQEC ELCTGRFAMS
QIVSMLKCVH RCCNECAKNY FTIQISDRNI TDAVCPYCKE PNLKDASEDE VLEYFSNLDI
QLKTLLDPPI HELFQRKLRD RTLMQDPNFK WCIQCSSGFY ADPDHKRLIC PDCRSVTCAF
CRRPWEKQHE GISCEKFAAW KDENDPDNQA AGLAKHLADN GIDCPKCKFR YSLSRGGCMH
FTCSQCKYEF CCGCGKAFMM GAKCAVSPYC AKLGLHAHHP RNCLFYLRDK EPAQLQQLLR
ENGINYDIEG PVGQRKCKVQ LQKETPTGVV DAVCNSDIVE GHAGLCRIHY VEYLVRKIRL
KQLEPLPLLN VDDLEMCVRR AGLKLPANWY GRDPEHYRND LVKHYIEYLA GLVLKDRLDP
VAIFDLNDAK QELRRRGKVP PAKDQEMSER DYLEACIQVT NTIPPCLLGP PLPTSPPLLS
VCFFNSFDSS SHLLR
//
