ID A0A195EV90_9HYME Unreviewed; 2274 AA.
AC A0A195EV90;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=GC-rich sequence DNA-binding factor 1 {ECO:0000313|EMBL:KYN31804.1};
GN ORFNames=ALC56_13943 {ECO:0000313|EMBL:KYN31804.1};
OS Trachymyrmex septentrionalis.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Trachymyrmex.
OX NCBI_TaxID=34720 {ECO:0000313|EMBL:KYN31804.1, ECO:0000313|Proteomes:UP000078541};
RN [1] {ECO:0000313|EMBL:KYN31804.1, ECO:0000313|Proteomes:UP000078541}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tsep2-gDNA-1 {ECO:0000313|EMBL:KYN31804.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYN31804.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Trachymyrmex septentrionalis WGS genome.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the GCF family. {ECO:0000256|ARBA:ARBA00010801}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00557}.
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DR EMBL; KQ981965; KYN31804.1; -; Genomic_DNA.
DR STRING; 34720.A0A195EV90; -.
DR Proteomes; UP000078541; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0005319; F:lipid transporter activity; IEA:InterPro.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:InterPro.
DR Gene3D; 1.25.10.20; Vitellinogen, superhelical; 1.
DR InterPro; IPR012890; GCFC2-like.
DR InterPro; IPR022783; GCFC_dom.
DR InterPro; IPR015819; Lipid_transp_b-sht_shell.
DR InterPro; IPR011030; Lipovitellin_superhlx_dom.
DR InterPro; IPR015816; Vitellinogen_b-sht_N.
DR InterPro; IPR015255; Vitellinogen_open_b-sht.
DR InterPro; IPR001747; Vitellogenin_N.
DR PANTHER; PTHR12214; GC-RICH SEQUENCE DNA-BINDING FACTOR; 1.
DR PANTHER; PTHR12214:SF0; LD29489P; 1.
DR Pfam; PF07842; GCFC; 1.
DR Pfam; PF01347; Vitellogenin_N; 1.
DR SMART; SM01169; DUF1943; 1.
DR SMART; SM00638; LPD_N; 1.
DR SUPFAM; SSF48431; Lipovitellin-phosvitin complex, superhelical domain; 1.
DR PROSITE; PS51211; VITELLOGENIN; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000313|EMBL:KYN31804.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000078541};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 879..1524
FT /note="Vitellogenin"
FT /evidence="ECO:0000259|PROSITE:PS51211"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 70..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 358..399
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 28..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2274 AA; 261885 MW; 3C580B23D9F3E689 CRC64;
MSLFNKPKRN IRRRPFDDED EDNENRMEVE DAQPVKVKTK KDKPKQTRLS FGEELEQGDD
GEVFIVKKSS RSKKLMKQLD HERRKKKGEE KMQVDTEQAN KSIKQEKDLE IKTDDLVVKI
KNTGPLILNG RAALAAGKDD YTSGEEEDEP CSHKFRKNTD KAETVKILLE SGCIPDAAMI
HAARKRRQKA RELGTDYIPI EEQSDDKGKS RLIREEDHDR SDDDDSQDRL DMTVNTEARD
KEKRREAFLA SQVPLKFSDN ESEHENEEEE WEAQQIRKGV TGAQVNNVKY LEYFDMQIAA
AQQDSMLQQQ YTMGMNVNQI IGSGVPLEMV LMPAPPPPPS IQPPDPTKVI PVTPQEVVNR
MRTRLDNLKE VHRRHQQDQE RLEGELQQTI KELDESEVRT PHYAQRFRYY QELRGYVTDL
VECLDEKFPL VIDLEQRWLD LYGERSVELM ERRRQDTRDQ AEEITTTARG QAMRRGPEVE
VHVRRATERE GRRARRRRAR ELASNIPKHI DGMSSDDEVT EQQNLVFKQA KDEIDNNCKD
IFSDVMEEYC TVRGILSKFE SWRETDMDAY TEAYVSLCLP KIISPIIRLQ LLTWNPIMES
GDLERTKWYN TLLLYALDSK QTEESLKRDP DVRLIPSTIE KIVIPKLTSI IEKIWDPMST
SQTLRLVGTI NRLIKEYPNL NDTSKQLETL FNAILDKIKA AIENDVFIPI FPKQIWDTKH
QFFQRQFAMA VKLLRNLLSW QGILGDIQLK NLALGSLLNR YLLAGLRVSC PTDALFKANM
IMSTLPRAWL QGETIEHLKM FATLIQQLSE QLDQANPAHN IILVYVYAQV ILYVFVSHSD
KNCLSFLDSS LISVLAQGIG KTLFIFLFLS TEIVAQSLFR SGKEYIYSYN AISSTGVLVP
SNAASSWNLH GKLVIHAEDD FVTIQLQSLK TNMHNGNVKE MIEDIDIYDD AVELLKPFRL
SYNKGLIENF STETEPVWTT NIKRSIAGIL QLDLFNLEKE IASHSKHYNS QINHYGKCDI
DYIVSPEDDN RLIRKSFDPR MCIGHPSHYW SNVPKVQCTD DDQNPILKSS ERVYQLKTDG
FVHNIISVNA SGGIYVQPFQ SMGEAHYHFV RRKNYFTLHR QTIELTSVKD IANKIIINNL
RTTVLQHELP EIDLTQGRGT PDKNFIFKSI SHLLDRLSHR LENPGLDTEI HNLHNTTISV
LLYYLGMLDR VDLRKAYTRI SGTSYKEETI RNMFLEALPQ VGSRESALFI LDLVQGNEVS
DMSAIQLLMR LPFHIKKPDV QLLVNLQPLL TLPNKICAEV QNTAILTYGT LIYKTCLVHC
PYEMLDDYVR LYLDKFTETT LYEQKIIWLE GLANIQLGKV VEFLEPIATD NNAESRHFRV
LAAWASIPTA PLRPDVIYPV YWPILLNRTE HLEMRVAALT LLIVSSPTPN RLISLYWYMQ
NEPNQHLYNY FYTMLKSMER TTYPCYRRIS KIAAQFSRVL RVPNNEYMIT GNYLIDYQDS
LRRFGAMLHG IIIANPSTNI PEVIYVTLNN YASGTHLNHV SLYIKAEGIS HSLATSFENP
TNIKDILKEF KLDERIKGPM HLEIITRIQE KTVLCVHWNE TNIVEGLKYL SSLSDNIYQM
YYNMEFHVNQ QRINVPLAIE SVQVTDFGTN VRLAMMGTSL FSMRGNFTRD FPGRNNHIIL
RTSVHGIETI ENYNPLVDLW HSAERVQSLH GYLPINITLG LDERPFISYD TLEERLKTGI
TVHAKTLTSI RGANVRTKLN RVCRSCSVSH TVIKSPSSNL QTVNILNVGL PELGGRLQVK
IFDCESMISY ETLINDIWSF HRSNYQTWPS MKFALIGLHF LDYFTFVPPK GSCGLAAYIE
ALKSGPSQTK LEYIKSENRH ILSLTHHDLQ SSQVLHQWNL AGLYEATSWL SDVIKFKATK
IVPNERVFKF CVEAERHMPW QWEILSNEPI ESYRIKLNFI WGLSDNAKGK CSGSSLSINL
IGEISSKQLE ESKRARWPYG ECKNESEGKR IVPYTNSCYE VSKEMSTLRK YKILAQYENL
PENLSKLVWK LYALYDLMGG NSSIARKSDQ LAITAIFPKD SNVGELQLNG DKVAIEYNSH
FIDLFLTRMR IHKYMEISLF RMFSSACIIT SDSIKSAYNT VYSFAKNSEV ILLGQCYDEN
PRFVLTAANG VYGINVNLTD ESGTTRIMAD KDRGILYNAT SSIQLQSDYE FHKLGTKKIK
MGDKAIDILL PNIFLYIRWT QEQVLIFFSN HVLEFSCGIC TLAHPNIDRL YEKL
//
