ID E2BDX3_HARSA Unreviewed; 2105 AA.
AC E2BDX3;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Vitellogenin {ECO:0000313|EMBL:EFN86099.1};
GN ORFNames=EAI_12558 {ECO:0000313|EMBL:EFN86099.1};
OS Harpegnathos saltator (Jerdon's jumping ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Ponerinae; Ponerini; Harpegnathos.
OX NCBI_TaxID=610380 {ECO:0000313|Proteomes:UP000008237};
RN [1] {ECO:0000313|EMBL:EFN86099.1, ECO:0000313|Proteomes:UP000008237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R22 G/1 {ECO:0000313|EMBL:EFN86099.1,
RC ECO:0000313|Proteomes:UP000008237};
RX PubMed=20798317; DOI=10.1126/science.1192428;
RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA Wang J., Liebig J.;
RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT saltator.";
RL Science 329:1068-1071(2010).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008954}.
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; GL447693; EFN86099.1; -; Genomic_DNA.
DR STRING; 610380.E2BDX3; -.
DR EnsemblMetazoa; XM_011138688.2; XP_011136990.1; LOC105181726.
DR InParanoid; E2BDX3; -.
DR OMA; YGHCHHR; -.
DR Proteomes; UP000008237; Unassembled WGS sequence.
DR GO; GO:0005319; F:lipid transporter activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR Gene3D; 1.25.10.20; Vitellinogen, superhelical; 1.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR015819; Lipid_transp_b-sht_shell.
DR InterPro; IPR011030; Lipovitellin_superhlx_dom.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR015816; Vitellinogen_b-sht_N.
DR InterPro; IPR015255; Vitellinogen_open_b-sht.
DR InterPro; IPR001747; Vitellogenin_N.
DR InterPro; IPR001846; VWF_type-D.
DR PANTHER; PTHR45688; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR45688:SF3; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR Pfam; PF09172; Vit_open_b-sht; 1.
DR Pfam; PF01347; Vitellogenin_N; 1.
DR Pfam; PF00094; VWD; 1.
DR SMART; SM01169; DUF1943; 1.
DR SMART; SM00638; LPD_N; 1.
DR SMART; SM00216; VWD; 1.
DR SUPFAM; SSF48431; Lipovitellin-phosvitin complex, superhelical domain; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
DR PROSITE; PS51211; VITELLOGENIN; 1.
DR PROSITE; PS51233; VWFD; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000008237};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 374..1154
FT /note="Vitellogenin"
FT /evidence="ECO:0000259|PROSITE:PS51211"
FT DOMAIN 1772..1971
FT /note="VWFD"
FT /evidence="ECO:0000259|PROSITE:PS51233"
FT REGION 685..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2105 AA; 241063 MW; A190AA9AE1A9E289 CRC64;
MFNVIASAIP APCPDVYRGK YRADDYPDED LGIKYAKDVG EICQNIEATG RGLCAYIAES
FVSVGGQIIP PQNYFRNAFK HVREAGGVCI VDEVQVGFGR VGTHMWAFQV YGEDVIPDIV
TVGKPMGNGH PVAAVVTTPE IASSFRASGI EYFNTYGGNP VSCAIANAVM EVIERENLLD
NASKVGSHLI AELKKLAERR KIIGDVRGVG LFVGIELVRD RTKRIPATAE AQHVVSRMKE
KKILVSSDGP DNNVLKLKPP MVFTIENVNH FVSVLEEVLE EIDIGFDEEP EPTTAIIQAT
FSPIDVDRST GRESGSTGAT EMFGLPLPSS FAPMATCVRN SSPRELHANP DSTRRDRRFD
YFSSALAHTD LLIWKPNHTY HYRVETQGLA GMNKVSQQFA GLQLRGELVI EVTEPNVLLV
HLQNVQHTQI LKELQDSWHT KVSDQQLHYK NSWIQTTYKV DFQHGNMQKI YTEPQSPRWQ
LNVMKGILSQ LQLSIVEPED LPMEKASFSE FIVDEQSVSG HCNTSYNIQP MAKSQLELHP
LVRIPALKDE MYWDVMKTRN YRDCLSMPMY QFSIVKNMDH DIHERYLKRS TQVNMVISRD
KDDLTTIRSS VMKGTIDVRP KLNDFANSNI LTKMKLTLTK LEPMTEMKDP PLNLVPAGNL
LYVHHLMHDH QLDKTRIEPK VDYLETDPKS DKSHESSSSE KASSSNFLRR SIHQKLNRFG
NNFMSNTEFH DREYGYFISK AEMHESMNNV LPSILGLNKN DGSKMLDPAE MMKQVVILVN
EMVSEVQSSD EVLRQHTLEK FMMLTSLLRH LNEKELATVE NDLSPKILPQ KSKEPLLRWK
IWRDAVVQAG TGPAFLTIRG WILEKKVRDF EAAQLLSRLP RVVHMPTAEY IKAFFELLKE
PSVKNEFLLN TTAPYAFAEL VRYVMVWDQK FFYPVRTFGM FVNNEEKKAL TDVYIPYLAQ
ELMDAQQKHH NSKILTYIIA LGNIGHPAIV PVLEPYLEGK LKITSFQRMT IVASLRKLME
HQPDVVRPIV YRIYQNDKEH QEVRIAAVQL LMMSHPPLDM LKRMAERTHY EPNGEVNNAV
VTGIRYLSKL SRERNRQDAH NAQAVRKLLN PKVKPNMRES YIFGQDYVNE QKEFEAAVYV
NTIRGFKRFS PASASVELGT NRSHLSPPNL KIAVASTGSE LLLRLLQLLF HPNLPTKSLS
AVDAVAKNLQ IPLQDEELLE TSFVMDSEYA VNLIVLDKHE IFDLLESFLR VFKLAEEDKS
DLMLASMMSW ELAISYPSEL GLPVTYRLQK PQLGYMRSKL HWKDKPNPYD LQMDVELDVL
LSRKVMSRLD FVTVFDNQRY LSGFDVNMQL HLPAKLKLHV DEAARQLNVV YEPPKDKLRT
TLLHYSVVPH NAIVDFCTIK PVLLHEQAYI LYWKQPPSKT VENMGDLVIT IETDHFRPNV
TMQNFLFPVV VEQITQLIDK DVHYNKIEVG TKFDPNTDNT ISFTISYDDI LPPNDMLHKR
IEDDFEISDD LWMSEMKKIS KQHKSDPKAM KLVRMDMKIP NKHIHWHMNE TIMQHSEHDT
TMHYKAILQT SHSAWKFAAV LDLESAPSAC PTLDLHSKHH NIWNALLHYE SPDKTKQTIH
LLAIQEQSEE LNNFLVNSEM HKKCMMEKER HTVGLKNCQE FCKFIDQKDE MHMTMKVGNK
PFHYMKYLFL KALAAHLMPI MHLELEDWEP QPQEHSHRSI SVMVNKPLYD EMLNITMVAP
PLRAYMHMDL IDLPDSFFNK HQLELLFGQS DARKCVLSAD HLVSFNGLEY SVRLGQKHPY
VLLINPTRQG LNERSNLISA IQGTPDETNV AVLVQQLDNG RRSLIIMKKE RTVEILPPAP
GSTDVRILVD GQNLESPLEL WHTLTQLDIH ISTLPSNVHE ILLDSSEITI WYDSTNVQIK
ASDKYNGELR GLCGAKANIR EHQLITPAGC YVEEPADVVE LYAYDPANED PLVEKAKEYA
TKNCIEHEHH QTDYVTDLET GKATQQQLWR EKFAGISFNH YCTTMKTHWL EKDDEYCFSL
RPLPYCNEGC KPTKMVSKAI AHFCEPINSE VVALKNRIQS GANPDFRDRK VSLHENLQVP
ASCRP
//