GenomeNet

Database: UniProt
Entry: E0VMX5_PEDHC
LinkDB: E0VMX5_PEDHC
Original site: E0VMX5_PEDHC 
ID   E0VMX5_PEDHC            Unreviewed;      2598 AA.
AC   E0VMX5;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 78.
DE   SubName: Full=Fetal alzheimer antigen, falz, putative {ECO:0000313|EMBL:EEB14731.1, ECO:0000313|EnsemblMetazoa:PHUM320320-PA};
DE            EC=2.3.1.48 {ECO:0000313|EMBL:EEB14731.1};
GN   Name=8236106 {ECO:0000313|EnsemblMetazoa:PHUM320320-PA};
GN   ORFNames=Phum_PHUM320320 {ECO:0000313|EMBL:EEB14731.1};
OS   Pediculus humanus subsp. corporis (Body louse).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Paraneoptera; Psocodea; Phthiraptera; Anoplura; Pediculidae;
OC   Pediculus.
OX   NCBI_TaxID=121224;
RN   [1] {ECO:0000313|EMBL:EEB14731.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=USDA {ECO:0000313|EMBL:EEB14731.1};
RA   Kirkness E., Hannick L., Hass B., Bruggner R., Lawson D., Bidwell S.,
RA   Joardar V., Caler E., Walenz B., Inman J., Schobel S., Galinsky K.,
RA   Amedeo P., Strausberg R.;
RT   "Annotation of Pediculus humanus corporis strain USDA.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EEB14731.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=USDA {ECO:0000313|EMBL:EEB14731.1};
RG   The Human Body Louse Genome Consortium;
RA   Kirkness E., Walenz B., Hass B., Bruggner R., Strausberg R.;
RT   "The genome of the human body louse.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblMetazoa:PHUM320320-PA}
RP   IDENTIFICATION.
RC   STRAIN=USDA {ECO:0000313|EnsemblMetazoa:PHUM320320-PA};
RG   EnsemblMetazoa;
RL   Submitted (FEB-2021) to UniProtKB.
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DR   EMBL; AAZO01003719; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; DS235327; EEB14731.1; -; Genomic_DNA.
DR   RefSeq; XP_002427469.1; XM_002427424.1.
DR   STRING; 121224.E0VMX5; -.
DR   EnsemblMetazoa; PHUM320320-RA; PHUM320320-PA; PHUM320320.
DR   GeneID; 8236106; -.
DR   KEGG; phu:Phum_PHUM320320; -.
DR   CTD; 8236106; -.
DR   VEuPathDB; VectorBase:PHUM320320; -.
DR   eggNOG; KOG1473; Eukaryota.
DR   eggNOG; KOG1632; Eukaryota.
DR   HOGENOM; CLU_000284_0_0_1; -.
DR   InParanoid; E0VMX5; -.
DR   OMA; PEQYTNV; -.
DR   OrthoDB; 2878869at2759; -.
DR   Proteomes; UP000009046; Unassembled WGS sequence.
DR   GO; GO:0016589; C:NURF complex; IEA:InterPro.
DR   GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR   CDD; cd05509; Bromo_gcn5_like; 1.
DR   CDD; cd15559; PHD1_BPTF; 1.
DR   CDD; cd15560; PHD2_3_BPTF; 1.
DR   Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 3.
DR   InterPro; IPR038028; BPTF.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR036427; Bromodomain-like_sf.
DR   InterPro; IPR018359; Bromodomain_CS.
DR   InterPro; IPR018501; DDT_dom.
DR   InterPro; IPR028941; WHIM2_dom.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR45975; NUCLEOSOME-REMODELING FACTOR SUBUNIT BPTF; 1.
DR   PANTHER; PTHR45975:SF2; NUCLEOSOME-REMODELING FACTOR SUBUNIT BPTF; 1.
DR   Pfam; PF00439; Bromodomain; 1.
DR   Pfam; PF02791; DDT; 1.
DR   Pfam; PF00628; PHD; 3.
DR   Pfam; PF15613; WSD; 1.
DR   PRINTS; PR00503; BROMODOMAIN.
DR   SMART; SM00297; BROMO; 1.
DR   SMART; SM00571; DDT; 1.
DR   SMART; SM00249; PHD; 3.
DR   SUPFAM; SSF47370; Bromodomain; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 3.
DR   PROSITE; PS00633; BROMODOMAIN_1; 1.
DR   PROSITE; PS50014; BROMODOMAIN_2; 1.
DR   PROSITE; PS50827; DDT; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 3.
PE   4: Predicted;
KW   Acyltransferase {ECO:0000313|EMBL:EEB14731.1};
KW   Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW   ProRule:PRU00035};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009046};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Transferase {ECO:0000313|EMBL:EEB14731.1};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00146}.
FT   DOMAIN          196..256
FT                   /note="DDT"
FT                   /evidence="ECO:0000259|PROSITE:PS50827"
FT   DOMAIN          347..394
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          2369..2420
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          2425..2476
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          2503..2573
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   REGION          1..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          122..164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1791..1834
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1944..1964
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2114..2160
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2246..2271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2315..2364
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          999..1034
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        38..68
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        122..144
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2130..2160
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2315..2333
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2598 AA;  294919 MW;  313D32464458A723 CRC64;
     MTGRPARKRG RPPKAVVLER PKKFQYHLLK KPKYLLNQEN KGSETPNSQD STPTHSRGAS
     PDISDISNKN SRSFRHKQRL SYGSVSKRGG KSVNYGRHYN FKSAAEKSSD YHYGSDFEDD
     FEEMKSESEM DDNIDIDPDA VLSDDCDSDS SNHSSDLPKN KVSYIKPPSP DPLWLQEIDL
     PPLDLPKSSE DLLVPKEYIM KTLSIYEVLR HFRNLARLSP FRLEEFCGAL MLEEQNVLLV
     EIHIMLLKAI FREEDSQQTH FGPLDQKDSV NACIYFIDPM TWPEVLRSYV ESDKSFDHSI
     LDILIPGDYP FCGVEKRLKV LQFLTDQFLV TNPVREDLIS EGPIHYDDHC RICHRLGDLL
     CCETCPAVYH LECVEPPLND VPEEDWQCNI CKSHRTSGVT DCIIPAEKTG TLSRHEHLGF
     DRHGRKYWFL CRRIFVEKDD GEVWYYSTKY QLDELLDKLD ENSMEKTLYR EITNLKDVIL
     KHMSITETVT NSAKAGRKSY LEVENAEEMN RILAESERTD QNEIPTLAGE AEIETEEVPL
     ALQELENLRL TRYRAQQIAS GTFLFKLGQD NNCKNYVNQY TSNIYALNKP QRNEERDKKR
     HLSHKFSLTA ASEFKWAGSV FGPKALLINT LRQTILQLES NIPTSFLHVN WPLLRKTWIA
     CVQSCIQPKD FGKALVVLQA CIKPVVYASV WHEQLGHVRL HRVTAIEREE RKKIEKREKK
     EKEDEEERNR LAINFVKYTL GLKHSVQKQK GEEYRIHGQW GWRWLSSTRK LIIKDARTMG
     LRAGPQKIMV QVKDGIKEVS NESNQQEWSK ESETDKRLNN LRVFRPIMEF ETIDVTKALT
     SPGRLQYPKI AKKSKLDDFL LRRSNLKLLE ERKFIQMGMV ANSSCQEMDS KKLDSDIDVE
     ALDEDKKNFD FASSSTNQDK LIEIAQEILV CKKRYKEVST SKTLCYSVSC RNNSSGVLLC
     YSPLCILQNA LKAKLATLLK SAQEITDSQT LQNVLITTEK NMKNVKENAT GELNEAAKKE
     LVNAVATAKN VEDDSIDFSK VSSKLEVKEE VPESYLEEEV ISMDTVICGE EVVTTDDTMK
     KEEEIDIEND SPNKIIGFDS GQTIKSNMIT NGQAVKSEGL LNKILSVKKT EVSEDLKQNV
     KGGLSKSGLD NFKVLEKVKL EDGSEVERVY SVTDTRGKIY LKKLTTAIVD RRRKKTPVKY
     PLYSTFLSKH GQYSLMILPK SELRKLARNG GKLTVNGFHH LAKSNTWQWP YPNSKPLFKT
     CWLYRTTTIQ SIPAISLQLR ILWACLRWDD MQVKPQSTDG KNQVTTDTEI MTLEILKHRH
     LGENLEKTQY LRRKIVIPLE LPKTIREVNP IRSGLRKRKR EETPQNTEPQ VSEEWVDEDK
     LELWEIKQYC DKLEKTNNMT LTRSRTGTLT PKTEIKIEAS TIKAENIITK GTPEEIKEKM
     EMQLRAQRAA HYQKKSVETM VKTTGGQIIK LLPATRKIYM SKDGTAKVVT SPATLVQKTT
     AAGNLQQSLI KIQPQTDQHT FSIQGGHPQR VQIIRGNDGK IQVRGLVPGQ QLIQMADGKL
     HVLTGQISSQ TQPSTTVGGQ STLVQTPSNT KITRTEGSGI TSPAQIIVKN AQGQQVRVVP
     SGQNLKQQLQ QNFHKSIILK QDGTKVVLSQ PQQTTQNIFA GQTFTPNSVV MRGNQVIGTT
     NEKGQVVITS RVQNLIPRND KTQSNVAISN QRPIAVSVSN ASTTSLASTV VQNSTLNSGT
     VNQTDAPALI QSGSVVVNNP VLAQQLAEGK LQLATLNGQQ VLIRTTSTNN ALNTNSQTSA
     TTNHLQKLLS PTKSAQSSSP STPKSSNVQV SATQDTPISS QNYCKTQTGL IQITQKDENS
     ESNIMTEEIP SRQLVQQQLR QQVLRNQRTA SAKLSVSSNQ KILQSRLQGS LEQNVNSEMI
     EKTSNESIVE SSAEFNQEMD AIENSDSNNE SQVEMRNQSA ETQENNPLAS TVLVDHNSEI
     ERQLLVSQPP GTIIKCVTAQ VIQTSEGPRI VLQGIQGADF TPQQLNLVQQ QVKQQLLKNQ
     ATTGKQGVLG PTKIYLAVQP PPQTNQSGNS PVNEETLLTP QNQKILVKQN TAKKTLSGNQ
     SVIVRQNANS HIENVAENLE TEETTDTDNN SKQMEASPTK DNSAAETLPK ENCENQTPDG
     QQQKKFILTH DYIHQTIKNA LKQENLNPEI EEKLIQLQRY QEKQMKNEPV NPVITRPQPR
     KRPSSVQGNN HDYEISLLKI FSPTKADGID EKNSRSRQKW KENQEEKRRQ AAQSKLNVLL
     FRHKELLKKD ILKKRALLEK ELQIDIQREI SVELSSRSKQ HENKTEEVIR TGSGKRKSVP
     VPAAALQPPK SGSRGVSGRP KNQTGKKEKL YCVCRTPYDD TKFYVGCDLC HNWYHGDCVG
     ITESMSKRMT EFVCTECRHA RETKELYCLC KQPYDESQFY ICCDKCQDWF HGRCVGILQS
     EADNIDEYIC PNCQVDSNIN FANMKKLNNR DYEALKKLVK QMQGHKSAWP FMEPVDPTEA
     PDYYKVIKEP MDLQTVELRI NEKHYKNLSE FIGDVTKLFD NCRYYNSKES PFFRCAEGLE
     SFFVQKVKGL REKIVENK
//
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