ID U5ET92_9DIPT Unreviewed; 1157 AA.
AC U5ET92;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Putative mbd-r2 {ECO:0000313|EMBL:JAB55388.1};
OS Corethrella appendiculata.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Chaoboridae;
OC Corethrella.
OX NCBI_TaxID=1370023 {ECO:0000313|EMBL:JAB55388.1};
RN [1] {ECO:0000313|EMBL:JAB55388.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Salivary glands {ECO:0000313|EMBL:JAB55388.1};
RA Ribeiro J.M.C., Chagas A.C., Pham V.M., Lounibos L.P., Calvo E.;
RT "An insight into the sialome of the frog biting fly, Corethrella
RT appendiculata.";
RL Insect Biochem. Mol. Biol. 44:23-32(2014).
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DR EMBL; GANO01004483; JAB55388.1; -; mRNA.
DR AlphaFoldDB; U5ET92; -.
DR GO; GO:0005694; C:chromosome; IEA:UniProt.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd20104; MBT_PHF20L1-like; 1.
DR CDD; cd01396; MeCP2_MBD; 1.
DR CDD; cd20386; Tudor_PHF20-like; 1.
DR Gene3D; 2.30.30.140; -; 2.
DR Gene3D; 6.20.210.20; THAP domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR016177; DNA-bd_dom_sf.
DR InterPro; IPR001739; Methyl_CpG_DNA-bd.
DR InterPro; IPR043449; PHF20-like.
DR InterPro; IPR006612; THAP_Znf.
DR InterPro; IPR038441; THAP_Znf_sf.
DR InterPro; IPR002999; Tudor.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR15856:SF51; MBD-R2; 1.
DR PANTHER; PTHR15856; PHD FINGER PROTEIN 20-RELATED; 1.
DR Pfam; PF01429; MBD; 1.
DR Pfam; PF20826; PHD_5; 1.
DR Pfam; PF05485; THAP; 1.
DR SMART; SM00692; DM3; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00980; THAP; 1.
DR SMART; SM00333; TUDOR; 2.
DR SMART; SM00355; ZnF_C2H2; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 1.
DR SUPFAM; SSF54171; DNA-binding domain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR PROSITE; PS50982; MBD; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50950; ZF_THAP; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00309};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00042}.
FT DOMAIN 1..85
FT /note="THAP-type"
FT /evidence="ECO:0000259|PROSITE:PS50950"
FT DOMAIN 372..441
FT /note="MBD"
FT /evidence="ECO:0000259|PROSITE:PS50982"
FT DOMAIN 498..523
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 112..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 591..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1138..1157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1142..1157
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1157 AA; 130822 MW; D449C19C2827DA42 CRC64;
MGVRKCVING CQSSTARDVD RGVTFHKFPI NPEVCKKWVE ACRVSQTLKL TKSVNVCSRH
FLKADFQDFK GTKYILKKEG VPSIFPWTTI GNEEVAIKQE NVAATSMTTI TTTNQMQEKP
DNSPSVVAEP PKKVARKLSN SNKDKAEKKL SVSPRKHSSN SNMNTNTTMY LPGTEIEAED
FNSKWHKARV IEVDSEDREY LIHFENNHDE WISMNSVRLR PLQQEVKQNP IDMTNIKVEP
TPTPSDGRHA VGDKVYARWS DSRKFPATIQ KVLDDDHYEV LFDDGFVKVV KAIHVTLKWG
KTDIKSTPSP AVQQQPLIPA QIAAEVLNPF KPNMEDFANL PEIPKDGEWC CHWVNDFPIG
EESFIDVKDG RIFSTIVQDW RLPPGWVKHI YQRISAYGKM DIILVSPAGR IFRSRNDFKT
YADETGEAMD PNIYDFALHK RRSKELGFYN YTDEYKQTIQ TDFSLRSSLI ADKISSTAMT
KDEVTIGGLK VTLKNNLYYC PQEDCNKTFR KENLLKIHIK HYHKPLAKDF GEFPTMTDLA
AQRSTVESEI EQPQVLSRKP LNLPSTEIAT NVATEIVTQV VTPTAEVPVF TPKEKPTTKR
TSSGASRPRI KKEKIDKSFS AEAVSLATGG QPMETKADEI QPSKLEQKLP EENSTILIKT
EKEITTTKPP VVTGDSVKLV EYFDPEQMIT THAVGKTQSN ESGPLLVPLE TQPTTSLIAP
IAPPISAKNQ NSKPTKSATK IKLFGGKRRK TSKLLQKRQQ QSKTLKPVIR KKRGPKPKSK
KIAAMSLENT FNDSDETRHS FGVNDSLLKQ QMLYQQLQHQ QQLYNDNNTE TSQNTNTSIC
GIYGDDSTTM YSGSNLLYQT PQNSNFINEN GEVIKIVRMK EEEIINCICN FGEEDGLMIQ
CELCLCWQHG ICNGFEKDTQ VPDKYVCFIC RHPQRGRLSK KYIHDQDWLY EGKLPVANYH
AANQKHSARF DILKQSHMLT GNLLDLKRFM HSLKVKINIS RRKDHPKMYL WSKKWDKSPP
KVGQQSSTGI SGLLKNIKEE KSEVKEDEEV NTPIIPQPEA AIDSSECQAI LLGHIQKQQS
IAMSRLQTIE AQIIALEALD DKANILESPS SSKSYPKSKQ VIQMLINDLG KMQKLADIHG
QSIPPPPLPL PQSTAPQ
//
