ID A0A1V9XRY5_9ACAR Unreviewed; 1323 AA.
AC A0A1V9XRY5;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 08-NOV-2023, entry version 31.
DE RecName: Full=MYND-type domain-containing protein {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=BIW11_07899 {ECO:0000313|EMBL:OQR76249.1};
OS Tropilaelaps mercedesae.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Mesostigmata; Gamasina; Dermanyssoidea; Laelapidae;
OC Tropilaelaps.
OX NCBI_TaxID=418985 {ECO:0000313|EMBL:OQR76249.1, ECO:0000313|Proteomes:UP000192247};
RN [1] {ECO:0000313|EMBL:OQR76249.1, ECO:0000313|Proteomes:UP000192247}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wuxi-XJTLU {ECO:0000313|EMBL:OQR76249.1};
RX PubMed=28327890; DOI=10.1093/gigascience/gix008;
RA Dong X., Armstrong S.D., Xia D., Makepeace B.L., Darby A.C., Kadowaki T.;
RT "Draft genome of the honey bee ectoparasitic mite, Tropilaelaps mercedesae,
RT is shaped by the parasitic life history.";
RL Gigascience 6:1-17(2017).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OQR76249.1}.
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DR EMBL; MNPL01005100; OQR76249.1; -; Genomic_DNA.
DR STRING; 418985.A0A1V9XRY5; -.
DR InParanoid; A0A1V9XRY5; -.
DR OrthoDB; 5314634at2759; -.
DR Proteomes; UP000192247; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003714; F:transcription corepressor activity; IEA:InterPro.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR Gene3D; 6.10.140.2220; -; 1.
DR Gene3D; 1.20.120.1110; TAFH/NHR1 domain; 1.
DR InterPro; IPR013289; CBFA2T1/2/3.
DR InterPro; IPR037249; TAFH/NHR1_dom_sf.
DR InterPro; IPR003894; TAFH_NHR1.
DR InterPro; IPR002893; Znf_MYND.
DR PANTHER; PTHR10379; MTG8 ETO EIGHT TWENTY ONE PROTEIN; 1.
DR PANTHER; PTHR10379:SF14; NERVY, ISOFORM D; 1.
DR Pfam; PF07531; TAFH; 1.
DR Pfam; PF01753; zf-MYND; 1.
DR PRINTS; PR01875; ETOFAMILY.
DR SUPFAM; SSF144232; HIT/MYND zinc finger-like; 1.
DR SUPFAM; SSF158553; TAFH domain-like; 1.
DR PROSITE; PS51119; TAFH; 1.
DR PROSITE; PS01360; ZF_MYND_1; 1.
DR PROSITE; PS50865; ZF_MYND_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000192247};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00134}.
FT DOMAIN 895..990
FT /note="TAFH"
FT /evidence="ECO:0000259|PROSITE:PS51119"
FT DOMAIN 1269..1305
FT /note="MYND-type"
FT /evidence="ECO:0000259|PROSITE:PS50865"
FT REGION 79..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 326..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 709..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 838..860
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1191..1234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..732
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1191..1214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OQR76249.1"
SQ SEQUENCE 1323 AA; 142034 MW; AE6BA279AF414826 CRC64;
VSADSMPVLP EAECSPGRWS LRNADEDTYK MEPTLNPTVV LESVRISKCL FNEAVNQSSK
ANNSEESALK LNFVLAHDTK DNQAEKNGDD NMTEEPPEKK AEDGEDTDVI DGSDSSGELT
IVQKEVEKEC KAEGPKSEGS GQAKGRRPQQ KIKKRKNMVN SKDTLNAPSI RYLVAKKRRL
EGAMQIKRAE ELSTAMENEA VAQRIAMEFS NIRRFRASPS NDVTKSERTS SPEASSAGVG
TKADVPSCRM QTSDSARRTP PASLILGPAG SQDPVSSVSL VTQSAFSGSV TCASKAQFAL
MSTWTPQSYP LSQVHHHIPV TDCPATRPAS FVSSPSRSAP HGSPLLETDS SSRENNLDDP
TEPAVSTVKR VDSNETTSES LHVEIASPPM IHIPSPLLSV DSLQTTECLG TNPRGNSRQT
NAADDTVTPL RNTHTARSRS PVGTPISASV LTYPTSASLS LGLKHLLIEN KCALPSSHTP
GEPHTDSGNQ LAAQEFRASQ AHAGPASVQA YRGRQSNDAL AIPSRNLSSE FNPKLNAFSV
DNLSKSDANN NDSLPTQGQP DTSGNSLSSI DPDVNSILVN KQQSCASDVY SRIASTGQAE
LNQSTSAKHK RETLLQLHGY SWRKMEALQP RSTTVGVSTC STLSGTSNLL VPHTACLPLW
NEGATCCTLS STSSNVRVVR QNDFEFAKPH TVPRKVRLSG GANLSAGPNA ASVLTPLGSD
TPSAQTLPRP SDSATFKGDR PAQTIFYPPC LTSCVPLGQP HSCRKSKSTM IWKHMEAQGG
PESMQTIDSA IKSVRARFVG ISGSSSAAGA SATSGSDSPL SNSNTILGCY LQGQKRSPLR
TDATDVRSVP PTGTSSSDTS GYVPSANVVV AYGRTALPKQ TITKPTIDSV SDRRSYNLHQ
LKRVLVTIQK FSTTVSLSVG KAVYHNIYAL VSGGSTIGDF VSRVKSAIRL TIRPGIAQFI
SLQLPHLQKE ITVQAASVRM SSSRYMRSNP ECLIDPTMEP GDPQEVFALE YEAPSTIHKQ
AIALAQPPSY ALLHSAQSRP PNVAQAGASC PLPSSLATAP LLLGGVHEVV PICGRRTPEV
NHPSYSPASS SVVELLEFDS GNSEPSVNSL AHHKPYIDMQ NNLMFAQEML DRVSKIIQTT
KKQINEVQQT EQWQLQCQQH KLQHQSNHRR QEQQQQQQVL QGLTNITSFD STLLDPSTAP
ESGPISQDSS LQRAARVNDA ADAREGTTEG KTASSLATFK NGSNFDANAA ASYEVSDLQT
TEPGVPERCW NCGRHAAETC SGCKLAKYCG PFCQHRDWEV HHRICLVIAA NRPCMASLAA
ALS
//
