ID K9IPF6_DESRO Unreviewed; 2045 AA.
AC K9IPF6;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 22-FEB-2023, entry version 39.
DE SubName: Full=Putative chromatin remodeling complex wstf-iswi large subunit {ECO:0000313|EMBL:JAA50080.1};
OS Desmodus rotundus (Vampire bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Phyllostomidae;
OC Desmodontinae; Desmodus.
OX NCBI_TaxID=9430 {ECO:0000313|EMBL:JAA50080.1};
RN [1] {ECO:0000313|EMBL:JAA50080.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Salivary gland {ECO:0000313|EMBL:JAA50080.1};
RA Francischetti I.M.B., Assumpcao T.C.F., Ma D., Vicente E.C.,
RA Ribeiro J.M.C.;
RT "The Vampirome: Transcriptome and Proteome Analysis of the Submandibular
RT and Accessory Glands of the Vampire Bat and Vector of Human Rabies,
RT Desmodus rotundus.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the WAL family. {ECO:0000256|ARBA:ARBA00007444}.
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DR EMBL; GABZ01003445; JAA50080.1; -; mRNA.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd05503; Bromo_BAZ2A_B_like; 1.
DR CDD; cd01397; HAT_MBD; 1.
DR CDD; cd15630; PHD_BAZ2B; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR037374; BAZ2A/B_Bromo.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR018501; DDT_dom.
DR InterPro; IPR016177; DNA-bd_dom_sf.
DR InterPro; IPR001739; Methyl_CpG_DNA-bd.
DR InterPro; IPR028941; WHIM2_dom.
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; PTHR45915:SF1; BROMODOMAIN ADJACENT TO ZINC FINGER DOMAIN PROTEIN 2B; 1.
DR PANTHER; PTHR45915; TRANSCRIPTION INTERMEDIARY FACTOR; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF02791; DDT; 1.
DR Pfam; PF01429; MBD; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF15613; WSD; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00571; DDT; 1.
DR SMART; SM00391; MBD; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF54171; DNA-binding domain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS50827; DDT; 1.
DR PROSITE; PS50982; MBD; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 2: Evidence at transcript level;
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
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:PRU00146}.
FT DOMAIN 579..650
FT /note="MBD"
FT /evidence="ECO:0000259|PROSITE:PS50982"
FT DOMAIN 927..992
FT /note="DDT"
FT /evidence="ECO:0000259|PROSITE:PS50827"
FT DOMAIN 1808..1858
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1954..2024
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 69..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 679..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 861..883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1106..1181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1260..1300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1320..1370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1420..1452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1874..1917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..226
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..568
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..710
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1139..1160
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1280..1296
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1324..1370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1428..1444
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2045 AA; 227342 MW; 24AEEEB54FBBBA67 CRC64;
MESGERLPSS TASATIPTSS SMPSVASSVS KGGLSTGAAS LSSTISPCGA EWWRTTDVHT
RTGAAFFPPL LGIPPLFAPP AQNHDSSSFH SRTSGKSNRN GPEKGVNGSI NGNSTSSVSG
INTSVLSTAA SSSVGQTKSI SSGGGNRKCN QDQNKNQPLD ARTNKIKDKK PRKEAIESSS
NSDSDSGTSS DTSSEGISSS DSDDLEEDEE EEEDQSIEES EDDDSGSESE AQHKSNNQVL
LHGISDPKAD GQKATEKAQE KRIHQPLPLV SESQTHSSFQ SQQKQPQVLS QQLPFIFQSS
QAKEESVNKH TSVIQSTGLV SNVKPLSLVN QAKKETYTKL IVPSPDVLKA GNKNTSEESS
PLTSELRSKR EQYKQTFPAQ LKKQESSKSL KKVIAALSNP KGTSSSPAHP KPTLENNHPN
PFLTNALLSN HQPNGVIQSV IQEAPLALTT KPKMQSKISE NIATASSTPF SSPVNLSIGG
RRTPGGQTAV MPSASPILHG QGKEKAVSNN VNPVKTQHHS HPAKSLAEQF RGTDSDIPSS
KDSEDSNEDE EEDDEEEDED DEDDESDDSQ SGTSKRRRVT DERELRIPLE YGWQRETRIR
NFGGRLQGEV AYYSPCGKKL RQYPEVIKYL SRNGIMDISR DNFSFSAKIR VGDFYEARDG
PQGMQWCLLK EEDVIPRIRA MEGRRGRPPN PDRQRAREES RARRRKGRPP NVGSAEFLEN
TDAKLLRKLQ AQEIARQAAQ IKLLRKLQKQ EQARVAKEAK KQQAIMAAEE KRKQKEQIKI
MKQQEKIKRI QQIRMEKELR AQQILEAKKK KKEEAANAKL LEAEKRIKEK EMRRQQAVLL
KHQERERRRQ HMMLMKAMEA RKKAEEKERL KQEKRDEKRL NKERKLEQRR LELEMAKELK
KPNEDMCLAD QKPLPELPRI PGLVLSGSTF SDCLMVVQFL RNFGKVLGFD VNIDVPNLSV
LQEGLLNIGD SMGEVQDLLV RLLSAAVCDP GLITGYKAKT ALGEHLLNVG VNRDNVSEIL
QIFMEAHCGQ TELTESLKTK AFQAHTPAQK ASVLAFLINE LACSKSVVSE IDKNIDYMSN
LRRDKWVVEG KLRKLRIIHA KKTGKRDTAG GIDLGEEQHP LGTPTPGRKR RRKGGDSDYD
DDDDDDSDDQ ADEDDEDEED KEDKKGKKTD ICEDEDEGDQ AASVEELEKQ IEKLSKQQSQ
YRRKLFDASH SLRSMMFGQD RYRRRYWILP QCGGIFVEGM ESGEGLEEIA KEREKLKKAE
SMQIKEERPE ISEDTLSCSN PDHCEQKEEP KEKDNTNLFL QKPGSFSKLS KLLEVAKMPP
ESDVMTSKPN SSGNGCTLSY QNSGKHSVGS IPSTATQSSM EKTDSNNLFN TGSGGAGKFY
SPLPSDQLLK ALTEKNRQWF SLLPRTPCDD TSLTHADMST ASLMTPPSQP PSKSPSPAPA
PPLGSSSAQN PVGLNPFALS PLQMKSGVSM MGLQLCGWPT GMLSSNIPFT SPLPSLGAGL
GLSEGNSNSF LIPNVASNKS ESPVPQNEKV SSAQPAAVEV AKPVDFPSPK PIPEEMQFGW
WRIIDPEDLK ALLKVLHLRG IREKALQKQI QKHLDYITQA CIRNKDVAII ELNENEENQV
TRDIVENWSV EEQAMELDLS ILQQVEDLER RVASASLQVK GWMCPEPASE REDLVYFEHK
SFSKLCKEHD GEFTGEEESS AHALERKSDN PLDIAVTRLA DLERNIERRY LKSPLSTTIQ
IKVDNVGTVT VPAPAPSISG DGDGIEEDIA PGLRVWRRAL SEARSAAQVA LCIQQLQKSI
AWEKSIMKVY CQICRKGDNE ELLLLCDGCD KGCHTYCHRP KITTIPDGDW FCPACIAKAS
GQTLKFKKLH VKGKKNNDSK KGKKGTLTGD TEDEDSASTS SSLKRGSKDL KKRKMEENTS
INLSKQESFA SVKKPKRDDS KDLALCSMIL TEMETHEDAW PFLLPVNLKL VPGYKKVIKK
PMDFSTIREK LSSGQYLNPE SFALDVRLVF DNCETFNEDD SDIGRAGHSM RKYFEKKWTD
TFKVS
//
