ID A0A183MI15_9TREM Unreviewed; 1636 AA.
AC A0A183MI15;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:VDP18928.1, ECO:0000313|WBParaSite:SMRZ_0001569101-mRNA-1};
GN ORFNames=SMRZ_LOCUS15690 {ECO:0000313|EMBL:VDP18928.1};
OS Schistosoma margrebowiei.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=48269 {ECO:0000313|WBParaSite:SMRZ_0001569101-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SMRZ_0001569101-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDP18928.1, ECO:0000313|Proteomes:UP000277204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zambia {ECO:0000313|EMBL:VDP18928.1,
RC ECO:0000313|Proteomes:UP000277204};
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00475}.
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DR EMBL; UZAI01016982; VDP18928.1; -; Genomic_DNA.
DR STRING; 48269.A0A183MI15; -.
DR WBParaSite; SMRZ_0001569101-mRNA-1; SMRZ_0001569101-mRNA-1; SMRZ_0001569101.
DR Proteomes; UP000277204; Unassembled WGS sequence.
DR GO; GO:0090535; C:WICH complex; IEA:InterPro.
DR GO; GO:0140801; F:histone H2AXY142 kinase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR047174; BAZ1B.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR028941; WHIM2_dom.
DR InterPro; IPR013136; WSTF_Acf1_Cbp146.
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; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46802; TYROSINE-PROTEIN KINASE BAZ1B; 1.
DR PANTHER; PTHR46802:SF1; TYROSINE-PROTEIN KINASE BAZ1B; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF00628; PHD; 2.
DR Pfam; PF10537; WAC_Acf1_DNA_bd; 1.
DR Pfam; PF15613; WSD; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51136; WAC; 1.
DR PROSITE; PS01359; ZF_PHD_1; 2.
DR PROSITE; PS50016; ZF_PHD_2; 2.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
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, ECO:0000256|PROSITE-
KW ProRule:PRU00475}; Reference proteome {ECO:0000313|Proteomes:UP000277204};
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:PRU00175}.
FT DOMAIN 32..136
FT /note="WAC"
FT /evidence="ECO:0000259|PROSITE:PS51136"
FT DOMAIN 1196..1246
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1199..1243
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1337..1386
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1529..1605
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 273..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 515..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 721..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1254..1331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1417..1518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 782..811
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 290..305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..332
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..537
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..769
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1306..1331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1427..1491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1498..1513
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1636 AA; 187204 MW; 471D83D6D50B2389 CRC64;
MPLISTKLHV LNPIWRKKKP RDTEQHEEHE PKPAFIVPET QEICTSAEEL QRKITIYNEN
IWTCRVTGKP NLTYREALKT EATAIRTLKK CFPKFFEKTI LERVHLKSLV HSCWTTIHEQ
FHIAEPVKLK TSVPDNTSPN NSDKENVTKK NSPIKVIFKP FRINRAPSKD HIKMFIRSHA
MRYGPNFTGP WIVNEELLRR HKIPLKSPGC QVDKVKLKQM SKALEEEYFV RVMNSRRQSN
GEGTSDDITS STPLNFKRIK RFSVLREDNT SKMLEENEDN LPLAQLKDRS QLKHSLEDSR
KKKMKQSTLF QFGKKTPTKD EIPDKPTINR PKKNTNERCA LPRVAQHLIK MFGEDRNNPA
IETQIRLCAK FISDVDILKL PVELRDPVRS KKEAFAFKKK LLTMSPTQRK QALQEMKEKQ
KIERIHANKL LDDQHLMTAL PQCPRLPEPS KLELPPSFNE SLFGRLLGLT EFFHVFHSLL
VEGSVDDTEV ENPSENNVLS GFCRFPVESL VAGVGEPGYS DDDDDGNTDE EEEEAGLTES
NAPLPKICIK SLRRLGLKRL LNAVTTNNPS AGAYRSLARP LSVLLRLVLR DEQIGKKREL
GLKLAKFPVT PYTAPELLRL TLLNEIPSNH ARTTILEQLR NHDAPVTDPN PFDQNSPVTQ
LIHHLSNSDL HELFPEIRVI ALEWAVDKIF DLDLIDDHIM ACQRRAADAW QRKIQVLRDK
NLRKKDKKDN ANEANKTSNN NNSNNLSTNQ LDESKSKADT PTATADDITD SENDLASIVK
RRRILAARAA IEKEEKENLE RQRRLEMAQE HAEERAINTV SRLHDIRSTE AKCVLRNNPI
GYDRYYRRVW YFRCSPDRLF LEANWASSSI MYSVDSFRKN ESVPITTLND ETIPQPAHDF
VKNDTLNSGT ISSSWSNWYF YDRPEQLDEL LNSLLTHGVR ESHLKSQLLA DGFLESLKKR
WRSGLSNELV IKADTTNGTP INVEKHPSHH KRDLPAGAAL AGALLKNILD TEVRLRSGGL
GGVPDFTKWQ ERLAQIQESY GIQQETLNVN LSSKPNLSAL SSLCELPNKA GLAMALIEVA
ENIIPRFLNV PDLCTNSKFD SNQNGTNDCH DLKTSFPDHV PFCRFSSGED SDASENNDRS
QELEKAVLDP EAHELRTRAW MTAWRTEVQN ARTLTRLNLL HACLDACVRW EKSVEDARCR
ICRRKTDDDN LLLCDGCNLA FHLYCLRPPL KRVPTGDWFC PTCGPASRAL EKRKREERLA
RSARRRKRAL SSDDEEQLNS DNNEESSGES EATQKIKRRN PRSFRCKGGN DSSAFNIKRS
VSPANRNSVS SRNIRHDTSC LVCSDSIGDL VLCSNCPNVF HLDCHDPPLH HIPRGDGWQC
SVCRSNKKRS TITSYFQSRD YRRKTYQAIF KKRAVSPDER SEDEFLNSTS FTRSTRSNNR
SRRNIAMSDT DDEQQSSEAS SDVDIRSNNQ RPISRRRSAS RSASALSSQL NKYPKRRRRH
LSDQEDTSET EQMDEKSQSL CSHILDAVYK HKHSWPFRKP VDRSQVPDYY EIITDPIDLS
MMRDWLSEGR YNTESTNAGL KKLVHDLGTM FYNAELYNAA DSDVWLAGEQ LEKFVKNQFA
HINTDVVYSR PALGDA
//
