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Database: UniProt
Entry: A0A1I8EB58_WUCBA
LinkDB: A0A1I8EB58_WUCBA
Original site: A0A1I8EB58_WUCBA 
ID   A0A1I8EB58_WUCBA        Unreviewed;      1290 AA.
AC   A0A1I8EB58;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=SAP domain-containing protein {ECO:0008006|Google:ProtNLM};
OS   Wuchereria bancrofti.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Wuchereria.
OX   NCBI_TaxID=6293 {ECO:0000313|WBParaSite:maker-PairedContig_1260-snap-gene-4.29-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:maker-PairedContig_1260-snap-gene-4.29-mRNA-1}
RP   IDENTIFICATION.
RC   STRAIN=pt0022
RC   {ECO:0000313|WBParaSite:maker-PairedContig_1260-snap-gene-4.29-mRNA-1};
RG   WormBaseParasite;
RL   Submitted (NOV-2016) to UniProtKB.
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DR   STRING; 6293.A0A1I8EB58; -.
DR   WBParaSite; maker-PairedContig_1260-snap-gene-4.29-mRNA-1; maker-PairedContig_1260-snap-gene-4.29-mRNA-1; maker-PairedContig_1260-snap-gene-4.29.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   Gene3D; 1.10.720.30; SAP domain; 1.
DR   InterPro; IPR045354; BURAN.
DR   InterPro; IPR025224; CCAR1/CCAR2.
DR   InterPro; IPR025954; DBC1/CARP1_inactive_NUDIX_dom.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR045353; LAIKA.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR025223; S1-like_RNA-bd_dom.
DR   InterPro; IPR003034; SAP_dom.
DR   InterPro; IPR036361; SAP_dom_sf.
DR   PANTHER; PTHR14304; CELL DIVISION CYCLE AND APOPTOSIS REGULATOR PROTEIN; 1.
DR   PANTHER; PTHR14304:SF11; SAP DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF19257; BURAN; 1.
DR   Pfam; PF14443; DBC1; 1.
DR   Pfam; PF19256; LAIKA; 1.
DR   Pfam; PF14444; S1-like; 1.
DR   Pfam; PF02037; SAP; 1.
DR   SMART; SM01122; DBC1; 1.
DR   SMART; SM00513; SAP; 1.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF68906; SAP domain; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
DR   PROSITE; PS50800; SAP; 1.
PE   4: Predicted;
KW   Activator {ECO:0000256|ARBA:ARBA00023159};
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT   DOMAIN          624..658
FT                   /note="SAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50800"
FT   DOMAIN          892..927
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   REGION          142..310
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          564..619
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          704..753
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          853..881
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          966..997
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1107..1177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1023..1078
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        267..283
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        292..307
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        568..600
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        968..985
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1111..1166
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1290 AA;  145313 MW;  66E281B4BC8BBAA2 CRC64;
     MSQFGPKNPA AWARPPGANQ QLNAGLFQNP LIGAQPFAQM GMINAAAFSQ QAVGNMGMNL
     GMLQTPSQTI RMQAQQQQKN RTFSGVVTKM HDNYGFIDDD VFFQVSNVRG ALPRTGDRVM
     VEASYNPTMP FKWNAYRVQL IGDKGGPGGG GPPTHTPPDR GRQPITGRGM IPGEQSWAGK
     TLEKPQAVTH INDSRSPPRS RSPIGPGRHR SPRGGQCGPP ALVQDMRRLS SPRRISPPRG
     LARRSPRRSP PRDYSKGQMG RISPKHSTPA RKHEGKREHS ASVSGRNRSP SQKHDPSTHD
     SLSPPRRRSR IIPRYQCYIP KPPILNGTRQ TVMQLRKRYP LLYIPSDFSD ISIEWPKTTP
     IENPISISTA PITYHILHKD IDCPSENLHA LNPPDADCRF SVKVVLMSHQ GLSLVHQKAF
     GLLVDGSIDE NVDSASLKRC LNFVVGTRNK EMMAVGGAWS PSLDGDNPET DPQVFVHTAI
     RTVRTLIGVD LSRCPRWYIR YYRAEKDRMD TCCLFLPDTS GLMPTEDCYQ QLLATLKDQL
     GNKLAAIDAQ KLVLPSTVAA TATDCGDAGE GTTVTTEPTA PTGDTQQQLQ QGQQQSDANK
     EQVQEVEEED DEDLNPTHWS KLDIRTMKVA ELRQELMARD LETKGVKSVL CARLQEALDQ
     EKTKDEDKED VCLKTLAVGM VEVAKPQEEN EEKQLTVEDK KAIEKSEKEK KEKKASLELA
     KPQEENEEKE LTDEDKKAIE KSEKEKKEKK ASLERHFTIP KEPGILVYPN RMAKGGKFDC
     KIVSLHTMLD YRIEDNKEHS FELAVMAECI SEMLDRSQAF IAYKTLSRAI DKESEKKRRE
     EAKLAEVIGA EEGTESVKAD KTEKPEEEKK KEDEKKEEEQ RKSLVEARKP IIIDRTVFQA
     FAHFDQNLCG YILEKDFEEI LFSIGLNISR AQVQKLLKRY LSRDRISYRY LTDSWANKDG
     TVTYRPGVIS DPPTTEQLTK GNMSKESIDA NKKTTSEAPD ISATGSVIYL GSLMNIPQVL
     EQVSKMESDS NAALQKVDVL EAQLKDGAKH VQVLEKKKKR LEEDVEKYRK RLHDAEKCLK
     NSVDDTVQMK SAIQEFRRIG ERMIGMAEKL MPNPKEEEKT SEKDEKDVKK EKKDDKDDKK
     VPKKKDSALT KVNGEAEEKK ELQLVDEVGG NDVGDEPMES DVIVLSEEVT GDEEKDVKKE
     ILSSQKTDST TETVESDTVT SLTFPNWGGS TWTERFRKLL AIISYFLVRA KFLNRSKMPR
     CGGTYILLWP HLGHQEIILD RYWSYMNCCE
//
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