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Database: UniProt
Entry: A0A1V9ZRG0_9STRA
LinkDB: A0A1V9ZRG0_9STRA
Original site: A0A1V9ZRG0_9STRA 
ID   A0A1V9ZRG0_9STRA        Unreviewed;      1480 AA.
AC   A0A1V9ZRG0;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Nephrocystin-3 {ECO:0000256|ARBA:ARBA00040387};
GN   ORFNames=THRCLA_05922 {ECO:0000313|EMBL:OQS00577.1};
OS   Thraustotheca clavata.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC   Thraustotheca.
OX   NCBI_TaxID=74557 {ECO:0000313|EMBL:OQS00577.1, ECO:0000313|Proteomes:UP000243217};
RN   [1] {ECO:0000313|EMBL:OQS00577.1, ECO:0000313|Proteomes:UP000243217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 34112 {ECO:0000313|EMBL:OQS00577.1,
RC   ECO:0000313|Proteomes:UP000243217};
RX   PubMed=25527045; DOI=10.1093/gbe/evu276;
RA   Misner I., Blouin N., Leonard G., Richards T.A., Lane C.E.;
RT   "The secreted proteins of Achlya hypogyna and Thraustotheca clavata
RT   identify the ancestral oomycete secretome and reveal gene acquisitions by
RT   horizontal gene transfer.";
RL   Genome Biol. Evol. 7:120-135(2014).
CC   -!- SIMILARITY: Belongs to the BicC family.
CC       {ECO:0000256|ARBA:ARBA00007662}.
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:OQS00577.1}.
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DR   EMBL; JNBS01001695; OQS00577.1; -; Genomic_DNA.
DR   STRING; 74557.A0A1V9ZRG0; -.
DR   OrthoDB; 50780at2759; -.
DR   Proteomes; UP000243217; Unassembled WGS sequence.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   CDD; cd00105; KH-I; 1.
DR   Gene3D; 3.30.1370.10; K Homology domain, type 1; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR   Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR024983; CHAT_dom.
DR   InterPro; IPR004087; KH_dom.
DR   InterPro; IPR004088; KH_dom_type_1.
DR   InterPro; IPR036612; KH_dom_type_1_sf.
DR   InterPro; IPR049052; nSTAND1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR45641:SF1; NEPHROCYSTIN-3; 1.
DR   PANTHER; PTHR45641; TETRATRICOPEPTIDE REPEAT PROTEIN (AFU_ORTHOLOGUE AFUA_6G03870); 1.
DR   Pfam; PF12770; CHAT; 1.
DR   Pfam; PF00013; KH_1; 1.
DR   Pfam; PF20703; nSTAND1; 1.
DR   Pfam; PF07647; SAM_2; 1.
DR   Pfam; PF13374; TPR_10; 1.
DR   Pfam; PF13424; TPR_12; 1.
DR   PRINTS; PR00364; DISEASERSIST.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00322; KH; 1.
DR   SMART; SM00454; SAM; 1.
DR   SMART; SM00028; TPR; 3.
DR   SUPFAM; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR   SUPFAM; SSF48452; TPR-like; 2.
DR   PROSITE; PS50084; KH_TYPE_1; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 1.
DR   PROSITE; PS50005; TPR; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000243217};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00117};
KW   TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW   ProRule:PRU00339}; Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687}.
FT   DOMAIN          4..84
FT                   /note="SAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50105"
FT   REPEAT          1195..1228
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REGION          1428..1480
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1428..1446
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1458..1480
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1480 AA;  166921 MW;  191B4480EF5BC17C CRC64;
     METWSKERVG EWLVKAGFTD LVQVFVENDI DGGTLLKERN WHHILFFVAL LPDLTNEILR
     NELKINSFGK RSQLLAAIRQ IKERDNVLDL AVLHAAPLVL KTTHNDVPTV LAMEKLDLEA
     ERLALQQALN SDFLGRIQLR FDVATADSFR TLLTTWKCKV LHFSGHGVGY NEMLCFEDGS
     GCAHLITPKA LCELIYSGAI EASDYLQVVF VSSCHSERLA NVFVEAGVPH VVAVHSDSRI
     LDSSGNTFAK HFYLSLFAGK SVLAAFDIAK TAVRALPPTN KRACCCAHLH ERTCRWALSG
     MDHSKHPPNR CCCKGESLSW PHDESSKFLL LGQPQKSMHD VVVFPKLPRG KLIDLTPHCP
     SNLPAMHGQF VGRNIDTYNL VRSVVKGNVT VCTGAPGIGK SSLVIAAAHY ILQRRICPDG
     VFYIDLEGLA GLDFSAVLYA CFLAISTADA TLLYRYAIAR NVGLTLGENT THTQLFAELG
     SKRCLLVLDK VEELLDKDRR NCEAFLGQLV ATAHHTRLLL GSRRIPNIPN VTVTSINIAE
     LPLSIATNLI RSMALQCTQA EAEKLATICG KLPLALRVVG RALANSRARI TPQDLIERLQ
     LEDHRLEEMN NLSEAGQKEC LDRCIRSSFT QLEWPLRLAF MAMGLFRGVF DLKAACAVLQ
     SSYQSPTLLK SHSSPSVLLD TRSPFTPPSL SRTFNSANQL NSHSMLDDGT SSVKSLGSEL
     YELDDYFDKD DALTSMSYSL LNLESEEEVV ASTCDVTQAI PALELLNQWS LVEKVMPMRN
     TKMHPQQARY RLHNMIQLFA EDEATKFSNE TSEGEALFLS WRRRFVRHYC LVVANASHAF
     RYEGLLLKFD SERSNIESAL RIAHQLSEHA EYVAREHQAS GVEESKYVPV VDVLLHSNLV
     VRGRFIFRAR MDPRYRLKLF AKSIKLSRSA RVLNCHCKHP ENDSTILDAS DTMSQYEPTQ
     TPKTIDACEC PGVMELLELE VLMLMEMGYA HFDVNEDPNA EHMYRESLRI QQEVLHRTDH
     SYVAEAMNYL GIVLSTRRGF SPVNAWKFRK AESLLLQAKE IRERVLGPVH PDFATSLNNL
     GNFYKSALAM IKDDAVTPGG LGYGGVLLKT NDEIRELYEK SLAIYKSHLV EDHPLVARSL
     NNMALFLVHT YDKIPKAKLP SREKLTEVDK EIESLYKQAL EIRRKKLGNK NPETAATLNN
     LGNLKYNQGE FTAAEAYLRE ALTIRQQYYT NTNDRVSTTM LNLGRILVAQ EKYKEAEMIY
     REAQAIRETL MPNSREHGFC IEKIGRCMIK QGREEEGKKL VLEGQLMKRK CAFQSRNSTA
     SNDIETESLA SESCTDTFKE HIFIHEYLSA EVISSSDFNV EGQIIGKQGI NLRRIEEQSG
     AQVHFFSQKR HRDGESANFE FVATCEDAVA QAKSLTIEHL KDIQFRYDKR QSKPRQFKDP
     NRRPPRHEDR RRHNRGRGNQ NANNAPSSMQ FSLEDLINKK
//
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