ID A0A1W0A1S2_9STRA Unreviewed; 1755 AA.
AC A0A1W0A1S2;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=PA14 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=THRCLA_03732 {ECO:0000313|EMBL:OQS03990.1};
OS Thraustotheca clavata.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Thraustotheca.
OX NCBI_TaxID=74557 {ECO:0000313|EMBL:OQS03990.1, ECO:0000313|Proteomes:UP000243217};
RN [1] {ECO:0000313|EMBL:OQS03990.1, ECO:0000313|Proteomes:UP000243217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 34112 {ECO:0000313|EMBL:OQS03990.1,
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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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:OQS03990.1}.
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DR EMBL; JNBS01000701; OQS03990.1; -; Genomic_DNA.
DR STRING; 74557.A0A1W0A1S2; -.
DR OrthoDB; 66411at2759; -.
DR Proteomes; UP000243217; Unassembled WGS sequence.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProt.
DR CDD; cd00055; EGF_Lam; 1.
DR Gene3D; 2.60.40.2030; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 5.
DR Gene3D; 3.90.182.10; Toxin - Anthrax Protective Antigen;domain 1; 1.
DR InterPro; IPR038081; CalX-like_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR044801; Filamin.
DR InterPro; IPR017868; Filamin/ABP280_repeat-like.
DR InterPro; IPR001298; Filamin/ABP280_rpt.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002049; LE_dom.
DR InterPro; IPR037524; PA14/GLEYA.
DR InterPro; IPR011658; PA14_dom.
DR PANTHER; PTHR38537; JITTERBUG, ISOFORM N; 1.
DR PANTHER; PTHR38537:SF17; JITTERBUG, ISOFORM N; 1.
DR Pfam; PF00630; Filamin; 3.
DR Pfam; PF07691; PA14; 1.
DR SMART; SM00557; IG_FLMN; 3.
DR SMART; SM00758; PA14; 1.
DR SUPFAM; SSF56988; Anthrax protective antigen; 2.
DR SUPFAM; SSF141072; CalX-like; 1.
DR SUPFAM; SSF81296; E set domains; 4.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01248; EGF_LAM_1; 1.
DR PROSITE; PS50194; FILAMIN_REPEAT; 3.
DR PROSITE; PS51820; PA14; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Reference proteome {ECO:0000313|Proteomes:UP000243217};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..1755
FT /note="PA14 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013003608"
FT DOMAIN 146..179
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 522..658
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
FT REPEAT 781..885
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 913..999
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 1019..1109
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT DISULFID 150..160
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 169..178
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1755 AA; 190130 MW; 942EA0D4D26CF254 CRC64;
MILPFIFLYL LRTRAFRIVN NSSATSTPLF NRYAHGIVGY YGDPTTTFFR EHVNPGAIFH
PDAPTQWNGP SISLSCPSMV GPLDNGEYYC NGKEYGYCDR RSGSCWCNKG YTGIDCTECI
PEYFQAGGIC YPRRTSFTIS GWLSLHLGNC LNDCSGQGSC NYMTGLCTCN PSRLGSDCSQ
VSCHVLDTLC QSCSDGQCLQ CFSGYYVTPM NACAPCTNFD PRCIECNAVK GCLTCADFQL
NSIKRSGPRT IDPWPMPSEE IVREFSLTNV YSSQSSHSFD EAEVYSVLPS SLNITQACQQ
GLSGDASWKC VNSPSSHIIC GHTGTITFAS PSYAIAQNST FLPITIVRTG GGYGEASVLY
ELVHRTSTKA DVSPTAYYTT TQRLTFPPSV IQLTFYITIH DNPAVKPYNP VFDLVLKEPS
ANVAIGNQRI STVVIYEGPG AINTKLQLAV NSTGVANISM PIAIYGPGLS LSSTMVGTAT
YTSGNLVDVD EIPLSLAFNG TQLVSSWLPV VSGNYTLLFF QLYAGGLLGT YYSTPSLEGS
VVVERMDAVI NFTFTDTQSY SIGYESVRWR GFIKATTSEL TTFQIDTLGS IRLWVQGKLV
VDGWVQLDAP NHSGSVQLQA NKLYSIQLDY RPHPITLDYI YLKWQTTTIP LQVIPTSQLY
TSTLLPWLNK SIIIQPNMPS QAWYRGPLSG IAGVPFTYSF YSVDSLNNIR RNLFFNTQDT
GVFRSYISSG LITLDAKLTF NVSSGLIKGS TVPTVAGLYT LSVLLNQQLL YGFPIGINLS
PSPNTGPQSF VSGPGIQVTG NVAATTTTIL IQGIDIYGNQ QSFGGGNFTI IATHLASAKV
DLGVVTDFGN GSYLVSYTPR FSGTYSITIT ILGIHVASSP YLIITVPNIA YGPSCSVISG
NTIVFNIHHD DLGAGISVGT TGVPAVFLVQ LRDVNSNTIV SGSATVSLNS TSLLQAPLCT
NLLNGTYSCS YIPTSAGTII LSVFVNNNPI ANSPFNVQMT TGVIMASSSI ATSPFGSTGL
YYGIAGENTW FLLQAQDTYG NNRSSVDLIG LSFQNATLAA VNATSTNITY LGSGLYNVNY
TIVKAGTYIM HVVVNGSTEI YQSPFTITIY PNVADIITTT ATILTPLPLT AGQSITAAIE
PRDIYGNPTT QTYYDFYTFG QIQLVKPSLT LTTFTPTVAG IHRFEPQIYL NGGGNVSVYS
MLTEFGAATY LTKQPLGFDQ DFNLLIDGVQ WVWDGYISSV TSERYVLTLD FHGHVEMYLN
NTLMVNSSAE SFQFEYTFTA SLKTKCHVVY TKSDTVQPHY FHVNWSSLTV QQRPIPLTCL
CSKWKITSIT PILQVYPAPP AQYQLLSSIP DVWNAGISVS FDVIALDMYG NIRAQGGDRL
GVYLSNAASS IVDHYNGSYS ITMTAFTAGS LQTLNIGVNA TPIDSAISPY AYIQSLSPIL
NSPFSVTILP STVQLKSTLF SSITSGIAGK PLSFTFTLVD SYNNVVITQQ PIQVYLGSLP
CTTTFIASTY TVNCIPQLAT LPNVRLVLGS SDLTFFSISI SPSSANATSS SITSFTSLQQ
ANQLQSFVVI LYDSYNNPLT TGGNYLGIIF SGKSELHVPA VDAGNGTYII YYSLPFPGVY
QAQVLLVSGS GLLGRYYASE SDPLPETSQV DSVLALTDHA KVIWSGFLVP TYSEVYLLTW
SVANVVVYLD NRLVEGSVTL IGNYPHAIQI QASGTIPALI LQWTSARTPK QPIPLSQMYP
WSDEILPRHN VYVVT
//
