ID A0A0P1AZQ7_PLAHL Unreviewed; 2137 AA.
AC A0A0P1AZQ7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Microtubule-associated protein {ECO:0000313|EMBL:CEG47969.1};
OS Plasmopara halstedii (Downy mildew of sunflower).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Plasmopara.
OX NCBI_TaxID=4781 {ECO:0000313|EMBL:CEG47969.1, ECO:0000313|Proteomes:UP000054928};
RN [1] {ECO:0000313|Proteomes:UP000054928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Sharma Rahul, Thines Marco;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TOG/XMAP215 family.
CC {ECO:0000256|ARBA:ARBA00025722}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CCYD01002887; CEG47969.1; -; Genomic_DNA.
DR STRING; 4781.A0A0P1AZQ7; -.
DR EnsemblProtists; CEG47969; CEG47969; CEG47969.
DR OMA; NWKERKE; -.
DR OrthoDB; 5477703at2759; -.
DR Proteomes; UP000054928; Unassembled WGS sequence.
DR GO; GO:0043232; C:intracellular non-membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0099080; C:supramolecular complex; IEA:UniProt.
DR GO; GO:0061863; F:microtubule plus end polymerase; IEA:InterPro.
DR GO; GO:0051010; F:microtubule plus-end binding; IEA:InterPro.
DR GO; GO:0030951; P:establishment or maintenance of microtubule cytoskeleton polarity; IEA:InterPro.
DR GO; GO:0046785; P:microtubule polymerization; IEA:InterPro.
DR GO; GO:0007051; P:spindle organization; IEA:InterPro.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 5.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR024395; CLASP_N_dom.
DR InterPro; IPR034085; TOG.
DR InterPro; IPR045110; XMAP215.
DR InterPro; IPR048491; XMAP215_CLASP_TOG.
DR PANTHER; PTHR12609:SF0; CYTOSKELETON-ASSOCIATED PROTEIN 5; 1.
DR PANTHER; PTHR12609; MICROTUBULE ASSOCIATED PROTEIN XMAP215; 1.
DR Pfam; PF12348; CLASP_N; 1.
DR Pfam; PF21041; XMAP215_CLASP_TOG; 2.
DR SMART; SM01349; TOG; 5.
DR SUPFAM; SSF48371; ARM repeat; 2.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000054928}.
FT DOMAIN 124..352
FT /note="TOG"
FT /evidence="ECO:0000259|SMART:SM01349"
FT DOMAIN 391..624
FT /note="TOG"
FT /evidence="ECO:0000259|SMART:SM01349"
FT DOMAIN 756..998
FT /note="TOG"
FT /evidence="ECO:0000259|SMART:SM01349"
FT DOMAIN 1019..1259
FT /note="TOG"
FT /evidence="ECO:0000259|SMART:SM01349"
FT DOMAIN 1368..1612
FT /note="TOG"
FT /evidence="ECO:0000259|SMART:SM01349"
FT REGION 622..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1276..1327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1668..1693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2108..2137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..671
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 710..741
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1675..1693
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2108..2127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2137 AA; 232949 MW; 1C72198F1F9F555C CRC64;
MDDRCLRNAT CKCSMCANFD VASLISISKA ISSNIKYGDS EDDDTEHNTI ASLPKISGVA
HSPPVPSQLA TVKADSPPLT ATMRPPPTPT IVQTISIAAS TDDVVMTDPE ASSLSKMEVD
SSTVNNEQND TIGIDVVLPK LTDTNWKVRK EGYEELKTLF EQSEFDSKQA EVVLDLFPKM
CEDTNASAME AGIAAVLTYT QAVEPFNEGI VSGVMTRVID KGFSARPGIV KLGTELTDAF
IAAGAAEKTV TALLEGTTNR KPKVPPVCAT CILDALKEYG PRVVPLQAIK AALPKLMEGA
VKVRPIAMSV MVEIHRWTGT ALLQDILANL RQAQQTEFEE KTKDIVPGQV VPTKFVRGAQ
SIKAAAGSSR RQDSMNGISL ADSSSAFDPR EFVETVDLLV KLSKSEFRKK LALPKWSEKV
EALKIVLELI GPVPKLANGD YYELVSTLKA LTNDSNVNIV AKSIEVLGVL ADGLRKNFTQ
YARIMFPELL RKLSDKKALI LSATNRALDL FLQHALTIEM MMEELKLACD STKNKAPPAR
VQTMAFIARA VENRYVDLND KTLIVSLGGM FLKGIDDTDP KVREAGQKYF IELLQATDQT
AGWLQIIMDE IARKNPRAHK TIQRGLSGGV SSAVSSRPNS AQSSRAESAS SSRPPSRPGS
AGSSASRSSF IESRKSEPDM DVEMESTPAA APAPVDPRRP LLKKRGPQTR TGIKFSTASN
TASTKRPPAS GPGSGMSNNG GASINFTPVA ISVTAEEAEE HLTALQIENW CTIKERFASS
KWMERKEAIE EIEGYVKEKS NTMNLSIIEA FTIYLSKQVK DFKDSNINVL KSAFQAVGTF
AESVAGKFSR GVVCLVTPRA CEKIGDKKAN ETIRTMMMQF CEATGPSYTM GCMIDYMPKV
RLPLAHFEAL SVLSDCVKDF GVSMCNPRAL IDYVKGPQGL EASNPKVRTA AISLLSTMYS
QLGPALVPIL NLDSWKPALA KSVEEEFQRV GFDPSKAMST VKRQVKGQEE VPAAADPGAL
FGRKDISSEI TKDLLDDMKN ETDKVAWKKR AEAMDRVQAM CESAGYAIEF TRPVQEVLRS
LKIRLNDANA NLKVKAANVI GVVASSVGPD IAKMSKILGA SLIAGVADNK KAMQAAAIQA
LHRWVRHNNK TSSTCMESLT ASLSEGLLNS VGRAELLGWA VEHLRNCDKL DLTCLVAPTV
QCIMDKSSEA REKAQVLLVE VMKSVGKETV LTIGCRDIKP AAMRALKPIL QKACEMVDAV
ENTASMDDAV SVAVATPSTP TTKSSAGHNS ADSSVMRRRA SPSASGNTPI KSRIARPSSI
RASLTSSSSL SENATKAVPL LKMSTNKTSR LSKGQFNKWI FETTSVSEMK SRKNEIEVEW
KPFLSPEFHA KLFAPSLDKG MLAALDELML CIINQKDEVI SSLDLILKWC TLRIVDNNVQ
ALAKLLEVLV KLLQMLKGAG YLLDDVEASI LLPYLLQESG QSKPRFRIRF RDVMKLVVDV
FSPERYVPYL IDCFNGSKNM KSRCECIDLV EYIVTVYGHH VIGRKCVREV SKYVVAHEKE
LRESAISLLV SVYTRTEGTN PDKFFRYAGI TTQQGMDLLT ARLKHLPVSS VPSVAASTLG
PKITFERENS QQRTGFGFAR ASAVAVPATM TNSVPETQEL AETQELAETQ ELAVDDDVDM
SRPASEADDD ESHGAAIEEL LLRPIEGLIN SSKEVIPAGS PAYKEGGNAL KGLYAIINRP
TDPSEIEFLH SYVNEIVLAL CDCIHGAFYA GNAEKRPEMY ILAISITTLT VVFNSEAVTS
LHRFTVERVL LELCSKIMDP RMEKFASKAN MPASEIAMLP PEEKRYLMVF KALYKAMRNL
TERAKPGDVY PSVINLLQRL MHNDVGDYNK NDTLKHLLKE DSLDQLVGRI LLKLSTIQAN
SLNPFEGIDI FGVLMQMHMF LSTLPGAEVM MVDIANDNMR SALKIMAESL IKTRSSVFEA
SMKDIPPTSP VRQALRDMGV GQKKEQEVTE STNLRHKETS IASIGTNSLS SSASRITSHF
GASSASNGAA TIPEESLTRR LFPPRGSSSV TQSVRTASAA LSSTGTALAG GTRGRSFTSF
HAFAANRGLA STTSRPSTTS AQLDNLRERL QMSRHFS
//