ID   V2X6J2_MONRO            Unreviewed;       825 AA.
AC   V2X6J2;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=HOOK-domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=Moror_14738 {ECO:0000313|EMBL:ESK88416.1};
OS   Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS   (Crinipellis roreri).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX   NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK88416.1, ECO:0000313|Proteomes:UP000017559};
RN   [1] {ECO:0000313|EMBL:ESK88416.1, ECO:0000313|Proteomes:UP000017559}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK88416.1,
RC   ECO:0000313|Proteomes:UP000017559};
RX   PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA   Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA   Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA   Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA   Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT   "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT   Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT   mechanisms of the biotrophic and necrotrophic phases.";
RL   BMC Genomics 15:164-164(2014).
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:ESK88416.1}.
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DR   EMBL; AWSO01000650; ESK88416.1; -; Genomic_DNA.
DR   RefSeq; XP_007852283.1; XM_007854092.1.
DR   AlphaFoldDB; V2X6J2; -.
DR   STRING; 1381753.V2X6J2; -.
DR   KEGG; mrr:Moror_14738; -.
DR   HOGENOM; CLU_017588_0_0_1; -.
DR   OrthoDB; 1366487at2759; -.
DR   Proteomes; UP000017559; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR   GO; GO:0031122; P:cytoplasmic microtubule organization; IEA:InterPro.
DR   GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; IEA:InterPro.
DR   CDD; cd22211; HkD_SF; 1.
DR   Gene3D; 1.10.418.10; Calponin-like domain; 1.
DR   InterPro; IPR036872; CH_dom_sf.
DR   InterPro; IPR008636; Hook_C.
DR   InterPro; IPR043936; HOOK_N.
DR   PANTHER; PTHR18947:SF28; GIRDIN, ISOFORM A; 1.
DR   PANTHER; PTHR18947; HOOK PROTEINS; 1.
DR   Pfam; PF05622; HOOK; 1.
DR   Pfam; PF19047; HOOK_N; 1.
DR   SUPFAM; SSF116907; Hook domain; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017559}.
FT   DOMAIN          8..145
FT                   /note="HOOK N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF19047"
FT   DOMAIN          196..455
FT                   /note="Hook C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05622"
FT   REGION          419..477
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          797..825
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          482..651
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          748..779
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        428..443
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        452..468
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        806..825
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   825 AA;  93940 MW;  CBCFA82056CFD11D CRC64;
     MSDSRKEIDA FINFFATFEL TSPVSSISDL GDGAALFQVL SLVDADYFRQ PSGQSADNWV
     LRFSALKRLY RLMTQYFSDV LQKPTSGLDV PDLQAMAKDF DVTATLSMCR LTIAIGVQCE
     KNKDFIVKIQ GLSEDDQHNL MKAIEQVMSR ISSGSSSDGL REATMTEDDH YYRIQSEKGK
     ILAEKEAAEQ AYQELLKEHR NLQTTHEDVV SERDEALAQV RQAKRDLDNR RVDNKADVMA
     RAEIDRLRSE LQKSEDNLAA AESEVEHKNN MVADLTRKVE DAENRAAEGQ KWKDKYDEMR
     HAAEKAQKME NVMDKYKKKL QEGAELRQTV KALEKQNSDL VDKNASLEEE YRKVAAFKPL
     LESYKNQIAD LESKNSNRAQ EIDQLKFELE QTRTQLKISK EERAKDSETL ELYQERVREL
     ELASNKPPKR ARSQTTSSDA FPQGEPLSEA VPSESGEEEF DDDATDMGLG GELNDALSGT
     TMTDLKIKVK KLERELESVR KNEADASKML VMENLLEDAN RMKQRYETDY LAAHREKLVL
     QQKLEEIRSG KSMGDGAEAA IALRQRLNET VEQLEELRKI HAELEVKFEA QDKELTIAKS
     DLTLVNRDQL DILASLRESV NEDKAGLEAD IEKLRKQNKE LSDKSRMQLE QVNALLLEKV
     NLQSEGIGQR EKMLQRERDF GELRASLSGK DLPEDIKQRL LALHEENVML KESNKTANEK
     LLKAKQFIKE QDKLFREQHA GSAPAGTFEE ARSQIKILED DLTRQKTLMK DLIKRYQREQ
     ALMLSVVHSM GMNTARGHLG GQLPSNSKPA WLSGVRNTSR LQRSG
//