ID A0A0D0CLB7_9AGAR Unreviewed; 793 AA.
AC A0A0D0CLB7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=HOOK N-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=GYMLUDRAFT_57431 {ECO:0000313|EMBL:KIK63774.1};
OS Collybiopsis luxurians FD-317 M1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Omphalotaceae; Collybiopsis;
OC Collybiopsis luxurians.
OX NCBI_TaxID=944289 {ECO:0000313|EMBL:KIK63774.1, ECO:0000313|Proteomes:UP000053593};
RN [1] {ECO:0000313|EMBL:KIK63774.1, ECO:0000313|Proteomes:UP000053593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FD-317 M1 {ECO:0000313|EMBL:KIK63774.1,
RC ECO:0000313|Proteomes:UP000053593};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN834763; KIK63774.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D0CLB7; -.
DR HOGENOM; CLU_017588_0_0_1; -.
DR OrthoDB; 1366487at2759; -.
DR Proteomes; UP000053593; 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:UP000053593}.
FT DOMAIN 10..148
FT /note="HOOK N-terminal"
FT /evidence="ECO:0000259|Pfam:PF19047"
FT DOMAIN 193..598
FT /note="Hook C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05622"
FT REGION 424..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 141..210
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 242..355
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 387..421
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 483..530
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 564..663
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 424..443
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 793 AA; 91009 MW; 2DC1FFB62698947C CRC64;
MSDSKQKEID AFFNFFSTFD LTNPVSSLTD LSDGQALFEI LSVVDADYFR QSTRPTAQTS
DNWVLRFSAL KRLYRLMTQY FMDVLHKPAS GLDVPNLHAM AKDSDDTATL IMCRLTIVIG
VQCHKNKVFI DKIQGLSQID QQSLMRVIEQ IINRINREEN NSSMLGEASM TEDDHYYRIQ
SEKSAILNEK ETLEKVYQQL LEEHRLLQTT HDDTLSERGD LIAQLKEARR EADSRRSDGK
ADAMLRAEID RLRTDLQKSE DNLAMMENEL DKQTALGTDL TRKVEDLQAQ ADEASKLKDR
VDELRHANEK LNKVENVLDK YKKKLQEASE LRQRLKTLEK QNADLVDQNA SLEEEYRKVA
AFKPLMESYK NQISDLEHKA SSRTQDMETL KFELEQARTK LKILTEERAK DSETIELYQE
RVRELELSDP RPPKSRARQD SIDHAASSGD ALASPGEEVD DEEDENAMGL GGELHDAESG
TTMTDLKLQI RKLKRELEAV RKNEADASRV LVLENLLDDA NRMKSRYEAD YLATHREKLV
LQRDLEEIRS GKSMGDGTLS AEAAIALRQR LNESVDQLDV LRKEHTELEV RFETQSKELT
IAKSDLTLVN KDQLDILASL RESVNEDKAG LEADIERLQR QNKELAEKNR MQLEQVNALL
LEKVNLQSEG IGQREKMLQR ERDFGDLRAS LSGKDLPEDI KQRLLALHED NVNLKESLKT
TSEKLTKAKA FIKNQDKLYR EEQAGKNVGN ASGMFEEGEV SMRSQIKILE DDLERQKALN
VELKKRYMLE QEV
//