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Database: UniProt
Entry: A0A068RED3_9FUNG
LinkDB: A0A068RED3_9FUNG
Original site: A0A068RED3_9FUNG 
ID   A0A068RED3_9FUNG        Unreviewed;      1180 AA.
AC   A0A068RED3;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=CAP-Gly domain-containing protein {ECO:0000259|PROSITE:PS50245};
GN   ORFNames=LCOR_00281.1 {ECO:0000313|EMBL:CDH48503.1};
OS   Lichtheimia corymbifera JMRC:FSU:9682.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Lichtheimiaceae; Lichtheimia.
OX   NCBI_TaxID=1263082 {ECO:0000313|EMBL:CDH48503.1, ECO:0000313|Proteomes:UP000027586};
RN   [1] {ECO:0000313|EMBL:CDH48503.1, ECO:0000313|Proteomes:UP000027586}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMRC:FSU:9682 {ECO:0000313|Proteomes:UP000027586};
RA   Schwartze V.U., Winter S., Shelest E., Marcet-Houben M., Horn F.,
RA   Wehner S., Hoffmann K., Riege K., Sammeth M., Nowrousian M., Valiante V.,
RA   Linde J., Jacobsen I.D., Marz M., Brakhage A.A., Gabaldon T., Bocker S.,
RA   Voigt K.;
RT   "Gene expansion shapes genome architecture in the human pathogen
RT   Lichtheimia corymbifera: an evolutionary genomics analysis in the ancient
RT   terrestrial Mucorales (Mucoromycotina).";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
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:CDH48503.1}.
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DR   EMBL; CBTN010000001; CDH48503.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A068RED3; -.
DR   STRING; 1263082.A0A068RED3; -.
DR   VEuPathDB; FungiDB:LCOR_00281.1; -.
DR   OrthoDB; 1364255at2759; -.
DR   Proteomes; UP000027586; Unassembled WGS sequence.
DR   GO; GO:0030286; C:dynein complex; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.287.1490; -; 1.
DR   Gene3D; 2.30.30.190; CAP Gly-rich-like domain; 1.
DR   InterPro; IPR036859; CAP-Gly_dom_sf.
DR   InterPro; IPR000938; CAP-Gly_domain.
DR   InterPro; IPR032108; CLIP1_ZNF.
DR   PANTHER; PTHR18916; DYNACTIN 1-RELATED MICROTUBULE-BINDING; 1.
DR   PANTHER; PTHR18916:SF94; RESTIN HOMOLOG; 1.
DR   Pfam; PF01302; CAP_GLY; 1.
DR   Pfam; PF16641; CLIP1_ZNF; 1.
DR   SMART; SM01052; CAP_GLY; 1.
DR   SUPFAM; SSF74924; Cap-Gly domain; 1.
DR   PROSITE; PS00845; CAP_GLY_1; 1.
DR   PROSITE; PS50245; CAP_GLY_2; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027586}.
FT   DOMAIN          151..194
FT                   /note="CAP-Gly"
FT                   /evidence="ECO:0000259|PROSITE:PS50245"
FT   REGION          1..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          83..128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          226..327
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          793..813
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          844..870
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1095..1118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          354..383
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          408..495
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          550..598
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        44..66
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        226..292
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        308..327
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1180 AA;  133584 MW;  DE9D11D206EB593D CRC64;
     MSRLPSARGG IPAPPQQKRL SRQPSLDLRR RRHHPDDAAP PVPSLKTSKS TRAPSMSRAS
     ISSYEEIESP SSLSRYSLSS IGSTQTAITS PRSSVASPRP TSVRKSVASV NGGGKHHPTN
     NNNSNSMGGL GVGERVAVDS MGIVGTLRFI GTTQFKEGMW AGIQLDIVGT GKNDGSVNGI
     RYFSCPPQTG LFVQASKVTS LNGRERSPSP RISPGSRAAR YVGMTASQLT QQQQQQQQQQ
     RPPSVQTKRS STMSARSSSG NGLRRPGSIQ SPTPTSTRRR PTADSLPSPA ATPNNEDEDD
     EDGYVGSSST EMMLTDTPAP TTLTMSKSTD SHTRLERMLG EAISQAPDQA AMRVQQLQLR
     VEVLEAENKY LKLENAQNKT AEQILERSVL LNGSDSDQQQ QQQQHFTLEG HKAIVEEIKQ
     EHEQAAKAWD QEKGQIQSTI RKLEERVKEL ETEQSELIKE RDTMQTQLSE ARKEKVQMEN
     KVRELEEKVT LAEAAAASKA AAAASTTSNF YSQDPEEMRQ RQMQMEMEME EVHEKMGSLM
     DAMRAKDMFL GSLSEQVETH RNMVEERERE IRRVKADADR HTREKDRLRD EIKELETKWM
     QHQDCATKEE FDKVKRQLTQ AKESLAHESN VVADYRARIE SLEQSVDELK RAGMESIELY
     ESSVELHRVD MEAIKASLDD ERRKVIALEE ERESLRKAGL EAIETYEATI EELKKERSET
     SEKSGRTQQE MQATIDKLKQ EIEQLVNARD TSDEVDKIKA VWESERKRLE DNLEATSQNL
     AKEREMYQSL KAESEKLREQ IKQADKHDKD NDKLQEQVQR LQANYDEQLN ARGKYLDDVR
     AAVESQKKTE GELRRLTEAK EKTERDLTTA QESLARAESA LADARKHGAD PDALIKEREQ
     HAKELAVLRQ EIKRLEAQNT MITKQKESIE LEAKSKSDNG LKQQFEKLQA EHQRLSKEYE
     SLTESHKQAQ NECLKLMDEV EKLHSEGDGS ETSLEGCNTD EERVARLQSQ LSDTKRKMES
     LIVKQSAEMR QLKEKHEEAE RAHQRQVATL NRDVSELESL VESKIFKESD MEEALEKERK
     QSKRLREELN ELKQQLKEQQ RDERMSSKNS STATSSNGPY TDDALFCELC DSPGHDLMSC
     KVVVPTSSEK KEQPARPFCV NCDEYGLHST EQCPNQNETF
//
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