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Database: UniProt
Entry: A0A072PQK5_9EURO
LinkDB: A0A072PQK5_9EURO
Original site: A0A072PQK5_9EURO 
ID   A0A072PQK5_9EURO        Unreviewed;      1335 AA.
AC   A0A072PQK5;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=CAP-Gly domain-containing protein {ECO:0000259|PROSITE:PS50245};
GN   ORFNames=A1O9_05680 {ECO:0000313|EMBL:KEF57760.1};
OS   Exophiala aquamarina CBS 119918.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=1182545 {ECO:0000313|EMBL:KEF57760.1, ECO:0000313|Proteomes:UP000027920};
RN   [1] {ECO:0000313|EMBL:KEF57760.1, ECO:0000313|Proteomes:UP000027920}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 119918 {ECO:0000313|EMBL:KEF57760.1,
RC   ECO:0000313|Proteomes:UP000027920};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala aquamarina CBS 119918.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245}.
CC   -!- SIMILARITY: Belongs to the dynactin 150 kDa subunit family.
CC       {ECO:0000256|ARBA:ARBA00011010}.
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:KEF57760.1}.
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DR   EMBL; AMGV01000004; KEF57760.1; -; Genomic_DNA.
DR   RefSeq; XP_013260350.1; XM_013404896.1.
DR   STRING; 1182545.A0A072PQK5; -.
DR   GeneID; 25280603; -.
DR   VEuPathDB; FungiDB:A1O9_05680; -.
DR   HOGENOM; CLU_002523_1_1_1; -.
DR   OrthoDB; 9423at2759; -.
DR   Proteomes; UP000027920; Unassembled WGS sequence.
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; IPR022157; Dynactin.
DR   PANTHER; PTHR18916; DYNACTIN 1-RELATED MICROTUBULE-BINDING; 1.
DR   PANTHER; PTHR18916:SF6; DYNACTIN SUBUNIT 1; 1.
DR   Pfam; PF01302; CAP_GLY; 1.
DR   Pfam; PF12455; Dynactin; 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   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Dynein {ECO:0000256|ARBA:ARBA00023017};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027920}.
FT   DOMAIN          26..68
FT                   /note="CAP-Gly"
FT                   /evidence="ECO:0000259|PROSITE:PS50245"
FT   REGION          75..306
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          307..442
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          471..567
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          603..637
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1032..1125
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1150..1177
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        76..102
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        115..233
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        250..274
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1335 AA;  149967 MW;  A41F5B8D6FEF9252 CRC64;
     MPDLNVKIGQ TIETQDKKQG IVRYIGPLHI AAGEWLGLEL PENSGKNDGS VKGERYFQCT
     PGYGIFVRKE SAARIVKQQP QASKPPGQPM SNGATAKSRS SSVVPADVAR KRQSMMSAGS
     GSTVGSRLSL RSPTKSPTKP TQSAASSSTS TPRTGTPATT ARTSDSSTKS RSSITGRPLM
     GPPASTSRTT TTTATNRQSL GVAPKPTITR PTSMPPRQST AGTRLSMSSK TLARPEKNDQ
     RPAVAIDQHS PPIEEEEAVT QEIHHAEDDP HQGSPVGHDT TSPVLSPRPH SIAVPRNAPP
     STIHEDRSRQ AQVIKQLETK IRALQKQKQE DQSQLENIQD LQNQTARYEG IIQTLQKKLK
     TNQQEIIELK AKYEDAEDRA SKLAEPSAEH ESELELATLD KEMAEERAMM FETELEALKS
     KHEELELEVD ILREENRELT SVMTPEERAG SGWLQMERET ERLRQALVML RDMSHQNEND
     LKSEIKELQE TLDELEQVAS KYEDTATKLG RAEETNTHLR EQLDALETND EILEVMGAER
     DQNRNSIENL KRQIQDLEEH IQVTDELEAF HVEEEKRLHH QLDESEALLN ERLRRTTEQD
     KTIEDLEYTL NKFRDVVQGL QNDIDELRRS RDISELEAHE MSSKSRAMMD LNLKLQNSAA
     KSQLKAIDLE LGKMRAEQAS LHLEIVQLFI PDTFEMDKQP IVALLCFKRI KAKALLSKNI
     LGERIRERPE LVQDGVSTVF AVMEKMNYIA NVCERFVQHM SSCSAENFMK FGGAPFELEP
     VEQAITSWVE ALRRDELAPD GAEHLHRMAG ILVDMAEKLI LETQESKSTE LLASMSMIEC
     YTDTIGSQAQ LLSKAVQTRL GPSENEDDPS IVFEKKMDQL GVKARTMKYV SSKIIQSLSD
     LRTRSMSPGE ASWGLFSEAE QLSEKLARLV RGISQAVIED LNKPDHDEQL SYSTVVELMA
     TAAVPMLQRD ESESGTSEDI FSILAKHLQV LQTRVDDLYS RSSDVNNAVE FEKLAAPWIA
     RAKEVKSQKI LSQALQEEMA RMRSRIQEQT IRVSERDKQI EEQQVKIELL ESRAKETKAK
     DDGVKAMKVE IENLQSEKQH ANESLQKLEA EYNTLLKSQQ DSRIELEAIK QSKLSDGQSL
     ALGVADESLS LRLKAEADLL KVELASLEAA VRFVKAENQR LRLPVTEAGV TAISNSWLDP
     DKLKPAKDTS QVQEMRSDSK QIFTELIHMA KQAKPVKLKA KSIYATEAKG HMSWWRPESD
     TTLYQLLRQK EDLERWNQAK TDVVKRARLM SRSSREDDFA VPRLGIGLPL AKLPVLEDID
     METESAGNGV RIVQN
//
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