ID B8NGH5_ASPFN Unreviewed; 1356 AA.
AC B8NGH5;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Dynactin, putative {ECO:0000313|EMBL:EED50839.1};
GN ORFNames=AFLA_136020 {ECO:0000313|EMBL:EED50839.1}, G4B84_005515
GN {ECO:0000313|EMBL:QMW30180.1};
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952 {ECO:0000313|EMBL:EED50839.1, ECO:0000313|Proteomes:UP000001875};
RN [1] {ECO:0000313|EMBL:EED50839.1, ECO:0000313|Proteomes:UP000001875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 /
RC SRRC 167 {ECO:0000313|Proteomes:UP000001875}, and NRRL3357
RC {ECO:0000313|EMBL:EED50839.1};
RX PubMed=25883274; DOI=10.1128/genomeA.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
RN [2] {ECO:0000313|EMBL:QMW30180.1, ECO:0000313|Proteomes:UP000515286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL3357 {ECO:0000313|EMBL:QMW30180.1,
RC ECO:0000313|Proteomes:UP000515286};
RA Fountain J.C., Clevenger J.P., Nadon B., Youngblood R.C., Korani W.,
RA Chang P.-K., Starr D., Wang H., Isett B., Johnston H.R., Wiggins R.,
RA Chu Y., Agarwal G., Kemerait R.C., Pandey M.K., Bhatnagar D.,
RA Ozias-Akins P., Varshney R.K., Scheffler B.E., Vaughn J.N., Guo B.;
RT "Two New Chromosome-Level Aspergillus flavus Reference Genomes Reveal a
RT Large Insertion Potentially Contributing to Isolate Stress Tolerance and
RT Aflatoxin Production.";
RL Submitted (JUL-2020) 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}.
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DR EMBL; EQ963478; EED50839.1; -; Genomic_DNA.
DR EMBL; CP059868; QMW30180.1; -; Genomic_DNA.
DR RefSeq; XP_002379615.1; XM_002379574.1.
DR STRING; 332952.B8NGH5; -.
DR EnsemblFungi; EED50839; EED50839; AFLA_136020.
DR VEuPathDB; FungiDB:AFLA_005965; -.
DR eggNOG; KOG0971; Eukaryota.
DR eggNOG; KOG4568; Eukaryota.
DR HOGENOM; CLU_002523_1_1_1; -.
DR OMA; LFEMEPV; -.
DR OrthoDB; 9423at2759; -.
DR Proteomes; UP000001875; Unassembled WGS sequence.
DR Proteomes; UP000515286; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0030286; C:dynein complex; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
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}.
FT DOMAIN 24..66
FT /note="CAP-Gly"
FT /evidence="ECO:0000259|PROSITE:PS50245"
FT REGION 75..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1300..1320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1058..1130
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 114..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1356 AA; 152316 MW; FE00B31EBF7BAA1B CRC64;
MADLTPGDVV TLTDGRQATV RFAGATHFAA GDWIGIELDE PTGKNDGAVQ GERYFDCEFG
YGMFVRPTAI AAIIGPPTKE TKPAAKGTAN APQTRGRAQT GSGLGIKKPS ALQAANTKRH
SGSSASPSPA AKPASQRLGL KQPQSPTKSQ SPTKQLSGAS TPRSSISGPS RPSATSKGRP
SIGAKSTSMG PPPPPSASRP SRPSISRASN RTVRPGLQGT TTAPAGVAKR PALRPTASKT
SEEQERGSPQ SEDIDTADNY AEGDEMESEE PTAKPSRLAS GSSRAGAARP GFSQTSSPRQ
AQSTALSREL EELKTKLRVM EKKRTEDREK LKALETLQQE RDKFESIIQK LQAKYQPQQL
EISDLRKKLR ESEAQLEEIE RIQAEHDSIL EMATLDREMA EETADAFRHE VETLKLRVEE
LQLEAEVLRE ENEELGQTMS PEEKSSHGWL QMERTNERLR EALIRLRDMT QQQESELKDQ
IKELQQDLEE YESIKSQYES TKEKLLVAEN NVEDLKQQLE TALGAEEMIE ELADKNMHYQ
EEINELNAAI EDLEALKEIN DELEYNHIET EKQMQEEIDY KDSLFNEQCR KVAQQDEVIE
DLEYTLARFR ELVSTLQGDL EDMRASQQIT EAEATDLTTR SRAMMDLNLK LQASVSKAQT
KTIDIELERL DAQEAAQHLS ILKLYLPEYF EGEKNGILAL LRFKRVSFKS SLMISTVRER
FPEQTSDPAA VEDGFTAHDV LEKLMWIGAI CDRFINYITN CSAESFDRIK ATLFEMEPVE
RTVNFWIESV RKNELNMKKC GIELQRSIAL LSHLAEVHLP TSLETFADEL CMRSSLTQSY
IDHAASLISR LRTLLQSKIT VLEGEEEEPN FLFSKMETLV TQARGLKVAM GKIYKALEDL
RSRSLALSQD VAGPFKETEE AAKNLSELAR HLGENIALIV SDESRTEPLT LEEATKSMSQ
VSTLYAQPSE SGSECSDTMS FIANRLRSLG GNLEELDSIS TDLSITSEFE RLPSPWIARA
SELKSNKAVS PDADEEIRRL KNEIHEASTA LGVKDKTIEE QALKVELVES RMQEASKKAS
MVKELETKIE TMRTKETELE GMVEKQRKEL QALETEREEI KARLDRVKRA SGTTGITTTE
GVVVDNALSL ATMRENEALR AEVESLQAAV RFLREENRRG NMLDPYSVQR SAEMYSWLDV
PLTQANGNAQ RDKIQQTASE SRDVFSHLLK LTKESNICDL KSTMSQENGN RASWRPSKTK
LRYQVLQQRE NFEHWTEWRD DIVNQEREQD RLVNTKKERL ARDRARRHAP KNSVFGGFPQ
GLGHGMMGRA WEILGMQQDH RKLADRPVEP SITPSF
//
