ID A0A0J8R215_COCIT Unreviewed; 2241 AA.
AC A0A0J8R215;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Dynein heavy chain {ECO:0000313|EMBL:KMU78781.1};
GN ORFNames=CISG_01821 {ECO:0000313|EMBL:KMU78781.1};
OS Coccidioides immitis RMSCC 3703.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=454286 {ECO:0000313|EMBL:KMU78781.1, ECO:0000313|Proteomes:UP000054559};
RN [1] {ECO:0000313|Proteomes:UP000054559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RMSCC 3703 {ECO:0000313|Proteomes:UP000054559};
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
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DR EMBL; DS268122; KMU78781.1; -; Genomic_DNA.
DR STRING; 454286.A0A0J8R215; -.
DR Proteomes; UP000054559; Unassembled WGS sequence.
DR GO; GO:0030286; C:dynein complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0045505; F:dynein intermediate chain binding; IEA:InterPro.
DR GO; GO:0051959; F:dynein light intermediate chain binding; IEA:InterPro.
DR GO; GO:0008569; F:minus-end-directed microtubule motor activity; IEA:InterPro.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR Gene3D; 1.10.287.2620; -; 1.
DR Gene3D; 1.10.8.710; -; 1.
DR Gene3D; 1.20.58.1120; -; 1.
DR Gene3D; 1.20.140.100; Dynein heavy chain, N-terminal domain 2; 1.
DR Gene3D; 3.20.180.20; Dynein heavy chain, N-terminal domain 2; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR035699; AAA_6.
DR InterPro; IPR026983; DHC_fam.
DR InterPro; IPR042222; Dynein_2_N.
DR InterPro; IPR043157; Dynein_AAA1S.
DR InterPro; IPR013602; Dynein_heavy_linker.
DR InterPro; IPR013594; Dynein_heavy_tail.
DR InterPro; IPR042228; Dynein_linker_3.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR46532:SF4; DYNEIN HEAVY CHAIN 8, AXONEMAL-LIKE PROTEIN; 1.
DR PANTHER; PTHR46532; MALE FERTILITY FACTOR KL5; 1.
DR Pfam; PF12774; AAA_6; 1.
DR Pfam; PF08385; DHC_N1; 2.
DR Pfam; PF08393; DHC_N2; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000054559}.
FT DOMAIN 263..654
FT /note="Dynein heavy chain tail"
FT /evidence="ECO:0000259|Pfam:PF08385"
FT DOMAIN 662..758
FT /note="Dynein heavy chain tail"
FT /evidence="ECO:0000259|Pfam:PF08385"
FT DOMAIN 1223..1624
FT /note="Dynein heavy chain linker"
FT /evidence="ECO:0000259|Pfam:PF08393"
FT DOMAIN 1766..2106
FT /note="Dynein heavy chain hydrolytic ATP-binding dynein
FT motor region"
FT /evidence="ECO:0000259|Pfam:PF12774"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1499..1526
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 2241 AA; 253419 MW; B6DFA7C6A242D557 CRC64;
MEVASQGVSN GLAPPTTFPT TDPTIVVQHL AEVLQGTLGA LRKDLESTGS LLSTSKYSET
LQRCSRFASE SQTAIYAHKE VAEVEDTNGT EEEPSSSTQY IYTLNSEISI ASNTVAAVAY
LKSPSPLDPA IPVSSQVQVL TLPGFSASSN TSISQGPATS PYEVLHSFVH LALAPYFEAY
TRGQDASKTK GDADAKTGVP GAKKKIAELE LSLLHLQQNI EIPALNLPMH EIVQSALDEA
QLRGVKPSVE LVPGAVLENH LVINSIQSTV NGWIKSIQSI TKMSRDPESG SAAQEINFWL
DMETALEGIE AQLQADGVQL TMDILRHAKR YQATLSFVAD TGLKEAAETV QKYNQLLRDF
PLPELQSATS LQKVQEALNL IFAHLNKKLR LCPYPIKRAL SLVEAISGDL DSRIHTLING
KAIMHLDFKE FRSLMRAAQV VWRAWDENIK EFTNVARDAM RRRNEKFIPI KVRSKHAETQ
DRLKYINTFR TNHEQLQRTI MNVLGPRSTQ PGGPLGTETD TIALDDIGDV DAVEEARSDG
FGKRLRIMKE HPGLKTLIIA RLRDRLATAQ NANEKFRVFS KFNALLVRPK IRSAIGKYQT
ELIDDVKKDI AALHERFKQQ YGHSEAHAMA QLRDLPPVSG AIIWARQIER QLDGAAGNAF
ELVVNFDAQI IALFKEVRNL VWLNFQIPHA INSISKEAKR VYPFAISLME SVRTLHQTIR
AIASMSQATI LLNGYQNDVQ ALIMKGLPLR WESFIHSYEL HVKQGIANGS VDPSVTPARG
ESKHVQFVRE FALSASVLQA KSATLTSIDE SVQKTILELK SCPYEADAFR QRLDQIQIAV
DKLNLENYAN LGFWVANLNN MVESILQDRL RRAIRHWIRS FQEAKHEQAH KISHGELSDS
AEEAQIQNIQ FPNLLHEISM RNQVMHLDPP LEFARANWFS HFDQWVGVLS RLQEISEYIE
KWLQFQSLWD LQSSYVYDVL GDDLSQWLQL LQEIRRSRAT FDTSEVRRSF GTIRIDYEQV
QTKVNAKYDQ WQREILLNFG GKLGTRMREV YAELQAARRD LEGQSLEASS TAHAVSFITI
VQQCKRKARV WEPEVDLFRQ GQATLARQRY QFPNDWLHVE QVDGEWLALN DILERRSKTV
QDQTDALRAK ITAEDKVIND KIAEIISQWN EEKPVSGSTP PEEASRTLSH FQSRLESLQS
EFEMVSKAKE ALDLPSSPET ALAAILEEVQ DFMAVWAALS TIWKSLNELR DVLWNSVQPR
KLRQSLDGLI RMTKEMPSRM RQYAAFEHIQ NILRQLLKVN PLLSDMKSEA VRERHWQKIF
KALKPGKRFS QVSLALGDVW DLNLAASEAV IRDIITQAQG EMALEEFLKM VRETWQSYSL
DLVNYQNKCR LIKGFDDLFA KCSENLNSLQ AMRHSPYYKE FEEEATSWED KLNRVHVLFD
VWIDVQRQWV YLEGVFTGNA DIKHLLPLES GRFQNINSEF FAVMKKVYKS PFVLDVLAIN
GVQKSLERLA ELLNKIQKAL GEYLERERVS FPRFYFVGDE DLLEIIGNSN DTLRVAKHFK
KMFAGLSGLV MDDDGNIVGF TSKEGEEVRL KKEVSLLKSP RINDWLAALE NSMKSTLAEL
LAEAIEQFES IYSATEIDQT AFSDYLANYP AQIVVLGSQV VWTNAVQKAL EDGGSGLQAL
YDSEVRVLDL LAVTVLGELD PITRKKCEHM ITEFVHQRDA IAKLIDNNAS SPTHYLWLLQ
MRYVYHAEGD FLQRLHVQMA NAKLDYGFEY LGVPERLVRT PLTDRCFLTL TQALCQRLGG
SPYGPAGTGK TESVKALGLQ LGRFTLVFCC DDTFDFQAMG RIFLGICQVG AWGCFDEFNR
LEERILSAVS QQIQNIQIGL KNTDDETKAQ IELVGRRLRV NPNTGIFITM NPGYAGRSNL
PDNLKKLFRS VAMSKPDKEL IAEVMLFSQG FKQAKALSRQ TVPFFDHCST RLTKQAHYDF
GLRALKSVLV SSGGLKRLRL ANSDGDIGPN EIVEPQIIVQ SVRETIAPKL IRQDVEMMLG
IQAEDFPGVE YVPANFEKLT QAIREIAVEN HFVATDTWIT KTLQLYQIQG IHHGVMMVGR
SGSGKSSAWK VLLQALQKVE GIEGVCHVID SKVMSKEALY GNLDSTTREW TDGLFTGILR
KIVDNLRGED SKRHWIVFDG DVDPEWVENL NSVLDDNKLL TLPNGERLNL PPNVRIMFEV
ENLKKHLHCF LTSYCKGTIL F
//
