ID A0A428S6Q7_9HYPO Unreviewed; 2143 AA.
AC A0A428S6Q7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Dynein heavy chain, cytoplasmic {ECO:0000313|EMBL:RSL85482.1};
GN ORFNames=CEP52_016131 {ECO:0000313|EMBL:RSL85482.1};
OS Fusarium oligoseptatum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium solani species complex.
OX NCBI_TaxID=2604345 {ECO:0000313|EMBL:RSL85482.1, ECO:0000313|Proteomes:UP000287144};
RN [1] {ECO:0000313|EMBL:RSL85482.1, ECO:0000313|Proteomes:UP000287144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL62579 {ECO:0000313|EMBL:RSL85482.1,
RC ECO:0000313|Proteomes:UP000287144};
RA Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA Kasson M.;
RT "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
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:RSL85482.1}.
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DR EMBL; NKCK01000320; RSL85482.1; -; Genomic_DNA.
DR STRING; 1325735.A0A428S6Q7; -.
DR Proteomes; UP000287144; 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; 1.
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; 1.
DR Pfam; PF08393; DHC_N2; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000287144}.
FT DOMAIN 271..852
FT /note="Dynein heavy chain tail"
FT /evidence="ECO:0000259|Pfam:PF08385"
FT DOMAIN 1364..1766
FT /note="Dynein heavy chain linker"
FT /evidence="ECO:0000259|Pfam:PF08393"
FT DOMAIN 1908..2131
FT /note="Dynein heavy chain hydrolytic ATP-binding dynein
FT motor region"
FT /evidence="ECO:0000259|Pfam:PF12774"
FT COILED 1182..1209
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 2143 AA; 243569 MW; 138FC90E78F331C4 CRC64;
MEVTSAAAPS AGSSANGVTA AAPFPTIEPE RVVEHLAAVC EIALGATRDE LEQLGSLLHK
ARYGETVSRC TRFASDSQNV LYIQKDIANP SAVEAGADPA APVTYNYTLS TEISSSPTTV
SSLVLIKSPQ PIDPTRPLTS QIFITNLPGP ASLNAGVGEQ GTALSPWEVL HSQVHHALVP
YFDANTKSQQ LANGSRGRAD VDAKTGIPVT KKRLNDLELS LLHLQQNVDI PEISLTFHSI
VQNVLDDAES RHTRPSLDAI PQNLLQDSTF LNRLQANVNT WIKSIQGITK LTKDPSSNAN
QEFNTASQEV NFWLSMESAL EGIEGQLRSE GVLLTLEILK HAKRFQATVS FTADTGLKEA
MDKVQKYNQL MRDFPLDELL SATSLSKAQE AIAQIFGHLN KKLRICPYPI RRALPLVEAI
SADLDEVLHR LLPGTELVNL DYQQFQTIMQ TCDDIFRTWE ENVKEFTNVA REVTRRRNEK
FIPIKINKKH SELESRIKYV STFRDNHEQL QRTIINVLGP QATIPGVTET TGSNGIVMEE
MGDVDAVEEV KQAWEALHNV DLLDVTDQGK ERWVRAENLY NERTTRVENS IIARLRDRLA
TAKTANEMFR VFSKFNALFV RPKIRGAIQE YQNQLMDHVK QAINGLHERF KQQYGHSETH
AMAQLRDLPP VSGAIIWARQ IEFQLDGYMR KVEAVLGPDW TMHTEGHKLQ EESELFKQKL
DTARIYEAWI ADVGRRKISI SGQLFEIARV RSAGGILELT VNFDPQVITL FKETRNLTWQ
SYSVPHAVTT VSKDAKRVYP YAVSLMESVR TLSQTLRQIS VMGEESVLLF GYRNDVYKLI
SEGVPLRWES FINSHELFYS DNRQTRPLLP GGTDFGLAKN TESKHGMFIR GFAAAVSVLQ
QKAVSLNFIH ATVEQALKEL NTCPYEEAAF HTRLDTIQAA VDQLNLEQYV NLDFWVRGLN
SKVQSILLTR LQSAVHAWIQ AFEDDTPEDE LRRKVNNNNE ETKPDGPTMK RLVLELAMRN
QVIYLDPPLE FARASWFLHL HEWLGIVCNL RKIKATRYQM TLTTTANDEP RFTDLPSECA
GLLQRVYVSV EKKLHEVSAY VDKWLQFQSL WDLQSEQVYD ALGEQLPRWL QLLQEIRKTR
STFDTQEVSR AFGHLTIDYD QVQTKVNAKY DQWQHEILMK FASRLGNRMR EINAEIEKAR
KHLESQSSDA SSTAQAVQFI TVVQSCKRNV KTWAPEIDMF RQGQSTLVRQ RYQFPNDWLH
IEQIDSQWEA LKEILEKKSR IVQDQTDALQ AKIVAEDKLI NERIAEIAAQ WNEEKPVSGT
IQPDVASATL SSFESRISKL QDDAQMVAKA KEALDIPASP DTSLEATLEE VRDFQSVWSN
LSTIWASLNE TRDILWTAVQ PRKIRSKVDD LIKSTKEMPS RMRQYAAFEH VQGILRGFLK
VNSILSDLKS DAIRERHWHK IYKQIKPQKR FSPSSMTLGD VWDLNLVATE VIVKDIIAQA
QGEMALEEFL KQVRETWQNY ALEMVNYQNK IRLIRGWDDL FAKCSENLNS LQAMKHSPYY
KEFEEEAVSW EDKLNRVHVL FDVWIDVQRQ WVYLEGVFTG NADIKHLLPI ESGRFQNINS
EFLAVMKKAN KSPYVLEVLN IPNVQKSLER LAEMLNKIQK ALGEYLEKER VSFPRFYFVG
DEDLLEMIGN SNDTLRIAKH FKKMFAGLSG LVMDDETVIS GFTSKEGEVV RLKKEISLAK
TPKINDWLAL LEGGMKSTLA ELLAEAVDHY TPIFESETID REALNEFMEA YPSQIVVLAT
QAVWTTAVDK SLTTGGETLK AIFDREVEVL RVLADTVLGE LEVILRKKCE QLITECVHQR
DTIEKLINVK ATSTSHYLWQ LQMRYVYEPQ GEYLDRLYIK MANAKLNYGF EYLGVPERLV
RTPLTDRCFL TLTQALCQRL GGSPYGPAGT GKTESVKALG VQLGRFTLVF CCDDTFDFQA
MGRIFLGICQ VGAWGCFDEF NRLEERILSA VSQQIQNIQL GLKQGVEDDQ SQIELVGRHL
HVNENTGIFI TMNPGYAGRS NLPDNLKKLF RSVAMSKPDK ELIAEVMLYS QGFNQAKQLS
KHTVPFFDQC SGKLSKQAHY DFGLRALKSV FGQLWWPQAC SLG
//
