ID X6P9W0_RETFI Unreviewed; 1572 AA.
AC X6P9W0;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Dynein heavy chain {ECO:0000313|EMBL:ETO35335.1};
DE Flags: Fragment;
GN ORFNames=RFI_01731 {ECO:0000313|EMBL:ETO35335.1};
OS Reticulomyxa filosa.
OC Eukaryota; Sar; Rhizaria; Retaria; Foraminifera; Monothalamids;
OC Reticulomyxidae; Reticulomyxa.
OX NCBI_TaxID=46433 {ECO:0000313|EMBL:ETO35335.1, ECO:0000313|Proteomes:UP000023152};
RN [1] {ECO:0000313|EMBL:ETO35335.1, ECO:0000313|Proteomes:UP000023152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24332546;
RA Glockner G., Hulsmann N., Schleicher M., Noegel A.A., Eichinger L.,
RA Gallinger C., Pawlowski J., Sierra R., Euteneuer U., Pillet L.,
RA Moustafa A., Platzer M., Groth M., Szafranski K., Schliwa M.;
RT "The Genome of the Foraminiferan Reticulomyxa filosa.";
RL Curr. Biol. 0:0-0(2013).
CC -!- SUBUNIT: Consists of at least two heavy chains and a number of
CC intermediate and light chains. {ECO:0000256|ARBA:ARBA00011655}.
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:ETO35335.1}.
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DR EMBL; ASPP01001715; ETO35335.1; -; Genomic_DNA.
DR EnsemblProtists; ETO35335; ETO35335; RFI_01731.
DR OMA; ENITHAM; -.
DR OrthoDB; 312195at2759; -.
DR Proteomes; UP000023152; Unassembled WGS sequence.
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 GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; 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 CDD; cd00009; AAA; 1.
DR Gene3D; 1.10.472.130; -; 1.
DR Gene3D; 1.10.8.710; -; 1.
DR Gene3D; 1.20.58.1120; -; 1.
DR Gene3D; 1.20.920.30; -; 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; 4.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR035699; AAA_6.
DR InterPro; IPR026983; DHC_fam.
DR InterPro; IPR042222; Dynein_2_N.
DR InterPro; IPR043157; Dynein_AAA1S.
DR InterPro; IPR041466; Dynein_AAA5_ext.
DR InterPro; IPR024317; Dynein_heavy_chain_D4_dom.
DR InterPro; IPR013602; Dynein_heavy_linker.
DR InterPro; IPR042228; Dynein_linker_3.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10676:SF314; CYTOPLASMIC DYNEIN 1 HEAVY CHAIN 1; 1.
DR PANTHER; PTHR10676; DYNEIN HEAVY CHAIN FAMILY PROTEIN; 1.
DR Pfam; PF12774; AAA_6; 2.
DR Pfam; PF12775; AAA_7; 1.
DR Pfam; PF12780; AAA_8; 1.
DR Pfam; PF08393; DHC_N2; 1.
DR Pfam; PF17852; Dynein_AAA_lid; 1.
DR SMART; SM00382; AAA; 3.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 4.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Dynein {ECO:0000256|ARBA:ARBA00023017};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000023152}.
FT DOMAIN 474..613
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 1120..1270
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 1437..1555
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT COILED 1531..1564
FT /evidence="ECO:0000256|SAM:Coils"
FT NON_TER 1572
FT /evidence="ECO:0000313|EMBL:ETO35335.1"
SQ SEQUENCE 1572 AA; 180488 MW; F899599CDE3BAE15 CRC64;
MDLSQHHKAI SEIVTIARGE SNVEHFLNEI TEKWGKTLFE VIDSKGKKCP LVKNWMELRE
QVGEALTNVM QMKQSPFYKS FERDGAVWEE KLNAAQAIFD VMTDVQRRWV YLQGVFQNSV
DVQKTLGYMF QKFKGFDREF VQLMRGIKQD PFVDHWITPE KNLLHMLETN QSTLNTIQKA
LNEYLESQRA AFSRFYFIGD EDLLEIIGSA KDPKAMNRHW SKMFAGISQV ELQPENDSII
VGMSSREGEQ VLFKHPIDVT KTERIQDWLM QVEQQMRLTL ASLLEEALFT HASPQQVKSY
FEWIAKYPAQ VVLLATQVRW SERVESVLQS KSKSSDKNEE NEEKDSNVNM CKLLEEIVST
LGLLANCVLQ GTLESKMRKL YEQLITELVY QRDVTRTLIK DHVCSTSDFQ WLSRMRFYWN
RFEKDVLKKL EIRISRAKFF YGFEYFGANE RLVQTPLTDK AYFTLCEALH SKLGGNPFGP
AGTGKTESVK ALGTQLGRFV LVFCCDETFD YNAMSRIFVG LCQCGAWGCF DEFNRLEEQI
LSAVSQQILT IQTGLRENAG EIELNTSRGL EKVRLNHDMG IFVTMNPGYA GRSELPDNLK
QLFRGIAMMQ PNRVLIAQVI DQLSKQSHYD FGLRALKAVL RSAGNLKRRE QMELTIVGNG
HELTRMSPEM EQGILIRSLM STVVPKLVLQ DKLLFDSLLA SAFPGANIEG IKEEELKTKI
KDVAEERHYR IDDQWITKLL QLHTIQHINW GVMLVGPSGT GKTSSRDVLM EAMRLEIDPK
SITKEQLFGV LDPTTLEWTD GVFTATLRMI IDNAHGEANK RHWIVFDGDV DPEWAENLNS
VLDDNKMLTL PNGERLALTD NVRILFETAN LNAATPATVS RCGMVWFSEE CVTLPMLFHN
QLESLRAKPT LTTSGGDMAR TLLDWQRVHH IVVDYLTPLF KNEVSFVYEA MRWVQRKPHV
MEFTELRAVW SLFSQLRGGI RNVLEYNETN EVSPLSDLQI RSYMGKYLLH SILWAFGGSM
TLDLRMEFGN VLCHMVRNSD NNDHDYDGVN NGIDIGLPDT NSDLSLIDYE VNVERQEWTA
WKDQVVNEEL APQRIKDANV VINTTDTLRH SRVIGSWLQE RRPVILCGPP GSGKSMTLTA
VLSSNPQYEM VTLNFSSTAD PSLLFKCFEQ HCKVLRTSQG YTLRPIIPNK TLVVFCDECN
LPAEDKYGTQ TIITFLRQLI EKGGYWNHAN RNWVQLENIQ IVGACNPPTD AGRIVLSPRF
LNHCPLVLID FPGRESLLEI YGTFVRALLK LTPSLKGLDE NITHAMVDVY QKSQQHFNVD
IQPHYVYSPR ELSRWVRGID RLVTTEEKDW TWKLIREVAD THLHAVDDLD QALVQPILFS
DYLSCQRNYL SVGKAELYEY VVQRVKAFNE EELDVALVIY DELLDHILRI DRVLRQPLGH
LLLVGASGAG KSVFSRFVSW LNGMSTFQIK VHKDYTQEHF DQDLRSVLIR AGVDGERITF
LFDESNILHS AFLERMNALL ASGEVPGLFE EAELQQLLAK LREAARKEEE LKETEEELYQ
WFTRRVQHNL HI
//
