ID A0A3B4VGS0_SERDU Unreviewed; 4030 AA.
AC A0A3B4VGS0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Dynein heavy chain 1, axonemal-like {ECO:0000313|Ensembl:ENSSDUP00000029767.1};
GN Name=DNAH1 {ECO:0000313|Ensembl:ENSSDUP00000029767.1};
OS Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000029767.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000029767.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium, flagellum
CC {ECO:0000256|ARBA:ARBA00004230}. Cytoplasm, cytoskeleton, cilium
CC axoneme {ECO:0000256|ARBA:ARBA00004430}.
CC -!- SIMILARITY: Belongs to the dynein heavy chain family.
CC {ECO:0000256|ARBA:ARBA00008887}.
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DR STRING; 41447.ENSSDUP00000029767; -.
DR Ensembl; ENSSDUT00000030280.1; ENSSDUP00000029767.1; ENSSDUG00000021400.1.
DR GeneTree; ENSGT00940000154791; -.
DR OMA; HNVAKMV; -.
DR Proteomes; UP000261420; Unplaced.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-KW.
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: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; 1.10.287.2620; -; 1.
DR Gene3D; 1.10.472.130; -; 1.
DR Gene3D; 1.10.8.1220; -; 1.
DR Gene3D; 1.10.8.710; -; 1.
DR Gene3D; 1.20.1270.280; -; 1.
DR Gene3D; 1.20.58.1120; -; 1.
DR Gene3D; 1.20.920.20; -; 1.
DR Gene3D; 1.20.920.30; -; 1.
DR Gene3D; 3.10.490.20; -; 1.
DR Gene3D; 6.10.140.1060; -; 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; 5.
DR Gene3D; 1.10.8.720; Region D6 of dynein motor; 1.
DR InterPro; IPR035699; AAA_6.
DR InterPro; IPR035706; AAA_9.
DR InterPro; IPR041658; AAA_lid_11.
DR InterPro; IPR042219; AAA_lid_11_sf.
DR InterPro; IPR026983; DHC_fam.
DR InterPro; IPR041589; DNAH3_AAA_lid_1.
DR InterPro; IPR042222; Dynein_2_N.
DR InterPro; IPR043157; Dynein_AAA1S.
DR InterPro; IPR041466; Dynein_AAA5_ext.
DR InterPro; IPR041228; Dynein_C.
DR InterPro; IPR043160; Dynein_C_barrel.
DR InterPro; IPR024743; Dynein_HC_stalk.
DR InterPro; IPR024317; Dynein_heavy_chain_D4_dom.
DR InterPro; IPR004273; Dynein_heavy_D6_P-loop.
DR InterPro; IPR013602; Dynein_heavy_linker.
DR InterPro; IPR042228; Dynein_linker_3.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR46961:SF18; DYNEIN AXONEMAL HEAVY CHAIN 1; 1.
DR PANTHER; PTHR46961; DYNEIN HEAVY CHAIN 1, AXONEMAL-LIKE PROTEIN; 1.
DR Pfam; PF12774; AAA_6; 1.
DR Pfam; PF12775; AAA_7; 1.
DR Pfam; PF12780; AAA_8; 1.
DR Pfam; PF12781; AAA_9; 1.
DR Pfam; PF17857; AAA_lid_1; 1.
DR Pfam; PF18198; AAA_lid_11; 1.
DR Pfam; PF08393; DHC_N2; 1.
DR Pfam; PF17852; Dynein_AAA_lid; 1.
DR Pfam; PF18199; Dynein_C; 1.
DR Pfam; PF03028; Dynein_heavy; 1.
DR Pfam; PF12777; MT; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 4.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Cilium {ECO:0000256|ARBA:ARBA00023069};
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}.
FT DOMAIN 825..1227
FT /note="Dynein heavy chain linker"
FT /evidence="ECO:0000259|Pfam:PF08393"
FT DOMAIN 1355..1681
FT /note="Dynein heavy chain hydrolytic ATP-binding dynein
FT motor region"
FT /evidence="ECO:0000259|Pfam:PF12774"
FT DOMAIN 1849..1932
FT /note="Dynein heavy chain AAA 5 extension"
FT /evidence="ECO:0000259|Pfam:PF17852"
FT DOMAIN 2186..2275
FT /note="Dynein heavy chain 3 AAA+ lid"
FT /evidence="ECO:0000259|Pfam:PF17857"
FT DOMAIN 2328..2589
FT /note="Dynein heavy chain AAA module D4"
FT /evidence="ECO:0000259|Pfam:PF12780"
FT DOMAIN 2603..2947
FT /note="Dynein heavy chain coiled coil stalk"
FT /evidence="ECO:0000259|Pfam:PF12777"
FT DOMAIN 2976..3197
FT /note="Dynein heavy chain ATP-binding dynein motor region"
FT /evidence="ECO:0000259|Pfam:PF12781"
FT DOMAIN 3441..3554
FT /note="Dynein heavy chain region D6 P-loop"
FT /evidence="ECO:0000259|Pfam:PF03028"
FT DOMAIN 3586..3725
FT /note="Dynein heavy chain AAA lid"
FT /evidence="ECO:0000259|Pfam:PF18198"
FT DOMAIN 3731..4026
FT /note="Dynein heavy chain C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18199"
FT REGION 75..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 581..608
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 784..811
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2832..2880
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 4030 AA; 458718 MW; 8F0DDBFF7595F67F CRC64;
SSDQYKFVDK DYHGPISQLS QNPYFCRRGD TPKVQLPYQT IPGQIPRKLA IERRRREYLK
LDFEQLLAEK GIDSNLIMPR NPSSSDEDAL GKAEGSPDQK PIPAKALLPT DNSTSSEDTK
SSCLEYSWHL VGVLDYSKDK CQYLVQKVHQ VSDEEGNPIL NEGHKNSKFP GLFLCTEHWV
PRIRLFFFAE DPRVFVERIQ FALRLRENTE ALLFYHLSVD CMPIWKGTPS LDTHSLQYMK
KALSTPGLSI EKCIGDLEKE VKLEYYRTVN CMTFDKVVMS NSEEFSHITL PKKDPEHLPQ
KGEPKNQAVF VFRSLLRKPE VICVLSEIRS ECNKVATMRL FNVTLTKPLQ LDEFEVIQTQ
IHTKVLLLLR ESWTNTLSNS IRSNLGNIGK GSYNVNESHW DMYKMSRLYG LMGVVRFRMQ
DSLRHLVQNS LVSLTRLVLD ACHSVLMCPQ DLVWGSDLIT SPYKPKKNPL FLVDLVLDQN
GVQYSTPLEN FETSIVNLFD KSILATYNVP QLDKFVMQKL FIGDDPLLES VNLWEPEVTE
QREKVRNALI QAAIPLRAYA TEYEEHLDLH NLDIDTLLNS HTHAEQTSQE VKKEVEQHLK
EMEKIQHSLP SCIVIGPFIV RVDTVRQALS SKRKALANAM LRHLALKLRK KVDDACEKCN
IISRKLQETP NSIEELTEKR DWMKQIPEQL KSYKELIGKT LSDYEVLEEL WYCLSDEDAN
KKWTAIGWPQ RIINQMEAAA VQHVEDEERF RKIQLTDQNN FGEHLDALQM LVAGFTAHVD
IDHAHDMANE MRRAREQLKE CQTLAQTYNT RERLFGLPVT NYDRLQKLVK DFQPFKDLWT
TTSEWLHSHE SWLNDSLSSI DPEQLERNVT DAHKTMHKCI KQFKDIPECQ MVATVIRNKI
EDFLPYIPLI QGLRNPGMKS RHWEMLSERI QMKVKPKANL TLSRCLELGL QNHVDDIAHV
AEVAGKEYTI EQALEKMEQE WTTVVFDVLP YKETGTYILK SPDEASQLLD DHIVMTQSMS
FSPFKKAFED RINTWESKLR MTQDVLEEWL TCQRSWLYLE PIFSSDDINQ QLPVEGKRYQ
HMEQIWKRVM KSAFNNRIVI KLCPDARLLD KLKECNALLE HVQKGLSEYL ETKRGSFPRF
YFLSDDELLE ILSQTKDPNA VQPHLRKCFE NIAQLQFQSD LQITHMYSGE GEEVKLFLPV
WPTGNVEDWL RNVEKSMKAT LRDNIDRSLK AYPEHPRVEW VLSWPGQVVI AGCQVFWTAE
VSEALERGDL ADHLYPQLQT QLGDLVQLVR QGLSMMQRAV LSALIVIEVH AKDVAAKLVE
QKVSSINDFE WISQLRYYWA KDDLYIRAVN AEFLYGYEYL GNSGRLVITQ LTDRCYLTLT
GALHLKFGGA PAGPAGTGKT ETTKDLGKAL AIQTVVFNCS DQLDFIAMGK FLKGLASSGA
WACFDEFNRI DVEVLSVVAQ QITTIQKAQQ QRAERFMFEG SEIPLVPSCA VFITMNPGYA
GRTELPDNLK ALFRPVAMMV PNYAMIAEIS LYSFGFSDAK VLSKKITTTF KLSSEQLSSQ
DHYDFGMRAV KTVISAAGNL KRENPNMNEE LICLRAIQDV NVPKFLQDDL KLFHGIVSDL
FPKTKQEPIN YGTLEESMRN VCTKKNLKDV DGYISKCIQL YETTVVRHGL MLVGPSGSGK
TKCYEILGAA ITALKGQPSV SGGVYEPVHT YVLNPKSITM GQLYGEYDLL THEWTDGILS
SLIRGGAASM DKEKKWYMFD GPVDAVWIEN MNTVLDDNKK LCLSSGEIIK LTDVMTMMFE
VQDLAVASPA TVSRCGMVYL EPSILGLIPF TECWLKQVPQ VLKPYTKQLN SLFEYIDECA
NMLPLPQKNL DCLNELIEPW FFFSLVWSVG ATGDAASCQR FSAWLKNKMA EEKIKLCFPE
EGLVYDYRLD DAGISNLEDD DEDEERKVQW VSWMKYAKSV VITPETNYAD IIIPTADTMR
MSFLMDMLLT NKKPVLCIGP TGTGKTLTMS DKLLKNMPSE YITNFLMFSA RTSANQTQDY
IDSKLDKRRK GVFGPPIGKH FIFFIDDLNM PMLETYGAQP PIELLRQWMD HGGWYDRKQI
GAFMHLVDIN FACAMGPPGG GRNPITQRFT RHFNFLSFTE MDDTSKKMIF STILGSWMGE
TVSLMCLNLK SYVRPVPAIQ PLNESLVDAT IRIYTTITSQ LLPTPSKSHY TFNLRDLSKV
FQGILMAEAG MIEEKLQLLQ LWYHESCRVF QDRLVSAEDR DWFNRLLKDC IQGFDCSFED
VVPCQPVLYG DFMIAGADHK VYTLIEDKEK VMMEEYMEDY NQISTTKMKL VLFMDAIEHV
CRISRILRQP LGNALLLGVG GSGRQSLTKL ASHMSEYECF QIELSKNYGQ TEWREDIKSI
MLKAGLQNQQ ITFLFVDTQI KSESFLEDIN NILNSGDVPN LYASDEQERI LAAMKPVVLD
LGQQPTKANL MAAYIRRVRS NIHNVLCMSP MGEVFRARLR QFPSLVTCCT IDWFSAWPEE
ALQAVATSFL NELPQLEASP TAMRGLTSMC VKIHQMVARK SEQYLVELSR YNYVTPKSFL
ELLKIFSDLI GQKKQELCAA RQRMKTGLDK LLSTAEDVSK MQEELETMRP LLEEAARETE
VTMETIKKDT VVAEETRKSV QAEEAKASEK ARFAGAIATD AQKDLDEALP ALDAALTSLK
SLNKNDVTEV RAMQRPPHGV KLVIEAVCIM KGIKPKKVPG EKPGTKINDY WEPGKGLLQD
PGKFLESLFK YDKENIPDSV ISLVQPYIDN EEFQPDSIAK ISKACTSICQ WVRAMHVYHF
VAKGVEPKRK ALQEAQEDLA STQLILDDAK DKLAAVEGGI ATLQAKYQDC LAKKDELDNK
YQLCEARLVR ADKLIGGLAD EKVRWKETVL HLDYMVNNVA GDVLLSAGYV AYLGPFTGEY
RVAMAEEWLH CFKELSVPHT EEPNLINTLG NPVKIRSWQI SGLPKDNLSV ENGVIAQYSL
RWALFIDPQG QANKWIKNME QDNALEVMKL SDRDFLRSLE NAICFGKPCL LENVGEELDP
ALEPVLLQQT FKQQGSTVLK LGDSVIPYHE GFKMYITTKL PNPHYSPEVS TNVTLINFTL
SPSGLEDQLL AQVVAEERPD LEDAKNQLII SNAQMKQELK EIEDEILSRL SSTEGNPVDN
VELIQVLGAS KIKAGEIKAK VMAAEKTERD IDATRLEYVP VAVRTQILFF CVSDLSIVDP
MYQYSLEWFL GIFMAGIANS ERADTVKKRI TNINEFFTFS LYSNVCRSLF EKHKLMFAFL
LCTRIMMNEN KIDKAEWRYL LSGGMPIQEM TNPAVSWLSE RAWQDILGLS ALDNFSKLAE
SFAKHLQGFK KIFDSNQPHR EPLPEEWDTE LDSFQKLLIL RCLRADCLVQ GLQDFVSAQL
GQRFIEPQTS DLSVVFAESS PSTSLIFVLS PGTDPAADLY KFADVMQFSK KMSAISLGQG
QGPWAETMMH AAMERGQWVF FQNCHLAPSW MPTLERLIEN INPVKVHKDF RLWLTSLPSN
RFPVSILQNG SKMTIEPPRG IKANLQKTYL RLTNDFISSS TKITNFKSLL LSLCLFHGIA
LERRKFGPLG FNIPYEFTDG DLNICISQLK MFLDEYQDIP YKVLKYTAGE INYGGRVTDD
WDRRCLLSVL EVFYCPAVLI DDHVYSSSGV YRQIDTNLDI KGYLAYIRGL PINDTPEIFG
LHDNANISFA QNETFALLGA VVRLQPRAAS AGGKSQEEEI VAGIAEKIPR PFSVQELMEK
YPVLYEESMN TVLIQEVIRY NKLLAVISQS LSDIVKALKG LVVMSSELEL MANSLFNNVV
PDMWKAKAYP SLKPLASWVS DLLQRISFLQ GWIYNGIPPV FWISGFFFPQ AFLTGTLQNY
ARRYSTSIDT IGFDFESVSE ITEKPNAGCY IQGLFLEGAR WDNGAGQLTE SRPKELYTEM
AVIWLIPMSN RKTPTSGVYV CPIYKTLTRA GTLSTTGHST NYVMSVELPT DRNQRHWIKR
GVALICALDY
//