ID V8NR57_OPHHA Unreviewed; 1738 AA.
AC V8NR57;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Dynein heavy chain 11, axonemal {ECO:0000313|EMBL:ETE64168.1};
DE Flags: Fragment;
GN Name=DNAH11 {ECO:0000313|EMBL:ETE64168.1};
GN ORFNames=L345_10064 {ECO:0000313|EMBL:ETE64168.1};
OS Ophiophagus hannah (King cobra) (Naja hannah).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus.
OX NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE64168.1, ECO:0000313|Proteomes:UP000018936};
RN [1] {ECO:0000313|EMBL:ETE64168.1, ECO:0000313|Proteomes:UP000018936}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Blood {ECO:0000313|EMBL:ETE64168.1};
RX PubMed=24297900; DOI=10.1073/pnas.1314702110;
RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J.,
RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J.,
RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A.,
RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C.,
RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M.,
RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., Dirks R.P.,
RA Spaink H.P., Duboule D., McGlinn E., Kini R.M., Richardson M.K.;
RT "The king cobra genome reveals dynamic gene evolution and adaptation in the
RT snake venom system.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013).
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:ETE64168.1}.
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DR EMBL; AZIM01002365; ETE64168.1; -; Genomic_DNA.
DR Proteomes; UP000018936; 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; 1.20.58.1120; -; 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; IPR013602; Dynein_heavy_linker.
DR InterPro; IPR013594; Dynein_heavy_tail.
DR InterPro; IPR042228; Dynein_linker_3.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10676:SF263; DYNEIN AXONEMAL HEAVY CHAIN 11; 1.
DR PANTHER; PTHR10676; DYNEIN HEAVY CHAIN FAMILY PROTEIN; 1.
DR Pfam; PF12774; AAA_6; 1.
DR Pfam; PF08385; DHC_N1; 2.
DR Pfam; PF08393; DHC_N2; 1.
DR SUPFAM; SSF56219; DNase I-like; 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:UP000018936}.
FT DOMAIN 13..364
FT /note="Dynein heavy chain tail"
FT /evidence="ECO:0000259|Pfam:PF08385"
FT DOMAIN 361..507
FT /note="Dynein heavy chain tail"
FT /evidence="ECO:0000259|Pfam:PF08385"
FT DOMAIN 984..1362
FT /note="Dynein heavy chain linker"
FT /evidence="ECO:0000259|Pfam:PF08393"
FT DOMAIN 1580..1738
FT /note="Dynein heavy chain hydrolytic ATP-binding dynein
FT motor region"
FT /evidence="ECO:0000259|Pfam:PF12774"
FT COILED 508..535
FT /evidence="ECO:0000256|SAM:Coils"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ETE64168.1"
FT NON_TER 1738
FT /evidence="ECO:0000313|EMBL:ETE64168.1"
SQ SEQUENCE 1738 AA; 204256 MW; B92FF1A53B3BC2FB CRC64;
MANRQNSQTR SVLHEIESIV IKWSRQIKDI LERNTAQPPF NQVHPDPQSE LKFWKERKDN
LLCIYDQLKS PIIQKLIGIL KIKKSSYYPT FQDIYKDVEN ALIEAQDIEL YLKTLERHIQ
FFQETEFPGI HILIPPLFHT ICLIWSHSKF YNMPARIISL LQEFCNLFIH QATLYLSPGD
IMEREAEETL EQIQSALNTL RSFKDAFFNE RKQVATYFTS SQENIFVTML EFEKLEKLEF
GGIKGKCLNA HISKLNEEFI EFCNTFKEKT YDPLDYNNME FEEDYSDFKH KNLEFERRLG
AIFCVAFLDC SGLESAFKLI TILGSFLEKP IIIEMFSANY KILLQMFDEE LRNCKCLYDE
HIKQKYIEIL KLFDQYEDQI YFKWKSKVDD ICLFNLDQPL IKRNGKDGLL SVNFDPKLVA
VLRDVKYLLL MDQPNIPSSA LELYKKKGTF AKYTGNLELV VQWYNKVKQT VLEVEYPLVE
KELIAADNLL KEAEKKLTWQ KENCWEYIEC IKAKVHDLEQ RLQKSKDNIK TIQQIMNYWM
EQPFFSRKDN RKEALLNLED KEDKIAKKIM SFQEDGCRMH KLVEENLKLF KADLDSDSWK
IYLEFVDDII ADGFFNAIAY NLNFFLENTE KVLKPAPLFQ VQMILSAVEI EFKPSLDKEA
GDGFYDLIDE LLSNIFKISA QVKRMASHLE IQHYQNDMDD ISELSSTREK IMNRVADVIT
EAMNFKNSLD CYAYLWVDDR SEFMKQFLFY GRIDIYENLY NQMSKLEDFR IFEGWLKVDL
KPFKHSFLNV IKKWSWMFKE YLVKFVTDSL ADLEEFIKMT NLGLQKQLSE IDYNGLIDIM
FHLLAVRDRQ SATDGLFEPL KDTIVLLENY GQKMPDHIYI QVEELPEKWN ATQKLAVSVK
HEVAPFLTSE VTILRKKCAA FDGKQIGFRE RFRADAPFHF DAQNPYALLD KANQELERME
EEMLHLHETA NLFEVTISEY KQIKECRQEI KLLKRVWDIN IYVTSSIDDW TKMHWREISM
EQMEEIWSLD KEVRSWNVYT SLELTIKNLL TSLRVVIELQ NPAIRDRHWY QLMETIGVPF
SITEDTTLAN LLALNLHNVE DYVRNIVDKA VKELGIEKIL IEISQTWAAM EFSYEEHFRT
NISLLKIDEQ LFETLDNNQI QLQTVLQSKY VEYFIEQVLT WQKKLNVADA VIYIWMEVQH
TWSHLESIFT GSNDIREQLP EDSKRFDCID MDFKGLMNDS TNTRNVLEAA TKPNMHEKLQ
DLQHRLSVCE KALAEYLETK RLAFPRFYFV TCHLIKLFDN IADLKFQDNE DEHSNIVLGM
YSKEKEYVPF NEQLECSGQV ETWLKCLEDT MHESVRYHIT EAISVYEEKP REQWIIDYPA
QVALTGSQIW WTTDVGIAFS RLEEGFETAL KDYHKKQITQ LNALIALLLG DLTPSDRQKI
MTICTVDVHA RDVVAKLLSQ KERKRGVVIY VKEDIISKLI YKDTLGRAVM VEVDIQNKKT
LLVGIYAPNK CQNEFYKNLY EKLTQFNSQR ICLMGDFNAI YEIKQDYNSQ AFPWLSQLRH
RWDWTLKHCF VNICDAHFQY YYEYLGNTPR LVITPLTDRC YITLTQSLHL TMSGAPAGPA
GTGKTETTKD LGHALGMMVY VFNCSEQMDY KSIGNIYKGL VQTGAWGSFD EFNRISVEVL
SVVAVQVKTI HDAIRHNKKQ FIFLGENITL KASVGIFITM NPGYAGRTEL PENLKTLF
//
