ID F4WD53_ACREC Unreviewed; 4463 AA.
AC F4WD53;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE SubName: Full=Dynein beta chain, ciliary {ECO:0000313|EMBL:EGI67861.1};
GN ORFNames=G5I_03503 {ECO:0000313|EMBL:EGI67861.1};
OS Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS echinatior).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Acromyrmex.
OX NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN [1] {ECO:0000313|EMBL:EGI67861.1}
RP NUCLEOTIDE SEQUENCE.
RA Nygaard S., Zhang G.;
RT "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT adaptations to social evolution and fungus farming.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the dynein heavy chain family.
CC {ECO:0000256|ARBA:ARBA00008887}.
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DR EMBL; GL888084; EGI67861.1; -; Genomic_DNA.
DR STRING; 103372.F4WD53; -.
DR eggNOG; KOG3595; Eukaryota.
DR InParanoid; F4WD53; -.
DR Proteomes; UP000007755; Unassembled WGS sequence.
DR GO; GO:0005930; C:axoneme; IEA:UniProt.
DR GO; GO:0030286; C:dynein complex; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0031514; C:motile cilium; IEA:UniProt.
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 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; IPR003593; AAA+_ATPase.
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; IPR013594; Dynein_heavy_tail.
DR InterPro; IPR042228; Dynein_linker_3.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR45703; DYNEIN HEAVY CHAIN; 1.
DR PANTHER; PTHR45703:SF8; DYNEINS HEAVY CHAIN; 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; PF08385; DHC_N1; 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 SMART; SM00382; AAA; 2.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000007755}.
FT DOMAIN 1848..1984
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 2453..2598
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT COILED 3042..3086
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 3272..3320
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 3571..3601
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 4463 AA; 508946 MW; 9F919E8E318C86A8 CRC64;
MTTPEAPADF RLEYIGGFVQ KSLKLKPEKW GRLLLTEEYR NVVLDFLDKS LPIALFVVLT
PNAQLVASSS FPIPCQRTKG VYAVKVTQAP LPKDKEACSA MLIVGDLSHR IVDQLATLVD
NIVAPLLTKP ENHKDLPEVA IHDICKHVHA LRGTLYQVKG QVNGRTVLPM PAGLEKVTEV
ERLVSVEGPQ AVDLYLKSAI EGVVIKWAYL VNDVVTHESS VAFDNGQNPT PNVELEYWST
RLANLRYIYD QLQEDRVKKM ATILEKTDSA YFPCFRTLFD NVVSSLAEAK DISLYLTPLA
KCFKTVEEID FAEAKPLMAT LIHSLGLAWA KCKSYQSSSK LIIMLRQICN LLIQEARRFL
DPTSIFQSDV DEALQRVKIS RGVLEEFKRQ FELRKHMPGL KPEAPPWTFN STAVFTRLDA
FLKRLADIEW LFDTVLEFFK LEKIEIGGIL GRSLSTRIIS VFKEFQQLFV SFTVRASDVL
EPDDESFVID CTKFAESITD LDSKLSAILC QAFDDCGNLE SVFKLINIAG SVLERPVIRK
QFSNRYTRIL ELLNMELSVV EVLFNRGSRD ALINLPPLAA ALTFTNMLQQ RIDLPVQSFK
AMPHPIVHSD EGNNIMSRYE RLIKIFADKE NDLFTEWAQT VPQTVDVGLR RHLLCRNTDD
NLLLNFDLDL LSILKEVSYL KQMSRSDIPQ EAIKVSESAE TFRKFRTMLS STVDSYNNIR
KTTKRVEFDL IELEIARIDS LISRGEDELW WRSDGLLEYI TELGDLVEGL WKRMKSAQSN
VGKIRNILEP WTKTPLIERK DRRKETLLAL EDRSEKVSKR YAEITKAAEQ IHSILEENKT
LFQINEIEQE VWQEYIKYID DIVIESLRKA VGCSLGYLAE SMEPIGQCEP LLEAKLELRE
PDLYYMPSLE PDDPDGLDQL ILGLLNDIIG MAALVPRLKN DSEGYAEELA SDADMKGMKD
EILTSVATAV EEATDFCSNF EGYAYLWLDD RDVVMQQFLE YSRQLSVEEI DMVATQDPKG
PTKSPPKMEQ FREQIDLYES LYVEIEEMNL SKVFCGWFKV DLRPFRQSVL NTVCKWSSMF
KKHLVDRVTS SLSNLGAFIR LADEGLLQQV QPGDYAALVS VMGFLLQVKE RQPTTDEMFH
PLEETIELLK FYDQDIPEEV NVLLQELPEQ WANTKKLALM VKQQVAPLQA GEVSRIRGRI
SAFDITINQY REAFRRYTFF KYDCKNPYEL LDEAHKEILM LERQMKDIQE SASLFEVTVP
EFKQLRQCRR ELKMLKQLWD YVNIVQSSIE GWKTTPWRKI DVENMDIECK KFAKEIRVAL
DKEMRPWGTY VSLEATVKNM LTSLRAVGEL QNPAIRERHW RQLMNSTKKL GNMTPEMTVR
FVMDESTTLA DLLELNLHDC EEEVKNIVDK AVKEMSMEKY MKELNVTWSK MEFEREVHTR
TGATLIRASE ELIETLEENQ VQLQNLITSK FIAHFLEEVS SWQKKLSIAD QVTTIWFEVQ
RTWMHLESIF MSSEDIRRQL PVDAERFDRI DKEFKEMTEE MAKTPNVVEA TNKDGLVSAL
DVLQKGLVLC EKALAEYLET KRLAFPRFYF VSSSDLLDIL SNGNQPEIVA KHLTKLFDSM
ARLNFDTKNT SLKRILGMFA KDGEYVDFAN YEMICEGAVE GWLNRLQKAM RVSIRHYFSE
AVVTYEEKPR EQWLFDYPAQ VSLCGTQIWW TTEVNLAFAR LEEGYDNSLK DYLKKQISQL
SILITLLIGE LTKQERQKVM TICTIDVHSR DVVTKLVQSK VESAQAFQWQ SQLRHRWDEK
EKDCFANICD AQFKYSHEYL GNTPRLVITP LTDRCYITLT QSLHLIMGGG PAGPAGTGKT
ETTKDLGRAL GIMVYVFNCS EQMDYKSCGN IYKGLAQTGA WGCFDEFNRI TVEVLSVVAV
QVKSIQDAIR DKKEHFNFMG ETIALEPTVG IFITMNPGYA GRTELPENLK ALFRPCAMVV
PDFELICEIM LVAEGFQDAR VLARKFITLY TLCKELLSKQ DHYDWGLRAI KSVLVVAGSL
KRGDPGRPEE QVLMRALRDF NIPKVVSDDL PVFMGLIADL FPALDVPRKR DIEFEKMVKQ
AAADLSLQPE DGFILKVVQL EELLEVRHSV FIVGITGSGK TQVWKTLFKT YHNMKRKPVY
NDLNPKAVTN DELFGIINPA TREWKDGLFS VIMREQANLG GENPKWIVLD GDIDPMWIES
LNTVMDDNKV LTLASNERIA LTPAMRLLFE ISNLRTATPA TVSRAGILYI NPQDLGWNPY
VTSWVEKRSL PSEKSNLVML FDKYIPTCLE TLRTRFKKIT PIADMAHVEM LCHLLHCLLK
PELTTGDFHK DHYELYFVFA AVWAFGSSMF QDQTVDYRVE FTKWWTNEFK QIKFPSQGTV
FDYYIDNETK SFLPWTERLP KFELDPEIPL QAVLVYTSES IRIKYFLDLL MPEKHPIMLV
GTAGCGKTVL VAEKLLQLSE NYAVSNVPFN FYTSSEMLQK ILEKSLEKKA GRNYGPPGNK
TLIYFIDDMN MPEVDAYGTV QPHTLIRQHL DYGHWYDRTK LTLKDIHNCQ YISCMNPTAG
SFTINPRLQR HFAVFAVSFP NVDSLTTIYS SILSQHLANV EHRFPVSVTE LCPNIVQASI
QLHHRCAQMF LPTAVKFHYI FNLRELSNCF QGLLFSGNEC LQSSVDLIRL WMHETQRVYG
DKLTDEKDIE SFLKLQLDIL KKNVEEVDEG AILEKPNIYC HFAGGVGEPK YMPVKDWTTL
HRLLSEAMVS YNDLVAAMNL VLFEDAMMHV CRVNRILESP RGSALLVGVG GSGKQSLSRL
AAFISSLEVF QVQLKKGYGV TDLKLELAAL YSKAGLKNLG IMFLMTDAQV PNEQFLVLIN
DMLASGEVPD LFAEDEMENI IAGVRNEVKG AGMLDTRENC WKFFIDRVRR QLRVVLCFSP
VGSTLRVRSR KFPAIINCTM INWFHEWPQE ALMSVSKRFL QELEELPEIY RESAAKFMAH
AHTSVNIASR HYLSSERRYN YTTPKSFLEQ ISLYTRLLKT KTSELRARVA RLENGLDKLR
STAVQVDKLK KKLAVQEVEL QQKNDAADAL IAIVGVETEK VQKEKAIADE EESKVAVIAE
EVSKKQKDCE ADLMKAEPAL LAAQEALNTL NKANLTELKS FGSPPGAVTN VTAAVMVLLA
PAGKVAKDRS WKAAKIMMAK VDTFLDSLIN YDKENIHPEV IKAIQPYLKD SEFEPEFVRS
KSAAAAGLCA WVINIIKFYE VFCDVEPKRK ALAHANAELA AAQDKLSGIK RKVASLEEQL
AKLTADFEKA TSEKLKCQQE ADATNSTIAL ANRLVGGLAS ENVRWADSVA NFMQQASTLP
GDVLLVTAFI SYVGCFTKQF RQDLLNKQWL QFIRSIEPTI PITEGLDPLS LLTDDTQIAK
WNNEGLPNDR MSTENATILS NSDRWPLMID PQLQGIKWIK EKYGDELKVI RLGQRGYLEV
IELALANGSI VLLENIGETV DPVLDPLLGR NLIKKGRAIK IGDKEVEYNS MFRLLLHTKL
ANPHYKPEMQ AQTTLINFTV TRDGLEDQLL AEVVKAERPD LEELKAELTR QQNDFKITLN
SLEDSLLSRL SSAGSNVLED TSLVENLETT KRTAAEIESK VTEARGTSRQ IDAARELYRP
AAARASLLYF ILNDLNTINP IYQFSLKAFS VVFQKAILKA DPAPDVAARV QNLIECITYS
VFMYTSRGLF ECDKLIFASQ MAFQILLVRN EVTTSELDFL LRFPITPHVT SPVDFLTNTS
WGGIRSLSTR EEFRNLDRDI ESSAKRWKKF VECECPEREK FPQEWKNKTA IQRLCMLRAL
RSDRMTYAIA AFIEEKLGAR YVEARTVEFA KSYEETSPGT PIFFILSPGV NPLKDVEDLG
RRLGFMSDNQ NFHNVSLGQG QETVAEQAID VAATNGHWVV LQNIHLVKKW LPLLEKKLET
AAEGSHPDYR MFMSAEPAST PAGHIIPQGI LESSIKITNE PPTGMQANLH KALDNFTQET
LEMCSKEAEF KAILFSLCYF HAVVAERRKF GPQGWNKIYP FNVGDLNISV SVLYNYLEAS
PKVPWEDLRY LFGEIMYGGH ITDDWDRRLC VSYLEELMQP DLIDGELQLA PGFPAPPNTD
LIGYHTYIDE AIPPESPYLY GLHPNAEIGF LTMTAENLFR TVFEMQPRDT GSSGGQTVKQ
VLDEIIEKLP EEFNMMEIMG KVEERTPYVI VAFQECERMN FLTTEIKRSL RELDLGLKGE
LTITSDMEDL ENALFFDQVP PVWASRAYPS LLGLTGWFVD LLLRIRELET WSTDFVLPAS
VWLAGFFNPQ SLLTAIMQST ARRHELPLDK MCLQCDVTKK NKEEFTSAPR DGAYVHGIFM
EGARWDIQTG IIVDSRPKEL YPGMPVINVR AITQDKQDLR NMYECPVYKT RTRGPTYVWT
FNLKTKDKPA KWTLAGVALL LQT
//
