ID W8B1D5_CERCA Unreviewed; 1740 AA.
AC W8B1D5;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 22-FEB-2023, entry version 33.
DE SubName: Full=Dynein heavy chain 2, axonemal {ECO:0000313|EMBL:JAB94915.1};
DE Flags: Fragment;
GN Name=DYH2 {ECO:0000313|EMBL:JAB94915.1};
OS Ceratitis capitata (Mediterranean fruit fly) (Tephritis capitata).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Tephritoidea;
OC Tephritidae; Ceratitis; Ceratitis.
OX NCBI_TaxID=7213 {ECO:0000313|EMBL:JAB94915.1};
RN [1] {ECO:0000313|EMBL:JAB94915.1}
RP NUCLEOTIDE SEQUENCE.
RA Geib S.;
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:JAB94915.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24495485; DOI=10.1186/1471-2164-15-98;
RA Calla B., Hall B., Hou S., Geib S.M.;
RT "A genomic perspective to assessing quality of mass-reared SIT flies used
RT in Mediterranean fruit fly (Ceratitis capitata) eradication in
RT California.";
RL BMC Genomics 15:98-98(2014).
CC -!- SIMILARITY: Belongs to the dynein heavy chain family.
CC {ECO:0000256|ARBA:ARBA00008887}.
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DR EMBL; GAMC01011640; JAB94915.1; -; mRNA.
DR GO; GO:0030286; C:dynein complex; 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; 1.10.8.1220; -; 1.
DR Gene3D; 1.20.1270.280; -; 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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR Gene3D; 1.10.8.720; Region D6 of dynein motor; 1.
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; 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; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR45703; DYNEIN HEAVY CHAIN; 1.
DR PANTHER; PTHR45703:SF32; DYNEINS HEAVY CHAIN; 1.
DR Pfam; PF12780; AAA_8; 1.
DR Pfam; PF12781; AAA_9; 1.
DR Pfam; PF18198; AAA_lid_11; 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; 1.
PE 2: Evidence at transcript level;
KW Coiled coil {ECO:0000256|SAM:Coils}.
FT DOMAIN 34..311
FT /note="Dynein heavy chain AAA module D4"
FT /evidence="ECO:0000259|Pfam:PF12780"
FT DOMAIN 325..655
FT /note="Dynein heavy chain coiled coil stalk"
FT /evidence="ECO:0000259|Pfam:PF12777"
FT DOMAIN 683..901
FT /note="Dynein heavy chain ATP-binding dynein motor region"
FT /evidence="ECO:0000259|Pfam:PF12781"
FT DOMAIN 1151..1264
FT /note="Dynein heavy chain region D6 P-loop"
FT /evidence="ECO:0000259|Pfam:PF03028"
FT DOMAIN 1296..1435
FT /note="Dynein heavy chain AAA lid"
FT /evidence="ECO:0000259|Pfam:PF18198"
FT DOMAIN 1443..1736
FT /note="Dynein heavy chain C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18199"
FT COILED 333..385
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 539..608
FT /evidence="ECO:0000256|SAM:Coils"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:JAB94915.1"
SQ SEQUENCE 1740 AA; 198891 MW; EA838F0138E5568E CRC64;
SNQGYYEDLP FEDLRKYINR QMEEYNNFPG MANMNLVFFK EAIEHVTRAV RVISQPRGHV
LNIGIGGSGR QALVRLAAFI CEFGTFSIEV TKKYKTNEFK EDLKNLYKVT GIKQRGTVFL
FSNEQVAESS FLEILNNMLS TGEANLFKSD EFEELKTELE RPAKKAGIQF TTESLYNFFM
QNVRENMHIS LAMSPIGEDF RSYIRQYPAL INNTSPNWFR LWPQEALLEV AQKFLAGFKI
NVSVPGKEDE KHRDSLILTT EDRLQKAVAY VFSVIHSSVA QMSVQMLAEV KRHNYVTSPN
YLELVSGFKA LLENKRFEVS SSANKLRNGL SKIQETQEKV SIMSEELKIS SEQVKILAKE
CEEFIAIIEI QKAEATDQKE KVDAEAIIIR QEEVVCLDLA ATAQADLDVV MPMIDAAIKA
LDALSKKDVA EVKSYGRPPM KIEKVMEAVL ILLGKEPTWE NAKKVLGEVN FLNDLKNFDR
DHVTDKTLKR IGLYTKNPEL EPDKVAIVSV ACKSLMQWIM AIENYAKVYR IVAPKQEKLD
NAMRSLAEKQ AMLAAAMKKL EELNAAIAEL YRQLNEKTEL LNELRIKEER LRKQLERAII
LVESLSGERE RWIETVASLD LAFEKLPGDC LLATAFTSYL GPFDTKYREI LVEKWIGLIV
SNQIPCTDEM KITLFLSDAV TIREWNIQGL PADDFSTENG VIVMGGQRWP LIIDPQSQAN
TWIKNYEANN DLKVIDFSQT DYLRSLERAL SAGNPVLLQN VGESLDQAIN PILRKSFTMQ
GGQKLIKFND KYITYNDAFK LYITTKITNP HYPPEISSKT TIVNFAVKQD GLQAQLLGII
VRKEKPALEE QKDELVLTIA RNKRTLIELD NEILRLLNES RGSLLEDDEL FATLQKSRQT
SVLVKESLAT AEVTEIEIDA ARQEYQPAAE RAAILFFVLM DMSKIDPMYE FSLAAYILLF
IQSIERSPKH QMVYERIQNI NDYHTYSVYK NTCRGLFEMH KLLFSIHMTA KILECAGKLV
EAEYDFILKG GIVLDKQNQP PNPNPNWISE QAWDNITELD RVAGFHGIID SFEQNPKLWQ
MWYATTTPET EDLVGEWNDK LTDFEKICVV RCLRPDRVSF CLTQFIINTL GPRFVEPPVL
DLKAAFDESM SQTPLIFVLS PGVDPTQSLI MLAEQCRMSQ RMFSLSLGQG QAPVATKMIM
DGVRDGNWVF LANCHLSLSW MPTLDKIIAT MQSMKLHKRF RLWLSSSPHP EFPISILQSS
IKMTTEPPRG IKANMRRLYN NINEQTFESV DETSKYKKLL FALCFFHTVL LERKKFLELG
WNVIYSFNDS DFEVSDVLLA LYLNEYEETP WGALKFLIAG INYGGHVTDD WDRRLLTTYI
NQFYCDGALT THKFRLSSLI NYFIPGDGDL QSYIDQIQQF PNFDKPEAFG QHPNADIASL
IGETRLLFET LVSMQVQTTT AVGESMETKV LRLAKDIFAS TPDEINYEQT AKLIGLNRTP
LEVVLLQEIE RYNFLLSRMK IHMRDLQRGI KGLVVMSTEL EDIYQSVYEG RVPAVWLKSY
PSLKPLAAWS RDLILRIEHF SHWAKTLKQP TLFWLAAYTF PTGFLTAVLQ TSARATRTPI
DELSWDFFVF IEDDAAAARI VREGGGVYVR GLFLEGAGWL RKLQCLQDPL PMELICPMPV
IHFKPVENLK KKTRGVYQCP AYYYPQRAGS FIIAVDLKSG NEKSDYWIKR GTALLLSLSV
//
