ID A0A183A957_9TREM Unreviewed; 1519 AA.
AC A0A183A957;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:VDP69671.1, ECO:0000313|WBParaSite:ECPE_0000349501-mRNA-1};
GN ORFNames=ECPE_LOCUS3492 {ECO:0000313|EMBL:VDP69671.1};
OS Echinostoma caproni.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Plagiorchiida; Echinostomata; Echinostomatoidea; Echinostomatidae;
OC Echinostoma.
OX NCBI_TaxID=27848 {ECO:0000313|Proteomes:UP000050740, ECO:0000313|WBParaSite:ECPE_0000349501-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:ECPE_0000349501-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDP69671.1, ECO:0000313|Proteomes:UP000272942}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Egypt {ECO:0000313|EMBL:VDP69671.1,
RC ECO:0000313|Proteomes:UP000272942};
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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; UZAN01040444; VDP69671.1; -; Genomic_DNA.
DR WBParaSite; ECPE_0000349501-mRNA-1; ECPE_0000349501-mRNA-1; ECPE_0000349501.
DR Proteomes; UP000050740; Unplaced.
DR Proteomes; UP000272942; Unassembled WGS sequence.
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; 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; 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; PTHR46532:SF4; DYNEIN HEAVY CHAIN 8, AXONEMAL-LIKE PROTEIN; 1.
DR PANTHER; PTHR46532; MALE FERTILITY FACTOR KL5; 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 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000272942}.
FT DOMAIN 30..260
FT /note="Dynein heavy chain AAA module D4"
FT /evidence="ECO:0000259|Pfam:PF12780"
FT DOMAIN 242..584
FT /note="Dynein heavy chain coiled coil stalk"
FT /evidence="ECO:0000259|Pfam:PF12777"
FT DOMAIN 612..782
FT /note="Dynein heavy chain ATP-binding dynein motor region"
FT /evidence="ECO:0000259|Pfam:PF12781"
FT DOMAIN 1029..1104
FT /note="Dynein heavy chain region D6 P-loop"
FT /evidence="ECO:0000259|Pfam:PF03028"
FT DOMAIN 1221..1366
FT /note="Dynein heavy chain AAA lid"
FT /evidence="ECO:0000259|Pfam:PF18198"
FT DOMAIN 1398..1476
FT /note="Dynein heavy chain C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18199"
FT REGION 1129..1166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 233..284
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 470..553
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1519 AA; 173264 MW; BB5AF431D7F8AEBC CRC64;
MPVYDIDQLH ERLLYLQNQL NEDEKTKSAE LIFFTDAIHH LVRTARAIRN PNGHILLVGL
SGSGKQSLAR LSARIAGYEV FSGLTVGPSQ LNNFIDDLKS IHRITGVQGS GAVLIFTDEK
VRNEACLEYV NQILTTGYIP NLFTREEMDD VITELDERLH EDNPKATPTH EELYEYYRNQ
VQMNLHLVLC FSPCGNNFRR RFTNYPGILA GCVIDWIDEW PQEALLSTYH ELNAQLNLNA
VRMESGVEKL NEAQKSIDEL RAVLAQKETE LTEASEKAEQ VLILVTEQAH VAEQVRNRVQ
QVKERCENIV LCINADRLAT QEQLSEAIPS LVEAEEALNT LRPHDISMLR KLQKPPYLIM
RVMDCVLLMF YARLEPVRPD HDRGTFQSSW NEALRMIHNP NFLSLLLNYP KHQMNEELID
LLEPYINSSD YNMPTARKVC GNVAGLLSWT LCMIRYFWVS RTVIPLQDNL ASLEQKLVKA
KAALQSTEVS LMEKTVILAK VQLEYEDALL KKMRIQEEAN VCYNRMCTAH KLIEGLSKEL
ARWTEQSMQL KTQLHELGGD CIQLAAFLTY SGAFNQQYRN RLMSSWQLEV VRQNLPHRPK
LDVISLFVDP ATITSFNDRS FPQHLEDTLN YGQPLLIEDA PEDLDPMIAC VVDYSGSVNG
KIKTVKLGDK ETTILPGFKL YIATHMANPN FPPELISHLT LIDFSITPKG LEDQLLARVI
SMEREKLEKS RLELISSVAV QKRQISQLEE NLLHRLASCE GSLVDDIDLI KMLQETKNTA
QVVAKQLAQT AETEVEIECA REEYRPVAVR GSILFFLISD LSTVNIMYQH GLSQFIKLFD
ESLVYSEKST TVQHRIHKII QFMTIAIWRF IVRSLFKRDR IIFTLMLAIR IWRQAGLIRH
EELDIFIKAG SACTLSECPP KPGRWIPDIS WINLKALSKL PIFSGIMNHV TQHERQWRHW
FEKDAPEEVP IPGPYETQMK PFTRLILIRC WCLDRMVSQA KRFISYALGP IFAEDVLLQP
EKLYQQADPG TPIINFLSMG SDPTQLIEQL AHKKHVNLKV VSMGQGQEIH AKQAIQAAQI
DGSWVLLQNC HLCVDYLNEL YVTIIDSVAK SAGSGKIFNR LVSDLSTSTM ENSGGSGSGT
LTGPASHSTT TTQPTSNATS TSQDTFRLWM TTEEHERFPV NLLQISIKFS NEPPEGIKAS
LRRTYADVTQ DSLEACIGGE WKVMLYTMAF LHCTLQERRK YGPSGWSIPY EFTQSDFNAS
IQFIQNHIDF VEFTKRNVKN SGIDWKCIRY MIAEIQYGGR ITDYFDLRLL NTFTKVFFQE
AMFTPEFELA TNYRVPRLSS VAQYEQYIQS LPSRDSPEAF HLHANADIDY STRASTYIIN
CIQAMEPKDG NLVSMGEMQI EGRESSLDEP DSRESVIIQV SNELLAKLPD PIAPQKLRDR
LELIGPLQPM TIFLRQEVDR MNHVLTTVST TLNELLXRRS GGHESIIART LKPEQLKNNG
NCSNVSDSFQ ECICQKLML
//