ID A0A183NS25_9TREM Unreviewed; 3201 AA.
AC A0A183NS25;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN ORFNames=SMTD_LOCUS4911 {ECO:0000313|EMBL:VDP25886.1};
OS Schistosoma mattheei.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=31246 {ECO:0000313|WBParaSite:SMTD_0000491001-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SMTD_0000491001-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDP25886.1, ECO:0000313|Proteomes:UP000269396}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Denwood {ECO:0000313|EMBL:VDP25886.1}, and Denwood, Zambia
RC {ECO:0000313|Proteomes:UP000269396};
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; UZAL01026772; VDP25886.1; -; Genomic_DNA.
DR STRING; 31246.A0A183NS25; -.
DR WBParaSite; SMTD_0000491001-mRNA-1; SMTD_0000491001-mRNA-1; SMTD_0000491001.
DR Proteomes; UP000269396; Unassembled WGS sequence.
DR GO; GO:0005930; C:axoneme; IEA:UniProt.
DR GO; GO:0030286; C:dynein complex; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; 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: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; 1.20.920.20; -; 1.
DR Gene3D; 1.20.920.30; -; 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 InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR035699; AAA_6.
DR InterPro; IPR035706; AAA_9.
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; IPR024743; Dynein_HC_stalk.
DR InterPro; IPR024317; Dynein_heavy_chain_D4_dom.
DR InterPro; IPR013602; Dynein_heavy_linker.
DR InterPro; IPR042228; Dynein_linker_3.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR46532:SF13; DYNEIN CYTOPLASMIC 1 HEAVY CHAIN 1; 1.
DR PANTHER; PTHR46532; MALE FERTILITY FACTOR KL5; 1.
DR Pfam; PF12774; AAA_6; 1.
DR Pfam; PF12775; AAA_7; 1.
DR Pfam; PF12780; AAA_8; 2.
DR Pfam; PF12781; AAA_9; 1.
DR Pfam; PF17857; AAA_lid_1; 1.
DR Pfam; PF08393; DHC_N2; 1.
DR Pfam; PF17852; Dynein_AAA_lid; 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}; Membrane {ECO:0000256|SAM:Phobius};
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:UP000269396};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 3119..3138
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1043..1179
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 1688..1828
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 138..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2263..2297
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2490..2531
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 141..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3201 AA; 367011 MW; 800F95E8567CEB51 CRC64;
SAVSRTTGTK SARECRKRLV EDAALRVLEH FHQRTVDTLT KLIRNTLDNL RKCLTLPSIL
AYDSVNSDGS VQLYFSCHAQ LSKPSIILHP SLDDFQKALN TATHLIISVT RHISVWDLRL
RNPYGSKEHS EIEESFSSIE EVKKSSQTDS STHSGNELTR EITVSSGTNE LVTYTTDERF
SVADDEYENK GDENYFNKIS QNKEINKLRG MLTNAFSSIQ QSAKSSLRHF DQYKSLWEKS
KTEEFDKFMS NNPSVTDFEE IIQQFYEKDQ LISNEPDVCD CSPLAIYTNH LKDGLLAETR
NWRLEYGRLC SSKFKTQVES LFATIEKYEK ILSRPINDLD DIRILMNALK DLREMEANVD
LQLGPIEESY SLLAKHSIPV DKEETDKADT LRYEWEKLCK QMLEVQNQLV DVQPEFRNNL
LENITTFNEN CSTFYDDYDK VGPMVRGIPP REASDRLIIF QNRFDNLYRS YITYSAGEQL
FGLPITEHTR LDDIRKQLNL LQKLYLLYNS VLNKTAGYYD IPWSDVKIDV ISQELQDFEN
RCLKLPKALR EYPAYDDLRQ TLANFDQIIP LLELMTNPAM RERHWKGLAT LTGRSFNVDD
SEFTLRNILE APLLEHYDDV EDICISAIKE QDIERKLINL KSEWSAQEFE FVQFKHRGEL
LLRGDHTLEL ISLMEDSLMA LASLLSNRYN APFRKDIQNF ISRLSNSNEI IEQWLAVQNL
WIYLEAVFIG GDIARQLPQE AKRFANVDKS WCRIMQRAHE TTHVLTCCIG DEMLSHLLPH
LMEQLELCQK SLTGYLEKKR LLFPRFFFVS DPTLLEILGQ ASDPHTIQAH LLSVFDNIKS
VKFHEKQYET ILTCYSQEGE VLELEHPVKA EGHVEVWLNK LLKEAQFSLH QIIREGYKVA
IDDDVNILEF LATFPAQVGL LGIQFIWTRD STNALKEARH NKKIMQMTDH EFGRLLNLLI
QQTTHNLTQV ERTKLETLIT IHLHQKDIFS SLVKDRIKSP TDFDWLKQTR FYYLEDSDIA
SINHNLDVSC YITLAQAIGM SMGGSPAGPA GTGKTETVKD MGRCLGKYVI VSNCSDQMDF
RGLGRIFKGL AQSGSWGCFD EFNRIELPVL SVAAQQIAII LTCKKERKPQ FVFTDGEIIT
MNPQFGIFLT MNPGYAGRQE LPENLKINFR TVAMMVPDRQ IIIRVKLASC GFIENIISAQ
KFYTLYKLCE EQLSKQIHYD FGLRNILSVL RTLGAVKRAN PNDTEFETVM RVLRDMNLSK
LVGPDEPLFL SLLDDLFPGI SLDKGGYPDL EKAIKQNLAE SHLISHPPWF LKVIQLYETQ
RVRHGMMTLG PSGTGKSCCI QALMKSAFEE FHTLIIQKQA MTECFEPHRE MRMNPKAITA
SQMFGRLDVA TNDWTDGIFS TLWRRTLKAK KGEHIWLILD GPVDALWIEN LNSVLDDSKL
LTLANGDRIP MAPCCKIIFE VDNVDNASPA TVSRNGMVYI STTTLHWLPI LQGWLMSRGK
SEADQLLQLF TASFESVYQY ATRHLNFKMS VLEAFVIRQA CDILSGILPK PEEKDSPSAI
EYNIMPYKLS LKLCPHAIDI TFKYMERIYI FALMWSIGAF LEGDDRAKFE AYLRKHETVK
FDLPEISTES HSTIFDYLVN DLGEWIHWDT KVDEFLYPTD HTPEYSSLLV PNVDNVRTEF
LIDLISKQQK CVLLIGEQGT AKTVILNKYL SSQNPEFHIF KTLNFSSVTT PLLFQRAIES
FVDKRMGSTY GPPAGRKMTV FIDDISMPLI NEWGDQVTNE IVRQLIEMKG FYNLEKPGDF
TSIVDVQFLA AMIHPGSGRN DIPHRLKRHF CIFNCTLPSN TSIDKIFGAI AQGHYCPERG
FTDSAVTETV KLLVPLTRIL WQKIKNKMLP TPAKFHYIFN LRDLSRIWQG MIGTIPEVIN
NTERLMMLWR HECSRVLADR FVSADDHQWF HMTTKRLVKE ELGMEYMTAI EGDPSYFIES
FQQLSSRLEM FLHQYNESVR GARMNLVLFR DTLTQIVRIS RIIYMPRGNA LLVGVGGSGK
QSFTKLASYI AGYQTFQITL TRTPTDQSLI GIYEAFLEYL NNVLSSGIMS NLFTRDETDE
ILQDLIPFMK KEHPRLTPTN ENLNDYFLSR TRKNLHVVLC FSPVGEKFRR RSLKFPGLLS
GCTTNWFHRW PKEALISVAN HYLIDFPIVC KQQTKTALIN TMGIVHDGIA EACIEYFSRY
RRQTHVTPKS YLSFLCSYKS VYSQQHNHYA NLAQRMDGGL QKLVEAQESV AQLSKELAVK
EKDLDIANKE AEEVLRTVTV QQNAATEVRN KVQVVKDKAQ AIVDDIDREK VLAEAKLEAA
KPALQEAEDA LNTIKPGDIA TVRRLGKPPH LIMRIMDCVL LLFQRHLEPY QPDPERTCPK
PNWSESLKLM TNTGFLSMLM SFPKDTINGE TVELLEPYLN MEDYTLEVGK KVCGNVAGLL
SWTKAMAYFY TINKDVLPMK DNLIKQEARL AKAMLDLNDA QAILDEKELE LAKVQAVYEE
ALRKKNTLIE DAELCRRKMT AASKLIGSLG DEQTRWTEQS QAFKENVECL VGDVLVATGF
LSYCGPFNQE FRQMLYQSWQ RILRQYNIPG STIVNLISML TRPTQLGEWK IQGLPSDELS
VQNGIIVDQA SRYPLLIDPQ GQGKSWIKSR EQKHDLIITT LWNKYFRQHL EDALSTGRPL
LIEDIGEDLD PAMDNVLEKN FIKQGSIHKV KIADKEVDVL PCFRLYITTK LPNPSFTPEI
SARTSIIDFT VTMKGLEEQL LGRVILSERH ELEAQRVQLM LDVQSNKTKI KELEDNLLSR
LASVQGSLVD DVDLIDVLSS TKVTASDVSR KLEIASETEI QITSAREEYR PIATRGSVLY
FLIVEMSLIN CMYQTSLRQF LALFDQSLSR SEKSPITTKR ITNVIDYMTY DVWKYIIRGL
YEVDKSTFSL LLALKIDMQA GRVRHEEFQC FIKGGASLDL NTVKPKPFKW IADMTWLNLV
ALSSLNQFAS ILDQVVSNER GWRQWTDKTS PELENIPDGY QSNLDTFRRL LLIRAWCPDR
IMNQANIYVG DCLGRKFAEG FVLDLDGVYH ESTPLWPIVG LLSTGSDPTT QIELLAKKYR
VSLFIFITIC LVVIIIVIRH TEHTSVCSAV LYNCNDHHYL QDVKMISCKG IVELSTFYHE
PVVAFENRGS NVIIILRPKT P
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