ID A0A2C6KSZ6_9APIC Unreviewed; 1438 AA.
AC A0A2C6KSZ6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Cytoplasmic dynein 2 heavy chain {ECO:0000313|EMBL:PHJ19465.1};
DE Flags: Fragment;
GN ORFNames=CSUI_006711 {ECO:0000313|EMBL:PHJ19465.1};
OS Cystoisospora suis.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Cystoisospora.
OX NCBI_TaxID=483139 {ECO:0000313|EMBL:PHJ19465.1, ECO:0000313|Proteomes:UP000221165};
RN [1] {ECO:0000313|EMBL:PHJ19465.1, ECO:0000313|Proteomes:UP000221165}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wien I {ECO:0000313|EMBL:PHJ19465.1,
RC ECO:0000313|Proteomes:UP000221165};
RX PubMed=28161402; DOI=10.1016/j.ijpara.2016.11.007;
RA Palmieri N., Shrestha A., Ruttkowski B., Beck T., Vogl C., Tomley F.,
RA Blake D.P., Joachim A.;
RT "The genome of the protozoan parasite Cystoisospora suis and a reverse
RT vaccinology approach to identify vaccine candidates.";
RL Int. J. Parasitol. 47:189-202(2017).
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:PHJ19465.1}.
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DR EMBL; MIGC01003433; PHJ19465.1; -; Genomic_DNA.
DR VEuPathDB; ToxoDB:CSUI_006711; -.
DR OrthoDB; 275566at2759; -.
DR Proteomes; UP000221165; Unassembled WGS sequence.
DR GO; GO:0030286; C:dynein complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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; 1.10.8.710; -; 1.
DR Gene3D; 1.20.58.1120; -; 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; 3.
DR InterPro; IPR035699; AAA_6.
DR InterPro; IPR011704; ATPase_dyneun-rel_AAA.
DR InterPro; IPR026983; DHC_fam.
DR InterPro; IPR043157; Dynein_AAA1S.
DR InterPro; IPR042228; Dynein_linker_3.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10676:SF352; CYTOPLASMIC DYNEIN 2 HEAVY CHAIN 1; 1.
DR PANTHER; PTHR10676; DYNEIN HEAVY CHAIN FAMILY PROTEIN; 1.
DR Pfam; PF07728; AAA_5; 1.
DR Pfam; PF12774; AAA_6; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000221165}.
FT DOMAIN 335..454
FT /note="Dynein heavy chain hydrolytic ATP-binding dynein
FT motor region"
FT /evidence="ECO:0000259|Pfam:PF12774"
FT DOMAIN 495..598
FT /note="Dynein heavy chain hydrolytic ATP-binding dynein
FT motor region"
FT /evidence="ECO:0000259|Pfam:PF12774"
FT DOMAIN 733..871
FT /note="ATPase dynein-related AAA"
FT /evidence="ECO:0000259|Pfam:PF07728"
FT REGION 279..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1438
FT /evidence="ECO:0000313|EMBL:PHJ19465.1"
SQ SEQUENCE 1438 AA; 158448 MW; E9360C5B50421D77 CRC64;
MFPRFYFLSD DEVVEVLSLF AACSHPVRMS GEFLPRLHHR LWRKMFQGVQ RVILGDHDNI
VPNPQASFIV LGGIEEEVVL VDVGLDGPQG VTGEGGSAET CLASLDVTLK DKLKELTETS
IRALEKGSEQ ADEDRLLRDT PSQIGSLVFS VDLTKRTEEA ICSGTLRDLK QSLILKLRKL
TNFLRHHRAE SLTGSFSLSA CSPPAASTVS VSGFTSSSQP SQSTKTPLEV SRTRFHVMFL
TEQMKIVEEL ISESCGTLED WSWFKQLKFE RSLAVTLGPR QEGGGVGTEK PDQRATSTPR
TLQFSQSHTN STEERRPPLR GVQYVARMAH CTQVYGFEYQ GAVPERVVYT PLTAKCYLSL
LNGLELGLGG NPYGPAGTGK TETVKALGAA LARHVLVFNC EEGIDFRSMG RLIVGLGACG
AWGCFDEFNR VLGEQLSAIS QFIFLFQKAV QTKRAPTLRA EGNAEEKDIW EELVRQAIGS
KGDNKQRKVS FGLRSLDEKA ALFVTLNPAV GTYAGGRSEL PVNLKHLFRP VLMAKPDVRI
IAEVFLLSEG FTDFKTLARK LACVFDEAAN LLPPQPHYDW GLRSVKTTLE VCADLFRCES
MSPSILHNSD VTQASTNLGV HPLEPPSRTG GRLPHSHCGG IRFELTCMRR AIETTTVGRL
VPGDADQFRR LLDATFLEIA EQGERQHQAP ATGHDVSMED VQRALVETGR LYEPEQGEKV
LQLHACMQQR MGTIVLGPPG SGKTTIWRTL FHALRQSQGP LSQLRCVVVH PKAMPRRQLM
GYREALTGEW KDGVLSRLAQ ELEKDESGNV WVVFDGDIDP EWAENLNSVL DDNHVFTLPT
GRRFYLNSQR VKFIFETHQL TFASPATTSR CAAIFVPFQT NVKLLLHPPL LSYRENSSET
PVLELDNDAL QALLRDVLKA LNYPPSLGSS CTDACSAAPS PVLTSIRRIF STAFTQMDWH
SRKTQDDCCL PVEPRQGETP LKKKLSRLEG MQLLRVCLLH ALQPYLYQGP STSLVTALLP
PETRGEYPAA DYFNLLGMPQ ENVTASPAEQ AENQADLSHT SGRTYISETL QSEAGCAKIP
FIPVASSLKA AWALKPLLES GERCIVVVGN RGCGKEAVVR HLSTSCYGSF PGNRQILCSS
ALIQATSGTN YGSSSTAFVR YACTPHTTVN DIVSTVRQYC TVAETSEGRT YRPAKPGKLL
LYIKNIDAPV PDKYGVSEVI EWVRQVGCTS TFIDPDLKIC RLEQIQIVAS VAADVAGKTR
GKELSIPTRL SACLPFVYIG EPSTTELEAI CNRLLQRHLV NAQEDTHQRE KFMATCFRLG
SFLKDLREAI NRDRVDKGLT VCQVTCRDVV ECAKAICQHA VATVDQLQRV CLDEVSLQIV
AGLGRSRAAQ QALGELVQSV AGKHEITLSA PELGEFFSTR LPGGGERRGH VFALAPFL
//