ID A0A1R2C3Q0_9CILI Unreviewed; 4114 AA.
AC A0A1R2C3Q0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OMJ83653.1};
GN ORFNames=SteCoe_15380 {ECO:0000313|EMBL:OMJ83653.1};
OS Stentor coeruleus.
OC Eukaryota; Sar; Alveolata; Ciliophora; Postciliodesmatophora;
OC Heterotrichea; Heterotrichida; Stentoridae; Stentor.
OX NCBI_TaxID=5963 {ECO:0000313|EMBL:OMJ83653.1, ECO:0000313|Proteomes:UP000187209};
RN [1] {ECO:0000313|EMBL:OMJ83653.1, ECO:0000313|Proteomes:UP000187209}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WM001 {ECO:0000313|EMBL:OMJ83653.1};
RA Slabodnick M., Ruby J.G., Reiff S.B., Swart E.C., Gosai S., Prabakaran S.,
RA Witkowska E., Larue G.E., Fisher S., Freeman R.M., Gunawardena J., Chu W.,
RA Stover N.A., Gregory B.D., Nowacki M., Derisi J., Roy S.W., Marshall W.F.,
RA Sood P.;
RT "The macronuclear genome of Stentor coeruleus: a giant cell with tiny
RT introns.";
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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:OMJ83653.1}.
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DR EMBL; MPUH01000296; OMJ83653.1; -; Genomic_DNA.
DR OrthoDB; 166463at2759; -.
DR Proteomes; UP000187209; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0030286; C:dynein complex; 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: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; 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; IPR042228; Dynein_linker_3.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR45703; DYNEIN HEAVY CHAIN; 1.
DR PANTHER; PTHR45703:SF34; DYNEIN HEAVY CHAIN, CYTOPLASMIC; 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; 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 SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 4.
DR SUPFAM; SSF57997; Tropomyosin; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
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:UP000187209}.
FT DOMAIN 933..1335
FT /note="Dynein heavy chain linker"
FT /evidence="ECO:0000259|Pfam:PF08393"
FT DOMAIN 1467..1793
FT /note="Dynein heavy chain hydrolytic ATP-binding dynein
FT motor region"
FT /evidence="ECO:0000259|Pfam:PF12774"
FT DOMAIN 1944..2054
FT /note="Dynein heavy chain AAA 5 extension"
FT /evidence="ECO:0000259|Pfam:PF17852"
FT DOMAIN 2275..2347
FT /note="Dynein heavy chain 3 AAA+ lid"
FT /evidence="ECO:0000259|Pfam:PF17857"
FT DOMAIN 2417..2672
FT /note="Dynein heavy chain AAA module D4"
FT /evidence="ECO:0000259|Pfam:PF12780"
FT DOMAIN 2688..3019
FT /note="Dynein heavy chain coiled coil stalk"
FT /evidence="ECO:0000259|Pfam:PF12777"
FT DOMAIN 3048..3276
FT /note="Dynein heavy chain ATP-binding dynein motor region"
FT /evidence="ECO:0000259|Pfam:PF12781"
FT DOMAIN 3518..3632
FT /note="Dynein heavy chain region D6 P-loop"
FT /evidence="ECO:0000259|Pfam:PF03028"
FT DOMAIN 3664..3799
FT /note="Dynein heavy chain AAA lid"
FT /evidence="ECO:0000259|Pfam:PF18198"
FT DOMAIN 3805..4110
FT /note="Dynein heavy chain C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18199"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2911..2973
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 3878..3905
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 4114 AA; 473066 MW; DEDB7ED4CB525431 CRC64;
MKRNQSAKTT GFRIAPRVSP NLQAGDSNKA QELRNRLIER GLSSKPLPSV KKPKVSQSSQ
KLQTVPTFAS LPDTKLLLRP SSSRISITGF TSIGALRPSS AVKNLKIPTS LTTRTANHPS
RPTTARTNIS TLQRIATRTL IDVSDTTRAM NLIDKLTNRP KTARQEAQET PIPKDIIEEI
YTDYEYQETK IDEFIRRIRE KRIEENEFVY LLRDNESQET DYYVVEAEEA RNDPNREFYT
LSAKGLSMFV SGSPVEFIRY QDFLSERKQF FSLQNVSFFK RFRAWKTVKM WQRNVNRIRR
SHRKKKLEEK LYSVDSQYSK VLLNHRYMCL DMEKMRFIDI PGHLEQMPLN DFLERQYQRI
EEVRKYIEDA NKTLRTNVRQ GVTNIMNQLR EEIVMDIAEK KNYGKLNLQM LPPVRRICAL
YEKMGFPENM SYDQRSDLRK ECSRYIRFSY LVDFIALESL QNMYLMSVRE LLLKIYEQIV
DLEDLNDNKV DKSIIIQAEG KKRNRVPLFK VDLKLNTNTE LVGTKIPIVY EFNSRKSSPD
DFHPNIHLSF DGENIHIPSF IIKDLEKCWL KLAPTRQYFI ESMETLINQG LACLKSLQRW
SRHPDIQDFV LALEDWDDKV ADKWDIAENL ELDILSWIEE APLYRKIHKK LTSLVYKAFT
HSEEKFILFE YPIQSYYKNL EINYNLLEKE NLLSKVDSFD WTFSMFKTQR SKVEKAPKFV
DSGLFRIDCQ EVRNFLILNS RDSLKKSYEI LMRIIREKVD FSRQWSSKSV KMLGSKIFTV
EDFVGQKLSL SEVNEKIAEV KRTIDLLGHM FNLGLRADIG LTPDDTDSYQ ITSGLMTTLN
GYIINIESTE AKNMVLYKKK LKLMVPDFLQ DVQAVNLKIQ EEKYLRLESD TDKTIIELKS
LLDKCSSFTD YSKSLSRFQE VLGEPLNTFH EVHALQEQVD IRYKMWTGFK EYEKIHKRIL
YTPLKLLDPY QATLQAEEYH KIVRRSESVI NSSTVLDRLK YMVEETLSIM PVISALRAPF
LDTHWKMLRD LLGQNFEINE NLTLMSLSKY KIKENTEEIQ AISIQATQEH ELKSQLNAIT
SIWEEMEIPI QQYKEKDLWI LGDIEPLVTN LEESLAKISL IAGNRYVTPL RDEVVTWRNH
LNTIQDVLDE WTTLQKTWLY FNAIFASQDI KRRLATETQI YESVDKFYRT FMKKLYLNNN
ALRVMVLEGK LLDYLKKHNN SLEIVQRNLS QYLEDKRIIF PRFYFISDEE LLKVLAQAGN
PLSLQPYIAK CFENIYRLEF GEDIKAADVI GMVSSEGESV SFGGRVLKAR GNVEEWLGNV
QNAMVDTLMK AMKYCKEDSE KAVFKTWVLS VYPAQIIATV GQINWCIETD VVLGSIHDAP
NAFPDWITHS AKNLLSLIDL VRSPTTELKR KLIVAMITTS VHNRDILANM LELQVETNSD
FAWQKQLRYY WDSDLCIIKQ INYSTQYAYE YLGCTSRLVV TPLTEKCWIT ITSALNVKLG
ACPSGPAGTG KTESTKDLAK ALGQFCIVFN CSEQITFKMT GRLFAGLIQQ GAWSCLDEFN
RIDIEVLSVI AQQLQTIKHA QVLNVKDFMF EGRKIALKSG FSVFVTMNPG YAGRTELPDN
LKVLFRPVAM MIPDYAMIAE IMLMAEGFQE GTRLSKKIVQ LYKLASEQLS IQHHYDFGLR
ALKSVLLTAG DIRRKLEETD EEIMLIQAMN ESNLPKLIAK DALLFKALVR DLFPGVIIKP
SDNSDLHEKI QKIIETQNYL CPENFEKKIF ELNDTVQVRF GSMLLGPAMS GKTTIYTILS
KIKGIKVHCL NPKSITIGEL YGDMNPLTQD WKDGLASSIF REITNGSNPE LNWVVFDGPV
DSLWIESMNT VLDDNMMLCL PNGERIKLKP TMRILFEVMD LSKASPATVS RCGMVFIPNE
SLTWQMLMNT WLKKYESKEH RDALNTLFNS ILPPLFRVYD YESDMVPTSE IHKVCSLCKF
LSILLEPLPK VKHITAIFAF AVIWTIGAFL DGSKQERFSN TIRHLFSQSS LFPIPDMVYD
YYLDKSCAFQ SWKDLIPSIV LSKEMSLAQV LIPTPITATY TYLLNKLYSQ NVSTLLIGGS
GVGKSSLITM HVNDQLAKQE IELVRANFSA RTTSEKVQQY IEAKLERKAA GVFTGASNRK
LLMFLDDVSM PAKDAYDTQA PIELLRQLMD TEGFYDRKKG FFKKICNFVL NCASGISGLQ
DLSPRFLRHF HVFYLPEPSH AIMSTIFSAI LNNHFDKSFA ESVRKSITVI IGGTIEIYEK
VVMKLKPTPS KFHYKYNLRD VSKVIQGSTF STPATIPNVD KLTKLWLHEC CRVFYDRLTT
SQDRLWFYTN LTSTGFKHFK VNFLQDDWLE AHPLIFSNLY TIDNLNPSYE EIIDKRRIKK
LIEDRLEDFN SKNKQKMNLE IFDEALSHIL HISRGIFPAR GHMMLIGVGG SGKQSLAMLG
SFLLSYIIYT IQLIKNYNID NFHDDLKKMM EISAVNNKNL AFVFSDQHMI HDSFLEDINA
LINSGEVTDL FTDEEMETII NNLRPDVVDK LKLADTKENI YNEFLNRVKD NLHVILCTSP
VGNVLRNRCR MFPALVNCST LDWFENWPEQ ALLSVASAKL TDFSSSICKT LSSLASSMHL
SSETTSSKFA EEMRRVAYVT PKIFFDFLEL FSLLVRKSNT NILGRKKKLS NGLEKLHETR
KIIAESQIEL QQMIPDLESE KKKAENYYIE VQKETKSAVE LQETVEKETE FIEIQAQECK
VRADDAEKDL AEAMPILEAA IKAVQALEKN KKDIIEFKKY LKPPEAVKMV MEAVCILLNE
RSDWTNAISV LGQMDFLQRL INYQRESVTN NIFKKLRAIV SRPEFQPETV AQSSEAARSL
CIWCIAMYKF TEAYQLVKPK REKVSAMQIK LKSDMEKLQS KQDELRAVED KVRLLKDECA
LTEAKVASLE KKIKITMDRV KRAELLLELL AEEGVKWRET LDKLEDSLKY IEGEAMINAG
CICYMGVYSD LYREGLRNMW YDMVKNLNVL ISEDYSIINS LGKPIQIRAW QIAGLPKDSL
SIENSIIVVN SIKWAMIIDP QEQARRWLKN TEKTNNLITA KASKTGTKEA KDLIRALEAG
LSQGKPVLLE DVGESIDSSL QNVICRKFYK KDDGRVMIKL ADLEISFDDN FRLFLICKYS
NPNFLPDIFG NLNVINFTVT SIGLEDQLLV EVVRLENPKL EKERDDIVVS MAYDQKTLED
LQNSILDMIA DSQGYILDNL ALIAALQKSK STSKDITRRV AATAQVEKSV NASRDTFRNI
AVRGTVLYFV IASIPGINPM YQYSLAFYTK LYCNAIQNTT ETKDRVQVII SNITKTIYNV
ICRGLFEKDK KLLAFLFAAA IERNANSIST EAWNYFIRGG GLLNKKNPKK NPLQGKLTEI
QWDLICKLDK LLPFDGLSDD ITFNKPQWSD YIFGNILQSE IPNKYNLIDT FSRILLIKVF
RPEKVMYTID EYAKKILGSY FAQAPISNIE ELFDESDKKT PIVFILSQGT DPVENIMKIT
KERGMGDKFL TISLGQGQGN KAQDAFEKSK SGGFWLLLQN CHLSKSWLPT LETLIDNLQD
DTGGHRDFRV ILTSMPSSYF PVSILQNSLK ITTEAPSGLK SNLMRVYSEV ASGGFGDMAR
PEVWKKMVFA VSFFHALVME RRKYGPLGFN IRYEFNESDF YTSIKLMKLL VEENEDIPWE
GIQYIIGNIN YGGRVTDNND RVCLMATFNK CCNSDMLEEN YNYTENEVYK IPNTQDYLEY
IGNLPNNDPP EIFGLNINAQ ITLETQTSES IIQCLIQTQP KAISSEASNS DKTIHAMCKS
ISISLPETMD FKAAHSDLLV QDQNGLIPSL STFLFQEIEK FNKLLETMRK TLKELRNAIK
GKNIMTDDLF SMYNCLLCST VPDIWAKVAY PSLKPLASWI TDLAARVKFI FDWLKYGNQN
CFWLSGFFFP QSFLTAVLQT HSRKYSLPID CLVFTFEVTP FMFSEFKKTV NDGVFIYGLY
LEGARWDSEE MILIDAQEKE IYFTMPVIQF LPTHNYVAKE GDYLCPVYKT GKRAGILSST
GLSTNFVVYV DLPSEEIPDK WTLLGTALLC QINI
//
