ID A0A016SIN8_9BILA Unreviewed; 3082 AA.
AC A0A016SIN8;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EYB90262.1};
GN Name=Acey_s0222.g2635 {ECO:0000313|EMBL:EYB90262.1};
GN ORFNames=Y032_0222g2635 {ECO:0000313|EMBL:EYB90262.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYB90262.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000256|ARBA:ARBA00001702};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000256|ARBA:ARBA00001702};
CC -!- SIMILARITY: Belongs to the dynein heavy chain family.
CC {ECO:0000256|ARBA:ARBA00008887}.
CC -!- SIMILARITY: Belongs to the tubulin family.
CC {ECO:0000256|ARBA:ARBA00009636}.
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:EYB90262.1}.
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DR EMBL; JARK01001558; EYB90262.1; -; Genomic_DNA.
DR STRING; 53326.A0A016SIN8; -.
DR Proteomes; UP000024635; 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: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:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0008569; F:minus-end-directed microtubule motor activity; IEA:InterPro.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR CDD; cd00009; AAA; 2.
DR CDD; cd02186; alpha_tubulin; 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; 1.20.920.20; -; 2.
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; 5.
DR Gene3D; 1.10.8.720; Region D6 of dynein motor; 1.
DR Gene3D; 3.30.1330.20; Tubulin/FtsZ, C-terminal domain; 1.
DR Gene3D; 3.40.50.1440; Tubulin/FtsZ, GTPase domain; 1.
DR InterPro; IPR003593; AAA+_ATPase.
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; IPR002452; Alpha_tubulin.
DR InterPro; IPR026983; DHC_fam.
DR InterPro; IPR043157; Dynein_AAA1S.
DR InterPro; IPR041466; Dynein_AAA5_ext.
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 InterPro; IPR008280; Tub_FtsZ_C.
DR InterPro; IPR000217; Tubulin.
DR InterPro; IPR037103; Tubulin/FtsZ-like_C.
DR InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
DR InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
DR InterPro; IPR017975; Tubulin_CS.
DR InterPro; IPR003008; Tubulin_FtsZ_GTPase.
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; PF18198; AAA_lid_11; 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 Pfam; PF00091; Tubulin; 1.
DR Pfam; PF03953; Tubulin_C; 1.
DR PRINTS; PR01162; ALPHATUBULIN.
DR PRINTS; PR01161; TUBULIN.
DR SMART; SM00382; AAA; 3.
DR SMART; SM00864; Tubulin; 1.
DR SMART; SM00865; Tubulin_C; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 4.
DR SUPFAM; SSF55307; Tubulin C-terminal domain-like; 1.
DR SUPFAM; SSF52490; Tubulin nucleotide-binding domain-like; 1.
DR PROSITE; PS00227; TUBULIN; 1.
PE 3: Inferred from homology;
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 GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
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:UP000024635}.
FT DOMAIN 67..264
FT /note="Tubulin/FtsZ GTPase"
FT /evidence="ECO:0000259|SMART:SM00864"
FT DOMAIN 266..411
FT /note="Tubulin/FtsZ 2-layer sandwich"
FT /evidence="ECO:0000259|SMART:SM00865"
FT DOMAIN 709..860
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 1071..1221
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 1414..1580
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT COILED 1686..1762
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1894..1949
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 3082 AA; 346718 MW; AB5EB2F4D2F57E18 CRC64;
MCPVGPFSSI NSAQQVSNKR EVISIHIGQA GVQIGNACWE LYCLEHGIQP DGQMPSDKSL
GGCDDSFSTF FSETGSGRHV PRAVMIDLEP TVIDEIRTGT YRSLFHPEQL ITGKEDAANN
YARGHYTIGK EIIDLTLDRI RRLADNCTGL QGFLVFHSFG GGTGSGFTSL LMERLSVDYG
KKAKLEFSVY PAPQVSTAVV EPYNSILTTH TTLEHSDCSF MVDNEAIYDI CRRNLDIERP
SYTNLNRLIG QIVSSITASL RFDGALNVDL TEFQTNLVPY PRIHFPLATF SPVISAEKAY
HEQLSVAEIT NMCFEPHNQM VKCDPRHGKY MAVCLLFRGD VVPKDVNAAI ATIKTKRSIQ
FVDWCPTGFK VGINYQPPTV VPGGDLAKVP RAVCMLSNTT AIAEAWARLD HKFDLMYAKR
AFVHWYVGEG MEEGEFSEAR EDLAALEKDY EEAMGRILVG LCQVGAWGCF DEFNRLEERM
LSAVSQQIQT IQEAVRAGGE MSVDLVGKRL NVNPNIGIFI TMNPGYSGRS NLPDNLKQLF
RSLAMTQPDR QLIAQVMLFS QGFRTAETLA NKIVPLFILC KEQLSAQCHY DFGLRALKYV
LVSAGNVKRD KLAKVGAAAL EDVAEQQMLI QSVCETLVPK LVSEDIALLF SLLSDVFPSV
HYTPNQMLEL RQHIAQVCDE SMLCHADVAG ELGAAWIEKV LQLYQITNLN HGLMLVGASG
SGKTTAWKVL LKALERYEKV EGVAHVIDAK AMSKDALYGV MDPNTREWTD GLFTSVIRKI
IDNVRGESEK RQWIIFDGDV DPEWVENLNS VLDDNKLLTL PNGERLGIPP NVRIIFEVAD
LKYATLATVS RCGMVWFSEE VVTTEMMFEH YLSRLRNISI ESEAVIAEDA APTRAVTLQR
QAAAALQSHF SPDGLVPLAL NYAIANLDHV MVPTQQRLLS SFFAMMNYSV RSVITHDNNQ
GDFPLSPDQV ETYVTRSMLT NMIWAFSGDG KWKCRQQMSD FIRNSTTLTL PPNQQAPLID
FEVQLSGEWQ PWLSRVPAME IEAHRVAAAD LVVPTIDTVR HEMLLSAWLS EHKPLVLCGP
PGSGKTMTLL AALRSQQDMD VVNVNFSSST TPELLMKTFD HYCEYRRTPN GIVLAPVQLS
RWLVIFCDEI NLPAPDKYGT QRVISFLRQL VELNGFYRGS DHSWVTLERI QFVGACNPPT
DPGRHPMTLR FLRHVPVVYV DYPGQTSLIQ IYGTFNRAML KTVPAVRGLA DPLTNAMVDV
YLASQEHFTQ DDQPHYVYSP RELTRWVRGI SEAIAPLDGI TAEQLVRLWA HEALRLFQDR
LVTEEERNWT DELVDSTAEK YFGGACSVKE ALKRPLLYSC WLSKNYVPVT REELKDYVSA
RLKGFYEEEL DVQLVLFDQM LDHVLRIDRI YRQPQGHLLL IGTAGAGKTT LSRFVAWLNG
LSVFQLKVHS KYTAADFDED MRTVLRRAGC RNEKMCFIMD ESNMLDTGFL ERLNTLLANG
EVPGLFEGDE HTTLMTQIKE GAQRQGLMLD SHDELYKWFT MQVMRNLHVV FTMNPSGSGL
RERASTSPAL FNRCVLNWFG DWADTALYQV GSELTTTLDM DRTDYEPPFS LPIVCDLIPT
PPTYRHAVIN TLVHVHKSVQ KLNEQEQKRG HRVMVVTPRH FLDLIKHFMN LFHEKRRDLE
EEKVHLNIGL NKIRETEEQV KELQKSLTLK SRELEEKKTA ANLKLKEMLA DQQKAEDEKR
LSEQLQKELA EQLTQIAAKK TEVQKDLSQV EPAVEEAQQA VKGIRKNQLV EVRSMASPPV
MVKLALEAIC ILLGENVGTD WKAIRGVMVK DDFMPRILAF DTDSITTDIL KQMDKYVNNP
DWDFDKVNRA SQACGPMVKW AKAQLLYSGM LHKVEPLRNE LKRLESDAKK KTTEGNEVKA
RIAQLEQSIA AYKEEYAQLI GQAESIKMDL ATVQEKVGRS TELLSSLRSE RDRWSGGCDG
FAQQMDTLVG DALLSGAFLA YAGYFDQQLR DVLFHRWIDH VQGAGVKFRP DLARIEYLST
VDDRLQWQKN ALPVDDLCSE NAIMLHRFNR YPLIIDPSGQ AAEYIMKQFA GRNIQKTSFL
DDSFRKNLES ALRFGNSLLV QDVESYDPIL NPVLNREVKR TGGRVLITIG DQDIDLSPAF
QIFLITRDAS VEFTPDVCSR VTFVNFTVTS SSLASQCLNQ VLRSERPDVD KKRNDLLKLQ
GEFAVRLRQL EKALLAALNE SKGKILDDNS VIGTLEKLKN EASEIAKKSA ETDKVMAEVE
AVSGQYQRLA AACSQIYHTL QQLNEVHFLY QYSLDFLLDI FTCVLKSPEL AQTQDHMQRL
NIITSNLFQT VYKRVSRGML HADKALLALL LMRISLRSVG GEPSYDAQWD LLLGRSELFS
SKTAHQSPPT ALPFLSSQQM GSLTKAQKLP GFEKILDTMC GQSSQIKQWL ASDNPESAVP
VLWDDPEQKL TTIGRAMNEL VVVHCLRPDR LMASAHRLVA AAFGDGFMQQ DKVIDLHDII
DNEVSSSDPV LLCSAIGYDA SGKIEDLGVQ TGRQVTSIAI GSAEGFSQAD AALTAASKSG
RWVLLKNVHL APQWLGNMEK RLHTLKPHAN FRLFLTAEIH PKLPASVLRA SRLVVFEPAT
GLKANLLRSL SALPGPRLAK APAERSRLYL LVCWLHALVQ ERLRYTPLGW ANAYEFSDAD
LRVACDTLDA AVDAVAQGRA NVAPEKLPWT TLRTLLSQCI YGGKIDNHFD QVLLDCILER
LFTAKSFEPE HVLVSKFDGD TPLHTPDATQ RDQLLAWVEG IKSQQLPAWL GLPNNAEKVL
LTLRGETMLK NLLKVSDDEL AFSGDGEKEA KPQWMAQLAE LAQQWLKLLP KDINKMKRTV
DNIKDPLFRF FEREINLGAQ LLRDIRHDLE EILAVCRAER KQSNETRALA SALQKGVVPT
NWQRYTVPRD VTVMDWVIDF NERVKQLIRI AASDNLKREE VWLGGTFSPE AYVTATRQQV
AQANTWSLEQ LHLHVTIGRT DRLDVVRLTD HINSLADILS FNGKTPKKQA LWKLPLPVAW
NSCGFLLVLF LDFALLGSPE YG
//
