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Database: UniProt
Entry: A0A183NWW3_9TREM
LinkDB: A0A183NWW3_9TREM
Original site: A0A183NWW3_9TREM 
ID   A0A183NWW3_9TREM        Unreviewed;      1893 AA.
AC   A0A183NWW3;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Paramyosin {ECO:0000256|ARBA:ARBA00018623};
GN   ORFNames=SMTD_LOCUS6599 {ECO:0000313|EMBL:VDP34700.1};
OS   Schistosoma mattheei.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=31246 {ECO:0000313|Proteomes:UP000050791, ECO:0000313|WBParaSite:SMTD_0000659801-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:SMTD_0000659801-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDP34700.1, ECO:0000313|Proteomes:UP000269396}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Denwood {ECO:0000313|EMBL:VDP34700.1}, and Denwood, Zambia
RC   {ECO:0000313|Proteomes:UP000269396};
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril
CC       {ECO:0000256|ARBA:ARBA00004657}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. {ECO:0000256|ARBA:ARBA00008314,
CC       ECO:0000256|PROSITE-ProRule:PRU00782}.
CC   -!- SIMILARITY: Belongs to the paramyosin family.
CC       {ECO:0000256|ARBA:ARBA00008447}.
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DR   EMBL; UZAL01027681; VDP34700.1; -; Genomic_DNA.
DR   STRING; 31246.A0A183NWW3; -.
DR   WBParaSite; SMTD_0000659801-mRNA-1; SMTD_0000659801-mRNA-1; SMTD_0000659801.
DR   Proteomes; UP000050791; Unplaced.
DR   Proteomes; UP000269396; Unassembled WGS sequence.
DR   GO; GO:0030016; C:myofibril; IEA:UniProtKB-SubCell.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR   GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR   CDD; cd01377; MYSc_class_II; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.10.287.1490; -; 1.
DR   Gene3D; 1.20.5.340; -; 3.
DR   Gene3D; 1.20.5.4820; -; 1.
DR   Gene3D; 1.20.58.530; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   Gene3D; 2.30.30.360; Myosin S1 fragment, N-terminal; 1.
DR   Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR004009; Myosin_N.
DR   InterPro; IPR008989; Myosin_S1_N.
DR   InterPro; IPR002928; Myosin_tail.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR   PANTHER; PTHR45615:SF40; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR   Pfam; PF00063; Myosin_head; 1.
DR   Pfam; PF02736; Myosin_N; 1.
DR   Pfam; PF01576; Myosin_tail_1; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF90257; Myosin rod fragments; 2.
DR   SUPFAM; SSF50084; Myosin S1 fragment, N-terminal domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF57997; Tropomyosin; 1.
DR   PROSITE; PS50096; IQ; 1.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW   ProRule:PRU00782};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00782}; Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW   ProRule:PRU00782};
KW   Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW   ProRule:PRU00782};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00782}; Reference proteome {ECO:0000313|Proteomes:UP000269396}.
FT   DOMAIN          1..701
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   REGION          579..601
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          795..815
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1828..1893
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1829..1893
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         70..77
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1893 AA;  218726 MW;  1062E77B22C2F9B1 CRC64;
     MGDNKRVSYS PMNAELLRDE KEPLREADLS SKDMVWVPHE REAFVAAIKL QEQGENVVVQ
     LVESGKKCTG ESGSGKTENT KKVIQYLACV ATSAKHQKTS AKNVMSKFNT KDFSIGELEA
     QLLKANPILE AFGNAKTIKN DNSSRFGKFI RINFDTSGFI AGANIETYLL EKARVIRQAV
     DERSFHIFYQ LLASATPAMQ QQLLLNHASA YRFLSNGMIE LPGIDEQQFF RETTEAMDIM
     GINNEDQNAI FRVISAVLHL GNLEFRQERS SDQATLPDHS VAEKVSHLLG IPLNEMVKAF
     LKPRIKVGKD LVSKAQTKTQ VEFAVEAISK SIYERLFLWL VARINKTLDK TRRPGXXXXX
     XXXXXXXXXX XXXXXXXFVG ILDIAGFEIF QVNSFEQLCI NYTNEKLQQL FNHTMFILEQ
     DEYTREGIPW EFIDFGLDLQ PTIDLIERPM GIFALLDEEC FFPKGTDKSF VEKLIKSQDK
     HPKLCKTEFR SNADFGVIHY AGRVEYNSNQ WLMKNMDPLN DNVVALLQAS NDPFVQAMWK
     DAEIVSMSAT TTTDTAFGSA RSVRRGMFRT VSQLYKDSLI RLMTVLKNTS PNFVRCIIPN
     HEKKPGRIDG PLVLEQLRCN GVLEGIRICR RGFPSRILFQ EFRQRYEILT PNVIPKGFMD
     GRKAVTEMLK ALDLSQDVYC IGHSKIFFKV GVLAQLEEDR DIHLTNSIIK FQAYARGYLA
     RRAKEQRIQN IQASKIIQRN CDAYLKLRNW PWWRLFTKVR PLLTVTRQED LVAVKEEELR
     KRSYEKLSNE KVQLNAELQQ EHDSNQNLQT ERDRLREKLQ TLEEDYMELE NRDSEEKSKL
     HNLEAEQKRL LEQISDLSDQ LELEEQQRQK LQVEKTSIEQ KVSQLNDGYV SIEDKYNKLV
     KDKKQLTDRI DLLTSQLAEE EERSKQLTKL KSKYESNLNE LQDKLVREQK SRQDIEVAKR
     RLETEASERL DQASESSRIV EELRATVAKL EAEVAQLQNR LDEEIVAKAV AQKSVREYKS
     HIQELKEDLE AERMARDKAD EAKRDLTEEV EAMRLELIDS GTNSEAQTQA LRKYESDLSN
     LRHQLEAQSN AHEATIQDMR KSHAATLETL NDQIEQLKKS KVSLERSKVQ QDSTTDALQK
     QIQSLKQDKT EIDKRRRQVE QQLNESLVKM QETEMQRNDL ESRLTKALNE IEGLNNAMEE
     IETKLGKVSR SETSAQSELN HLRARLEEET QAKLSLQLQL RQVEDERETV KDSLDAEEQA
     KTALEKHIIA LTTQMQDAKK KVEEDTHYLE TLEDARKKLQ RELDDTRNRN EELVSQVEKL
     EKSRKKLQSE LEDMNHVMAS QRSDQANNER RIKKLESTHA ETVNQLNSFQ AQKDAFYQEM
     LEKDTKLFTQ KNEMEKLKEQ LEESERQRSL LARELEELGS HGDDAGKSLV GLEQTNYRLN
     ERLKETQQQI EELEDEISTF TMEKQRAEVQ MNAVRTQLER ELASRDDLLE EQRRQSLKRI
     RELETELEEE QRERASHLNV RKKLETDLAD ISQRFELANR QKEEAVKQLK KYQGVTGGIQ
     RELEDAARAR DQAIDSAREL DKKYRMLDAD KARLQEDLGV SERTCRNLKS DLNEALEELS
     IANNAKTLAL EEKKRLEARI TALEDQLEEI QSAMDATEER HKRVYCQMEQ AQTDLSVEKN
     NFLRSECQRV SLEKQVKELR DRLVEAEKEG GRRGKAQIAT LEARLTTLDE QLEAEKLEKL
     NANKNFRRAE KKCKDLILQN DDLRRCAEAL KESFEKAQSS CKQNKREIAG LEEENARINA
     RCRRLQRDLE EVMEAKRTIE RDLQNLRKLS RSTTRPNRQL PAVLSTLSPD VTVDEHNSVN
     ELDSMTSDFG SSGSVATHNN NNNNASTPSA NEN
//
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