ID A0A0V1P056_9BILA Unreviewed; 1159 AA.
AC A0A0V1P056;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Unconventional myosin-If {ECO:0000313|EMBL:KRZ89679.1};
GN Name=MYO1F {ECO:0000313|EMBL:KRZ89679.1};
GN ORFNames=T08_2136 {ECO:0000313|EMBL:KRZ89679.1};
OS Trichinella sp. T8.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ89679.1, ECO:0000313|Proteomes:UP000054924};
RN [1] {ECO:0000313|EMBL:KRZ89679.1, ECO:0000313|Proteomes:UP000054924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS272 {ECO:0000313|EMBL:KRZ89679.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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:KRZ89679.1}.
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DR EMBL; JYDM01000066; KRZ89679.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1P056; -.
DR Proteomes; UP000054924; Unassembled WGS sequence.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.4820; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 2.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR010926; Myosin_TH1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR13140:SF729; HEAVY CHAIN, UNCONVENTIONAL MYOSIN; 1.
DR PANTHER; PTHR13140; MYOSIN; 1.
DR Pfam; PF00063; Myosin_head; 2.
DR Pfam; PF06017; Myosin_TH1; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS51757; TH1; 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};
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:UP000054924};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 27..675
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 713..905
FT /note="TH1"
FT /evidence="ECO:0000259|PROSITE:PS51757"
FT DOMAIN 1015..1076
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 551..573
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 909..935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 967..986
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 997..1019
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 120..127
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1159 AA; 133087 MW; F26D6226E67DAA10 CRC64;
MLSSIQRTKQ SAMDKHLHWQ WHGIDQVGVH DMVLLATVDE DAIVQNLRKR YMNSIMFTYI
GPVLLSVNPF TQMPYFSEKQ MDQYQGANQY ENPPHIYALT DDMYRNMLID SENHCVIISG
ESGSGKTVSA KYIMNYVAHI SGGGPEVERI KQIILETNAV LEAFGNAKTI RNDNSSRFTR
VVHQNLDERN FHIFYQLCAG CDDQLKRNLG ITEPSYFNYL NQSGTCEIAD VNDGQLYKVT
MKAMEIVGID NSTKIEILKI VSAILHIGNI KFKEVNNYAD IEDPADLEYP AYLLNVDPDA
IRKKLISRRM ESKWGAENDV LDVKLNVDQA IYTRDALAKA LYHRLFDHLV QLVNNALTFD
ANDCRKIGIL DIYGFEIFEK NGFEQFCINF VNEKLQQVFI ELTLKAEQEE YKHEGVQWIP
VDYFNNKIVC DLIEANKPPG IFSILNDVCA QTHGQSGGDD HFLQKMNSSV GNHQHYRRAS
GRFLIVHYAG NVEYDVEGFC EKNRDTLFDD LIQLMQSSGN ELVLSLFPEK VPKKCVKTRT
TTFGSKIRKQ ANELLTSLMG SVPHYIRCIK PNEQKRPFTF DDARVKHQVK YLGLKENIRV
RRAGFAYRRP YDKFVKRYAI LIDDLQNNSP RNDMAKTKTI LKSMNFDTDD AFCMGQTKIF
IKNPETVFQL EEKREEKYAH FAKIIQRAWR RCRMNKKTND MAQRASDILY GHKQRRRASI
NRKFFGDYIG LDQKPELKIL VGKREKIWFA DSVCKYDRRF KACSRYLLLT SKAVLIVQHI
HGKTKRHSNQ SDYVVKRHVE LEKIVSVMLS PNQDDFILLT VLNEHATLVE CVFKTEFLMK
LCKCYQDRTG KTMPIKFSEI FEYTVKKSNW PSCQTKFVKF EIDAQCLNKA HLKSHGNTLH
VAVGAGLKNT TRPNAKPIAP ITPHTGSYST QCSSTSVHNS NQSDCFSPAS VGSAGYGSVK
QVNSYRRKAP PLPHAHSQQP SNSRTELKAQ LERITNNSIS KANGAPKNKP PIPPKPRPKL
RMLYSYEGQD DDELCFHSND IIEIIQEDSS GWWQGHLRGK HAEFNHYVEY LIEKMVVILK
ISMNFIPHDE IVQRFSNNML KSKESSAEKS AYFTKDQLHH FTLIASTQHS LNKALNSSTT
VSTSPRLAGV MEFRRRIIV
//
