ID A0A1I8A592_9BILA Unreviewed; 1324 AA.
AC A0A1I8A592;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Myosin motor domain-containing protein {ECO:0000313|WBParaSite:L893_g32820.t1};
OS Steinernema glaseri.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Steinernematidae;
OC Steinernema.
OX NCBI_TaxID=37863 {ECO:0000313|Proteomes:UP000095287, ECO:0000313|WBParaSite:L893_g32820.t1};
RN [1] {ECO:0000313|WBParaSite:L893_g32820.t1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR WBParaSite; L893_g32820.t1; L893_g32820.t1; L893_g32820.
DR Proteomes; UP000095287; Unplaced.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0032982; C:myosin filament; IEA:UniProtKB-KW.
DR GO; GO:0030017; C:sarcomere; IEA:UniProt.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:InterPro.
DR Gene3D; 1.20.5.340; -; 4.
DR Gene3D; 1.20.5.370; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 6.20.240.20; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 4.10.270.10; Myosin, subunit A; 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; IPR002928; Myosin_tail.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014751; XRCC4-like_C.
DR PANTHER; PTHR45615:SF40; MYOSIN HEAVY CHAIN, MUSCLE-RELATED; 1.
DR PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF01576; Myosin_tail_1; 2.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF90257; Myosin rod fragments; 6.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175};
KW Muscle protein {ECO:0000256|ARBA:ARBA00023179};
KW Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Thick filament {ECO:0000256|ARBA:ARBA00022433}.
FT DOMAIN 1..298
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 173..195
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 410..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 543..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 729..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1162..1324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..563
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 731..748
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1162..1178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1183..1256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1288..1305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1324 AA; 150833 MW; 97DF456CFF62E8C0 CRC64;
MFVLEQEEYQ REGIKWEFID FGLDLQACIE LIEKPLGIIS MLDEECIVPK ATDMTLAQKL
NDQHLGKHPN FQKPRPPKGK QADAHLAIVH YAGTVRYNVK AWLEKNKDPL NDTAVSVLKG
NTGMQLLSDI WDDYKTQEDV AAMQKIKGKS VGGKKKGKSA SFMTVSMLYR ESLNNLMHML
HQTHPHFIRC IIPNEQKKCG VIEANLVLNQ LTCNGVLEGI RICRKGFPNR LPYMDFKQRY
TCLAADAAKA GKDPRDSGVR VLDVLVKNGS LKPEEFQCGS TKVFFKAGVL AHLEELRDEA
LSIIMTKFQS ACRAYLSQCD YKRRLDQKVG LVIIQRNVRS WCTLRTWQWF RLYGRVKPLI
KGNKKXXXXT CAAGQQEGRG VRGSGEEVPR LGGGALPGWS STLRLAGGAP TRSCRAPATP
TPIGAGARXX XXEKKCRDLE EALSQGGRQL SDSQAALQRA SAERQQLQLQ LEQERELLAE
GDERSAKLLA QKAEAEKQLA ELNEQLNYQE DQNSALSKAR KRTEADCEAL KKNVGELEQT
VKKQEAEKLS KDHQMRSLQD EIAAQDEEDQ NSALSKARKR TEADCEALKK NVGELEQTVK
KQEAEKLSKD HQMRSLQDEI AAQDEVIGKL NKEKKNQEEV NRRLLEDIQA EEDKVNHLNK
IKNKLEHSLD EMEDNLERER RSRQDLEKQR RKVEGELKVA QENIDDLTRQ KMEMDSVIKK
SDPLYXXXXE MEDNLERERR SRQDLEKQRR KVEGELKVAQ ENIDDLTRQK MEMDSVIKKK
EAETLALASR LEDEQSLVSK LQRQIKELLA RVQELEEELD AERQARSKAE KMRNELQHEL
EELSDRLDEA GGATQTQMEQ NKKREAELAK LRRDLEETAL SQENAMATLK KKHGDAIAEL
SDQMDAVQKL RAKVEKEKTI LQRDVEDLQN SLDGECKQRQ NIERLAKQLE TQLTETQLKS
DEQARQIQEL LSHKNRAHAE NGEMLRQLED AESQVAVLGR LKSQLAAQLE EARRQVDQET
RDRQSVASQL ANYQLECQQL REALEEEQEG KTELQRLVSK ANAETQQWRT RYEGEGMSRA
EELEEARRKL QAKVQEMQET VETAHQKIGS LEKSRQRLQQ ELEDAQVDAD RANSLANALD
KKQKGFDRVV EEWKRKCDAL SQELEASQQE TRNAGTENFR LRNALDEAAE REEATRRENK
VLAQELKDLT DQLGEGGKSV HELQKSRRRL ELEKEELQQA LDDAEGALEA EESKLMRAQV
EXXXXRSRRA SIVSSRSGSG RAEGLDGPAG RGRQERTRTA KKPPAPRARE GGVAAGVGRR
RGRS
//
