ID A0A1I8CA66_9BILA Unreviewed; 1390 AA.
AC A0A1I8CA66;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Myosin motor domain-containing protein {ECO:0000313|WBParaSite:RSKR_0000235800.1};
OS Rhabditophanes sp. KR3021.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Alloionematidae;
OC Rhabditophanes.
OX NCBI_TaxID=114890 {ECO:0000313|Proteomes:UP000095286, ECO:0000313|WBParaSite:RSKR_0000235800.1};
RN [1] {ECO:0000313|WBParaSite:RSKR_0000235800.1}
RP IDENTIFICATION.
RC STRAIN=KR3021 {ECO:0000313|WBParaSite:RSKR_0000235800.1};
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {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; RSKR_0000235800.1; RSKR_0000235800.1; RSKR_0000235800.
DR Proteomes; UP000095286; Unplaced.
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:0005096; F:GTPase activator activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000146; F:microfilament motor activity; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd00029; C1; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 3.30.60.20; -; 2.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR Gene3D; 4.10.270.10; Myosin, subunit A; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR046987; Myo9.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR46184:SF5; HEAVY CHAIN, UNCONVENTIONAL MYOSIN; 1.
DR PANTHER; PTHR46184; UNCONVENTIONAL MYOSIN-IXB-LIKE PROTEIN; 1.
DR Pfam; PF00130; C1_1; 2.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00109; C1; 2.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 2.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
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}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 1..414
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 714..765
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 961..1010
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1026..1216
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 486..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 637..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1303..1331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..553
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1316..1331
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 24..31
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1390 AA; 158693 MW; 623330F7A528840C CRC64;
XAIADITYHN MLRVKESQCV VISGESGSGK TESTNFLLHH LTTLSQKGST TGTSIEQTLL
SAGPVLEAFG NAVTIQNNNS SRFGKFIKVN YRENGMISGA NVEIYLLEKS RIISQALGER
NYHVFYYLLE GCTPEERVKC HLLNIEDYHY LNQNDPFTCE SINAKAEFNR LRHSMEAVGF
TPATQHKIWS VLSGVLLLGN VRFIKRSGYH SDENAYIENE DTLAKITELL DLKDKQLLQA
LTMRRTMLRN ETLITRYTIE EAINTRHAMA KCLYNALFHW IVLKMNQALL KKEATLGKKG
FYIGILDIFG FEDIGGKLNS FEQLCINYAN EHLQAYFNQH IFEFEQEEYL KENISWTNIE
YTDNTECVHL FQAKPYGILR LIDEESNINN GTNLSMLEKL NTFLKNNDYY EIPHKKEDAF
IKAWRAARER KNFLKIRAGI VEFQAACRSY LVKVHILEKH HAATVIQSNW RRFAQEKRYH
EMRKVVYNGN PPPNKSHDKK NGKKNGKLKF EIGSVIKKID LPTFNLNDPS SLAQFADSHS
SSSEGSSDVF TDSENEVSDV DDDNGSGTTF YLNQCEDFVL DEKEEDDLDL ECTFVLEDTK
LKLIEEEPSE TVHFIRRQSI ATTSSTAKLK TLRRAASTES DQLQRLEPQN SGKDRTKSRK
MNFIRAKKHL KALLTRKSDN STIVFSDEES GDAEVGLPLE KVKSLSTKTN IKIRHSFKLS
RLHKSEVCAR CHKVMSGLLV QACKCANCKL SFHKECSANA AEIDCIFPGS DLIAKPPCTI
LSSFEGKVVP SPRTSLSPIT GFSVTPANHG TFNLTKTKAQ TDPSHLVIQS LDDLRMFSAY
IFKKQYGLDQ NKKRETMIDA VFKQSLKEFH MELIGYEAVL ADEGNVLKYH NLITTFDGLL
IKVSNRENIT FPTTLGVNAF RGFLNDFIQE QDKRKTVSKK GGIFKSVRKK RRKSDITIHN
GHRFRPELVH VPTYCELCNQ FMWHSEKIFI CELCRLSCHK KCHLKVKYMC SKFNKNGGTA
TTFFGASLTY LMDASETVPP ILNALLINIE VRALFVEGIY RKTGSLTTVR ATRKEVEACD
GPEHLNLDDV PIHVVTTLIK AFFRELCEPV ITYELYENFI NVSEVTDYME RARCLSVMIE
LLPKCNKVVL DRLMYHLARV AYQESVNRMT ASNLALIFAP CIMRRQQVVQ AQEQLLDVHK
QAVCVQTLIE EKLRQYKATL TQIVEIEHAT EKVSENLRRI DEHRRLSETN QKMNLERYEN
KDGIQVKSKS TPNMEAARQL FVEQLDFLDK EKEKLIQEFP TMGAPVASSE DLSSTEEHSP
SPHELSREEY AIDFDNPPVY SKLNEAVKNK PKRCGIRVPS KYLKLMPGYV KETIHEDATP
TNGPANIFIN
//
