ID A0A0P5ZFF5_9CRUS Unreviewed; 2198 AA.
AC A0A0P5ZFF5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Putative Myosin-IXa {ECO:0000313|EMBL:KZS08653.1};
DE SubName: Full=Unconventional myosin-IXb {ECO:0000313|EMBL:JAM59334.1};
GN ORFNames=APZ42_027332 {ECO:0000313|EMBL:KZS08653.1};
OS Daphnia magna.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX NCBI_TaxID=35525 {ECO:0000313|EMBL:JAM59334.1};
RN [1] {ECO:0000313|EMBL:JAM59334.1}
RP NUCLEOTIDE SEQUENCE.
RA Gilbert D., Podicheti R., Orsini L., Colbourne J., Pfrender M.;
RT "Daphnia magna gene sets from two clonal populations assembled and
RT annotated with EvidentialGene.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:JAM59334.1}
RP NUCLEOTIDE SEQUENCE.
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KZS08653.1, ECO:0000313|Proteomes:UP000076858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xinb3 {ECO:0000313|EMBL:KZS08653.1,
RC ECO:0000313|Proteomes:UP000076858};
RC TISSUE=Complete organism {ECO:0000313|EMBL:KZS08653.1};
RA Gilbert D.G., Choi J.-H., Mockaitis K., Colbourne J., Pfrender M.;
RT "EvidentialGene: Evidence-directed Construction of Genes on Genomes.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|ARBA:ARBA00008314,
CC ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR EMBL; GDIP01044381; JAM59334.1; -; Transcribed_RNA.
DR EMBL; LRGB01002190; KZS08653.1; -; Genomic_DNA.
DR STRING; 35525.A0A0P5ZFF5; -.
DR Proteomes; UP000076858; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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:UniProtKB-KW.
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; cd20818; C1_Myosin-IX; 1.
DR CDD; cd01385; MYSc_Myo9; 1.
DR CDD; cd01779; RA_Myosin-IX; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.190; -; 2.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 3.30.60.20; -; 2.
DR Gene3D; 6.20.240.20; -; 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; 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; IPR036023; MYSc_Myo9.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR000159; RA_dom.
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; PF00612; IQ; 3.
DR Pfam; PF00063; Myosin_head; 2.
DR Pfam; PF00788; RA; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00109; C1; 2.
DR SMART; SM00015; IQ; 4.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00314; RA; 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; 2.
DR PROSITE; PS50096; IQ; 3.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS50200; RA; 1.
DR PROSITE; PS50238; RHOGAP; 1.
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}; GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW 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}; Reference proteome {ECO:0000313|Proteomes:UP000076858};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 5..144
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 173..973
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1428..1479
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1703..1754
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1796..1999
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 737..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 855..877
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1069..1102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1212..1253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1353..1402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1489..1536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1658..1694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1759..1788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2065..2084
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2110..2198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1214..1243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1517..1536
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1676..1694
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2065..2082
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 266..273
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 2198 AA; 245406 MW; E51DC0BE64D545AE CRC64;
MEPESRYIVQ VFVGALSPEF EALSIEALKG TTADEMVCCI VDKLQLPLPV ESYELAEVVG
NAIGQECKER RLASQELPVA LMLLWPKVSS PAQETASALA ALAAHRKLLQ RSVSRTSETR
PIERADADES QQSEYRFYLR EKLNDTLWSE ALNADPQVIR DYFYRFLYQP RDREYPDLCQ
LPDLNEETLM DNLRARFQAG HIYTYVGSIL IAVNPFKFYP IYNPKYVKLY QNRRLGELPP
HIFAVADAAY NAMMRDRKPQ CIVISGESGS GKTESTNFLL HHLTALSQKG SQGCGVEQTI
LSAGPVLEAF GNAKTSHNNN SSRFGKFIQV NYRENGQVHG ALVQKYLLEK TRICFQAKNE
RNYHVFYHLL VGSSAQEKQA LHLLPPEAYR YLNQSDYHNL DEGDECYELS RLKQSMEFVG
FCTETQRRIF AVLSAVLHIG NLEFQPKKST YNHDESVTVK NTAVVATIAQ LLRVKEEILH
QALISKRARA SGETLVINYR MPEAIAARDA MAKCLYGSLF DWIVMQLNHA LLAKKDADKM
QRAYSIGVLD IFGFEDFGHM NSFEQFCINY ANEHLQYYFN QHVFKYEQEE YKREGIHWVN
IQFVDNTGCL QLYESKPNGL LCILDDQCNF PGATNETLLQ KFNSVNKDNE YYEVPQKREA
AFIVRHYAGK VKYQSNEFRE KNLDLMKADI VAVLKSSQYA FVRELVGGDP VAVFRWAILR
AFIRAYFAFI ESGKRHRETH ASGPDSLTGK GKIGDSGRKN RVSKARSRPS KNWRNLETVK
TLAGRLGHSS SSLNSSVIAS VSSSHERLTI TPSGSTTVTI SSASSHQSIR GESLLVVHKN
VKKAQTVGAQ FQHSLQSLMV ALNTANPFFV RCIKSNRLKG PNQFDEEIVL RQLRYTGMLE
TVRIRQAGFN VRLTFEEFIH HYRILLPRGL LSSQSDVHDF LCRMNLNPEH YQIGHQKIFL
RESEKAKLDY RLHQAILASI VTIQRWFRTC LERRNFLSLR RAVVRIQSYV RMINAQRHVM
NLRVRHMAAT FIQKVWRGYR VRHWYTNLRC SVVSFQCRAR GNLARRRFEQ MKQQGDAHSG
KSTDEAFLSK GSSQEELDKE TKDLIEQLSS EESSGIQEDS ESELIYAELA SGILSCALNF
PLQSMDEKRD DLKSKKGKPS IVTAAANVAG VAGSVGHSPR IGSIEELLRG SGESGRTEKS
SALHKAKKHL KTLMGGGAKR EKSDSLRQMA VQGSEDRDSD SESTLVSASR STSTLNSASD
LEYDMRYARE REARREERRR IIAERLAIRS RANSISDESH SPTCPNPVLC RRYSRDIEAA
SSSIYGYGHS HGHLHQSHCW TYSHAVTSHL PIARRGSKDG GRSVSVDGSW RGSRDSLRER
AVGTAAGMTA SPLARRQDRD SSQASVAVSV TSSNSSSTAT VRSSLSQVHK LTRMSKLAKN
EACSLCSKTM SSFFTHGYKC TSCHLVFHAK CVQQGMTSSQ ALPPTVLECA RPSASPTHPD
PDPVQKGRKG SRETVDSSAG VIPSAGNESS KWNLTGTSEF TDSTQEVVNG GQQLHRLDEF
IGRKIQNLVD DTRGDADRVF LSALRELRGS LISAYGVASC HGGEEENPAI RLTYRDLIAN
FSKIVESVSR DDTKFPKTLV VNAFRGYLNE FVVQQRTDDK ENRAKGGKRR KERWKKPTTD
KNQRGRETKR AKAQDDGLLR YMGHEFTTLN SVITIPTACE VCSSFTWLKE KGLVCQSCKF
TCHKKCYTRI TTACTASAAT PSAGAGSSGA SSMSATISMS GLPNPSTESP GSLFGVTLDK
LVASSGAASG SQQRLPPIIE RLISTIELVG LYTEGLYRKS GVSSRVQQLK KLLEEECASS
KEGAASIVDL QEQPIHVLTA VLKAFLRELP QPLLTYERYD DFLRAADIVD TKERISSLMA
LVQELPPHHF DLLERLVFHL TRVALNEKSN RMGPNALSIV FAPCILRTSK IQQAQDSLSN
VSKQTSVVET ILTEQLRRVT ETLADIDSLD SVCLAYVARL GTLRSSKMFP SSSGVGTWVL
PQSDPSTPDG AAAVAKNQHQ RIFPTVSAPA SSSSSSLSSL SARDHVTEER LIQQHLEELR
EEKAALAATL PSLARTPSDD DLLSTDGDLD DQDSPIGGSV DDLPASSQSR SDSRPKDYEE
EEDDLEFIDA SYPKRASLPF VSPLPLRSKA AQRQLSVD
//