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Conserved domains on  [gi|281362442|ref|NP_001014650|]
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jaguar, isoform H [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MYSc_Myo6 cd01382
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ...
71-754 0e+00

class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the minus-end of actin filaments, in contrast to most other myosins which moves towards the plus-end of actin filaments. It is thought that myosin VI, unlike plus-end directed myosins, does not use a pure lever arm mechanism, but instead steps with a mechanism analogous to the kinesin neck-linker uncoupling model. It has been implicated in a myriad of functions including: the transport of cytoplasmic organelles, maintenance of normal Golgi morphology, endocytosis, secretion, cell migration, border cell migration during development, and in cancer metastasis playing roles in deafness and retinal development among others. While how this is accomplished is largely unknown there are several interacting proteins that have been identified such as disabled homolog 2 (DAB2), GIPC1, synapse-associated protein 97 (SAP97; also known as DLG1) and optineurin, which have been found to target myosin VI to different cellular compartments. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the minus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


:

Pssm-ID: 276833  Cd Length: 649  Bit Score: 1279.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   71 ATFLDNLKTRYYKDKIYTYVANILIAVNPYREIKELYAPDTIKKYNGRSLGELPPHVFAIADKAIRDMRVYKLSQSIIVS 150
Cdd:cd01382     1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPKLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  151 GESGAGKTESTKYLLKYLCYSHDS-AGPIETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEVHYDAKCQVVGGYISHYL 229
Cdd:cd01382    81 GESGAGKTESTKYILRYLTESWGSgAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  230 LEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLslgkpddyrylsgctqyfanakteqlipgsqksknhqqkgpLKDPI 309
Cdd:cd01382   161 LEKSRICVQSKEERNYHIFYRLCAGAPEDLREKL-----------------------------------------LKDPL 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  310 IDDYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEIPDDVRGGCQVSEASEQSLTITSGLLGVDQTELRTA 389
Cdd:cd01382   200 LDDVGDFIRMDKAMKKIGLSDEEKLDIFRVVAAVLHLGNIEFEENGSDSGGGCNVKPKSEQSLEYAAELLGLDQDELRVS 279
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  390 LVSRVMQSKGGGFKGTVIMVPLKIYEASNARDALAKAIYSRLFDRIVGLINQSIPFQASNFYIGVLDIAGFEYFTVNSFE 469
Cdd:cd01382   280 LTTRVMQTTRGGAKGTVIKVPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFETSSYFIGVLDIAGFEYFEVNSFE 359
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  470 QFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITFTDNQDIIELIEAKSNGIFTLLDEESKLPKPSYSHFTAEVHK 549
Cdd:cd01382   360 QFCINYCNEKLQQFFNERILKEEQELYEKEGLGVKEVEYVDNQDCIDLIEAKLVGILDLLDEESKLPKPSDQHFTSAVHQ 439
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  550 SWANHYRLGLPRSSRLKAHRTLRDEEGFLVRHFAGAVCYNTEQFIEKNNDALHASLEGLVQECDNPLLQTLFPS-----G 624
Cdd:cd01382   440 KHKNHFRLSIPRKSKLKIHRNLRDDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESstnnnK 519
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  625 SSTSVRGKLNFISVGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQFEGSLALAQLKCSGTISVLELMEHGYPSRV 704
Cdd:cd01382   520 DSKQKAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRT 599
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|
gi 281362442  705 LFADLYSMYKSVLPPELVSLPARTFCEAMFQSLNLSAKDFKFGITKVFFR 754
Cdd:cd01382   600 SFHDLYNMYKKYLPPKLARLDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
CBD_MYO6-like cd21759
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, ...
765-913 1.74e-59

calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, which are actin-based motor molecules with ATPase activity, include unconventional myosins that serve in intracellular movements. Myosin-VI, also called unconventional myosin-6 (MYO6), is a reverse-direction motor protein that moves towards the minus-end of actin filaments. It is required for the structural integrity of the Golgi apparatus via the p53-dependent pro-survival pathway. Myosin-VI appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells. It modulates RNA polymerase II-dependent transcription. As part of the DISP (DOCK7-Induced Septin disPlacement) complex, Myosin-VI may regulate the association of septins with actin and thereby regulate the actin cytoskeleton. Myosin-VI is encoded by gene MYO6, the human homolog of the gene responsible for deafness in Snell's waltzer mice. It is mutated in autosomal dominant non-syndromic hearing loss. This family also includes Drosophila melanogaster unconventional myosin VI Jaguar (Jar; also called myosin heavy chain 95F (Mhc95F), or 95F MHC), which is a motor protein necessary for the morphogenesis of epithelial tissues during Drosophila development. Jar is required for basal protein targeting and correct spindle orientation in mitotic neuroblasts. It contributes to synaptic transmission and development at the Drosophila neuromuscular junction. Together with CLIP-190 (CAP-Gly domain-containing/cytoplasmic linker protein 190), Jar may coordinate the interaction between the actin and microtubule cytoskeleton. Jar may link endocytic vesicles to microtubules and possibly be involved in transport in the early embryo and in the dynamic process of dorsal closure; its function is believed to change during the life cycle. This model corresponds to the calmodulin (CaM) binding domain (CBD), which consists of three subdomains: a unique insert (Insert 2 or Ins2), an IQ motif, and a proximal tail domain (PTD, also known as lever arm extension or LAE).


:

Pssm-ID: 409646 [Multi-domain]  Cd Length: 149  Bit Score: 200.81  E-value: 1.74e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  765 MRSDPENMLAIVAKVKKWLIRSRWVKSALGALCVIKLRNRIIYRNKCVLIAQRIARGFLARKQHRPRYQGIGKINKIRTN 844
Cdd:cd21759     1 MKSDPENLKELVKKVKKWLIRSRWRKAQWCALSVIKLKNKILYRREALIKIQKTVRGYLARKKHRPRIKGLRKIRALEKQ 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281362442  845 TLKTIEIASGLKMGREEIISGVNDIYRQIDDAIKKIKMNPRITQREMDSMYTVVMANMNKLTVDLNTKL 913
Cdd:cd21759    81 LKEMEEIASQLKKDKDKWTKQVKELKKEIDALIKKIKTNDMITRKEIDKLYNALVKKVDKQLAELQKKL 149
Myosin-VI_CBD pfam16521
Myosin VI cargo binding domain; Myosin-VI_CBD is a C-terminal family that allows ...
1160-1246 9.14e-57

Myosin VI cargo binding domain; Myosin-VI_CBD is a C-terminal family that allows unconventional myosin-VI to recognize and select its binding cargoes. Several adaptor proteins have been reported to interact specifically with the CBD, thus defining the specific subcellular functions of myosin VI. The crystal structure determination of the myosin VI CBD/Dab2 (an endocytic adaptor protein Disabled-2 that is a cargo) complex shows that the Myosin-VI_CBD forms a cargo-induced dimer, suggesting that the motor undergoes monomer-to-dimer conversion that is dependent upon cargo binding. In the absence of cargo myosin VI exists as a stable monomer. This cargo binding-mediated monomer-to-dimer conversion mechanism adopted by myosin VI may be shared by other unconventional myosins, such as myosin VII and myosin X.


:

Pssm-ID: 465157  Cd Length: 90  Bit Score: 190.57  E-value: 9.14e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  1160 HRYFRIPFMRANAPDNT---KRGLWYAHFDGQWIARQMELHADKPPILLVAGTDDMQMCELSLEETGLTRKRGAEILEHE 1236
Cdd:pfam16521    1 QRYFRIPFVRPSDKKRDggrKKGWWYAHFDGQWIARQMELHPDKPPVLLVAGKDDMQMCELSLEETGLTRKRGAEILEEE 80
                           90
                   ....*....|
gi 281362442  1237 FNREWERNGG 1246
Cdd:pfam16521   81 FEEEWKKHGG 90
MyUb_Myo6 cd21958
myosin VI ubiquitin-binding domain (MyUb) found in unconventional myosin-VI and similar ...
1076-1116 9.82e-25

myosin VI ubiquitin-binding domain (MyUb) found in unconventional myosin-VI and similar proteins; Unconventional myosin VI, also called Myo6, or unconventional myosin-6, is a monomeric myosin, which moves towards the minus-end of actin filaments, in contrast to most other myosins which moves towards the plus-end of actin filaments. It is thought that myosin VI, unlike plus-end directed myosins, does not use a pure lever arm mechanism, but instead steps with a mechanism analogous to the kinesin neck-linker uncoupling model. It has been implicated in a myriad of functions including the transport of cytoplasmic organelles, maintenance of normal Golgi morphology, endocytosis, secretion, cell migration, border cell migration during development, cancer metastasis, deafness, and retinal development, among others. For example, the GIPC1 (GAIP interacting protein, C-terminus 1) adaptor protein mediates endocytosis by tethering PlexinD1, a transmembrane receptor that regulates neuronal and cardiovascular development and cargo protein of GIPC1, to myosin VI motor through a regulated oligomerization mechanism, forming a PlexinD1/GIPC/myosin VI complex. This model corresponds to the myosin VI ubiquitin-binding domain (MyUb) that binds to ubiquitin chains, especially those linked via K63, K11, and K29.


:

Pssm-ID: 439319 [Multi-domain]  Cd Length: 41  Bit Score: 97.44  E-value: 9.82e-25
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 281362442 1076 QKYDLSKWKYSELRDAINTSCDIELLEACRQEFHRRLKVYH 1116
Cdd:cd21958     1 KKYDLSKWKYAELRDTINTSCDIELLEACREEFHRRLKVYH 41
Myosin_N pfam02736
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ...
7-49 1.14e-07

Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the N-terminus of many but not all myosins. The function of this domain is unknown.


:

Pssm-ID: 460670  Cd Length: 45  Bit Score: 49.35  E-value: 1.14e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 281362442     7 LVWVRDAAEGYIQGRITEIGAKEFEVTPTDRKypKRTCHFDDI 49
Cdd:pfam02736    5 LVWVPDPKEGFVKGEIKEEEGDKVTVETEDGK--TVTVKKDDV 45
MYO6_MIU_linker super family cl46503
MIU-linker domain found in unconventional myosin-VI; Myosins are actin-based motor molecules ...
1002-1093 4.05e-07

MIU-linker domain found in unconventional myosin-VI; Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins function in intracellular movements. Myosin-VI, also called unconventional myosin-6 (MYO6), is a reverse-direction motor protein that moves towards the minus-end of actin filaments. It is required for the structural integrity of the Golgi apparatus via the p53-dependent pro-survival pathway. It appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells. It modulates RNA polymerase II-dependent transcription. As part of the DISP complex, Myosin-VI may regulate the association of septins with actin and thereby regulate the actin cytoskeleton. Myosin-VI is encoded by the MYO6 gene, the human homologue of the gene responsible for deafness in Snell's waltzer mice. It is mutated in autosomal dominant nonsyndromic hearing loss. This model corresponds to a conserved region of myosin-VI, which consist of three helices: MIU (Motif Interacting with Ubiquitin), a common linker helix (linker-alpha1) and an isoform-specific helix (linker-alpha2).


The actual alignment was detected with superfamily member cd22294:

Pssm-ID: 480843 [Multi-domain]  Cd Length: 69  Bit Score: 48.36  E-value: 4.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442 1002 LEQERRDHELALRLAnESNGQ--VEDSPPVIRngvndaspmgpnklisfsqvvsniasryLNKSENVRAQQQALGKQKYD 1079
Cdd:cd22294     5 LEQERRDRELAMRIA-QSEAEliSEETQPDLA----------------------------LRRSAGTQAVSAGGGKKKMT 55
                          90
                  ....*....|....
gi 281362442 1080 LSKWKYSELRDAIN 1093
Cdd:cd22294    56 MEEMAKEMSEDLSR 69
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
954-1020 2.00e-05

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


:

Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 45.29  E-value: 2.00e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281362442   954 RLKAEMETRRKAAEAQRLRQEEEdRRAALALQEQLEKEAKDDAKYRQQLEQERRDH-ELALRLANESN 1020
Cdd:pfam20492   34 ETAEELEEERRQAEEEAERLEQK-RQEAEEEKERLEESAEMEAEEKEQLEAELAEAqEEIARLEEEVE 100
 
Name Accession Description Interval E-value
MYSc_Myo6 cd01382
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ...
71-754 0e+00

class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the minus-end of actin filaments, in contrast to most other myosins which moves towards the plus-end of actin filaments. It is thought that myosin VI, unlike plus-end directed myosins, does not use a pure lever arm mechanism, but instead steps with a mechanism analogous to the kinesin neck-linker uncoupling model. It has been implicated in a myriad of functions including: the transport of cytoplasmic organelles, maintenance of normal Golgi morphology, endocytosis, secretion, cell migration, border cell migration during development, and in cancer metastasis playing roles in deafness and retinal development among others. While how this is accomplished is largely unknown there are several interacting proteins that have been identified such as disabled homolog 2 (DAB2), GIPC1, synapse-associated protein 97 (SAP97; also known as DLG1) and optineurin, which have been found to target myosin VI to different cellular compartments. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the minus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276833  Cd Length: 649  Bit Score: 1279.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   71 ATFLDNLKTRYYKDKIYTYVANILIAVNPYREIKELYAPDTIKKYNGRSLGELPPHVFAIADKAIRDMRVYKLSQSIIVS 150
Cdd:cd01382     1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPKLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  151 GESGAGKTESTKYLLKYLCYSHDS-AGPIETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEVHYDAKCQVVGGYISHYL 229
Cdd:cd01382    81 GESGAGKTESTKYILRYLTESWGSgAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  230 LEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLslgkpddyrylsgctqyfanakteqlipgsqksknhqqkgpLKDPI 309
Cdd:cd01382   161 LEKSRICVQSKEERNYHIFYRLCAGAPEDLREKL-----------------------------------------LKDPL 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  310 IDDYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEIPDDVRGGCQVSEASEQSLTITSGLLGVDQTELRTA 389
Cdd:cd01382   200 LDDVGDFIRMDKAMKKIGLSDEEKLDIFRVVAAVLHLGNIEFEENGSDSGGGCNVKPKSEQSLEYAAELLGLDQDELRVS 279
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  390 LVSRVMQSKGGGFKGTVIMVPLKIYEASNARDALAKAIYSRLFDRIVGLINQSIPFQASNFYIGVLDIAGFEYFTVNSFE 469
Cdd:cd01382   280 LTTRVMQTTRGGAKGTVIKVPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFETSSYFIGVLDIAGFEYFEVNSFE 359
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  470 QFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITFTDNQDIIELIEAKSNGIFTLLDEESKLPKPSYSHFTAEVHK 549
Cdd:cd01382   360 QFCINYCNEKLQQFFNERILKEEQELYEKEGLGVKEVEYVDNQDCIDLIEAKLVGILDLLDEESKLPKPSDQHFTSAVHQ 439
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  550 SWANHYRLGLPRSSRLKAHRTLRDEEGFLVRHFAGAVCYNTEQFIEKNNDALHASLEGLVQECDNPLLQTLFPS-----G 624
Cdd:cd01382   440 KHKNHFRLSIPRKSKLKIHRNLRDDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESstnnnK 519
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  625 SSTSVRGKLNFISVGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQFEGSLALAQLKCSGTISVLELMEHGYPSRV 704
Cdd:cd01382   520 DSKQKAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRT 599
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|
gi 281362442  705 LFADLYSMYKSVLPPELVSLPARTFCEAMFQSLNLSAKDFKFGITKVFFR 754
Cdd:cd01382   600 SFHDLYNMYKKYLPPKLARLDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
Myosin_head pfam00063
Myosin head (motor domain);
59-754 0e+00

Myosin head (motor domain);


Pssm-ID: 395017 [Multi-domain]  Cd Length: 674  Bit Score: 974.06  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442    59 HDDNCELMLLNEATFLDNLKTRYYKDKIYTYVANILIAVNPYREIKeLYAPDTIKKYNGRSLGELPPHVFAIADKAIRDM 138
Cdd:pfam00063    1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLP-IYSEDMIKAYRGKRRGELPPHIFAIADEAYRSM 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   139 RVYKLSQSIIVSGESGAGKTESTKYLLKYLCYSHDSA-----GPIETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEVH 213
Cdd:pfam00063   80 LQDKENQSILISGESGAGKTENTKKIMQYLASVSGSGsagnvGRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQ 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   214 YDAKCQVVGGYISHYLLEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSLGKPDDYRYLSGCTQYFAnakteqlipgs 293
Cdd:pfam00063  160 FDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQSGCYTI----------- 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   294 qksknhqqkgplkdPIIDDYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEIPDDVRGgcqVSEASEQsLT 373
Cdd:pfam00063  229 --------------DGIDDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQA---VPDDTEN-LQ 290
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   374 ITSGLLGVDQTELRTALVSRVMQSkgggfKGTVIMVPLKIYEASNARDALAKAIYSRLFDRIVGLINQSIPFQAS--NFY 451
Cdd:pfam00063  291 KAASLLGIDSTELEKALCKRRIKT-----GRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIekASF 365
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   452 IGVLDIAGFEYFTVNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITFTDNQDIIELIEAKSNGIFTLLDE 531
Cdd:pfam00063  366 IGVLDIYGFEIFEKNSFEQLCINYVNEKLQQFFNHHMFKLEQEEYVREGIEWTFIDFGDNQPCIDLIEKKPLGILSLLDE 445
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   532 ESKLPKPSYSHFTAEVHKSWANHYRLGLPRssrlkahrtLRDEEGFLVRHFAGAVCYNTEQFIEKNNDALHASLEGLVQE 611
Cdd:pfam00063  446 ECLFPKATDQTFLDKLYSTFSKHPHFQKPR---------LQGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKS 516
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   612 CDNPLLQTLFP------------SGSSTSVRGKL-NFISVGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQFEGS 678
Cdd:pfam00063  517 SSDPLLAELFPdyetaesaaaneSGKSTPKRTKKkRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNS 596
                          650       660       670       680       690       700       710
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281362442   679 LALAQLKCSGTISVLELMEHGYPSRVLFADLYSMYKSVLPPELVSL--PARTFCEAMFQSLNLSAKDFKFGITKVFFR 754
Cdd:pfam00063  597 LVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRYRILAPKTWPKWkgDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
MYSc smart00242
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...
58-766 0e+00

Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical interaction between myosin and actin. The core of the myosin structure is similar in fold to that of kinesin.


Pssm-ID: 214580 [Multi-domain]  Cd Length: 677  Bit Score: 932.34  E-value: 0e+00
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442     58 DHDDNCELMLLNEATFLDNLKTRYYKDKIYTYVANILIAVNPYREIkELYAPDTIKKYNGRSLGELPPHVFAIADKAIRD 137
Cdd:smart00242    7 GVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQL-PIYTDEVIKKYRGKSRGELPPHVFAIADNAYRN 85
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442    138 MRVYKLSQSIIVSGESGAGKTESTKYLLKYLCY---SHDSAGPIETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEVHY 214
Cdd:smart00242   86 MLNDKENQSIIISGESGAGKTENTKKIMQYLASvsgSNTEVGSVEDQILESNPILEAFGNAKTLRNNNSSRFGKFIEIHF 165
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442    215 DAKCQVVGGYISHYLLEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSLGKPDDYRYLSgctqyfanakteqlipgsq 294
Cdd:smart00242  166 DAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLN------------------- 226
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442    295 ksknhqQKGPLKDPIIDDYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEIPDDVRGGCQvseASEQSLTI 374
Cdd:smart00242  227 ------QGGCLTVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTV---KDKEELSN 297
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442    375 TSGLLGVDQTELRTALVSRVMQSKGGgfkgtVIMVPLKIYEASNARDALAKAIYSRLFDRIVGLINQSIPFQ-ASNFYIG 453
Cdd:smart00242  298 AAELLGVDPEELEKALTKRKIKTGGE-----VITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKdGSTYFIG 372
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442    454 VLDIAGFEYFTVNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITFTDNQDIIELIEAKSNGIFTLLDEES 533
Cdd:smart00242  373 VLDIYGFEIFEVNSFEQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFFDNQDCIDLIEKKPPGILSLLDEEC 452
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442    534 KLPKPSYSHFTAEVHKSWANHYRLGLPRSsrlkahrtlRDEEGFLVRHFAGAVCYNTEQFIEKNNDALHASLEGLVQECD 613
Cdd:smart00242  453 RFPKGTDQTFLEKLNQHHKKHPHFSKPKK---------KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSK 523
                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442    614 NPLLQTLFPSGsSTSVRGKLNFISVGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQFEGSLALAQLKCSGTISVL 693
Cdd:smart00242  524 NPLIASLFPSG-VSNAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENI 602
                           650       660       670       680       690       700       710
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281362442    694 ELMEHGYPSRVLFADLYSMYKSVLPPEL--VSLPARTFCEAMFQSLNLSAKDFKFGITKVFFRPGKFVEFDRIMR 766
Cdd:smart00242  603 RIRRAGFPYRLPFDEFLQRYRVLLPDTWppWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
COG5022 COG5022
Myosin heavy chain [General function prediction only];
3-826 0e+00

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 614.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442    3 EDTQLVWVRDAAEGYIQGRITEIGAKEFEVTPTDRKypkRTCHFDDIHSSC-DGPqdhDDNCELMLLNEATFLDNLKTRY 81
Cdd:COG5022    17 EEKGWIWAEIIKEAFNKGKVTEEGKKEDGESVSVKK---KVLGNDRIKLPKfDGV---DDLTELSYLNEPAVLHNLEKRY 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   82 YKDKIYTYVANILIAVNPYREIKeLYAPDTIKKYNGRSLGELPPHVFAIADKAIRDMRVYKLSQSIIVSGESGAGKTEST 161
Cdd:COG5022    91 NNGQIYTYSGLVLIAVNPYRDLG-IYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENA 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  162 KYLLKYLCY----SHDSAGPIETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEVHYDAKCQVVGGYISHYLLEKSRICT 237
Cdd:COG5022   170 KRIMQYLASvtssSTVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSRVVH 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  238 QSAEERNYHVFYMLLAGAPQQLRDKLSLGKPDDYRYLS--GCTQyfanakteqlIPGsqksknhqqkgplkdpiIDDYQH 315
Cdd:COG5022   250 QNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSqgGCDK----------IDG-----------------IDDAKE 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  316 FHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEIPDDvrggcQVSEASEQSLTITSGLLGVDQTELRTALVSRVM 395
Cdd:COG5022   303 FKITLDALKTIGIDEEEQDQIFKILAAILHIGNIEFKEDRNG-----AAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQI 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  396 QSkgggfKGTVIMVPLKIYEASNARDALAKAIYSRLFDRIVGLINQSI--PFQASNFyIGVLDIAGFEYFTVNSFEQFCI 473
Cdd:COG5022   378 KT-----GGEWIVVPLNLEQALAIRDSLAKALYSNLFDWIVDRINKSLdhSAAASNF-IGVLDIYGFEIFEKNSFEQLCI 451
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  474 NYCNEKLQKFFNDNILKNEQELYKREGLNVPEITFTDNQDIIELIEAKSN-GIFTLLDEESKLPKPSYSHFTAEVHKswa 552
Cdd:COG5022   452 NYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFIDYFDNQPCIDLIEKKNPlGILSLLDEECVMPHATDESFTSKLAQ--- 528
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  553 nhyRLGLPRSSRLKAHRtLRDeEGFLVRHFAGAVCYNTEQFIEKNNDALHASLEGLVQECDNPLLQTLFPSGSSTSVRGK 632
Cdd:COG5022   529 ---RLNKNSNPKFKKSR-FRD-NKFVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENIESKGR 603
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  633 lnFISVGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQFEGSLALAQLKCSGTISVLELMEHGYPSRVLFADLYSM 712
Cdd:COG5022   604 --FPTLGSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQR 681
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  713 YKsVLPPELV-------SLPARTFCEAMFQSLNLSAKDFKFGITKVFFRPGkfvefdrimrsdpenMLAIV--AKVKKW- 782
Cdd:COG5022   682 YR-ILSPSKSwtgeytwKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAG---------------VLAALedMRDAKLd 745
                         810       820       830       840
                  ....*....|....*....|....*....|....*....|....*...
gi 281362442  783 ----LIRSRWVKSAlgalcvikLRNRIIYRNKCVLIAQRIARGFLARK 826
Cdd:COG5022   746 niatRIQRAIRGRY--------LRRRYLQALKRIKKIQVIQHGFRLRR 785
PTZ00014 PTZ00014
myosin-A; Provisional
56-830 4.18e-157

myosin-A; Provisional


Pssm-ID: 240229 [Multi-domain]  Cd Length: 821  Bit Score: 491.85  E-value: 4.18e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   56 PQDHDDNCELMLLNEATFLDNLKTRYYKDKIYTYVANILIAVNPYREIKeLYAPDTIKKY-NGRSLGELPPHVFAIADKA 134
Cdd:PTZ00014   95 PMTYGDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLG-NTTNDWIRRYrDAKDSDKLPPHVFTTARRA 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  135 IRDMRVYKLSQSIIVSGESGAGKTESTKYLLKYLCYSH--DSAGPIETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEV 212
Cdd:PTZ00014  174 LENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFASSKsgNMDLKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQL 253
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  213 HYDAKCQVVGGYISHYLLEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSLGKPDDYRYLS-GCTQyfanakteqlIP 291
Cdd:PTZ00014  254 QLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINpKCLD----------VP 323
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  292 GsqksknhqqkgplkdpiIDDYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEIpdDVRGGCQVSEASEQS 371
Cdd:PTZ00014  324 G-----------------IDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGK--EEGGLTDAAAISDES 384
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  372 LTI---TSGLLGVDQTELRTALvsrVMQSKGGGfkGTVIMVPLKIYEASNARDALAKAIYSRLFDRIVGLINQSI-PFQA 447
Cdd:PTZ00014  385 LEVfneACELLFLDYESLKKEL---TVKVTYAG--NQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIePPGG 459
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  448 SNFYIGVLDIAGFEYFTVNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITFTDNQDIIELIEAKSNGIFT 527
Cdd:PTZ00014  460 FKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGKSVLS 539
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  528 LLDEESKLPKPSYSHFTAEVHKSWANHYRLglprssrLKAHRTLRdeEGFLVRHFAGAVCYNTEQFIEKNNDALHASLEG 607
Cdd:PTZ00014  540 ILEDQCLAPGGTDEKFVSSCNTNLKNNPKY-------KPAKVDSN--KNFVIKHTIGDIQYCASGFLFKNKDVLRPELVE 610
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  608 LVQECDNPLLQTLFPSGSSTsvRGKL---NFIsvGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQFEGSLALAQL 684
Cdd:PTZ00014  611 VVKASPNPLVRDLFEGVEVE--KGKLakgQLI--GSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQL 686
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  685 KCSGTISVLELMEHGYPSRVLFADLYSMYKSV-LP-PELVSLPARTFCEAMFQSLNLSAKDFKFGITKVFFRPGKFVEFD 762
Cdd:PTZ00014  687 HSLSILEALQLRQLGFSYRRTFAEFLSQFKYLdLAvSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLKKDAAKELT 766
                         730       740       750       760       770       780
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281362442  763 RIMRSdpenmlaivaKVKKWlirsRWVKSALGALCV-IKLRNRIIYRNKCVLIAQRIARGFLARKQHRP 830
Cdd:PTZ00014  767 QIQRE----------KLAAW----EPLVSVLEALILkIKKKRKVRKNIKSLVRIQAHLRRHLVIAEIKP 821
CBD_MYO6-like cd21759
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, ...
765-913 1.74e-59

calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, which are actin-based motor molecules with ATPase activity, include unconventional myosins that serve in intracellular movements. Myosin-VI, also called unconventional myosin-6 (MYO6), is a reverse-direction motor protein that moves towards the minus-end of actin filaments. It is required for the structural integrity of the Golgi apparatus via the p53-dependent pro-survival pathway. Myosin-VI appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells. It modulates RNA polymerase II-dependent transcription. As part of the DISP (DOCK7-Induced Septin disPlacement) complex, Myosin-VI may regulate the association of septins with actin and thereby regulate the actin cytoskeleton. Myosin-VI is encoded by gene MYO6, the human homolog of the gene responsible for deafness in Snell's waltzer mice. It is mutated in autosomal dominant non-syndromic hearing loss. This family also includes Drosophila melanogaster unconventional myosin VI Jaguar (Jar; also called myosin heavy chain 95F (Mhc95F), or 95F MHC), which is a motor protein necessary for the morphogenesis of epithelial tissues during Drosophila development. Jar is required for basal protein targeting and correct spindle orientation in mitotic neuroblasts. It contributes to synaptic transmission and development at the Drosophila neuromuscular junction. Together with CLIP-190 (CAP-Gly domain-containing/cytoplasmic linker protein 190), Jar may coordinate the interaction between the actin and microtubule cytoskeleton. Jar may link endocytic vesicles to microtubules and possibly be involved in transport in the early embryo and in the dynamic process of dorsal closure; its function is believed to change during the life cycle. This model corresponds to the calmodulin (CaM) binding domain (CBD), which consists of three subdomains: a unique insert (Insert 2 or Ins2), an IQ motif, and a proximal tail domain (PTD, also known as lever arm extension or LAE).


Pssm-ID: 409646 [Multi-domain]  Cd Length: 149  Bit Score: 200.81  E-value: 1.74e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  765 MRSDPENMLAIVAKVKKWLIRSRWVKSALGALCVIKLRNRIIYRNKCVLIAQRIARGFLARKQHRPRYQGIGKINKIRTN 844
Cdd:cd21759     1 MKSDPENLKELVKKVKKWLIRSRWRKAQWCALSVIKLKNKILYRREALIKIQKTVRGYLARKKHRPRIKGLRKIRALEKQ 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281362442  845 TLKTIEIASGLKMGREEIISGVNDIYRQIDDAIKKIKMNPRITQREMDSMYTVVMANMNKLTVDLNTKL 913
Cdd:cd21759    81 LKEMEEIASQLKKDKDKWTKQVKELKKEIDALIKKIKTNDMITRKEIDKLYNALVKKVDKQLAELQKKL 149
Myosin-VI_CBD pfam16521
Myosin VI cargo binding domain; Myosin-VI_CBD is a C-terminal family that allows ...
1160-1246 9.14e-57

Myosin VI cargo binding domain; Myosin-VI_CBD is a C-terminal family that allows unconventional myosin-VI to recognize and select its binding cargoes. Several adaptor proteins have been reported to interact specifically with the CBD, thus defining the specific subcellular functions of myosin VI. The crystal structure determination of the myosin VI CBD/Dab2 (an endocytic adaptor protein Disabled-2 that is a cargo) complex shows that the Myosin-VI_CBD forms a cargo-induced dimer, suggesting that the motor undergoes monomer-to-dimer conversion that is dependent upon cargo binding. In the absence of cargo myosin VI exists as a stable monomer. This cargo binding-mediated monomer-to-dimer conversion mechanism adopted by myosin VI may be shared by other unconventional myosins, such as myosin VII and myosin X.


Pssm-ID: 465157  Cd Length: 90  Bit Score: 190.57  E-value: 9.14e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  1160 HRYFRIPFMRANAPDNT---KRGLWYAHFDGQWIARQMELHADKPPILLVAGTDDMQMCELSLEETGLTRKRGAEILEHE 1236
Cdd:pfam16521    1 QRYFRIPFVRPSDKKRDggrKKGWWYAHFDGQWIARQMELHPDKPPVLLVAGKDDMQMCELSLEETGLTRKRGAEILEEE 80
                           90
                   ....*....|
gi 281362442  1237 FNREWERNGG 1246
Cdd:pfam16521   81 FEEEWKKHGG 90
MyUb_Myo6 cd21958
myosin VI ubiquitin-binding domain (MyUb) found in unconventional myosin-VI and similar ...
1076-1116 9.82e-25

myosin VI ubiquitin-binding domain (MyUb) found in unconventional myosin-VI and similar proteins; Unconventional myosin VI, also called Myo6, or unconventional myosin-6, is a monomeric myosin, which moves towards the minus-end of actin filaments, in contrast to most other myosins which moves towards the plus-end of actin filaments. It is thought that myosin VI, unlike plus-end directed myosins, does not use a pure lever arm mechanism, but instead steps with a mechanism analogous to the kinesin neck-linker uncoupling model. It has been implicated in a myriad of functions including the transport of cytoplasmic organelles, maintenance of normal Golgi morphology, endocytosis, secretion, cell migration, border cell migration during development, cancer metastasis, deafness, and retinal development, among others. For example, the GIPC1 (GAIP interacting protein, C-terminus 1) adaptor protein mediates endocytosis by tethering PlexinD1, a transmembrane receptor that regulates neuronal and cardiovascular development and cargo protein of GIPC1, to myosin VI motor through a regulated oligomerization mechanism, forming a PlexinD1/GIPC/myosin VI complex. This model corresponds to the myosin VI ubiquitin-binding domain (MyUb) that binds to ubiquitin chains, especially those linked via K63, K11, and K29.


Pssm-ID: 439319 [Multi-domain]  Cd Length: 41  Bit Score: 97.44  E-value: 9.82e-25
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 281362442 1076 QKYDLSKWKYSELRDAINTSCDIELLEACRQEFHRRLKVYH 1116
Cdd:cd21958     1 KKYDLSKWKYAELRDTINTSCDIELLEACREEFHRRLKVYH 41
Myosin_N pfam02736
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ...
7-49 1.14e-07

Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the N-terminus of many but not all myosins. The function of this domain is unknown.


Pssm-ID: 460670  Cd Length: 45  Bit Score: 49.35  E-value: 1.14e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 281362442     7 LVWVRDAAEGYIQGRITEIGAKEFEVTPTDRKypKRTCHFDDI 49
Cdd:pfam02736    5 LVWVPDPKEGFVKGEIKEEEGDKVTVETEDGK--TVTVKKDDV 45
MYO6_MIU_linker cd22294
MIU-linker domain found in unconventional myosin-VI; Myosins are actin-based motor molecules ...
1002-1093 4.05e-07

MIU-linker domain found in unconventional myosin-VI; Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins function in intracellular movements. Myosin-VI, also called unconventional myosin-6 (MYO6), is a reverse-direction motor protein that moves towards the minus-end of actin filaments. It is required for the structural integrity of the Golgi apparatus via the p53-dependent pro-survival pathway. It appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells. It modulates RNA polymerase II-dependent transcription. As part of the DISP complex, Myosin-VI may regulate the association of septins with actin and thereby regulate the actin cytoskeleton. Myosin-VI is encoded by the MYO6 gene, the human homologue of the gene responsible for deafness in Snell's waltzer mice. It is mutated in autosomal dominant nonsyndromic hearing loss. This model corresponds to a conserved region of myosin-VI, which consist of three helices: MIU (Motif Interacting with Ubiquitin), a common linker helix (linker-alpha1) and an isoform-specific helix (linker-alpha2).


Pssm-ID: 412090 [Multi-domain]  Cd Length: 69  Bit Score: 48.36  E-value: 4.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442 1002 LEQERRDHELALRLAnESNGQ--VEDSPPVIRngvndaspmgpnklisfsqvvsniasryLNKSENVRAQQQALGKQKYD 1079
Cdd:cd22294     5 LEQERRDRELAMRIA-QSEAEliSEETQPDLA----------------------------LRRSAGTQAVSAGGGKKKMT 55
                          90
                  ....*....|....
gi 281362442 1080 LSKWKYSELRDAIN 1093
Cdd:cd22294    56 MEEMAKEMSEDLSR 69
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
954-1020 2.00e-05

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 45.29  E-value: 2.00e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281362442   954 RLKAEMETRRKAAEAQRLRQEEEdRRAALALQEQLEKEAKDDAKYRQQLEQERRDH-ELALRLANESN 1020
Cdd:pfam20492   34 ETAEELEEERRQAEEEAERLEQK-RQEAEEEKERLEESAEMEAEEKEQLEAELAEAqEEIARLEEEVE 100
UDM1_RNF168_RNF169-like cd22249
UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, ...
955-1015 2.11e-05

UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, RNF169 and similar proteins; This model represents the UDM1 (ubiquitin-dependent double-strand break [DSB] recruitment module 1) found in RING finger proteins, RNF168 and RNF169. RNF168 is an E3 ubiquitin-protein ligase that promotes non-canonical K27 ubiquitination to signal DNA damage. It functions, together with RNF8, as a DNA damage response (DDR) factor that promotes a series of ubiquitylation events on substrates such as H2A and H2AX. With H2AK13/15 ubiquitylation, it facilitates recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of double-strand breaks (DSBs), and inhibits homologous recombination (HR) in cells deficient in the tumor suppressor BRCA1. RNF168 also promotes H2A neddylation, which antagonizes ubiquitylation of H2A and regulates DNA damage repair. In addition, RNF168 forms a functional complex with RAD6A or RAD6B during the DNA damage response. RNF169 is an uncharacterized E3 ubiquitin-protein ligase paralogous to RNF168. It functions as a negative regulator of the DNA damage signaling cascade. RNF169 recognizes polyubiquitin structures but does not itself contribute to double-strand break (DSB)-induced chromatin ubiquitylation. It contributes to the regulation of DSB repair pathway utilization via functionally competing with recruiting repair factors, 53BP1 and RAP80-BRCA1, for association with RNF168-modified chromatin, independent of its catalytic activity, limiting the magnitude of the RNF8/RNF168-dependent signaling response to DSBs. The UDM1 domain comprises LRM1 (LR motif 1), UMI (ubiquitin-interacting motif [UIM]- and MIU-related UBD) and MIU1 (motif interacting with ubiquitin 1). Mutations of Ub-interacting residues in UDM1 have little effect on the accumulation of RNF168 to DSB sites, suggesting that it may not be the main site of binding ubiquitylated and polyubiquitylated targets.


Pssm-ID: 409016 [Multi-domain]  Cd Length: 66  Bit Score: 43.41  E-value: 2.11e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281362442  955 LKAEMETRRKAAEAQRLRQEEEDRRAALALQEQLEKEAKDDAKyRQQLEQERRDHELALRL 1015
Cdd:cd22249     7 IREEYEAQLKKLEEERRKEREEEEKASEELIRKLQEEEERQRK-REREEQLKQDEELAKQL 66
Caldesmon pfam02029
Caldesmon;
955-1079 1.14e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 42.93  E-value: 1.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   955 LKAEMETRRKaaeaqrLRQEEEDRRAalalQEQLEKEAKDDAKYRQQLEQ-ERRDHELA-LRLANESNGQVEDSPPvirn 1032
Cdd:pfam02029  282 LKKKREERRK------LLEEEEQRRK----QEEAERKLREEEEKRRMKEEiERRRAEAAeKRQKLPEDSSSEGKKP---- 347
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 281362442  1033 gVNDASPMGPNKLISFSqvvSNIASRYLNKSENVRAQQQALGKQKYD 1079
Cdd:pfam02029  348 -FKCFSPKGSSLKITER---AEFLNKSLQKSSSVKKTHPPAVVSKID 390
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
956-1018 7.40e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 40.17  E-value: 7.40e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281362442  956 KAEMETRRKAAEAQRLRQEEEDRRAALALQEQLEKEAKDDAKYRQQLEQERRDHELALRLANE 1018
Cdd:PRK09510   88 QAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAE 150
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
953-1026 8.92e-03

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 40.02  E-value: 8.92e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281362442  953 KRLKAEMETRRKAAEAQRLRQEEEDRRAALALQEQLEKE-AKDDAKYRQQLEQERRDHELALRLANESNGQVEDS 1026
Cdd:COG3064    58 REAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEkAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEE 132
 
Name Accession Description Interval E-value
MYSc_Myo6 cd01382
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ...
71-754 0e+00

class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the minus-end of actin filaments, in contrast to most other myosins which moves towards the plus-end of actin filaments. It is thought that myosin VI, unlike plus-end directed myosins, does not use a pure lever arm mechanism, but instead steps with a mechanism analogous to the kinesin neck-linker uncoupling model. It has been implicated in a myriad of functions including: the transport of cytoplasmic organelles, maintenance of normal Golgi morphology, endocytosis, secretion, cell migration, border cell migration during development, and in cancer metastasis playing roles in deafness and retinal development among others. While how this is accomplished is largely unknown there are several interacting proteins that have been identified such as disabled homolog 2 (DAB2), GIPC1, synapse-associated protein 97 (SAP97; also known as DLG1) and optineurin, which have been found to target myosin VI to different cellular compartments. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the minus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276833  Cd Length: 649  Bit Score: 1279.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   71 ATFLDNLKTRYYKDKIYTYVANILIAVNPYREIKELYAPDTIKKYNGRSLGELPPHVFAIADKAIRDMRVYKLSQSIIVS 150
Cdd:cd01382     1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPKLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  151 GESGAGKTESTKYLLKYLCYSHDS-AGPIETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEVHYDAKCQVVGGYISHYL 229
Cdd:cd01382    81 GESGAGKTESTKYILRYLTESWGSgAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  230 LEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLslgkpddyrylsgctqyfanakteqlipgsqksknhqqkgpLKDPI 309
Cdd:cd01382   161 LEKSRICVQSKEERNYHIFYRLCAGAPEDLREKL-----------------------------------------LKDPL 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  310 IDDYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEIPDDVRGGCQVSEASEQSLTITSGLLGVDQTELRTA 389
Cdd:cd01382   200 LDDVGDFIRMDKAMKKIGLSDEEKLDIFRVVAAVLHLGNIEFEENGSDSGGGCNVKPKSEQSLEYAAELLGLDQDELRVS 279
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  390 LVSRVMQSKGGGFKGTVIMVPLKIYEASNARDALAKAIYSRLFDRIVGLINQSIPFQASNFYIGVLDIAGFEYFTVNSFE 469
Cdd:cd01382   280 LTTRVMQTTRGGAKGTVIKVPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFETSSYFIGVLDIAGFEYFEVNSFE 359
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  470 QFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITFTDNQDIIELIEAKSNGIFTLLDEESKLPKPSYSHFTAEVHK 549
Cdd:cd01382   360 QFCINYCNEKLQQFFNERILKEEQELYEKEGLGVKEVEYVDNQDCIDLIEAKLVGILDLLDEESKLPKPSDQHFTSAVHQ 439
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  550 SWANHYRLGLPRSSRLKAHRTLRDEEGFLVRHFAGAVCYNTEQFIEKNNDALHASLEGLVQECDNPLLQTLFPS-----G 624
Cdd:cd01382   440 KHKNHFRLSIPRKSKLKIHRNLRDDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESstnnnK 519
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  625 SSTSVRGKLNFISVGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQFEGSLALAQLKCSGTISVLELMEHGYPSRV 704
Cdd:cd01382   520 DSKQKAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRT 599
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|
gi 281362442  705 LFADLYSMYKSVLPPELVSLPARTFCEAMFQSLNLSAKDFKFGITKVFFR 754
Cdd:cd01382   600 SFHDLYNMYKKYLPPKLARLDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
Myosin_head pfam00063
Myosin head (motor domain);
59-754 0e+00

Myosin head (motor domain);


Pssm-ID: 395017 [Multi-domain]  Cd Length: 674  Bit Score: 974.06  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442    59 HDDNCELMLLNEATFLDNLKTRYYKDKIYTYVANILIAVNPYREIKeLYAPDTIKKYNGRSLGELPPHVFAIADKAIRDM 138
Cdd:pfam00063    1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLP-IYSEDMIKAYRGKRRGELPPHIFAIADEAYRSM 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   139 RVYKLSQSIIVSGESGAGKTESTKYLLKYLCYSHDSA-----GPIETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEVH 213
Cdd:pfam00063   80 LQDKENQSILISGESGAGKTENTKKIMQYLASVSGSGsagnvGRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQ 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   214 YDAKCQVVGGYISHYLLEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSLGKPDDYRYLSGCTQYFAnakteqlipgs 293
Cdd:pfam00063  160 FDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQSGCYTI----------- 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   294 qksknhqqkgplkdPIIDDYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEIPDDVRGgcqVSEASEQsLT 373
Cdd:pfam00063  229 --------------DGIDDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQA---VPDDTEN-LQ 290
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   374 ITSGLLGVDQTELRTALVSRVMQSkgggfKGTVIMVPLKIYEASNARDALAKAIYSRLFDRIVGLINQSIPFQAS--NFY 451
Cdd:pfam00063  291 KAASLLGIDSTELEKALCKRRIKT-----GRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIekASF 365
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   452 IGVLDIAGFEYFTVNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITFTDNQDIIELIEAKSNGIFTLLDE 531
Cdd:pfam00063  366 IGVLDIYGFEIFEKNSFEQLCINYVNEKLQQFFNHHMFKLEQEEYVREGIEWTFIDFGDNQPCIDLIEKKPLGILSLLDE 445
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   532 ESKLPKPSYSHFTAEVHKSWANHYRLGLPRssrlkahrtLRDEEGFLVRHFAGAVCYNTEQFIEKNNDALHASLEGLVQE 611
Cdd:pfam00063  446 ECLFPKATDQTFLDKLYSTFSKHPHFQKPR---------LQGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKS 516
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   612 CDNPLLQTLFP------------SGSSTSVRGKL-NFISVGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQFEGS 678
Cdd:pfam00063  517 SSDPLLAELFPdyetaesaaaneSGKSTPKRTKKkRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNS 596
                          650       660       670       680       690       700       710
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281362442   679 LALAQLKCSGTISVLELMEHGYPSRVLFADLYSMYKSVLPPELVSL--PARTFCEAMFQSLNLSAKDFKFGITKVFFR 754
Cdd:pfam00063  597 LVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRYRILAPKTWPKWkgDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
MYSc smart00242
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...
58-766 0e+00

Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical interaction between myosin and actin. The core of the myosin structure is similar in fold to that of kinesin.


Pssm-ID: 214580 [Multi-domain]  Cd Length: 677  Bit Score: 932.34  E-value: 0e+00
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442     58 DHDDNCELMLLNEATFLDNLKTRYYKDKIYTYVANILIAVNPYREIkELYAPDTIKKYNGRSLGELPPHVFAIADKAIRD 137
Cdd:smart00242    7 GVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQL-PIYTDEVIKKYRGKSRGELPPHVFAIADNAYRN 85
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442    138 MRVYKLSQSIIVSGESGAGKTESTKYLLKYLCY---SHDSAGPIETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEVHY 214
Cdd:smart00242   86 MLNDKENQSIIISGESGAGKTENTKKIMQYLASvsgSNTEVGSVEDQILESNPILEAFGNAKTLRNNNSSRFGKFIEIHF 165
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442    215 DAKCQVVGGYISHYLLEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSLGKPDDYRYLSgctqyfanakteqlipgsq 294
Cdd:smart00242  166 DAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLN------------------- 226
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442    295 ksknhqQKGPLKDPIIDDYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEIPDDVRGGCQvseASEQSLTI 374
Cdd:smart00242  227 ------QGGCLTVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTV---KDKEELSN 297
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442    375 TSGLLGVDQTELRTALVSRVMQSKGGgfkgtVIMVPLKIYEASNARDALAKAIYSRLFDRIVGLINQSIPFQ-ASNFYIG 453
Cdd:smart00242  298 AAELLGVDPEELEKALTKRKIKTGGE-----VITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKdGSTYFIG 372
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442    454 VLDIAGFEYFTVNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITFTDNQDIIELIEAKSNGIFTLLDEES 533
Cdd:smart00242  373 VLDIYGFEIFEVNSFEQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFFDNQDCIDLIEKKPPGILSLLDEEC 452
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442    534 KLPKPSYSHFTAEVHKSWANHYRLGLPRSsrlkahrtlRDEEGFLVRHFAGAVCYNTEQFIEKNNDALHASLEGLVQECD 613
Cdd:smart00242  453 RFPKGTDQTFLEKLNQHHKKHPHFSKPKK---------KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSK 523
                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442    614 NPLLQTLFPSGsSTSVRGKLNFISVGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQFEGSLALAQLKCSGTISVL 693
Cdd:smart00242  524 NPLIASLFPSG-VSNAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENI 602
                           650       660       670       680       690       700       710
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281362442    694 ELMEHGYPSRVLFADLYSMYKSVLPPEL--VSLPARTFCEAMFQSLNLSAKDFKFGITKVFFRPGKFVEFDRIMR 766
Cdd:smart00242  603 RIRRAGFPYRLPFDEFLQRYRVLLPDTWppWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
MYSc cd00124
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ...
71-754 0e+00

Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276950 [Multi-domain]  Cd Length: 633  Bit Score: 765.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   71 ATFLDNLKTRYYKDKIYTYVANILIAVNPYREIkELYAPDTIKKYNGRSLG-ELPPHVFAIADKAIRDMRVYKLSQSIIV 149
Cdd:cd00124     1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWL-PLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  150 SGESGAGKTESTKYLLKYLCY--------SHDSAGPIETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEVHYDAKCQVV 221
Cdd:cd00124    80 SGESGAGKTETTKLVLKYLAAlsgsgsskSSSSASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  222 GGYISHYLLEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSLGKPDDYRYLSgctqyfanakteqlipgsqksKNHQQ 301
Cdd:cd00124   160 GASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLN---------------------DYLNS 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  302 KGPLKDPIIDDYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEIPDDvrGGCQVSEASEQSLTITSGLLGV 381
Cdd:cd00124   219 SGCDRIDGVDDAEEFQELLDALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEED--EDSSAEVADDESLKAAAKLLGV 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  382 DQTELRTALVSRVMQSKGGgfkgtVIMVPLKIYEASNARDALAKAIYSRLFDRIVGLINQSI---PFQASNFYIGVLDIA 458
Cdd:cd00124   297 DAEDLEEALTTRTIKVGGE-----TITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALsptDAAESTSFIGILDIF 371
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  459 GFEYFTVNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITFTDNQDIIELIEAKSNGIFTLLDEESKLPKP 538
Cdd:cd00124   372 GFENFEVNSFEQLCINYANEKLQQFFNQHVFKLEQEEYEEEGIDWSFIDFPDNQDCLDLIEGKPLGILSLLDEECLFPKG 451
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  539 SYSHFTAEVHKSWANHyrlglprsSRLKAHRTLRDEEgFLVRHFAGAVCYNTEQFIEKNNDALHASLEGLVQEcdnpllq 618
Cdd:cd00124   452 TDATFLEKLYSAHGSH--------PRFFSKKRKAKLE-FGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRS------- 515
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  619 tlfpsgsstsvrgklnfisvGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQFEGSLALAQLKCSGtisVLELME- 697
Cdd:cd00124   516 --------------------GSQFRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAG---VLEAVRi 572
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281362442  698 --HGYPSRVLFADLYSMYKSVLPP--ELVSLPARTFCEAMFQSLNLSAKDFKFGITKVFFR 754
Cdd:cd00124   573 rrAGYPVRLPFDEFLKRYRILAPGatEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
MYSc_Myo11 cd01384
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ...
74-754 0e+00

class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle transport. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle.


Pssm-ID: 276835  Cd Length: 647  Bit Score: 658.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   74 LDNLKTRYYKDKIYTYVANILIAVNPYREIKELYAPDTIKKYNGRSLGELPPHVFAIADKAIRDMRVYKLSQSIIVSGES 153
Cdd:cd01384     4 LHNLKVRYELDEIYTYTGNILIAVNPFKRLPHLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVSGES 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  154 GAGKTESTKYLLKYLCY----SHDSAGPIETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEVHYDAKCQVVGGYISHYL 229
Cdd:cd01384    84 GAGKTETTKMLMQYLAYmggrAVTEGRSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAAIRTYL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  230 LEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSLGKPDDYRYLSgctqyfanakteqlipgsqKSKNHQQKGplkdpi 309
Cdd:cd01384   164 LERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLN-------------------QSKCFELDG------ 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  310 IDDYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEIPDDVRGGCqVSEASEQSLTITSGLLGVDQTELRTA 389
Cdd:cd01384   219 VDDAEEYRATRRAMDVVGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVP-KDEKSEFHLKAAAELLMCDEKALEDA 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  390 LVSRVMQSKGGgfkgtVIMVPLKIYEASNARDALAKAIYSRLFDRIVGLINQSIPFQA-SNFYIGVLDIAGFEYFTVNSF 468
Cdd:cd01384   298 LCKRVIVTPDG-----IITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPnSKRLIGVLDIYGFESFKTNSF 372
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  469 EQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITFTDNQDIIELIEAKSNGIFTLLDEESKLPKPSYSHFTAEVH 548
Cdd:cd01384   373 EQFCINLANEKLQQHFNQHVFKMEQEEYTKEEIDWSYIEFVDNQDVLDLIEKKPGGIIALLDEACMFPRSTHETFAQKLY 452
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  549 KSWANHYRLGLPRSSRlkahrtlrdeEGFLVRHFAGAVCYNTEQFIEKNNDALHASLEGLVQECDNPLLQTLFPSGSSTS 628
Cdd:cd01384   453 QTLKDHKRFSKPKLSR----------TDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPREG 522
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  629 VRGKLNFISVGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQFEGSLALAQLKCSGtisVLELME---HGYPSR-- 703
Cdd:cd01384   523 TSSSSKFSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGG---VLEAVRiscAGYPTRkp 599
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....
gi 281362442  704 -VLFADLYSMyksvLPPELVSL--PARTFCEAMFQSLNLsaKDFKFGITKVFFR 754
Cdd:cd01384   600 fEEFLDRFGL----LAPEVLKGsdDEKAACKKILEKAGL--KGYQIGKTKVFLR 647
MYSc_Myo22 cd14883
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ...
72-754 0e+00

class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ motifs such as found in class V, VIII, XI, and XIII myosins. These myosins are defined by two tandem MyTH4 and FERM domains. The apicomplexan, but not diatom myosins contain 4-6 WD40 repeats near the end of the C-terminal tail which suggests a possible function of these myosins in signal transduction and transcriptional regulation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276849 [Multi-domain]  Cd Length: 661  Bit Score: 645.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   72 TFLDNLKTRYYKDKIYTYVANILIAVNPYREIKeLYAPDTIKKYNGRSLGELPPHVFAIADKAIRDMRVYKLSQSIIVSG 151
Cdd:cd14883     2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELP-IYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  152 ESGAGKTESTKYLLKYLCYSHDSAGPIETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEVHYDAKCQVVGGYISHYLLE 231
Cdd:cd14883    81 ESGAGKTETTKLILQYLCAVTNNHSWVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGAIIQDYLLE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  232 KSRICTQSAEERNYHVFYMLLAGA--PQQLRDKLSLGKPDDYRYL--SGCTQyfanakteqlIPGsqksknhqqkgplkd 307
Cdd:cd14883   161 QSRITFQAPGERNYHVFYQLLAGAkhSKELKEKLKLGEPEDYHYLnqSGCIR----------IDN--------------- 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  308 piIDDYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEIpDDVRggCQVSEASEQSLTITSGLLGVDQTELR 387
Cdd:cd14883   216 --INDKKDFDHLRLAMNVLGIPEEMQEGIFSVLSAILHLGNLTFEDI-DGET--GALTVEDKEILKIVAKLLGVDPDKLK 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  388 TALVSRVMQskgggFKGTVIMVPLKIYEASNARDALAKAIYSRLFDRIVGLINQSI-PFQASNFYIGVLDIAGFEYFTVN 466
Cdd:cd14883   291 KALTIRQIN-----VRGNVTEIPLKVQEARDNRDAMAKALYSRTFAWLVNHINSCTnPGQKNSRFIGVLDIFGFENFKVN 365
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  467 SFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITFTDNQDIIELIEAKSNGIFTLLDEESKLPKPSYSHFTAE 546
Cdd:cd14883   366 SFEQLCINYTNEKLHKFFNHYVFKLEQEEYEKEGINWSHIVFTDNQECLDLIEKPPLGILKLLDEECRFPKGTDLTYLEK 445
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  547 VHKSWANHyrlglprSSRLKAHRTLRDEEgFLVRHFAGAVCYNTEQFIEKNNDALHASLEGLVQECDNPLLQTLF----- 621
Cdd:cd14883   446 LHAAHEKH-------PYYEKPDRRRWKTE-FGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFtypdl 517
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  622 --------PSGSSTSVRGKLNFI-SVGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQFEGSLALAQLKCSGTISV 692
Cdd:cd14883   518 laltglsiSLGGDTTSRGTSKGKpTVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEI 597
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281362442  693 LELMEHGYPSRVLFADLYSMYKSVLPPELVSLPARTF--CEAMFQSLNLSAKDFKFGITKVFFR 754
Cdd:cd14883   598 IRIRKEGFPIHLTFKEFVDRYLCLDPRARSADHKETCgaVRALMGLGGLPEDEWQVGKTKVFLR 661
MYSc_class_II cd01377
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ...
71-754 0e+00

class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. Thus, myosin II has two heads. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276951 [Multi-domain]  Cd Length: 662  Bit Score: 632.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   71 ATFLDNLKTRYYKDKIYTYVANILIAVNPYREIKeLYAPDTIKKYNGRSLGELPPHVFAIADKAIRDMRVYKLSQSIIVS 150
Cdd:cd01377     1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLP-IYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILIT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  151 GESGAGKTESTKYLLKYLCY----------SHDSAGPIETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEVHYDAKCQV 220
Cdd:cd01377    80 GESGAGKTENTKKVIQYLASvaasskkkkeSGKKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  221 VGGYISHYLLEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSLGKPDDYRYLSgctqyfanakteqlipgsqksknhq 300
Cdd:cd01377   160 AGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFL------------------------- 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  301 QKGPLKDPIIDDYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEipddvRGGCQVSEA-SEQSLTITSGLL 379
Cdd:cd01377   215 SQGELTIDGVDDAEEFKLTDEAFDILGFSEEEKMSIFKIVAAILHLGNIKFKQ-----RRREEQAELdGTEEADKAAHLL 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  380 GVDQTELRTAL------VSRVMQSKGggfkgtvimvpLKIYEASNARDALAKAIYSRLFDRIVGLINQSIPF-QASNFYI 452
Cdd:cd01377   290 GVNSSDLLKALlkprikVGREWVTKG-----------QNKEQVVFSVGALAKALYERLFLWLVKRINKTLDTkSKRQYFI 358
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  453 GVLDIAGFEYFTVNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLnvpEITFT----DNQDIIELIEAKSNGIFTL 528
Cdd:cd01377   359 GVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQEEYKKEGI---EWTFIdfglDLQPTIDLIEKPNMGILSI 435
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  529 LDEESKLPKPSYSHFTAEVHKSWANHyrlglprSSRLKAHRTLRDEEGFLVRHFAGAVCYNTEQFIEKNNDALHASLEGL 608
Cdd:cd01377   436 LDEECVFPKATDKTFVEKLYSNHLGK-------SKNFKKPKPKKSEAHFILKHYAGDVEYNIDGWLEKNKDPLNENVVAL 508
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  609 VQECDNPLLQTLFPSGSSTSVRGKLN------FISVGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQFEGSLALA 682
Cdd:cd01377   509 LKKSSDPLVASLFKDYEESGGGGGKKkkkggsFRTVSQLHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLH 588
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281362442  683 QLKCSGtisVLE---LMEHGYPSRVLFADLYSMYkSVLPPELVSL---PARTFCEAMFQSLNLSAKDFKFGITKVFFR 754
Cdd:cd01377   589 QLRCNG---VLEgirICRKGFPNRIIFAEFKQRY-SILAPNAIPKgfdDGKAACEKILKALQLDPELYRIGNTKVFFK 662
MYSc_Myo1 cd01378
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ...
73-754 0e+00

class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, and class I myosins have been implicated in phagocytosis and vesicle transport. Myosin I, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. There are 5 myosin subclasses with subclasses c/h, d/g, and a/b have an IQ domain and a TH1 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276829  Cd Length: 652  Bit Score: 617.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   73 FLDNLKTRYYKDKIYTYVANILIAVNPYREIkELYAPDTIKKYNGRSLGELPPHVFAIADKAIRDMRVYKLSQSIIVSGE 152
Cdd:cd01378     3 INENLKKRFENDEIYTYIGHVLISVNPFKDL-GIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  153 SGAGKTESTKYLLKYLCY-SHDSAGPIET---KILDANPVLEAFGNAKTTRNNNSSRFGKFIEVHYDAKCQVVGGYISHY 228
Cdd:cd01378    82 SGAGKTEASKRIMQYIAAvSGGSESEVERvkdMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGHITNY 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  229 LLEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSLGKPDDYRYL--SGCTqyfanakteqlipgsqksknhqqkgplK 306
Cdd:cd01378   162 LLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYskSGCF---------------------------D 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  307 DPIIDDYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEipdDVRGGCQVSeaSEQSLTITSGLLGVDQTEL 386
Cdd:cd01378   215 VDGIDDAADFKEVLNAMKVIGFTEEEQDSIFRILAAILHLGNIQFAE---DEEGNAAIS--DTSVLDFVAYLLGVDPDQL 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  387 RTALVSRVMQSKGGGfkGTVIMVPLKIYEASNARDALAKAIYSRLFDRIVGLINQSI--PFQASNFYIGVLDIAGFEYFT 464
Cdd:cd01378   290 EKALTHRTIETGGGG--RSVYEVPLNVEQAAYARDALAKAIYSRLFDWIVERINKSLaaKSGGKKKVIGVLDIYGFEIFE 367
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  465 VNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITFTDNQDIIELIEAKSNGIFTLLDEESKLP-KPSYSHF 543
Cdd:cd01378   368 KNSFEQFCINYVNEKLQQIFIELTLKAEQEEYVREGIEWTPIKYFNNKIICDLIEEKPPGIFAILDDACLTAgDATDQTF 447
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  544 TAEVHKSWANHyrlglPRSSRLKAHRTLRDEEgFLVRHFAGAVCYNTEQFIEKNNDALHASLEGLVQECDNPLLQTLFPS 623
Cdd:cd01378   448 LQKLNQLFSNH-----PHFECPSGHFELRRGE-FRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPE 521
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  624 GSSTSVRGKLnfISVGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQFEGSLALAQLKcsgtisVLELMEH----- 698
Cdd:cd01378   522 GVDLDSKKRP--PTAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVK------YLGLLENvrvrr 593
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  699 -GYPSRVLFADLYSMYKSvLPPEL---VSLPARTFCEAMFQSLNLSAKDFKFGITKVFFR 754
Cdd:cd01378   594 aGFAYRQTYEKFLERYKL-LSPKTwpaWDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
COG5022 COG5022
Myosin heavy chain [General function prediction only];
3-826 0e+00

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 614.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442    3 EDTQLVWVRDAAEGYIQGRITEIGAKEFEVTPTDRKypkRTCHFDDIHSSC-DGPqdhDDNCELMLLNEATFLDNLKTRY 81
Cdd:COG5022    17 EEKGWIWAEIIKEAFNKGKVTEEGKKEDGESVSVKK---KVLGNDRIKLPKfDGV---DDLTELSYLNEPAVLHNLEKRY 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   82 YKDKIYTYVANILIAVNPYREIKeLYAPDTIKKYNGRSLGELPPHVFAIADKAIRDMRVYKLSQSIIVSGESGAGKTEST 161
Cdd:COG5022    91 NNGQIYTYSGLVLIAVNPYRDLG-IYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENA 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  162 KYLLKYLCY----SHDSAGPIETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEVHYDAKCQVVGGYISHYLLEKSRICT 237
Cdd:COG5022   170 KRIMQYLASvtssSTVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSRVVH 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  238 QSAEERNYHVFYMLLAGAPQQLRDKLSLGKPDDYRYLS--GCTQyfanakteqlIPGsqksknhqqkgplkdpiIDDYQH 315
Cdd:COG5022   250 QNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSqgGCDK----------IDG-----------------IDDAKE 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  316 FHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEIPDDvrggcQVSEASEQSLTITSGLLGVDQTELRTALVSRVM 395
Cdd:COG5022   303 FKITLDALKTIGIDEEEQDQIFKILAAILHIGNIEFKEDRNG-----AAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQI 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  396 QSkgggfKGTVIMVPLKIYEASNARDALAKAIYSRLFDRIVGLINQSI--PFQASNFyIGVLDIAGFEYFTVNSFEQFCI 473
Cdd:COG5022   378 KT-----GGEWIVVPLNLEQALAIRDSLAKALYSNLFDWIVDRINKSLdhSAAASNF-IGVLDIYGFEIFEKNSFEQLCI 451
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  474 NYCNEKLQKFFNDNILKNEQELYKREGLNVPEITFTDNQDIIELIEAKSN-GIFTLLDEESKLPKPSYSHFTAEVHKswa 552
Cdd:COG5022   452 NYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFIDYFDNQPCIDLIEKKNPlGILSLLDEECVMPHATDESFTSKLAQ--- 528
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  553 nhyRLGLPRSSRLKAHRtLRDeEGFLVRHFAGAVCYNTEQFIEKNNDALHASLEGLVQECDNPLLQTLFPSGSSTSVRGK 632
Cdd:COG5022   529 ---RLNKNSNPKFKKSR-FRD-NKFVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENIESKGR 603
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  633 lnFISVGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQFEGSLALAQLKCSGTISVLELMEHGYPSRVLFADLYSM 712
Cdd:COG5022   604 --FPTLGSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQR 681
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  713 YKsVLPPELV-------SLPARTFCEAMFQSLNLSAKDFKFGITKVFFRPGkfvefdrimrsdpenMLAIV--AKVKKW- 782
Cdd:COG5022   682 YR-ILSPSKSwtgeytwKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAG---------------VLAALedMRDAKLd 745
                         810       820       830       840
                  ....*....|....*....|....*....|....*....|....*...
gi 281362442  783 ----LIRSRWVKSAlgalcvikLRNRIIYRNKCVLIAQRIARGFLARK 826
Cdd:COG5022   746 niatRIQRAIRGRY--------LRRRYLQALKRIKKIQVIQHGFRLRR 785
MYSc_Myo5 cd01380
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ...
74-754 0e+00

class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins that transport a variety of intracellular cargo processively along actin filaments, such as melanosomes, synaptic vesicles, vacuoles, and mRNA. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains a IQ domain and a globular DIL domain. Myosin V is a class of actin-based motor proteins involved in cytoplasmic vesicle transport and anchorage, spindle-pole alignment and mRNA translocation. The protein encoded by this gene is abundant in melanocytes and nerve cells. Mutations in this gene cause Griscelli syndrome type-1 (GS1), Griscelli syndrome type-3 (GS3) and neuroectodermal melanolysosomal disease, or Elejalde disease. Multiple alternatively spliced transcript variants encoding different isoforms have been reported, but the full-length nature of some variants has not been determined. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Note that the Dictyostelium myoVs are not contained in this child group. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276831 [Multi-domain]  Cd Length: 629  Bit Score: 601.07  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   74 LDNLKTRYYKDK-IYTYVANILIAVNPYREIkELYAPDTIKKYNGRSLGELPPHVFAIADKAIRDMRVYKLSQSIIVSGE 152
Cdd:cd01380     4 LHNLKVRFCQRNaIYTYCGIVLVAINPYEDL-PIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSGE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  153 SGAGKTESTKYLLKYL---CYSHDSAGPIETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEVHYDAKCQVVGGYISHYL 229
Cdd:cd01380    83 SGAGKTVSAKYAMRYFatvGGSSSGETQVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANMRTYL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  230 LEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSLGKPDDYRYLS--GCTQyfanakteqlIPGsqksknhqqkgplkd 307
Cdd:cd01380   163 LEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNqgGSPV----------IDG--------------- 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  308 piIDDYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEIpddvRGGCQVSEASEQSLTITSGLLGVDQTELR 387
Cdd:cd01380   218 --VDDAAEFEETRKALTLLGISEEEQMEIFRILAAILHLGNVEIKAT----RNDSASISPDDEHLQIACELLGIDESQLA 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  388 TALVSRVMQSKGGgfkgtVIMVPLKIYEASNARDALAKAIYSRLFDRIVGLINQSI----PFQASNFyIGVLDIAGFEYF 463
Cdd:cd01380   292 KWLCKRKIVTRSE-----VIVKPLTLQQAIVARDALAKHIYAQLFDWIVDRINKALaspvKEKQHSF-IGVLDIYGFETF 365
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  464 TVNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITFTDNQDIIELIEAKSnGIFTLLDEESKLPKPSyshf 543
Cdd:cd01380   366 EVNSFEQFCINYANEKLQQQFNQHVFKLEQEEYVKEEIEWSFIDFYDNQPCIDLIEGKL-GILDLLDEECRLPKGS---- 440
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  544 taevHKSWAN--HYRLGLPRSSRLKAHRTlrDEEGFLVRHFAGAVCYNTEQFIEKNNDALhasLEGLVQecdnpLLQtlf 621
Cdd:cd01380   441 ----DENWAQklYNQHLKKPNKHFKKPRF--SNTAFIVKHFADDVEYQVEGFLEKNRDTV---SEEHLN-----VLK--- 503
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  622 psgsSTSVRGKlnfiSVGSKFKTQLGELMEKLeqNGTN--FIRCIKPNSKMIDRQFEGSLALAQLKCSGtisVLELME-- 697
Cdd:cd01380   504 ----ASKNRKK----TVGSQFRDSLILLMETL--NSTTphYVRCIKPNDEKLPFTFDPKRVVQQLRACG---VLETIRis 570
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 281362442  698 -HGYPSRVLFADLYSMYKSVLP-PELVSLPARTFCEAMFQSLNLSAKDFKFGITKVFFR 754
Cdd:cd01380   571 aAGFPSRWTYEEFFSRYRVLLPsKEWLRDDKKKTCENILENLILDPDKYQFGKTKIFFR 629
MYSc_Myo8 cd01383
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ...
74-754 0e+00

class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated with endocytosis, cytokinesis, cell-to-cell coupling and gating at plasmodesmata. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains IQ domains Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276834  Cd Length: 647  Bit Score: 598.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   74 LDNLKTRYYKDKIYTYVANILIAVNPYREIkELYAPDTIKKYNGRSLgeLPPHVFAIADKAIRDMRVYKLSQSIIVSGES 153
Cdd:cd01383     4 LHNLEYRYSQDIIYTKAGPVLIAVNPFKDV-PLYGNEFITAYRQKLL--DSPHVYAVADTAYREMMRDEINQSIIISGES 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  154 GAGKTESTKYLLKYLCY--SHDSAgpIETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEVHYDAKCQVVGGYISHYLLE 231
Cdd:cd01383    81 GAGKTETAKIAMQYLAAlgGGSSG--IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQTYLLE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  232 KSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSLGKPDDYRYLSgctqyfanakteqlipgsqksknhqQKGPLKDPIID 311
Cdd:cd01383   159 KSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLN-------------------------QSNCLTIDGVD 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  312 DYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFeeipdDVRGGCQVSEASE-QSLTITSGLLGVDQTELRTAL 390
Cdd:cd01383   214 DAKKFHELKEALDTVGISKEDQEHIFQMLAAVLWLGNISF-----QVIDNENHVEVVAdEAVSTAASLLGCNANDLMLAL 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  391 VSRVMQSKGGgfkgtVIMVPLKIYEASNARDALAKAIYSRLFDRIVGLINQSipFQASNF----YIGVLDIAGFEYFTVN 466
Cdd:cd01383   289 STRKIQAGGD-----KIVKKLTLQQAIDARDALAKAIYASLFDWLVEQINKS--LEVGKRrtgrSISILDIYGFESFQKN 361
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  467 SFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITFTDNQDIIELIEAKSNGIFTLLDEESKLPKPSYSHFTAE 546
Cdd:cd01383   362 SFEQLCINYANERLQQHFNRHLFKLEQEEYELDGIDWTKVDFEDNQECLDLIEKKPLGLISLLDEESNFPKATDLTFANK 441
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  547 VhkswanhyrlglprSSRLKAHRTLRDEEG--FLVRHFAGAVCYNTEQFIEKNNDALHASLEGLVQECDNPLLQTL---- 620
Cdd:cd01383   442 L--------------KQHLKSNSCFKGERGgaFTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQLPQLFaskm 507
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  621 --------FPSGSSTSVRGKLnfiSVGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQFEGSLALAQLKCSGTISV 692
Cdd:cd01383   508 ldasrkalPLTKASGSDSQKQ---SVATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEV 584
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281362442  693 LELMEHGYPSRVLFADLYSMYKSVLPPEL-VSLPARTFCEAMFQSLNLSAKDFKFGITKVFFR 754
Cdd:cd01383   585 VRISRSGYPTRMTHQEFARRYGFLLPEDVsASQDPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
MYSc_Myo7 cd01381
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ...
71-754 0e+00

class VII myosin, motor domain; These monomeric myosins have been associated with functions in sensory systems such as vision and hearing. Mammalian myosin VII has a tail with 2 MyTH4 domains, 2 FERM domains, and a SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276832  Cd Length: 648  Bit Score: 598.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   71 ATFLDNLKTRYYKDKIYTYVANILIAVNPYrEIKELYAPDTIKKYNGRSLGELPPHVFAIADKAIRDMRVYKLSQSIIVS 150
Cdd:cd01381     1 AGILRNLLIRYREKLIYTYTGSILVAVNPY-QILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVIS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  151 GESGAGKTESTKYLLKYLCY---SHDSagpIETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEVHYDAKCQVVGGYISH 227
Cdd:cd01381    80 GESGAGKTESTKLILQYLAAisgQHSW---IEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKIEQ 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  228 YLLEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSLGKPDDYRYLSgctqyfanakteqlipgsqksknhqQKGPLKD 307
Cdd:cd01381   157 YLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLT-------------------------QGNCLTC 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  308 PIIDDYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEIPDDVRGGCQVSEASeqSLTITSGLLGVDQTELR 387
Cdd:cd01381   212 EGRDDAAEFADIRSAMKVLMFTDEEIWDIFKLLAAILHLGNIKFEATVVDNLDASEVRDPP--NLERAAKLLEVPKQDLV 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  388 TALVSRVMQSKGGgfkgTVImVPLKIYEASNARDALAKAIYSRLFDRIVGLINQSI----PFQASNFYIGVLDIAGFEYF 463
Cdd:cd01381   290 DALTTRTIFTRGE----TVV-SPLSAEQALDVRDAFVKGIYGRLFIWIVNKINSAIykprGTDSSRTSIGVLDIFGFENF 364
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  464 TVNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITFTDNQDIIELIEAKSNGIFTLLDEESKLPKPSYSHF 543
Cdd:cd01381   365 EVNSFEQLCINFANENLQQFFVRHIFKLEQEEYDKEGINWQHIEFVDNQDVLDLIALKPMNIMSLIDEESKFPKGTDQTM 444
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  544 TAEVHKSWANHyRLGLPRSSRLKAHrtlrdeegFLVRHFAGAVCYNTEQFIEKNNDALHASLEGLVQECDNPLLQTLFPS 623
Cdd:cd01381   445 LEKLHSTHGNN-KNYLKPKSDLNTS--------FGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNE 515
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  624 --GSSTSVRGKLnfISVGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQFEGSLALAQLKCSGTISVLELMEHGYP 701
Cdd:cd01381   516 diSMGSETRKKS--PTLSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYP 593
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 281362442  702 SRVLFADLYSMY----KSVLPPELVSLPA--RTFCEAMFqslnLSAKDFKFGITKVFFR 754
Cdd:cd01381   594 IRHTFEEFVERYrvlvPGIPPAHKTDCRAatRKICCAVL----GGDADYQLGKTKIFLK 648
MYSc_Myo4 cd14872
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ...
71-754 0e+00

class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or C-terminal to their motor domain and a tail with a MyTH4 domain followed by a SH3 domain in some instances. The monomeric Acanthamoebas were the first identified members of this group and have been joined by Stramenopiles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276839  Cd Length: 644  Bit Score: 560.55  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   71 ATFLDNLKTRYYKDKIYTYVANILIAVNPYREIKeLYAPDTIKKYNGRSLGELPPHVFAIADKAIRDMRVYKLSQSIIVS 150
Cdd:cd14872     1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLP-LYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILIS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  151 GESGAGKTESTKYLLKYLCYSHDSAGPIETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEVHYDAKCQVVGGYISHYLL 230
Cdd:cd14872    80 GESGAGKTEATKQCLSFFAEVAGSTNGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGASTENYLL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  231 EKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSLGKPDDYRYLSGCTQyfanakteqlIPGsqksknhqqkgplkdpiI 310
Cdd:cd14872   160 EKSRVVYQIKGERNFHIFYQLLASPDPASRGGWGSSAAYGYLSLSGCIE----------VEG-----------------V 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  311 DDYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEIpDDVRGGCQVSEASEQSLTITSGLLGVDQTELRTAL 390
Cdd:cd14872   213 DDVADFEEVVLAMEQLGFDDADINNVMSLIAAILKLGNIEFASG-GGKSLVSGSTVANRDVLKEVATLLGVDAATLEEAL 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  391 VSRVMQSKGGgfKGTVImvPLKIYEASNARDALAKAIYSRLFDRIVGLINQSIPFQ--ASNFYIGVLDIAGFEYFTVNSF 468
Cdd:cd14872   292 TSRLMEIKGC--DPTRI--PLTPAQATDACDALAKAAYSRLFDWLVKKINESMRPQkgAKTTFIGVLDIFGFEIFEKNSF 367
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  469 EQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITFTDNQDIIELIEAKSNGIFTLLDEESKLPKPSYSHFTAEVH 548
Cdd:cd14872   368 EQLCINFTNEKLQQHFNQYTFKLEEALYQSEGVKFEHIDFIDNQPVLDLIEKKQPGLMLALDDQVKIPKGSDATFMIAAN 447
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  549 KSWANhYRLGLPRSSRlkahrtlRDEEGFLVRHFAGAVCYNTEQFIEKNNDALHASLEGLVQECDNPLLQTLFPSGSSTS 628
Cdd:cd14872   448 QTHAA-KSTFVYAEVR-------TSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPPSEGDQ 519
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  629 VRGKlnfISVGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQFEGSLALAQLKCSGTISVLELMEHGYPSRVLFAD 708
Cdd:cd14872   520 KTSK---VTLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHER 596
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*...
gi 281362442  709 LYSMYKSVLPPELVSLPA--RTFCEAMFQSLNLSAKDFKFGITKVFFR 754
Cdd:cd14872   597 FLKRYRFLVKTIAKRVGPddRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
MYSc_Myo30 cd14891
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ...
71-754 0e+00

class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal SH3-like domain, two IQ motifs, a coiled-coil region and a PX domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276856  Cd Length: 645  Bit Score: 556.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   71 ATFLDNLKTRYYKD--KIYTYVANILIAVNPYREIKElyaPDtIKKYNGRSLGELPPHVFAIADKAIRDMRV---YKLSQ 145
Cdd:cd14891     1 AGILHNLEERSKLDnqRPYTFMANVLIAVNPLRRLPE---PD-KSDYINTPLDPCPPHPYAIAEMAYQQMCLgsgRMQNQ 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  146 SIIVSGESGAGKTESTKYLLKYLCY-----SHDSAGPIET--------------KILDANPVLEAFGNAKTTRNNNSSRF 206
Cdd:cd14891    77 SIVISGESGAGKTETSKIILRFLTTravggKKASGQDIEQsskkrklsvtsldeRLMDTNPILESFGNAKTLRNHNSSRF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  207 GKFIEVHYDA-KCQVVGGYISHYLLEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSLGKPDDYRYL--SGCTqyfan 283
Cdd:cd14891   157 GKFMKLQFTKdKFKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLnqSGCV----- 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  284 akteqlipgsqksknhqqkgplKDPIIDDYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEIpDDVRGGC- 362
Cdd:cd14891   232 ----------------------SDDNIDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEE-DTSEGEAe 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  363 QVSEASEQSLTITSGLLGVDQTELRTALVSRVMQSKGGGFKgtvimVPLKIYEASNARDALAKAIYSRLFDRIVGLINQS 442
Cdd:cd14891   289 IASESDKEALATAAELLGVDEEALEKVITQREIVTRGETFT-----IKRNAREAVYSRDAIAKSIYERLFLWIVQQINTS 363
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  443 IPFQASNF-YIGVLDIAGFEYF-TVNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITFTDNQDIIELIEA 520
Cdd:cd14891   364 LGHDPDPLpYIGVLDIFGFESFeTKNDFEQLLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWPDNRECLDLIAS 443
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  521 KSNGIFTLLDEESKLPKPSYSHFTAEVHKSWANHYRLGLPRSSRLKahrtlrdeEGFLVRHFAGAVCYNTEQFIEKNNDA 600
Cdd:cd14891   444 KPNGILPLLDNEARNPNPSDAKLNETLHKTHKRHPCFPRPHPKDMR--------EMFIVKHYAGTVSYTIGSFIDKNNDI 515
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  601 LHASLEglvqecdnpllqtlfpsgsstsvrgklNFISVGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQFEGSLA 680
Cdd:cd14891   516 IPEDFE---------------------------DLLASSAKFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYV 568
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281362442  681 LAQLKCSGTISVLELMEHGYPSRVLFADLYSMYKSVLPPE---LVSLPARTFCEAMFQSLNLSAKDFKFGITKVFFR 754
Cdd:cd14891   569 VDQLRCSGILQTCEVLKVGLPTRVTYAELVDVYKPVLPPSvtrLFAENDRTLTQAILWAFRVPSDAYRLGRTRVFFR 645
MYSc_Myo29 cd14890
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ...
71-754 0e+00

class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have very long tail domains consisting of three IQ motifs, short coiled-coil regions, up to 18 CBS domains, a PB1 domain, and a carboxy-terminal transmembrane domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276855 [Multi-domain]  Cd Length: 662  Bit Score: 553.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   71 ATFLDNLKTRYYKDKIYTYVANILIAVNPYREIKELYAPDTIKKYNGRSLGELPPHVFAIADKA----IRDMRVYKLSQS 146
Cdd:cd14890     1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPDLYSEERMLLYHGTTAGELPPHVFAIADHAytqlIQSGVLDPSNQS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  147 IIVSGESGAGKTESTKYLLKYLC----YSHDSAGP---------------IETKILDANPVLEAFGNAKTTRNNNSSRFG 207
Cdd:cd14890    81 IIISGESGAGKTEATKIIMQYLAritsGFAQGASGegeaaseaieqtlgsLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  208 KFIEVHYDAKCQVVGGYISHYLLEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSLGKPDDY-RYLSGCTQyfanakt 286
Cdd:cd14890   161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYfYLRGECSS------- 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  287 eqlIPGSqksknhqqkgplkdpiiDDYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEIPDDVRGGCqvsE 366
Cdd:cd14890   234 ---IPSC-----------------DDAKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLED---A 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  367 ASEQSLTITSGLLGVDQTELRTALVSRVMQskgggFKGTVIMVPLKIYEASNARDALAKAIYSRLFDRIVGLINQSIPFQ 446
Cdd:cd14890   291 TTLQSLKLAAELLGVNEDALEKALLTRQLF-----VGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSP 365
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  447 ASNF-YIGVLDIAGFEYFTVNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITFTDNQDIIELIEAKSN-- 523
Cdd:cd14890   366 DDKWgFIGVLDIYGFEKFEWNTFEQLCINYANEKLQRHFNQHMFEVEQVEYSNEGIDWQYITFNDNQACLELIEGKVNgk 445
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  524 -GIFTLLDEESKLPKPSYS-HFTAEVHKSW--------ANHYRLGLPR--SSRLKAHRTlrdeegFLVRHFAGAVCYNTE 591
Cdd:cd14890   446 pGIFITLDDCWRFKGEEANkKFVSQLHASFgrksgsggTRRGSSQHPHfvHPKFDADKQ------FGIKHYAGDVIYDAS 519
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  592 QFIEKNNDALHASLEGLVQEcdnpllqtlfpsgSSTSVRGklnfISVGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMI 671
Cdd:cd14890   520 GFNEKNNETLNAEMKELIKQ-------------SRRSIRE----VSVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKA 582
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  672 DRQFEGSLALAQLKCSGTISVLELMEHGYPSRVLFADLYSMYKSVLPP-----ELVslpartfcEAMFQSLNLSAKDFKF 746
Cdd:cd14890   583 PGKFDGLDCLRQLKYSGMMEAIQIRQQGFALREEHDSFFYDFQVLLPTaenieQLV--------AVLSKMLGLGKADWQI 654

                  ....*...
gi 281362442  747 GITKVFFR 754
Cdd:cd14890   655 GSSKIFLK 662
MYSc_Myo36 cd14897
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ...
71-754 3.53e-179

class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain followed by a GlcAT-I (Beta1,3-glucuronyltransferase I) domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276862 [Multi-domain]  Cd Length: 635  Bit Score: 543.13  E-value: 3.53e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   71 ATFLDNLKTRYYKDKIYTYVANILIAVNPYREIkELYAPDTIKKYNGRSL-GELPPHVFAIADKAIRDMRVYKLSQSIIV 149
Cdd:cd14897     1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPL-PIFDKKHHEEYSNLSVrSQRPPHLFWIADQAYRRLLETGRNQCILV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  150 SGESGAGKTESTKYLLKYLCYSHDSAGP-IETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEVHYDAKCQVVGGYISHY 228
Cdd:cd14897    80 SGESGAGKTESTKYMIKHLMKLSPSDDSdLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAKIDDY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  229 LLEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSLGKPDDYRYLSGCTQYFANAK-TEQLipgsqksKNHQQKgplkd 307
Cdd:cd14897   160 LLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILRDDNRNRPVFNdSEEL-------EYYRQM----- 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  308 piiddyqhFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEiPDDVRGgcqVSEASEQSLTITSGLLGVDQTELR 387
Cdd:cd14897   228 --------FHDLTNIMKLIGFSEEDISVIFTILAAILHLTNIVFIP-DEDTDG---VTVADEYPLHAVAKLLGIDEVELT 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  388 TALVSRVMQskgggFKGTVIMVPLKIYEASNARDALAKAIYSRLFDRIVGLINQSIPFQ------ASNFYIGVLDIAGFE 461
Cdd:cd14897   296 EALISNVNT-----IRGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLWPDkdfqimTRGPSIGILDMSGFE 370
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  462 YFTVNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITFTDNQDIIELIEAKSNGIFTLLDEESKLPKPSYS 541
Cdd:cd14897   371 NFKINSFDQLCINLSNERLQQYFNDYVFPRERSEYEIEGIEWRDIEYHDNDDVLELFFKKPLGILPLLDEESTFPQSTDS 450
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  542 HFTAEVHKSWANHYRLGLPRSSRLKahrtlrdeegFLVRHFAGAVCYNTEQFIEKNNDALHASLEGLVQECDNPLLQTLF 621
Cdd:cd14897   451 SLVQKLNKYCGESPRYVASPGNRVA----------FGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLF 520
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  622 PsgsstsvrgklnfisvgSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQFEGSLALAQLKCSGTISVLELMEHGYP 701
Cdd:cd14897   521 T-----------------SYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYP 583
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....
gi 281362442  702 SRVLFADLYSMYKSVLP-PELVSLPARTFCEAMFQSLNLsaKDFKFGITKVFFR 754
Cdd:cd14897   584 IRIKYEDFVKRYKEICDfSNKVRSDDLGKCQKILKTAGI--KGYQFGKTKVFLK 635
MYSc_Myo27 cd14888
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ...
71-754 4.20e-176

class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276853 [Multi-domain]  Cd Length: 667  Bit Score: 536.20  E-value: 4.20e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   71 ATFLDNLKTRYYKDKIYTYVANILIAVNPYREIKELYAPDTIKKYNGRSlGELPPHVFAIADKAIRDMRVYKLSQSIIVS 150
Cdd:cd14888     1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPGLYSDEMLLKFIQPS-ISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  151 GESGAGKTESTKYLLKYLC----YSHDSAGPIETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEVHYD---------AK 217
Cdd:cd14888    80 GESGAGKTESTKYVMKFLAcagsEDIKKRSLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSklkskrmsgDR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  218 CQVVGGYISHYLLEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSLGKPDDYRYLSGCTQYFANAKTeqlipgSQKSK 297
Cdd:cd14888   160 GRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYEENDEKLAKGADAKPISIDMS------SFEPH 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  298 NHQQK----GPLKDPIIDDYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEiPDDVRGGCQVSEASEQSLT 373
Cdd:cd14888   234 LKFRYltksSCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFEN-NEACSEGAVVSASCTDDLE 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  374 ITSGLLGVDQTELRTALVSRVMQSKGGGFKGtvimvPLKIYEASNARDALAKAIYSRLFDRIVGLINQSIPF--QASNFY 451
Cdd:cd14888   313 KVASLLGVDAEDLLNALCYRTIKTAHEFYTK-----PLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYskDNSLLF 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  452 IGVLDIAGFEYFTVNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITFTDNQDIIELIEAKSNGIFTLLDE 531
Cdd:cd14888   388 CGVLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFPDNQDCVDLLQEKPLGIFCMLDE 467
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  532 ESKLPKPSYSHFTAEVHKSWANHyrlglprsSRLKAHRTlrDEEGFLVRHFAGAVCYNTEQFIEKNNDALHASLEGLVQE 611
Cdd:cd14888   468 ECFVPGGKDQGLCNKLCQKHKGH--------KRFDVVKT--DPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKN 537
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  612 CDNPLLQTLFPS--GSSTSVRGKLN-FISVGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQFEGSLALAQLKCSG 688
Cdd:cd14888   538 SKNPFISNLFSAylRRGTDGNTKKKkFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGG 617
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281362442  689 TISVLELMEHGYPSRVLFADLYSMYKSVLPPElvslpartfceamfqsLNLSAKDFKFGITKVFFR 754
Cdd:cd14888   618 VLQAVQVSRAGYPVRLSHAEFYNDYRILLNGE----------------GKKQLSIWAVGKTLCFFK 667
MYSc_Myo10 cd14873
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ...
71-754 6.84e-170

class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a monomer. In mammalian cells, the motor is found to localize to filopodia. Myosin X walks towards the barbed ends of filaments and is thought to walk on bundles of actin, rather than single filaments, a unique behavior. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are a variable number of IQ domains, 2 PH domains, a MyTH4 domain, and a FERM domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276840 [Multi-domain]  Cd Length: 651  Bit Score: 519.35  E-value: 6.84e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   71 ATFLDNLKTRYYKDKIYTYVANILIAVNPYREIKELYAPDTIKKYNGRSLGELPPHVFAIADKAIRDMRVYKLSQSIIVS 150
Cdd:cd14873     1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAGLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  151 GESGAGKTESTKYLLKYLCY-SHDSAGP--------IETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEVHYDAKCQVV 221
Cdd:cd14873    81 GESGAGKTESTKLILKFLSViSQQSLELslkektscVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  222 GGYISHYLLEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSLGKPDDYRYLSgctqyfanakteqlipgsqksknhqQ 301
Cdd:cd14873   161 GGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLN-------------------------Q 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  302 KGPLKDPIIDDYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEeipddVRGGCQVSeaSEQSLTITSGLLGV 381
Cdd:cd14873   216 SGCVEDKTISDQESFREVITAMEVMQFSKEEVREVSRLLAGILHLGNIEFI-----TAGGAQVS--FKTALGRSAELLGL 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  382 DQTELRTALVSRVMQskgggFKGTVIMVPLKIYEASNARDALAKAIYSRLFDRIVGLINQSIPFQASNFYIGVLDIAGFE 461
Cdd:cd14873   289 DPTQLTDALTQRSMF-----LRGEEILTPLNVQQAVDSRDSLAMALYARCFEWVIKKINSRIKGKEDFKSIGILDIFGFE 363
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  462 YFTVNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITFTDNQDIIELIEAKSnGIFTLLDEESKLPKPSYS 541
Cdd:cd14873   364 NFEVNHFEQFNINYANEKLQEYFNKHIFSLEQLEYSREGLVWEDIDWIDNGECLDLIEKKL-GLLALINEESHFPQATDS 442
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  542 HFTAEVHKSWANHYRLGLPRSSrlkahrtlrdEEGFLVRHFAGAVCYNTEQFIEKNNDALHASLEGLVQECDNPLLQTLF 621
Cdd:cd14873   443 TLLEKLHSQHANNHFYVKPRVA----------VNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLF 512
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  622 PSGSSTSVRGKLNFIS------VGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQFEGSLALAQLKCSGTISVLEL 695
Cdd:cd14873   513 EHVSSRNNQDTLKCGSkhrrptVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRI 592
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 281362442  696 MEHGYPSRVLFADLYSMYKSVLPPELVSLPARTFCEAMFQSLNLSAKDFKFGITKVFFR 754
Cdd:cd14873   593 RKAGYAVRRPFQDFYKRYKVLMRNLALPEDVRGKCTSLLQLYDASNSEWQLGKTKVFLR 651
MYSc_Myo42 cd14903
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ...
71-754 8.41e-170

class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276868 [Multi-domain]  Cd Length: 658  Bit Score: 519.33  E-value: 8.41e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   71 ATFLDNLKTRYYKDKIYTYVANILIAVNPYREIKELYAPDTIKKYNGRSLGELPPHVFAIADKAIRDMRVYKLSQSIIVS 150
Cdd:cd14903     1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPELYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  151 GESGAGKTESTKYLLKYLCY----SHDSagpIETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEVHYDAKCQVVGGYIS 226
Cdd:cd14903    81 GESGAGKTETTKILMNHLATiaggLNDS---TIKKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLVGAKCR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  227 HYLLEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSLGkpDDYRYlsgctqyfANAKTEQLIPGsqksknhqqkgplk 306
Cdd:cd14903   158 TYLLEKTRVISHERPERNYHIFYQLLASPDVEERLFLDSA--NECAY--------TGANKTIKIEG-------------- 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  307 dpiIDDYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEIPDDVRGgcQVSEASEQSLTITSGLLGVDQTEL 386
Cdd:cd14903   214 ---MSDRKHFARTKEALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEK--SAIAPGDQGAVYATKLLGLSPEAL 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  387 RTALVSRVMQSkgggfKGTVIMVPLKIYEASNARDALAKAIYSRLFDRIVGLINQSIPFQA-SNFYIGVLDIAGFEYFTV 465
Cdd:cd14903   289 EKALCSRTMRA-----AGDVYTVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAkMANHIGVLDIFGFEHFKH 363
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  466 NSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITFTDNQDIIELIEAKSnGIFTLLDEESKLPKPSYSHFTA 545
Cdd:cd14903   364 NSFEQFCINYANEKLQQKFTQDVFKTVQIEYEEEGIRWAHIDFADNQDVLAVIEDRL-GIISLLNDEVMRPKGNEESFVS 442
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  546 EV---HKSWANhyRLGLPRSSRLKahrtlrdeegFLVRHFAGAVCYNTEQFIEKNNDALHASLEGLVQECDNPLLQTLF- 621
Cdd:cd14903   443 KLssiHKDEQD--VIEFPRTSRTQ----------FTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFk 510
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  622 -----PSGSSTSVR--------GKLNFISVGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQFEGSLALAQLKCSG 688
Cdd:cd14903   511 ekvesPAAASTSLArgarrrrgGALTTTTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAG 590
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281362442  689 TISVLELMEHGYPSRVLFADLYSMYKSVLPP-ELVSLPARTFCEAMFQSLNL-SAKDFKFGITKVFFR 754
Cdd:cd14903   591 VIEAIRISRAAYPNRLLHEEFLDKFWLFLPEgRNTDVPVAERCEALMKKLKLeSPEQYQMGLTRIYFQ 658
MYSc_Myo15 cd01387
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ...
71-754 2.73e-168

class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, myosin XV appears to be expressed in sensory tissue and play a role in hearing. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are 2 MyTH4 domain, a FERM domain, and a SH3 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276838 [Multi-domain]  Cd Length: 657  Bit Score: 515.46  E-value: 2.73e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   71 ATFLDNLKTRYYKDKIYTYVANILIAVNPYREIkELYAPDTIKKYNGRSLGELPPHVFAIADKAIRDMRVYKLSQSIIVS 150
Cdd:cd01387     1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMF-DIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVIS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  151 GESGAGKTESTKYLLKYLCYSHDSAG-PIETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEVHYDaKCQVVGGYISHYL 229
Cdd:cd01387    80 GESGSGKTEATKLIMQYLAAVNQRRNnLVTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFFE-GGVIVGAITSQYL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  230 LEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSLGKPDDYRYLSgctqyfanakteqlipgsqksknhqQKGPLKDPI 309
Cdd:cd01387   159 LEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLN-------------------------QGGNCEIAG 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  310 IDDYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEIPD-DVRGGCQVSEASEqsLTITSGLLGVDQTELRT 388
Cdd:cd01387   214 KSDADDFRRLLAAMQVLGFSSEEQDSIFRILASVLHLGNVYFHKRQLrHGQEGVSVGSDAE--IQWVAHLLQISPEGLQK 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  389 ALVSRVMQSKGggfkgTVIMVPLKIYEASNARDALAKAIYSRLFDRIVGLINQSI--PFQaSNFYIGVLDIAGFEYFTVN 466
Cdd:cd01387   292 ALTFKVTETRR-----ERIFTPLTIDQALDARDAIAKALYALLFSWLVTRVNAIVysGTQ-DTLSIAILDIFGFEDLSEN 365
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  467 SFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITFTDNQDIIELIEAKSNGIFTLLDEESKLPKPSYSHFTAE 546
Cdd:cd01387   366 SFEQLCINYANENLQYYFNKHVFKLEQEEYIREQIDWTEIAFADNQPVINLISKKPVGILHILDDECNFPQATDHSFLEK 445
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  547 VHkswANHyrlglpRSSRLKAHRTLRDEEgFLVRHFAGAVCYNTEQFIEKNNDALHASLEGLVQECDNPLLQTLF----- 621
Cdd:cd01387   446 CH---YHH------ALNELYSKPRMPLPE-FTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFsshra 515
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  622 ------PSGS-STSVRGKLNFISVGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQFEGSLALAQLKCSGTISVLE 694
Cdd:cd01387   516 qtdkapPRLGkGRFVTMKPRTPTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIR 595
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281362442  695 LMEHGYPSRVLFADLYSMYKSVLPPELVSLPARTFCEAMFQSLNLSA--KDFKFGITKVFFR 754
Cdd:cd01387   596 IRKEGYPVRLPFQVFIDRYRCLVALKLPRPAPGDMCVSLLSRLCTVTpkDMYRLGATKVFLR 657
MYSc_Myo9 cd01385
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ...
71-754 5.98e-165

class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play a role in signalling. It has a N-terminal RA domain, an IQ domain, a C1_1 domain, and a RhoGAP domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276836 [Multi-domain]  Cd Length: 690  Bit Score: 507.68  E-value: 5.98e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   71 ATFLDNLKTRYYKDKIYTYVANILIAVNPYReIKELYAPDTIKKYNGRSLGELPPHVFAIADKAIRDMRVYKLSQSIIVS 150
Cdd:cd01385     1 QTLLENLRARFKHGKIYTYVGSILIAVNPFK-FLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVIS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  151 GESGAGKTESTKYLLKYLCY-SHDSAGP-IETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEVHYDAKCQVVGGYISHY 228
Cdd:cd01385    80 GESGSGKTESTNFLLHHLTAlSQKGYGSgVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVEKY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  229 LLEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSLGKPDDYRYLSgctqyfanakteqlipgsqKSKNHQQKGplkdp 308
Cdd:cd01385   160 LLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLN-------------------QSDCYTLEG----- 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  309 iIDDYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFeeIPDDVRGGCQVSEASEQSLTITSGLLGVDQTELRT 388
Cdd:cd01385   216 -EDEKYEFERLKQAMEMVGFLPETQRQIFSVLSAVLHLGNIEY--KKKAYHRDESVTVGNPEVLDIISELLRVKEETLLE 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  389 ALVSRVMQSKGggfkGTVIMvPLKIYEASNARDALAKAIYSRLFDRIVGLINQSI-----PFQASNFYIGVLDIAGFEYF 463
Cdd:cd01385   293 ALTTKKTVTVG----ETLIL-PYKLPEAIATRDAMAKCLYSALFDWIVLRINHALlnkkdLEEAKGLSIGVLDIFGFEDF 367
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  464 TVNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITFTDNQDIIELIEAKSNGIFTLLDEESKLPKPsySHF 543
Cdd:cd01385   368 GNNSFEQFCINYANEHLQYYFNQHIFKLEQEEYKKEGISWHNIEYTDNTGCLQLISKKPTGLLCLLDEESNFPGA--TNQ 445
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  544 T-----AEVHKSwaNHYRLGLPRSsrlkahrtlrdEEGFLVRHFAGAVCYNTEQFIEKNND------------------- 599
Cdd:cd01385   446 TllakfKQQHKD--NKYYEKPQVM-----------EPAFIIAHYAGKVKYQIKDFREKNLDlmrpdivavlrssssafvr 512
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  600 ------------------------ALHASLEGLVQECDNPLLQTLFPSGSSTSVRGKLN-FISVGSKFKTQLGELMEKLE 654
Cdd:cd01385   513 eligidpvavfrwavlrafframaAFREAGRRRAQRTAGHSLTLHDRTTKSLLHLHKKKkPPSVSAQFQTSLSKLMETLG 592
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  655 QNGTNFIRCIKPNSKMIDRQFEGSLALAQLKCSGTISVLELMEHGYPSRVLFADLYSMYKSVLPPELVSLPARTFceAMF 734
Cdd:cd01385   593 QAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVLLPKGLISSKEDIK--DFL 670
                         730       740
                  ....*....|....*....|
gi 281362442  735 QSLNLSAKDFKFGITKVFFR 754
Cdd:cd01385   671 EKLNLDRDNYQIGKTKVFLK 690
MYSc_Myo31 cd14892
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ...
71-754 8.49e-162

class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of 17 IQ motifs and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276857 [Multi-domain]  Cd Length: 656  Bit Score: 498.52  E-value: 8.49e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   71 ATFLDNLKTRYYKDKIYTYVANILIAVNPYREIKELY---APDTIKKY-NGRSLGelPPHVFAIADKAIRDMRV----YK 142
Cdd:cd14892     1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYdvpGFDSQRKEeATASSP--PPHVFSIAERAYRAMKGvgkgQG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  143 LSQSIIVSGESGAGKTESTKYLLKYLC-YSHDSAGP------------IETKILDANPVLEAFGNAKTTRNNNSSRFGKF 209
Cdd:cd14892    79 TPQSIVVSGESGAGKTEASKYIMKYLAtASKLAKGAstskgaanahesIEECVLLSNLILEAFGNAKTIRNDNSSRFGKY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  210 IEVHYDAKCQVVGGYISHYLLEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSLGKPDDYRYLS--GCTQYFAnakte 287
Cdd:cd14892   159 IQIHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNqgNCVEVDG----- 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  288 qlipgsqksknhqqkgplkdpiIDDYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEIPDDVRGGCQVSEA 367
Cdd:cd14892   234 ----------------------VDDATEFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDVFAQSADG 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  368 SeqSLTITSGLLGVDQTELRTALVSRVMQSKgggfKGTVIMVPLKIYEASNARDALAKAIYSRLFDRIVGLINQSIPFQA 447
Cdd:cd14892   292 V--NVAKAAGLLGVDAAELMFKLVTQTTSTA----RGSVLEIKLTAREAKNALDALCKYLYGELFDWLISRINACHKQQT 365
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  448 SNF-----------YIGVLDIAGFEYFTVNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITFTDNQDIIE 516
Cdd:cd14892   366 SGVtggaasptfspFIGILDIFGFEIMPTNSFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQDNQDCLD 445
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  517 LIEAKSNGIFTLLDEESKLP-KPSYSHFTAEVHKswaNHyrlgLPRSSRLKAHRTLRDEegFLVRHFAGAVCYNTEQFIE 595
Cdd:cd14892   446 LIQKKPLGLLPLLEEQMLLKrKTTDKQLLTIYHQ---TH----LDKHPHYAKPRFECDE--FVLRHYAGDVTYDVHGFLA 516
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  596 KNNDALHASLEGLVQEcdnpllqtlfpsgsstsvrgklnfisvGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQF 675
Cdd:cd14892   517 KNNDNLHDDLRDLLRS---------------------------SSKFRTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGF 569
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  676 EGSLALAQLKCSGTISVLELMEHGYPSRVLFADLYSMYKSVL---------PPELVSLPARTFCEAMFQSlNLSAKDFKF 746
Cdd:cd14892   570 SCELVRDQLIYSGVLEVVRIRREGFPIRRQFEEFYEKFWPLArnkagvaasPDACDATTARKKCEEIVAR-ALERENFQL 648

                  ....*...
gi 281362442  747 GITKVFFR 754
Cdd:cd14892   649 GRTKVFLR 656
MYSc_Myo46 cd14907
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ...
71-713 1.06e-160

class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276872 [Multi-domain]  Cd Length: 669  Bit Score: 496.09  E-value: 1.06e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   71 ATFLDNLKTRYYKDKIYTYVANILIAVNPYREIKELYAPDTIKKY------NGRS--LGELPPHVFAIADKAIRDMRVYK 142
Cdd:cd14907     1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDNLFSEEVMQMYkeqiiqNGEYfdIKKEPPHIYAIAALAFKQLFENN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  143 LSQSIIVSGESGAGKTESTKYLLKYLCYSHD--------------------SAGPIETKILDANPVLEAFGNAKTTRNNN 202
Cdd:cd14907    81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQqeqnseevltltssiratskSTKSIEQKILSCNPILEAFGNAKTVRNDN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  203 SSRFGKFIEVHYDAKCQ-VVGGYISHYLLEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSLgKPDDYRYLSgctqYF 281
Cdd:cd14907   161 SSRFGKYVSILVDKKKRkILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGL-KNQLSGDRY----DY 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  282 ANakteqlipgsqKSKNHQQKgplkdpIIDDYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEIPDDVRGG 361
Cdd:cd14907   236 LK-----------KSNCYEVD------TINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTLDDNSP 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  362 CQVSeaSEQSLTITSGLLGVDQTELRTALVSRVMQSKGGgfkgtVIMVPLKIYEASNARDALAKAIYSRLFDRIVGLINQ 441
Cdd:cd14907   299 CCVK--NKETLQIIAKLLGIDEEELKEALTTKIRKVGNQ-----VITSPLSKKECINNRDSLSKELYDRLFNWLVERLND 371
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  442 SI---------PFQASNFYIGVLDIAGFEYFTVNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLN--VPEITFTD 510
Cdd:cd14907   372 TImpkdekdqqLFQNKYLSIGLLDIFGFEVFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdyLNQLSYTD 451
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  511 NQDIIELIEAKSNGIFTLLDEESKLPKPSYSHFTAEVHKSWANHYRLGLPRSSRlkahrtlrdEEGFLVRHFAGAVCYNT 590
Cdd:cd14907   452 NQDVIDLLDKPPIGIFNLLDDSCKLATGTDEKLLNKIKKQHKNNSKLIFPNKIN---------KDTFTIRHTAKEVEYNI 522
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  591 EQFIEKNNDALHASLEGLVQECDNPLLQTLF---------PSGSSTSVRGKLNFIsvGSKFKTQLGELMEKLEQNGTNFI 661
Cdd:cd14907   523 EGFREKNKDEISQSIINCIQNSKNRIISSIFsgedgsqqqNQSKQKKSQKKDKFL--GSKFRNQMKQLMNELMQCDVHFI 600
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|..
gi 281362442  662 RCIKPNSKMIDRQFEGSLALAQLKCSGTISVLELMEHGYPSRVLFADLYSMY 713
Cdd:cd14907   601 RCIKPNEEKKADLFIQGYVLNQIRYLGVLESIRVRKQGYPYRKSYEDFYKQY 652
PTZ00014 PTZ00014
myosin-A; Provisional
56-830 4.18e-157

myosin-A; Provisional


Pssm-ID: 240229 [Multi-domain]  Cd Length: 821  Bit Score: 491.85  E-value: 4.18e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   56 PQDHDDNCELMLLNEATFLDNLKTRYYKDKIYTYVANILIAVNPYREIKeLYAPDTIKKY-NGRSLGELPPHVFAIADKA 134
Cdd:PTZ00014   95 PMTYGDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLG-NTTNDWIRRYrDAKDSDKLPPHVFTTARRA 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  135 IRDMRVYKLSQSIIVSGESGAGKTESTKYLLKYLCYSH--DSAGPIETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEV 212
Cdd:PTZ00014  174 LENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFASSKsgNMDLKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQL 253
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  213 HYDAKCQVVGGYISHYLLEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSLGKPDDYRYLS-GCTQyfanakteqlIP 291
Cdd:PTZ00014  254 QLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINpKCLD----------VP 323
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  292 GsqksknhqqkgplkdpiIDDYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEIpdDVRGGCQVSEASEQS 371
Cdd:PTZ00014  324 G-----------------IDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGK--EEGGLTDAAAISDES 384
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  372 LTI---TSGLLGVDQTELRTALvsrVMQSKGGGfkGTVIMVPLKIYEASNARDALAKAIYSRLFDRIVGLINQSI-PFQA 447
Cdd:PTZ00014  385 LEVfneACELLFLDYESLKKEL---TVKVTYAG--NQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIePPGG 459
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  448 SNFYIGVLDIAGFEYFTVNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITFTDNQDIIELIEAKSNGIFT 527
Cdd:PTZ00014  460 FKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGKSVLS 539
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  528 LLDEESKLPKPSYSHFTAEVHKSWANHYRLglprssrLKAHRTLRdeEGFLVRHFAGAVCYNTEQFIEKNNDALHASLEG 607
Cdd:PTZ00014  540 ILEDQCLAPGGTDEKFVSSCNTNLKNNPKY-------KPAKVDSN--KNFVIKHTIGDIQYCASGFLFKNKDVLRPELVE 610
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  608 LVQECDNPLLQTLFPSGSSTsvRGKL---NFIsvGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQFEGSLALAQL 684
Cdd:PTZ00014  611 VVKASPNPLVRDLFEGVEVE--KGKLakgQLI--GSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQL 686
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  685 KCSGTISVLELMEHGYPSRVLFADLYSMYKSV-LP-PELVSLPARTFCEAMFQSLNLSAKDFKFGITKVFFRPGKFVEFD 762
Cdd:PTZ00014  687 HSLSILEALQLRQLGFSYRRTFAEFLSQFKYLdLAvSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLKKDAAKELT 766
                         730       740       750       760       770       780
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281362442  763 RIMRSdpenmlaivaKVKKWlirsRWVKSALGALCV-IKLRNRIIYRNKCVLIAQRIARGFLARKQHRP 830
Cdd:PTZ00014  767 QIQRE----------KLAAW----EPLVSVLEALILkIKKKRKVRKNIKSLVRIQAHLRRHLVIAEIKP 821
MYSc_Myo3 cd01379
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ...
72-754 6.20e-157

class III myosin, motor domain; Myosin III has been shown to play a role in the vision process in insects and in hearing in mammals. Myosin III, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They are characterized by an N-terminal protein kinase domain and several IQ domains. Some members also contain WW, SH2, PH, and Y-phosphatase domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276830 [Multi-domain]  Cd Length: 633  Bit Score: 484.86  E-value: 6.20e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   72 TFLDNLKTRYYKDKIYTYVANILIAVNPYREIKeLYAPDTIKKYNGRSLGELPPHVFAIADKAIRDMRVYKLSQSIIVSG 151
Cdd:cd01379     2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLG-IYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  152 ESGAGKTESTKYLLKYLCY-SHDSAGPIETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEVHYDAKCQVVGGYISHYLL 230
Cdd:cd01379    81 ESGAGKTESANLLVQQLTVlGKANNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEYLL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  231 EKSRICTQSAEERNYHVFYMLLAG--APQQLRD-KLSLGKPDDYRYLSGCTqyfanakteqLIPGSQKSKNHQQkgplkd 307
Cdd:cd01379   161 EKSRVVHQAIGERNFHIFYYIYAGlaEDKKLAKyKLPENKPPRYLQNDGLT----------VQDIVNNSGNREK------ 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  308 piiddyqhFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEIPDDVRGGCQVSEASEQSLTITSGLLGVDQTELR 387
Cdd:cd01379   225 --------FEEIEQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTEVESNHQTDKSSRISNPEALNNVAKLLGIEADELQ 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  388 TALVSRVMQSKGggfkgTVIMVPLKIYEASNARDALAKAIYSRLFDRIVGLINQSIPFQASNFY----IGVLDIAGFEYF 463
Cdd:cd01379   297 EALTSHSVVTRG-----ETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLKPDRSASDeplsIGILDIFGFENF 371
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  464 TVNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITFTDNQDIIELIEAKSNGIFTLLDEESKLPKPSYSHF 543
Cdd:cd01379   372 QKNSFEQLCINIANEQIQYYFNQHIFAWEQQEYLNEGIDVDLIEYEDNRPLLDMFLQKPMGLLALLDEESRFPKATDQTL 451
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  544 TAEVHKSWANHYRLglprssrlkahRTLRDEEGFLVRHFAGAVCYNTEQFIEKNNDALHASLEGLVQECDNPLLQTlfps 623
Cdd:cd01379   452 VEKFHNNIKSKYYW-----------RPKSNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVRQ---- 516
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  624 gsstsvrgklnfiSVGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQFEGSLALAQLKCSGTISVLELMEHGYPSR 703
Cdd:cd01379   517 -------------TVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHR 583
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 281362442  704 VLFADL---YSM--YKSVLPPElvslPARTFCEAMFQSLNLSakDFKFGITKVFFR 754
Cdd:cd01379   584 ILFADFlkrYYFlaFKWNEEVV----ANRENCRLILERLKLD--NWALGKTKVFLK 633
MYSc_Myo40 cd14901
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ...
71-752 3.31e-155

class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276866 [Multi-domain]  Cd Length: 655  Bit Score: 481.21  E-value: 3.31e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   71 ATFLDNLKTRYYKDKIYTYVANILIAVNPYREIKeLYAPDTIKKY--NGRS----LGELPPHVFAIADKAIRDM----RV 140
Cdd:cd14901     1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLP-LYDDETKEAYyeHGERraagERKLPPHVYAVADKAFRAMlfasRG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  141 YKLSQSIIVSGESGAGKTESTKYLLKYLCY-----SHDSAGP----IETKILDANPVLEAFGNAKTTRNNNSSRFGKFIE 211
Cdd:cd14901    80 QKCDQSILVSGESGAGKTETTKIIMNYLASvssatTHGQNATerenVRDRVLESNPILEAFGNARTNRNNNSSRFGKFIR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  212 VHYDAKCQVVGGYISHYLLEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSLGKPDDYRYLsgctqyfanakteqlip 291
Cdd:cd14901   160 LGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYL----------------- 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  292 gsqkskNHQQKGPLKDPIiDDYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFeeIPDDVRGGcQVSEASEQS 371
Cdd:cd14901   223 ------NSSQCYDRRDGV-DDSVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCF--VKKDGEGG-TFSMSSLAN 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  372 LTITSGLLGVDQTELRTALVSRVMQSkGGGFkgtvIMVPLKIYEASNARDALAKAIYSRLFDRIVGLINQSIPFQASNF- 450
Cdd:cd14901   293 VRAACDLLGLDMDVLEKTLCTREIRA-GGEY----ITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGa 367
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  451 --YIGVLDIAGFEYFTVNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITFTDNQDIIELIEAKSNGIFTL 528
Cdd:cd14901   368 srFIGIVDIFGFEIFATNSLEQLCINFANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYPNNDACVAMFEARPTGLFSL 447
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  529 LDEESKLPKPSYSHFTAEVHKSWANHYRLGLPRSSRLKAHrtlrdeegFLVRHFAGAVCYNTEQFIEKNNDALHASLEGL 608
Cdd:cd14901   448 LDEQCLLPRGNDEKLANKYYDLLAKHASFSVSKLQQGKRQ--------FVIHHYAGAVCYATDGFCDKNKDHVHSEALAL 519
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  609 VQECDNPLLQTlfpsgsstsvrgklnfiSVGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQFEGSLALAQLKCSG 688
Cdd:cd14901   520 LRTSSNAFLSS-----------------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSG 582
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281362442  689 TISVLELMEHGYPSRVLFADLYSMYKSVLPP------ELVSLPARTFCEAMFQSLNLSAKD-FKFGITKVF 752
Cdd:cd14901   583 VLEAVKISRSGYPVRFPHDAFVHTYSCLAPDgasdtwKVNELAERLMSQLQHSELNIEHLPpFQVGKTKVF 653
MYSc_Myo43 cd14904
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ...
71-754 1.78e-149

class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276869  Cd Length: 653  Bit Score: 465.96  E-value: 1.78e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   71 ATFLDNLKTRYYKDKIYTYVANILIAVNPYREIKELYAPDTIKKYNGRSLGELPPHVFAIADKAIRDMRVYKLSQSIIVS 150
Cdd:cd14904     1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDNLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  151 GESGAGKTESTKYLLKYLCyshDSAGPIE----TKILDANPVLEAFGNAKTTRNNNSSRFGKFIEVHYDAKCQVVGGYIS 226
Cdd:cd14904    81 GESGAGKTETTKIVMNHLA---SVAGGRKdktiAKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAKCE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  227 HYLLEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSLGKPDDYRYLSGCTQyfanaktEQLIPGsqksknhqqkgplk 306
Cdd:cd14904   158 TYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLGDSLA-------QMQIPG-------------- 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  307 dpiIDDYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEIPDDvrgGCQVSEASEqsLTITSGLLGVDQTEL 386
Cdd:cd14904   217 ---LDDAKLFASTQKSLSLIGLDNDAQRTLFKILSGVLHLGEVMFDKSDEN---GSRISNGSQ--LSQVAKMLGLPTTRI 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  387 RTALVSRVMQSKGGGfkgtvIMVPLKIYEASNARDALAKAIYSRLFDRIVGLINQSIPFQASNFY--IGVLDIAGFEYFT 464
Cdd:cd14904   289 EEALCNRSVVTRNES-----VTVPLAPVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKgqIGVLDIFGFEDFA 363
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  465 VNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITFTDNQDIIELIEAKSnGIFTLLDEESKLPKPSYShft 544
Cdd:cd14904   364 HNGFEQFCINYANEKLQQKFTTDVFKTVEEEYIREGLQWDHIEYQDNQGIVEVIDGKM-GIIALMNDHLRQPRGTEE--- 439
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  545 AEVHKSWANHYRLGLPRSSRL-KAHRTlrdeeGFLVRHFAGAVCYNTEQFIEKNNDALHASLEGLVQECDNPLLQTLF-- 621
Cdd:cd14904   440 ALVNKIRTNHQTKKDNESIDFpKVKRT-----QFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFgs 514
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  622 ---PSGSSTSVRGKLNFI--SVGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQFEGSLALAQLKCSGTISVLELM 696
Cdd:cd14904   515 seaPSETKEGKSGKGTKApkSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRIT 594
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 281362442  697 EHGYPSRVLFADLYSMYKSVLPPELVSLPARTFCEAMFQSLNL-SAKDFKFGITKVFFR 754
Cdd:cd14904   595 RSGYPSRLTPKELATRYAIMFPPSMHSKDVRRTCSVFMTAIGRkSPLEYQIGKSLIYFK 653
MYSc_Myo14 cd14876
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ...
74-752 2.22e-149

class XIV myosin, motor domain; These myosins localize to plasma membranes of the intracellular parasites and may be involved in the cell invasion process. Their known functions include: transporting phagosomes to the nucleus and perturbing the developmentally regulated elimination of the macronucleus during conjugation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to their motor domain these myosins have a MyTH4-FERM protein domain combination. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276843  Cd Length: 649  Bit Score: 465.62  E-value: 2.22e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   74 LDNLKTRYYKDKIYTYVANILIAVNPYREIKELyAPDTIKKY-NGRSLGELPPHVFAIADKAIRDMRVYKLSQSIIVSGE 152
Cdd:cd14876     4 LDFLKHRYLKNQIYTTADPLLVAINPFKDLGNA-TDEWIRKYrDAPDLTKLPPHVFYTARRALENLHGVNKSQTIIVSGE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  153 SGAGKTESTKYLLKYLCYSHDSA--GPIETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEVHYDAKCQVVGGYISHYLL 230
Cdd:cd14876    83 SGAGKTEATKQIMRYFASAKSGNmdLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIRYGSVVAFLL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  231 EKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSLGKPDDYRYLSG-CTQyfanakteqlIPGsqksknhqqkgplkdpi 309
Cdd:cd14876   163 EKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLNPkCLD----------VPG----------------- 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  310 IDDYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEIPDD-VRGGCQVSEASEQSLTITSGLLGVDQTELRT 388
Cdd:cd14876   216 IDDVADFEEVLESLKSMGLTEEQIDTVFSIVSGVLLLGNVKITGKTEQgVDDAAAISNESLEVFKEACSLLFLDPEALKR 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  389 ALVSRVmqSKGGGfkgTVIMVPLKIYEASNARDALAKAIYSRLFDRIVGLINQSI-PFQASNFYIGVLDIAGFEYFTVNS 467
Cdd:cd14876   296 ELTVKV--TKAGG---QEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIePPGGFKNFMGMLDIFGFEVFKNNS 370
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  468 FEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITFTDNQDIIELIEAKSNGIFTLLDEESKLPKPSYSHFTAEV 547
Cdd:cd14876   371 LEQLFINITNEMLQKNFIDIVFERESKLYKDEGIPTAELEYTSNAEVIDVLCGKGKSVLSILEDQCLAPGGSDEKFVSAC 450
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  548 HKSWANH-YRLGLPRSSRLKahrtlrdeegFLVRHFAGAVCYNTEQFIEKNNDALHASLEGLVQECDNPLLQTLFpSGSS 626
Cdd:cd14876   451 VSKLKSNgKFKPAKVDSNIN----------FIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALF-EGVV 519
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  627 TSvRGKLNFIS-VGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQFEGSLALAQLKCSGTISVLELMEHGYPSRVL 705
Cdd:cd14876   520 VE-KGKIAKGSlIGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRP 598
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*....
gi 281362442  706 FADLYSMYKSVLP--PELVSLPARTFCEAMFQSLNLSAKDFKFGITKVF 752
Cdd:cd14876   599 FEEFLYQFKFLDLgiANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVF 647
MYSc_Myo41 cd14902
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ...
71-718 1.28e-143

class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276867 [Multi-domain]  Cd Length: 716  Bit Score: 452.42  E-value: 1.28e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   71 ATFLDNLKTRYYKDKIYTYVANILIAVNPYREIKELYAPDTIKKY--------NGRSLGELPPHVFAIADKAIRDMR-VY 141
Cdd:cd14902     1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPDLYSESQLNAYkasmtstsPVSQLSELPPHVFAIGGKAFGGLLkPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  142 KLSQSIIVSGESGAGKTESTKYLLKYLC----------YSHDSAGPIETKILDANPVLEAFGNAKTTRNNNSSRFGKFIE 211
Cdd:cd14902    81 RRNQSILVSGESGSGKTESTKFLMQFLTsvgrdqssteQEGSDAVEIGKRILQTNPILESFGNAQTIRNDNSSRFGKFIK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  212 VHYDAKCQVVGGYISHYLLEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSLGKPDDYRYLSGCTQYFANAKTEQlip 291
Cdd:cd14902   161 IQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELLNSYGPSFARKRAVA--- 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  292 gsqksknhqqkgplkdpiIDDYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEIpDDVRGGCQVSEASEQS 371
Cdd:cd14902   238 ------------------DKYAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAE-NGQEDATAVTAASRFH 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  372 LTITSGLLGVDQTELRTALVSRVMQSkgggfKGTVIMVPLKIYEASNARDALAKAIYSRLFDRIVGLINQSIPFQASNFY 451
Cdd:cd14902   299 LAKCAELMGVDVDKLETLLSSREIKA-----GVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINYFDSAVS 373
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  452 ----------IGVLDIAGFEYFTVNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITFTDNQDIIELIEAK 521
Cdd:cd14902   374 isdedeelatIGILDIFGFESLNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYPSNAACLALFDDK 453
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  522 SNGIFTLLDEESKLPKPSyshftaevHKSWANhyrlglprssrlKAHRTLRDEEGFLVRHFAGAVCYNTEQFIEKNNDAL 601
Cdd:cd14902   454 SNGLFSLLDQECLMPKGS--------NQALST------------KFYRYHGGLGQFVVHHFAGRVCYNVEQFVEKNTDAL 513
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  602 HASLEGLVQECDNPLLQTLFPS---GSSTSVRGK--------LNFISVGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKM 670
Cdd:cd14902   514 PADASDILSSSSNEVVVAIGADenrDSPGADNGAagrrrysmLRAPSVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVK 593
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*...
gi 281362442  671 IDRQFEGSLALAQLKCSGTISVLELMEHGYPSRVLFADLYSMYKSVLP 718
Cdd:cd14902   594 KPGIFDRERMVEQMRSVGVLEAVRIARHGYSVRLAHASFIELFSGFKC 641
MYSc_Myo34 cd14895
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ...
72-754 4.87e-143

class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short coiled-coil region, 5 tandem ANK repeats, and a carboxy-terminal FYVE domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276860 [Multi-domain]  Cd Length: 704  Bit Score: 450.56  E-value: 4.87e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   72 TFLDNLKTRYYKDKIYTYVANILIAVNPYREIKELYapdTIKKYNGRSLG--ELPPHVFAIADKAIRDMR-------VYK 142
Cdd:cd14895     2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIPGLY---DLHKYREEMPGwtALPPHVFSIAEGAYRSLRrrlhepgASK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  143 LSQSIIVSGESGAGKTESTKYLLKYLCYSHDSAGP----------IETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEV 212
Cdd:cd14895    79 KNQTILVSGESGAGKTETTKFIMNYLAESSKHTTAtssskrrraiSGSELLSANPILESFGNARTLRNDNSSRFGKFVRM 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  213 HY-----DAKCQVVGGYISHYLLEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSLG--KPDDYRYLSGCTQYFANak 285
Cdd:cd14895   159 FFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLEllSAQEFQYISGGQCYQRN-- 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  286 teqlipgsqksknhqqkgplkDPIIDDYQhFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAF--------EEIPDD 357
Cdd:cd14895   237 ---------------------DGVRDDKQ-FQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFvassedegEEDNGA 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  358 VRGGCQVSEASEQSLT------ITSGLLGVDQTELRTALVSRVMQSKGGGFkgtviMVPLKIYEASNARDALAKAIYSRL 431
Cdd:cd14895   295 ASAPCRLASASPSSLTvqqhldIVSKLFAVDQDELVSALTTRKISVGGETF-----HANLSLAQCGDARDAMARSLYAFL 369
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  432 FDRIVGLINQSIP------------FQASNFYIGVLDIAGFEYFTVNSFEQFCINYCNEKLQKFFNDNILKNEQELYKRE 499
Cdd:cd14895   370 FQFLVSKVNSASPqrqfalnpnkaaNKDTTPCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEE 449
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  500 GLNVPEITFTDNQDIIELIEAKSNGIFTLLDEESKLPKPSYSHFTAEVHKSWANHyrlglprsSRLKAHRTLRDEEGFLV 579
Cdd:cd14895   450 GIKWNAVDYEDNSVCLEMLEQRPSGIFSLLDEECVVPKGSDAGFARKLYQRLQEH--------SNFSASRTDQADVAFQI 521
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  580 RHFAGAVCYNTEQFIEKNNDALHASLEGLVQECDNPLLQTLF-----------PSGSSTSVRGK--LNFISVGSKFKTQL 646
Cdd:cd14895   522 HHYAGAVRYQAEGFCEKNKDQPNAELFSVLGKTSDAHLRELFeffkasesaelSLGQPKLRRRSsvLSSVGIGSQFKQQL 601
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  647 GELMEKLEQNGTNFIRCIKPNSKMIDRQFEGSLALAQLKCSGTISVLELMEHGYPSRVLFADLYSMYKsvlppELVSLPA 726
Cdd:cd14895   602 ASLLDVVQQTQTHYIRCIKPNDESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYR-----LLVAAKN 676
                         730       740
                  ....*....|....*....|....*...
gi 281362442  727 RTFCEAMFQSLNLSAKDFKFGITKVFFR 754
Cdd:cd14895   677 ASDATASALIETLKVDHAELGKTRVFLR 704
MYSc_Myo39 cd14900
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ...
72-716 1.25e-140

class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276865  Cd Length: 627  Bit Score: 441.67  E-value: 1.25e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   72 TFLDNLKTRYYKDKIYTYVANILIAVNPYREIKELYAPDTIKKY-------NGRSLGE----LPPHVFAIADKAIRDMRV 140
Cdd:cd14900     2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPGLYSSDTMAKYllsfearSSSTRNKgsdpMPPHIYQVAGEAYKAMML 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  141 YKLS----QSIIVSGESGAGKTESTKYLLKYLCYSHDSAGP-----------IETKILDANPVLEAFGNAKTTRNNNSSR 205
Cdd:cd14900    82 GLNGvmsdQSILVSGESGSGKTESTKFLMEYLAQAGDNNLAasvsmgkstsgIAAKVLQTNILLESFGNARTLRNDNSSR 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  206 FGKFIEVHYDAKCQVVGGYISHYLLEKSRICTQSAEERNYHVFY-MLLAGAPQQLrdklslgkpddyrylsgctqyfana 284
Cdd:cd14900   162 FGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYeMAIGASEAAR------------------------- 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  285 kteqlipgsqKSKNHQQkgplkdpiiddyqhfhnLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEIPDDVRGG--- 361
Cdd:cd14900   217 ----------KRDMYRR-----------------VMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGqlk 269
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  362 CQVSEASEQSLTITSGLLGVDQTELRTALVSRVMQSkGGGFKgtviMVPLKIYEASNARDALAKAIYSRLFDRIVGLIN- 440
Cdd:cd14900   270 SDLAPSSIWSRDAAATLLSVDATKLEKALSVRRIRA-GTDFV----SMKLSAAQANNARDALAKALYGRLFDWLVGKMNa 344
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  441 -----QSIPFQASNFYIGVLDIAGFEYFTVNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITFTDNQDII 515
Cdd:cd14900   345 flkmdDSSKSHGGLHFIGILDIFGFEVFPKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFCDNQDCV 424
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  516 ELIEAKSNGIFTLLDEESKLPKPSYSHFTAEVHKSWANHyrlglprsSRLKAHRTLRDEEGFLVRHFAGAVCYNTEQFIE 595
Cdd:cd14900   425 NLISQRPTGILSLIDEECVMPKGSDTTLASKLYRACGSH--------PRFSASRIQRARGLFTIVHYAGHVEYSTDGFLE 496
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  596 KNNDALHASLEGLVQECdnpllqtlfpsgsstsvrgklnfisvgSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQF 675
Cdd:cd14900   497 KNKDVLHQEAVDLFVYG---------------------------LQFKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIY 549
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|.
gi 281362442  676 EGSLALAQLKCSGTISVLELMEHGYPSRVLFADLYSMYKSV 716
Cdd:cd14900   550 ERERVLNQLRCNGVMEAVRVARAGFPIRLLHDEFVARYFSL 590
MYSc_Myo28 cd14889
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ...
73-754 1.94e-140

class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The tail regions of these class-XXVIII myosins consist of an IQ motif, a short coiled-coil region, and an SH2 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276854  Cd Length: 659  Bit Score: 442.04  E-value: 1.94e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   73 FLDNLKTRYYKDKIYTYVANILIAVNPYREIkELYAPDTIKKYNGRSLGELPPHVFAIADKAIRDMRVYKLS----QSII 148
Cdd:cd14889     3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYL-HIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLGRLARgpknQCIV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  149 VSGESGAGKTESTKYLLKYLCYSHDSAGPIETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEVHYdAKCQVVGGYISHY 228
Cdd:cd14889    82 ISGESGAGKTESTKLLLRQIMELCRGNSQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RNGHVKGAKINEY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  229 LLEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSLGKPDDYRYLSGctqYFANAKTeqliPGSQKSKnhqqkgplkdp 308
Cdd:cd14889   161 LLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLLDPGKYRYLNN---GAGCKRE----VQYWKKK----------- 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  309 iiddyqhFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEeiPDDvRGGCQVSEASEQSLTITSGLLGVDQTELRT 388
Cdd:cd14889   223 -------YDEVCNAMDMVGFTEQEEVDMFTILAGILSLGNITFE--MDD-DEALKVENDSNGWLKAAAGQFGVSEEDLLK 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  389 ALVSRVMQSKGGGFKgtvimvplKIY---EASNARDALAKAIYSRLFDRIVGLINQSIP----FQASNFYIGVLDIAGFE 461
Cdd:cd14889   293 TLTCTVTFTRGEQIQ--------RHHtkqQAEDARDSIAKVAYGRVFGWIVSKINQLLApkddSSVELREIGILDIFGFE 364
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  462 YFTVNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITFTDNQDIIELIEAKSNGIFTLLDEESKLPKPSYS 541
Cdd:cd14889   365 NFAVNRFEQACINLANEQLQYFFNHHIFLMEQKEYKKEGIDWKEITYKDNKPILDLFLNKPIGILSLLDEQSHFPQATDE 444
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  542 HFTAEVHKSWANHYRLGLPRSSRLKahrtlrdeegFLVRHFAGAVCYNTEQFIEKNNDALHASLEGLVQECDNPLLQTLF 621
Cdd:cd14889   445 SFVDKLNIHFKGNSYYGKSRSKSPK----------FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLF 514
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  622 PSGSSTS----------VRGKLNF-----ISVGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQFEGSLALAQLKC 686
Cdd:cd14889   515 TATRSRTgtlmpraklpQAGSDNFnstrkQSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRY 594
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281362442  687 SGTISVLELMEHGYPSRVLFADLYSMYKS-VLPPELVSlpARTFCEAMFQSLNLsaKDFKFGITKVFFR 754
Cdd:cd14889   595 NGLLETIRIRREGFSWRPSFAEFAERYKIlLCEPALPG--TKQSCLRILKATKL--VGWKCGKTRLFFK 659
MYSc_Myh10 cd14920
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ...
71-754 3.02e-138

class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy chain 10 (also called NMMHCB). Mutations in this gene have been associated with May-Hegglin anomaly and developmental defects in brain and heart. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276952 [Multi-domain]  Cd Length: 673  Bit Score: 436.75  E-value: 3.02e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   71 ATFLDNLKTRYYKDKIYTYVANILIAVNPYREIKeLYAPDTIKKYNGRSLGELPPHVFAIADKAIRDMRVYKLSQSIIVS 150
Cdd:cd14920     1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  151 GESGAGKTESTKYLLKYLCY---SHDSA------GPIETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEVHYDAKCQVV 221
Cdd:cd14920    80 GESGAGKTENTKKVIQYLAHvasSHKGRkdhnipGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  222 GGYISHYLLEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSLGKPDDYRYLSGCTqyfanakteQLIPGSQKSKNHQQ 301
Cdd:cd14920   160 GANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGY---------IPIPGQQDKDNFQE 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  302 kgplkdpiiddyqhfhNLDkALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEipddVRGGCQVSEASEQSLTITSGLLGV 381
Cdd:cd14920   231 ----------------TME-AMHIMGFSHEEILSMLKVVSSVLQFGNISFKK----ERNTDQASMPENTVAQKLCHLLGM 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  382 DQTEL-RTALVSRVmqsKGGgfKGTVIMVPLKiYEASNARDALAKAIYSRLFDRIVGLINQSI---PFQASNFyIGVLDI 457
Cdd:cd14920   290 NVMEFtRAILTPRI---KVG--RDYVQKAQTK-EQADFAVEALAKATYERLFRWLVHRINKALdrtKRQGASF-IGILDI 362
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  458 AGFEYFTVNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITF-TDNQDIIELIEAKSN--GIFTLLDEESK 534
Cdd:cd14920   363 AGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLALLDEECW 442
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  535 LPKPSYSHFTAEVHKSWANHyrlglprsSRLKAHRTLRDEEGFLVRHFAGAVCYNTEQFIEKNNDA--------LHASLE 606
Cdd:cd14920   443 FPKATDKTFVEKLVQEQGSH--------SKFQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPlndnvatlLHQSSD 514
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  607 GLVQECDNPLLQTLFPSGSS----TSVRGKLN-----FISVGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQFEG 677
Cdd:cd14920   515 RFVAELWKDVDRIVGLDQVTgmteTAFGSAYKtkkgmFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDP 594
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  678 SLALAQLKCSGTISVLELMEHGYPSRVLFADLYSMYKsVLPPElvSLPaRTF------CEAMFQSLNLSAKDFKFGITKV 751
Cdd:cd14920   595 HLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE-ILTPN--AIP-KGFmdgkqaCERMIRALELDPNLYRIGQSKI 670

                  ...
gi 281362442  752 FFR 754
Cdd:cd14920   671 FFR 673
MYSc_Myh16 cd14934
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ...
71-754 1.39e-135

class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 pseudogene (also called MHC20, MYH16, and myh5), encoding a sarcomeric myosin heavy chain expressed in nonhuman primate masticatory muscles, is inactivated in humans. This cd contains Myh16 in mammals. MYH16 has intermediate fibres between that of slow type 1 and fast 2B fibres, but exert more force than any other fibre type examined. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.


Pssm-ID: 276896 [Multi-domain]  Cd Length: 659  Bit Score: 429.45  E-value: 1.39e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   71 ATFLDNLKTRYYKDKIYTYVANILIAVNPYREIKeLYAPDTIKKYNGRSLGELPPHVFAIADKAIRDMRVYKLSQSIIVS 150
Cdd:cd14934     1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLP-IYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLIT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  151 GESGAGKTESTKYLLKYLC-------YSHDSAGPIETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEVHYDAKCQVVGG 223
Cdd:cd14934    80 GESGAGKTENTKKVIQYFAniggtgkQSSDGKGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  224 YISHYLLEKSRICTQSAEERNYHVFYMLLAG-APQQLRDKLSLGKPDDYRYLSGCTQYFANakteqlipgsqksknhqqk 302
Cdd:cd14934   160 DIESYLLEKSRVISQQAAERGYHIFYQILSNkKPELIESLLLVPNPKEYHWVSQGVTVVDN------------------- 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  303 gplkdpiIDDYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEIPDDVRGGCQVSEASEQsltiTSGLLGVD 382
Cdd:cd14934   221 -------MDDGEELQITDVAFDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADK----VAHLMGLN 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  383 QTELRTAlVSRVMQSKGGGF--KGTvimvplKIYEASNARDALAKAIYSRLFDRIVGLINQSIPFQAS-NFYIGVLDIAG 459
Cdd:cd14934   290 SGELQKG-ITRPRVKVGNEFvqKGQ------NMEQCNNSIGALGKAVYDKMFKWLVVRINKTLDTKMQrQFFIGVLDIAG 362
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  460 FEYFTVNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITF-TDNQDIIELIEaKSNGIFTLLDEESKLPKP 538
Cdd:cd14934   363 FEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKREGIEWVFIDFgLDLQACIDLLE-KPMGIFSILEEQCVFPKA 441
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  539 SYSHFTAEVHKswaNHyrlgLPRSSRL---KAHRTLRDEEGFLVRHFAGAVCYNTEQFIEKNNDALHASLEGLVQECDNP 615
Cdd:cd14934   442 TDATFKAALYD---NH----LGKSSNFlkpKGGKGKGPEAHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLG 514
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  616 LLQTLF-----PSGSSTSVRGKlNFISVGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQFEGSLALAQLKCSGTI 690
Cdd:cd14934   515 LLALLFkeeeaPAGSKKQKRGS-SFMTVSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVL 593
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281362442  691 SVLELMEHGYPSRVLFADLYSMYKsVLPPELVS---LPARTFCEAMFQSLNLSAKDFKFGITKVFFR 754
Cdd:cd14934   594 EGIRICRKGFPNRLQYPEFKQRYQ-VLNPNVIPqgfVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
MYSc_Myh3 cd14913
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ...
74-754 2.15e-134

class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle myosin heavy chain 3 (MYHC-EMB, MYHSE1, HEMHC, SMHCE) in tetrapods including mammals, lizards, and frogs. This gene is a member of the MYH family and encodes a protein with an IQ domain and a myosin head-like domain. Mutations in this gene have been associated with two congenital contracture (arthrogryposis) syndromes, Freeman-Sheldon syndrome and Sheldon-Hall syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276878 [Multi-domain]  Cd Length: 668  Bit Score: 426.39  E-value: 2.15e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   74 LDNLKTRYYKDKIYTYVANILIAVNPYREIKeLYAPDTIKKYNGRSLGELPPHVFAIADKAIRDMRVYKLSQSIIVSGES 153
Cdd:cd14913     4 LYNLKDRYTSWMIYTYSGLFCVTVNPYKWLP-VYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  154 GAGKTESTKYLLKY---------LCYSHDSA--GPIETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEVHYDAKCQVVG 222
Cdd:cd14913    83 GAGKTVNTKRVIQYfatiaatgdLAKKKDSKmkGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  223 GYISHYLLEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSLG-KPDDYRYLSgctqyfanakteqlipgsqksknhqq 301
Cdd:cd14913   163 ADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITtNPYDYPFIS-------------------------- 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  302 KGPLKDPIIDDYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEIPDDVRGGCQVSEASEQsltiTSGLLGV 381
Cdd:cd14913   217 QGEILVASIDDAEELLATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADK----TAYLMGL 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  382 DQTELRTALV-SRVMQSKGGGFKGTVIMvplkiyEASNARDALAKAIYSRLFDRIVGLINQSIPFQ-ASNFYIGVLDIAG 459
Cdd:cd14913   293 NSSDLLKALCfPRVKVGNEYVTKGQTVD------QVHHAVNALSKSVYEKLFLWMVTRINQQLDTKlPRQHFIGVLDIAG 366
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  460 FEYFTVNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLnvpEITFTD-NQDI---IELIEaKSNGIFTLLDEESKL 535
Cdd:cd14913   367 FEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGI---EWTFIDfGMDLaacIELIE-KPMGIFSILEEECMF 442
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  536 PKPSYSHFTAEV---HKSWANHYRLGLPRSSRLKAHrtlrdeegFLVRHFAGAVCYNTEQFIEKNNDALHASLEGLVQEC 612
Cdd:cd14913   443 PKATDTSFKNKLydqHLGKSNNFQKPKVVKGRAEAH--------FSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKS 514
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  613 DNPLLQTLFPS-----GSSTSVRGKL----NFISVGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQFEGSLALAQ 683
Cdd:cd14913   515 SNRLLAHLYATfatadADSGKKKVAKkkgsSFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQ 594
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281362442  684 LKCSGTISVLELMEHGYPSRVLFADLYSMYKSVLP---PELVSLPARTFCEAMFQSLNLSAKDFKFGITKVFFR 754
Cdd:cd14913   595 LRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNAsaiPEGQFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
MYSc_Myh15_mammals cd14929
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ...
71-754 1.01e-133

class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy chain 15 in mammals (also called KIAA1000) . MYH15 is a slow-twitch myosin. Myh15 is a ventricular myosin heavy chain. Myh15 is absent in embryonic and fetal muscles and is found in orbital layer of extraocular muscles at birth. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276892 [Multi-domain]  Cd Length: 662  Bit Score: 424.39  E-value: 1.01e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   71 ATFLDNLKTRYYKDKIYTYVANILIAVNPYREIKeLYAPDTIKKYNGRSLGELPPHVFAIADKAIRDMRVYKLSQSIIVS 150
Cdd:cd14929     1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLP-VYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  151 GESGAGKTESTKYLLKYLCY------SHDSAGPIETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEVHYDAKCQVVGGY 224
Cdd:cd14929    80 GESGAGKTVNTKHIIQYFATiaamieSKKKLGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSAD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  225 ISHYLLEKSRICTQSAEERNYHVFYMLLAGApQQLRDKLSLG-KPDDYRYLSgCtqyfanakteqlipgsqksknhqqkG 303
Cdd:cd14929   160 IDIYLLEKSRVIFQQPGERNYHIFYQILSGK-KELRDLLLVSaNPSDFHFCS-C-------------------------G 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  304 PLKDPIIDDYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEIPDDVrggcQVSEASEQSLTITSGLLGVDQ 383
Cdd:cd14929   213 AVAVESLDDAEELLATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREE----QLEADGTENADKAAFLMGINS 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  384 TELRTALV-SRVmqsKGGGfkgTVIMVPLKIYEASNARDALAKAIYSRLFDRIVGLINQSIPFQ-ASNFYIGVLDIAGFE 461
Cdd:cd14929   289 SELVKGLIhPRI---KVGN---EYVTRSQNIEQVTYAVGALSKSIYERMFKWLVARINRVLDAKlSRQFFIGILDITGFE 362
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  462 YFTVNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITF-TDNQDIIELIEaKSNGIFTLLDEESKLPKPSY 540
Cdd:cd14929   363 ILDYNSLEQLCINFTNEKLQQFFNQHMFVLEQEEYRKEGIDWVSIDFgLDLQACIDLIE-KPMGIFSILEEECMFPKATD 441
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  541 SHFTAEV---HKSWANHYRLGLPRSSRLKAHrtlrdeegFLVRHFAGAVCYNTEQFIEKNNDALHASLEGLVQECDNPLL 617
Cdd:cd14929   442 LTFKTKLfdnHFGKSVHFQKPKPDKKKFEAH--------FELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLL 513
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  618 QTLF----------PSGSSTSVRGKlNFISVGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQFEGSLALAQLKCS 687
Cdd:cd14929   514 ASLFenyistdsaiQFGEKKRKKGA-SFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCN 592
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281362442  688 GTISVLELMEHGYPSRVLFADLYSMYkSVLPPELVS----LPARTFCEAMFQSLNLSAKDFKFGITKVFFR 754
Cdd:cd14929   593 GVLEGIRICREGFPNRLLYADFKQRY-CILNPRTFPkskfVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
MYSc_Myo45 cd14906
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ...
71-717 2.69e-133

class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds Dictyostelium and Polysphondylium. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276871 [Multi-domain]  Cd Length: 715  Bit Score: 425.16  E-value: 2.69e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   71 ATFLDNLKTRYYKDKIYTYVANILIAVNPYREIKELYAPDTIKKYNG-RSLGELPPHVFAIADKAIRDMRVYKLSQSIIV 149
Cdd:cd14906     1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISSIYSNLILNEYKDiNQNKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  150 SGESGAGKTESTKYLLKYLCYSHDSA-----------GPIETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEVHYDAKC 218
Cdd:cd14906    81 SGESGSGKTEASKTILQYLINTSSSNqqqnnnnnnnnNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  219 QVV-GGYISHYLLEKSRICTQ-SAEERNYHVFYMLLAGAPQQLRDKLSL-GKPDDYRYLsgctqyfaNAKTEQLIPGSQK 295
Cdd:cd14906   161 GKIdGASIETYLLEKSRISHRpDNINLSYHIFYYLVYGASKDERSKWGLnNDPSKYRYL--------DARDDVISSFKSQ 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  296 SKNHQQKGPLKDPIIDDYQhfhNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEiPDDVRGGCQVSEASEQSLTIT 375
Cdd:cd14906   233 SSNKNSNHNNKTESIESFQ---LLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEE-DSDFSKYAYQKDKVTASLESV 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  376 SGLLGVDQTELRTALVSRVMqsKGGGfKGTVIMVPLKIYEASNARDALAKAIYSRLFDRIVGLIN------------QSI 443
Cdd:cd14906   309 SKLLGYIESVFKQALLNRNL--KAGG-RGSVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINrkfnqntqsndlAGG 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  444 PFQASNFYIGVLDIAGFEYFTVNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITFTDNQDIIELIEAKSN 523
Cdd:cd14906   386 SNKKNNLFIGVLDIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNFIDNKECIELIEKKSD 465
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  524 GIFTLLDEESKLPKPSYSHFTAEVHKSWANhyrlglprsSRLKAHRTLrDEEGFLVRHFAGAVCYNTEQFIEKNNDALHA 603
Cdd:cd14906   466 GILSLLDDECIMPKGSEQSLLEKYNKQYHN---------TNQYYQRTL-AKGTLGIKHFAGDVTYQTDGWLEKNRDSLYS 535
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  604 SLEGLVQECDNPLLQTLFP---SGSSTSVRGKLNFISVGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQFEGSLA 680
Cdd:cd14906   536 DVEDLLLASSNFLKKSLFQqqiTSTTNTTKKQTQSNTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHV 615
                         650       660       670
                  ....*....|....*....|....*....|....*..
gi 281362442  681 LAQLKCSGTISVLELMEHGYPSRVLFADLYSMYKSVL 717
Cdd:cd14906   616 LSQLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIV 652
MYSc_Myh2_insects_mollusks cd14911
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ...
71-754 6.05e-133

class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in insects and mollusks. This gene encodes a member of the class II or conventional myosin heavy chains, and functions in skeletal muscle contraction. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276876 [Multi-domain]  Cd Length: 674  Bit Score: 422.85  E-value: 6.05e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   71 ATFLDNLKTRYYKDKIYTYVANILIAVNPYREIKeLYAPDTIKKYNGRSLGELPPHVFAIADKAIRDMRVYKLSQSIIVS 150
Cdd:cd14911     1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLP-IYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  151 GESGAGKTESTKYLLKYLCYSHDS------------------AGPIETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEV 212
Cdd:cd14911    80 GESGAGKTENTKKVIQFLAYVAASkpkgsgavphpavnpavlIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  213 HYDAKCQVVGGYISHYLLEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSLGKPDDYRYLSgctqyfanakteqlipg 292
Cdd:cd14911   160 NFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLS----------------- 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  293 sqksknhqqKGPLKDPIIDDYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEipddVRGGCQVSEASEQSL 372
Cdd:cd14911   223 ---------NGSLPVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQ----ERNNDQATLPDNTVA 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  373 TITSGLLGVDQTELRTA-LVSRVmqsKGGgfKGTVIMVPLKiYEASNARDALAKAIYSRLFDRIVGLINQSI---PFQAS 448
Cdd:cd14911   290 QKIAHLLGLSVTDMTRAfLTPRI---KVG--RDFVTKAQTK-EQVEFAVEAIAKACYERMFKWLVNRINRSLdrtKRQGA 363
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  449 NFyIGVLDIAGFEYFTVNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITF-TDNQDIIELIEaKSNGIFT 527
Cdd:cd14911   364 SF-IGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLID-KPGGIMA 441
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  528 LLDEESKLPKPSYSHFTAEVHKSWANHyrlglPRSSRlkahRTLRDEEGFLVRHFAGAVCYNTEQFIEKNNDALHASLEG 607
Cdd:cd14911   442 LLDEECWFPKATDKTFVDKLVSAHSMH-----PKFMK----TDFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVS 512
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  608 LVQECDNPLL--------------QTLFPSGSSTSVRgKLNFISVGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDR 673
Cdd:cd14911   513 LLQGSQDPFVvniwkdaeivgmaqQALTDTQFGARTR-KGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAG 591
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  674 QFEGSLALAQLKCSGTISVLELMEHGYPSRVLFADLYSMYKsVLPPELVS---LPARTFCEAMFQSLNLSAKDFKFGITK 750
Cdd:cd14911   592 KIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYE-LLTPNVIPkgfMDGKKACEKMIQALELDSNLYRVGQSK 670

                  ....
gi 281362442  751 VFFR 754
Cdd:cd14911   671 IFFR 674
MYSc_Myo13 cd14875
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ...
71-754 1.27e-132

class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain binding domain, and a C-terminal GPA/Q-rich domain. There is little known about the function of this myosin class. Two of the earliest members identified in this class are green alga Acetabularia cliftonii, Aclmyo1 and Aclmyo2. They are striking with their short tail of Aclmyo1 of 18 residues and the maximum of 7 IQ motifs in Aclmyo2. It is thought that these myosins are involved in organelle transport and tip growth. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276842 [Multi-domain]  Cd Length: 664  Bit Score: 421.53  E-value: 1.27e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   71 ATFLDNLKTRYYK-DKIYTYVANILIAVNPYREIKeLYAPDTIKKY-NGRSLGELPPHVFAIADKAIRDMRVYKL-SQSI 147
Cdd:cd14875     1 ATLLHCIKERFEKlHQQYSLMGEMVLSVNPFRLMP-FNSEEERKKYlALPDPRLLPPHIWQVAHKAFNAIFVQGLgNQSV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  148 IVSGESGAGKTESTKYLLKYL---CYSHdSAGPIETKILD--------ANPVLEAFGNAKTTRNNNSSRFGKFIEVHYDA 216
Cdd:cd14875    80 VISGESGSGKTENAKMLIAYLgqlSYMH-SSNTSQRSIADkidenlkwSNPVMESFGNARTVRNDNSSRFGKYIKLYFDP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  217 KCQV-VGGYISHYLLEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKL-SLGKPDDYRYLSGctqyfANAKTEQLIPGSQ 294
Cdd:cd14875   159 TSGVmVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKCLNG-----GNTFVRRGVDGKT 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  295 ksknhqqkgplkdpiIDDYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEIPDDvrggcQVSEASEQSLTI 374
Cdd:cd14875   234 ---------------LDDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQND-----KAQIADETPFLT 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  375 TSGLLGVDQTELRTALVSRVmqskgggfKGTVIMVPLKIYEASNARDALAKAIYSRLFDRIVGLINQSIPFQASNF---Y 451
Cdd:cd14875   294 ACRLLQLDPAKLRECFLVKS--------KTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITPQGDCSgckY 365
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  452 IGVLDIAGFEYFTVNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITFTDNQDIIELIEAKSNGIFTLLDE 531
Cdd:cd14875   366 IGLLDIFGFENFTRNSFEQLCINYANESLQNHYNKYTFINDEEECRREGIQIPKIEFPDNSECVNMFDQKRTGIFSMLDE 445
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  532 ESKLPKPSYSHFTAEVHKSWANH--YRLgLPRSsrlkahrTLRDEegFLVRHFAGAVCYNTEQFIEKNNDALHASLEGLV 609
Cdd:cd14875   446 ECNFKGGTTERFTTNLWDQWANKspYFV-LPKS-------TIPNQ--FGVNHYAAFVNYNTDEWLEKNTDALKEDMYECV 515
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  610 QECDNPLLQTLFPSGSSTSVRGKlnfiSVGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQFEGSLALAQLKCSGT 689
Cdd:cd14875   516 SNSTDEFIRTLLSTEKGLARRKQ----TVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGV 591
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281362442  690 ISVLELMEHGYPSRVLFADLYSMYKSVLPPELVSL--------PARTFCeAMFQSL-NLSAKDFKFGITKVFFR 754
Cdd:cd14875   592 LQTIALKRQGYPVRRPIEQFCRYFYLIMPRSTASLfkqekyseAAKDFL-AYYQRLyGWAKPNYAVGKTKVFLR 664
MYSc_Myh18 cd14932
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ...
71-754 3.79e-132

class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain 18. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276895 [Multi-domain]  Cd Length: 676  Bit Score: 420.59  E-value: 3.79e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   71 ATFLDNLKTRYYKDKIYTYVANILIAVNPYREIKeLYAPDTIKKYNGRSLGELPPHVFAIADKAIRDMRVYKLSQSIIVS 150
Cdd:cd14932     1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLP-IYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  151 GESGAGKTESTKYLLKYLCYSHDSA-------------GPIETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEVHYDAK 217
Cdd:cd14932    80 GESGAGKTENTKKVIQYLAYVASSFktkkdqssialshGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  218 CQVVGGYISHYLLEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSLGKPDDYRYLSgctqyfaNAKTEqlIPGSQksk 297
Cdd:cd14932   160 GYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLS-------NGNVT--IPGQQ--- 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  298 nhqqkgplkdpiidDYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEipddVRGGCQVSEASEQSLTITSG 377
Cdd:cd14932   228 --------------DKELFAETMEAFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKK----ERNSDQASMPDDTAAQKVCH 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  378 LLGVDQTELRTALVS-RVMQSKgggfkgTVIMVPLKIYEASNARDALAKAIYSRLFDRIVGLINQSI---PFQASNFyIG 453
Cdd:cd14932   290 LLGMNVTDFTRAILSpRIKVGR------DYVQKAQTQEQAEFAVEALAKASYERMFRWLVMRINKALdktKRQGASF-IG 362
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  454 VLDIAGFEYFTVNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITF-TDNQDIIELIEAKSN--GIFTLLD 530
Cdd:cd14932   363 ILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIELIEKPNGppGILALLD 442
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  531 EESKLPKPSYSHFTAEVHKSWANHYRLGLPRSsrlkahrtLRDEEGFLVRHFAGAVCYNTEQFIEKNNDALHASLEGLVQ 610
Cdd:cd14932   443 EECWFPKATDKSFVEKVVQEQGNNPKFQKPKK--------LKDDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLN 514
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  611 ECDNPLLQTLFP-----------SGSSTSVRGKLN-----FISVGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQ 674
Cdd:cd14932   515 QSTDKFVSELWKdvdrivgldkvAGMGESLHGAFKtrkgmFRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGK 594
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  675 FEGSLALAQLKCSGTISVLELMEHGYPSRVLFADLYSMYKsVLPPELVS---LPARTFCEAMFQSLNLSAKDFKFGITKV 751
Cdd:cd14932   595 LAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE-ILTPNAIPkgfMDGKQACVLMVKALELDPNLYRIGQSKV 673

                  ...
gi 281362442  752 FFR 754
Cdd:cd14932   674 FFR 676
MYSc_Myo19 cd14880
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ...
71-752 5.62e-132

class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor for mitochondrial movement in vertebrate cells. It contains a variable number of IQ domains. Human myo19 contains a motor domain, three IQ motifs, and a short tail. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276846 [Multi-domain]  Cd Length: 658  Bit Score: 419.64  E-value: 5.62e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   71 ATFLDNLKTRYYKDKIYTYVANILIAVNPYREIKELYAPDTIKKYNGRSLGE-LPPHVFAIADKAIRDMR--VYKLSQSI 147
Cdd:cd14880     1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPQLYSPELMREYHAAPQPQkLKPHIFTVGEQTYRNVKslIEPVNQSI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  148 IVSGESGAGKTESTKYLLKYL---------CYSHDSAGPIETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEVHYDAKC 218
Cdd:cd14880    81 VVSGESGAGKTWTSRCLMKFYavvaasptsWESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  219 QVVGGYISHYLLEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSLGKPDDYRYLsgctqyfanakteqliPGSQKSKN 298
Cdd:cd14880   161 QMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWL----------------PNPERNLE 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  299 HqqkgplkdpiiDDyqhFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEiPDDVRGGCQVSEASEQSLTITSGL 378
Cdd:cd14880   225 E-----------DC---FEVTREAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFAD-SEDEAQPCQPMDDTKESVRTSALL 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  379 LGVDQTELRTALVSRVMQSkggGFKGTVIMVPLKIYEASNARDALAKAIYSRLFDRIVGLINQSIPFQAS--NFYIGVLD 456
Cdd:cd14880   290 LKLPEDHLLETLQIRTIRA---GKQQQVFKKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDswTTFIGLLD 366
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  457 IAGFEYFTVNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITFTDNQDIIELIEAKSNGIFTLLDEESKLP 536
Cdd:cd14880   367 VYGFESFPENSLEQLCINYANEKLQQHFVAHYLRAQQEEYAVEGLEWSFINYQDNQTCLDLIEGSPISICSLINEECRLN 446
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  537 KPSYSH-FTAEVHKSWANHYRLGlprssrlkaHRTLRDEEGFLVRHFAGAVCYNTEQFIEKNNDALHASLEGLVQECDNP 615
Cdd:cd14880   447 RPSSAAqLQTRIESALAGNPCLG---------HNKLSREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDP 517
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  616 LLQTLFPS--GSSTSVRGKLN----FISVGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQFEGSLALAQLKCSGT 689
Cdd:cd14880   518 LLQKLFPAnpEEKTQEEPSGQsrapVLTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGL 597
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281362442  690 ISVLELMEHGYPSRVLFADLYSMYKSVLPpelvSLPARTFCEAMFQSLNLSAKDFKFGITKVF 752
Cdd:cd14880   598 VETIHISAAGFPIRVSHQNFVERYKLLRR----LRPHTSSGPHSPYPAKGLSEPVHCGRTKVF 656
MYSc_Myh7b cd14927
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ...
71-754 8.60e-132

class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta myosin heavy chain 7b (also called KIAA1512, dJ756N5.1, MYH14, MHC14). MYH7B is a slow-twitch myosin. Mutations in this gene result in one form of autosomal dominant hearing impairment. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276953 [Multi-domain]  Cd Length: 676  Bit Score: 419.74  E-value: 8.60e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   71 ATFLDNLKTRYYKDKIYTYVANILIAVNPYREIKeLYAPDTIKKYNGRSLGELPPHVFAIADKAIRDMRVYKLSQSIIVS 150
Cdd:cd14927     1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLIT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  151 GESGAGKTESTKYLLKYL---------------CYSHDSAGPIETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEVHYD 215
Cdd:cd14927    80 GESGAGKTVNTKRVIQYFaivaalgdgpgkkaqFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  216 AKCQVVGGYISHYLLEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSLG-KPDDYRYlsgCTQyfanakteqlipGSQ 294
Cdd:cd14927   160 PTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSmNPYDYHF---CSQ------------GVT 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  295 KSKNhqqkgplkdpiIDDYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEIPDDVRGGCQVSEASEQSlti 374
Cdd:cd14927   225 TVDN-----------MDDGEELMATDHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKA--- 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  375 tSGLLGVDQTELRTALVS-RVMQSKGGGFKGTvimvplKIYEASNARDALAKAIYSRLFDRIVGLINQSIPFQ-ASNFYI 452
Cdd:cd14927   291 -AYLMGVSSADLLKGLLHpRVKVGNEYVTKGQ------SVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKlPRQFFI 363
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  453 GVLDIAGFEYFTVNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITF-TDNQDIIELIEaKSNGIFTLLDE 531
Cdd:cd14927   364 GVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWVFIDFgLDLQACIDLIE-KPLGILSILEE 442
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  532 ESKLPKPSYSHFTAevhKSWANHyrLG-LPRSSRLKAHRTLRDEEGFLVRHFAGAVCYNTEQFIEKNNDALHASLEGLVQ 610
Cdd:cd14927   443 ECMFPKASDASFKA---KLYDNH--LGkSPNFQKPRPDKKRKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQ 517
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  611 ECDNPLLQTLF------------PSGSSTSVRGKLNFISVGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQFEGS 678
Cdd:cd14927   518 KSQNKLLATLYenyvgsdstedpKSGVKEKRKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPF 597
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281362442  679 LALAQLKCSGTISVLELMEHGYPSRVLFADLYSMYKSVLP---PELVSLPARTFCEAMFQSLNLSAKDFKFGITKVFFR 754
Cdd:cd14927   598 LVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPsaiPDDKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
MYSc_Myo35 cd14896
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ...
74-754 3.91e-128

class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 domains, a single FERM domain, and an SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276861 [Multi-domain]  Cd Length: 644  Bit Score: 408.78  E-value: 3.91e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   74 LDNLKTRYYKDKIYTYVANILIAVNPYREIKeLYAPDTIKKYNGRSLGELPPHVFAIADKAirdmrvYKLSQS------I 147
Cdd:cd14896     4 LLCLKKRFHLGRIYTFGGPILLSLNPHRSLP-LFSEEVLASYHPRKALNTTPHIFAIAASA------YRLSQStgqdqcI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  148 IVSGESGAGKTESTKYLLKYLC-YSHDSAGPIETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEVHYDAKCqVVGGYIS 226
Cdd:cd14896    77 LLSGHSGSGKTEAAKKIVQFLSsLYQDQTEDRLRQPEDVLPILESFGHAKTILNANASRFGQVLRLHLQHGV-IVGASVS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  227 HYLLEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSLGKPDDYRYLsgctqyfanakteqlipgsqkskNHQQKGPLK 306
Cdd:cd14896   156 HYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYL-----------------------NQGGACRLQ 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  307 DPiiDDYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEIPDDVRGGCQVSeaSEQSLTITSGLLGVDQTEL 386
Cdd:cd14896   213 GK--EDAQDFEGLLKALQGLGLCAEELTAIWAVLAAILQLGNICFSSSERESQEVAAVS--SWAEIHTAARLLQVPPERL 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  387 RTALVSRVMQSKGGGfkgtvIMVPLKIYEASNARDALAKAIYSRLFDRIVGLINQ--SIPFQA-SNFYIGVLDIAGFEYF 463
Cdd:cd14896   289 EGAVTHRVTETPYGR-----VSRPLPVEGAIDARDALAKTLYSRLFTWLLKRINAwlAPPGEAeSDATIGVVDAYGFEAL 363
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  464 TVNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITFTDNQDIIELIEAKSNGIFTLLDEESKLPKPSYSHF 543
Cdd:cd14896   364 RVNGLEQLCINLASERLQLFSSQTLLAQEEEECQRELLPWVPIPQPPRESCLDLLVDQPHSLLSILDDQTWLSQATDHTF 443
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  544 TAEVHKSWANH--Y---RLGLPRssrlkahrtlrdeegFLVRHFAGAVCYNTEQFIEKNNDALHASLEGLVQECDNPLLQ 618
Cdd:cd14896   444 LQKCHYHHGDHpsYakpQLPLPV---------------FTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVG 508
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  619 TLFPSGSSTSvRGKLNFISVGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQFEGSLALAQLKCSGTISVLELMEH 698
Cdd:cd14896   509 SLFQEAEPQY-GLGQGKPTLASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSE 587
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 281362442  699 GYPSRVLFADLYSMYKSVLPPELVSLPARTFCEAMF-QSLNLSAKDFKFGITKVFFR 754
Cdd:cd14896   588 GFPVRVPFQAFLARFGALGSERQEALSDRERCGAILsQVLGAESPLYHLGATKVLLK 644
MYSc_Myh9 cd14919
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ...
71-754 2.04e-127

class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy chain 9 (also called NMMHCA, NMHC-II-A, MHA, FTNS, EPSTS, and DFNA17). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. The encoded protein is a myosin IIA heavy chain that contains an IQ domain and a myosin head-like domain which is involved in several important functions, including cytokinesis, cell motility and maintenance of cell shape. Defects in this gene have been associated with non-syndromic sensorineural deafness autosomal dominant type 17, Epstein syndrome, Alport syndrome with macrothrombocytopenia, Sebastian syndrome, Fechtner syndrome and macrothrombocytopenia with progressive sensorineural deafness. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276883 [Multi-domain]  Cd Length: 670  Bit Score: 407.94  E-value: 2.04e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   71 ATFLDNLKTRYYKDKIYTYVANILIAVNPYREIKeLYAPDTIKKYNGRSLGELPPHVFAIADKAIRDMRVYKLSQSIIVS 150
Cdd:cd14919     1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  151 GESGAGKTESTKYLLKYLCY---SHDSA---GPIETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEVHYDAKCQVVGGY 224
Cdd:cd14919    80 GESGAGKTENTKKVIQYLAHvasSHKSKkdqGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  225 ISHYLLEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSLGKPDDYRYLSgctqyfanaKTEQLIPGSQksknhqqkgp 304
Cdd:cd14919   160 IETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLS---------NGHVTIPGQQ---------- 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  305 lkdpiidDYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEipddVRGGCQVSEASEQSLTITSGLLGVDQT 384
Cdd:cd14919   221 -------DKDMFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKK----ERNTDQASMPDNTAAQKVSHLLGINVT 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  385 EL-RTALVSRVMQSKgggfkgTVIMVPLKIYEASNARDALAKAIYSRLFDRIVGLINQSI---PFQASNFyIGVLDIAGF 460
Cdd:cd14919   290 DFtRGILTPRIKVGR------DYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALdktKRQGASF-IGILDIAGF 362
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  461 EYFTVNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITF-TDNQDIIELIE--AKSNGIFTLLDEESKLPK 537
Cdd:cd14919   363 EIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIEkpAGPPGILALLDEECWFPK 442
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  538 PSYSHFTAEVHKSWANHYRLGLPRSsrlkahrtLRDEEGFLVRHFAGAVCYNTEQFIEKNNDALHASLEGLVQECDNPLL 617
Cdd:cd14919   443 ATDKSFVEKVVQEQGTHPKFQKPKQ--------LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFV 514
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  618 QTLF------------PSGSSTSVRGKLN-----FISVGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQFEGSLA 680
Cdd:cd14919   515 SELWkdvdriigldqvAGMSETALPGAFKtrkgmFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLV 594
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281362442  681 LAQLKCSGTISVLELMEHGYPSRVLFADLYSMYKSVLPPELVS--LPARTFCEAMFQSLNLSAKDFKFGITKVFFR 754
Cdd:cd14919   595 LDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKgfMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
MYSc_Myo47 cd14908
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ...
71-754 4.79e-127

class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not much is known about this myosin class. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276873 [Multi-domain]  Cd Length: 682  Bit Score: 407.37  E-value: 4.79e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   71 ATFLDNLKTRYYKDKIYTYVANILIAVNPYREIkELYAPDTIKKY---------NGRSLGELPPHVFAIADKAIRDM-RV 140
Cdd:cd14908     1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRL-PLYGKEILESYrqegllrsqGIESPQALGPHVFAIADRSYRQMmSE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  141 YKLSQSIIVSGESGAGKTESTKYLLKYLC------------YSHDSAGPIETKILDANPVLEAFGNAKTTRNNNSSRFGK 208
Cdd:cd14908    80 IRASQSILISGESGAGKTESTKIVMLYLTtlgngeegapneGEELGKLSIMDRVLQSNPILEAFGNARTLRNDNSSRFGK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  209 FIEVHYDAKCQVVGGYISHYLLEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKlslgkpddYRYLSGCTQYFANAKTEQ 288
Cdd:cd14908   160 FIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEK--------YEFHDGITGGLQLPNEFH 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  289 LIpgSQKSKNHQQKgplkdpiIDDYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEIPDDvrGGCQVSE-A 367
Cdd:cd14908   232 YT--GQGGAPDLRE-------FTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEED--GAAEIAEeG 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  368 SEQSLTITSGLLGVDQTELRTALVSRVMQSKGggfkgTVIMVPLKIYEASNARDALAKAIYSRLFDRIVGLINQSIPFQA 447
Cdd:cd14908   301 NEKCLARVAKLLGVDVDKLLRALTSKIIVVRG-----KEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWEN 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  448 SN---FYIGVLDIAGFEYFTVNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITFTDNQDIIELIEAKSNG 524
Cdd:cd14908   376 DKdirSSVGVLDIFGFECFAHNSFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFPDNQDCLDTIQAKKKG 455
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  525 IFTLLDEESKLP-KPSYSHFTAEVHKSWANHYRLGLPRSSRLKAHRTLRDEEGFLVRHFAGAVCYNTEQ-FIEKNNDALH 602
Cdd:cd14908   456 ILTMLDDECRLGiRGSDANYASRLYETYLPEKNQTHSENTRFEATSIQKTKLIFAVRHFAGQVQYTVETtFCEKNKDEIP 535
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  603 ASLEGLVQEcdnpllqtlfpsgsstsvrgklnfisvGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQFEGSLALA 682
Cdd:cd14908   536 LTADSLFES---------------------------GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTE 588
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  683 QLKCSGTISVLELMEHGYPSRVLFADLYSMYKSVLP--PELV-----------SLPARTFC---------EAMFQSLNLS 740
Cdd:cd14908   589 QLRYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLLPliPEVVlswsmerldpqKLCVKKMCkdlvkgvlsPAMVSMKNIP 668
                         730
                  ....*....|....
gi 281362442  741 AKDFKFGITKVFFR 754
Cdd:cd14908   669 EDTMQLGKSKVFMR 682
MYSc_Myh11 cd14921
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ...
71-754 1.69e-126

class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin heavy chain 11 (also called SMMHC, SMHC). The gene product is a subunit of a hexameric protein that consists of two heavy chain subunits and two pairs of non-identical light chain subunits. It functions as a major contractile protein, converting chemical energy into mechanical energy through the hydrolysis of ATP. The gene encoding a human ortholog of rat NUDE1 is transcribed from the reverse strand of this gene, and its 3' end overlaps with that of the latter. Inversion of the MYH11 locus is one of the most frequent chromosomal aberrations found in acute myeloid leukemia. Alternative splicing generates isoforms that are differentially expressed, with ratios changing during muscle cell maturation. Mutations in MYH11 have been described in individuals with thoracic aortic aneurysms leading to acute aortic dissections with patent ductus arteriosus. MYH11 mutations are also thought to contribute to human colorectal cancer and are also associated with Peutz-Jeghers syndrome. The mutations found in human intestinal neoplasia result in unregulated proteins with constitutive motor activity, similar to the mutant myh11 zebrafish. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276885 [Multi-domain]  Cd Length: 673  Bit Score: 405.55  E-value: 1.69e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   71 ATFLDNLKTRYYKDKIYTYVANILIAVNPYREIKeLYAPDTIKKYNGRSLGELPPHVFAIADKAIRDMRVYKLSQSIIVS 150
Cdd:cd14921     1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLP-IYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  151 GESGAGKTESTKYLLKYLCY---SH----DSA--GPIETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEVHYDAKCQVV 221
Cdd:cd14921    80 GESGAGKTENTKKVIQYLAVvasSHkgkkDTSitGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  222 GGYISHYLLEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSLGKPDDYRYLSgctqyfanakteqlipgsqksknhqq 301
Cdd:cd14921   160 GANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLS-------------------------- 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  302 KGPLKDPIIDDYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEipddVRGGCQVSEASEQSLTITSGLLGV 381
Cdd:cd14921   214 NGFVPIPAAQDDEMFQETLEAMSIMGFSEEEQLSILKVVSSVLQLGNIVFKK----ERNTDQASMPDNTAAQKVCHLMGI 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  382 DQTEL-RTALVSRVMQSKgggfkgTVIMVPLKIYEASNARDALAKAIYSRLFDRIVGLINQSI---PFQASNFyIGVLDI 457
Cdd:cd14921   290 NVTDFtRSILTPRIKVGR------DVVQKAQTKEQADFAIEALAKATYERLFRWILTRVNKALdktHRQGASF-LGILDI 362
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  458 AGFEYFTVNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITF-TDNQDIIELIEAKSN--GIFTLLDEESK 534
Cdd:cd14921   363 AGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIELIERPNNppGVLALLDEECW 442
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  535 LPKPSYSHFTAEVHKSWANHYRLGLPRSsrlkahrtLRDEEGFLVRHFAGAVCYNTEQFIEKNNDALHASLEGLVQECDN 614
Cdd:cd14921   443 FPKATDKSFVEKLCTEQGNHPKFQKPKQ--------LKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSD 514
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  615 PLLQTLF--------------------PSGSSTSvrgKLNFISVGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQ 674
Cdd:cd14921   515 KFVADLWkdvdrivgldqmakmtesslPSASKTK---KGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGK 591
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  675 FEGSLALAQLKCSGTISVLELMEHGYPSRVLFADLYSMYK----SVLPPELvsLPARTFCEAMFQSLNLSAKDFKFGITK 750
Cdd:cd14921   592 LDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEilaaNAIPKGF--MDGKQACILMIKALELDPNLYRIGQSK 669

                  ....
gi 281362442  751 VFFR 754
Cdd:cd14921   670 IFFR 673
MYSc_Myh1_insects_crustaceans cd14909
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ...
71-754 1.59e-124

class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in insects and crustaceans. Myh1 is a type I skeletal muscle myosin that in Humans is encoded by the MYH1 gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276874  Cd Length: 666  Bit Score: 399.98  E-value: 1.59e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   71 ATFLDNLKTRYYKDKIYTYVANILIAVNPYREIKeLYAPDTIKKYNGRSLGELPPHVFAIADKAIRDMRVYKLSQSIIVS 150
Cdd:cd14909     1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYP-VYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLIT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  151 GESGAGKTESTKYLLKYLCY---------SHDSAGPIETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEVHYDAKCQVV 221
Cdd:cd14909    80 GESGAGKTENTKKVIAYFATvgaskktdeAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  222 GGYISHYLLEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSLGKP-DDYRYLSgctqyfanakteqlipgsqksknhq 300
Cdd:cd14909   160 GADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLSDNiYDYYIVS------------------------- 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  301 qKGPLKDPIIDDYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEipddvRGGCQVSEAS-EQSLTITSGLL 379
Cdd:cd14909   215 -QGKVTVPNVDDGEEFSLTDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQ-----RGREEQAEQDgEEEGGRVSKLF 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  380 GVDQTELRTALVSRVMQSkGGGFkgtvIMVPLKIYEASNARDALAKAIYSRLFDRIVGLINQSIPF-QASNFYIGVLDIA 458
Cdd:cd14909   289 GCDTAELYKNLLKPRIKV-GNEF----VTQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTqQKRQHFIGVLDIA 363
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  459 GFEYFTVNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITF-TDNQDIIELIEaKSNGIFTLLDEESKLPK 537
Cdd:cd14909   364 GFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQEEYKREGIDWAFIDFgMDLLACIDLIE-KPMGILSILEEESMFPK 442
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  538 PSYSHF-----TAEVHKSwANHYRLGLPRSSRLKAHrtlrdeegFLVRHFAGAVCYNTEQFIEKNNDALHASLEGLVQEC 612
Cdd:cd14909   443 ATDQTFsekltNTHLGKS-APFQKPKPPKPGQQAAH--------FAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKS 513
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  613 DNPLLQTLF--------PSGSSTSVRGKLN--FISVGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQFEGSLALA 682
Cdd:cd14909   514 QNKLLIEIFadhagqsgGGEQAKGGRGKKGggFATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMH 593
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281362442  683 QLKCSGTISVLELMEHGYPSRVLFADLYSMYKSVLPPELVSLPARTFC-EAMFQSLNLSAKDFKFGITKVFFR 754
Cdd:cd14909   594 QLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGIQGEEDPKKAaEIILESIALDPDQYRLGHTKVFFR 666
MYSc_Myh4 cd14915
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ...
74-754 7.00e-123

class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 4 (also called MYH2B, MyHC-2B, MyHC-IIb). Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276879 [Multi-domain]  Cd Length: 671  Bit Score: 395.64  E-value: 7.00e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   74 LDNLKTRYYKDKIYTYVANILIAVNPYREIKeLYAPDTIKKYNGRSLGELPPHVFAIADKAIRDMRVYKLSQSIIVSGES 153
Cdd:cd14915     4 LYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  154 GAGKTESTKYLLKYLCY-------------SHDSAGPIETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEVHYDAKCQV 220
Cdd:cd14915    83 GAGKTVNTKRVIQYFATiavtgekkkeeaaSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  221 VGGYISHYLLEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSL-GKPDDYRYLSgctqyfanakteqlipgsqksknh 299
Cdd:cd14915   163 ASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLItTNPYDFAFVS------------------------ 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  300 qqKGPLKDPIIDDYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEIPDDVRGGCQVSEASEQSLTITSgll 379
Cdd:cd14915   219 --QGEITVPSIDDQEELMATDSAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTS--- 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  380 gVDQTELRTALV-SRVMQSKGGGFKGTVIMvplKIYeasNARDALAKAIYSRLFDRIVGLINQSIPF-QASNFYIGVLDI 457
Cdd:cd14915   294 -LNSADLLKALCyPRVKVGNEYVTKGQTVQ---QVY---NSVGALAKAIYEKMFLWMVTRINQQLDTkQPRQYFIGVLDI 366
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  458 AGFEYFTVNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITF-TDNQDIIELIEaKSNGIFTLLDEESKLP 536
Cdd:cd14915   367 AGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELIE-KPMGIFSILEEECMFP 445
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  537 KPSYSHFTA---EVHKSWANHYRLGLPRSSRLKAHrtlrdeegFLVRHFAGAVCYNTEQFIEKNNDALHASLEGLVQECD 613
Cdd:cd14915   446 KATDTSFKNklyEQHLGKSNNFQKPKPAKGKAEAH--------FSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSG 517
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  614 NPLLQTLFPSGSSTSVRG----------KLNFISVGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQFEGSLALAQ 683
Cdd:cd14915   518 MKTLAFLFSGGQTAEAEGgggkkggkkkGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQ 597
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281362442  684 LKCSGTISVLELMEHGYPSRVLFADLYSMYK---SVLPPELVSLPARTFCEAMFQSLNLSAKDFKFGITKVFFR 754
Cdd:cd14915   598 LRCNGVLEGIRICRKGFPSRILYADFKQRYKvlnASAIPEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
MYSc_Myo25 cd14886
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ...
71-754 2.82e-122

class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell adhesion and filopodia formation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276851  Cd Length: 650  Bit Score: 393.48  E-value: 2.82e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   71 ATFLDNLKTRYYKDKIYTYVANILIAVNPYREIKELYAPDTIKKYNG--RSLG---ELPPHVFAIADKAIRDMRVYKLSQ 145
Cdd:cd14886     1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRNLYGTEVIGRYRQadTSRGfpsDLPPHSYAVAQSALNGLISDGISQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  146 SIIVSGESGAGKTESTKYLLKYLCYSHDSAG-PIETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEVHYDAKCQVVGGY 224
Cdd:cd14886    81 SCIVSGESGAGKTETAKQLMNFFAYGHSTSStDVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGLKGGK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  225 ISHYLLEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSLGKPDDYRYLSGCTQYFAnakteqlipgsqksknhqqkgp 304
Cdd:cd14886   161 ITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCYDA---------------------- 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  305 lkdPIIDDYQHFHNLDKALGRLgLSDTEKLGIYSLVAAVLHLGNIAFEEIPDDVrggcqVSEASEQSLTITSG----LLG 380
Cdd:cd14886   219 ---PGIDDQKEFAPVRSQLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDMG-----VINAAKISNDEDFGkmceLLG 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  381 VDQTELRTALVSRVMqskggGFKGTVIMVPLKIYEASNARDALAKAIYSRLFDRIVGLINQSIPFQA-SNFYIGVLDIAG 459
Cdd:cd14886   290 IESSKAAQAIITKVV-----VINNETIISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDAdARPWIGILDIYG 364
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  460 FEYFTVNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITFTDNQDIIELIEAKSNGIFTLLDEESKLPKPS 539
Cdd:cd14886   365 FEFFERNTYEQLLINYANERLQQYFINQVFKSEIQEYEIEGIDHSMITFTDNSNVLAVFDKPNLSIFSFLEEQCLIQTGS 444
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  540 YSHFTAEVHKSWANHyrLGLP-RSSRLKahrtlrdeegFLVRHFAGAVCYNTEQFIEKNNDALHASLEGLVQECDNPLLQ 618
Cdd:cd14886   445 SEKFTSSCKSKIKNN--SFIPgKGSQCN----------FTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVN 512
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  619 TLFP--SGSSTSVRGKLnfisVGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQFEGSLALAQLKCSGTISVLELM 696
Cdd:cd14886   513 KAFSdiPNEDGNMKGKF----LGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTI 588
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281362442  697 EHGYPSRVLFA------DLYSMYKSVLPPELVSLpaRTFCEAMFQSLNLSAKDFKFGITKVFFR 754
Cdd:cd14886   589 HRGFAYNDTFEeffhrnKILISHNSSSQNAGEDL--VEAVKSILENLGIPCSDYRIGKTKVFLR 650
MYSc_Myh19 cd15896
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ...
71-754 6.12e-122

class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain 19. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276899 [Multi-domain]  Cd Length: 675  Bit Score: 393.28  E-value: 6.12e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   71 ATFLDNLKTRYYKDKIYTYVANILIAVNPYREIKeLYAPDTIKKYNGRSLGELPPHVFAIADKAIRDMRVYKLSQSIIVS 150
Cdd:cd15896     1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  151 GESGAGKTESTKYLLKYLCY---SHD----------SAGPIETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEVHYDAK 217
Cdd:cd15896    80 GESGAGKTENTKKVIQYLAHvasSHKtkkdqnslalSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  218 CQVVGGYISHYLLEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSLGKPDDYRYLSgctqyfanaKTEQLIPGSQksk 297
Cdd:cd15896   160 GYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLS---------NGNVTIPGQQ--- 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  298 nhqqkgplkdpiidDYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEipddVRGGCQVSEASEQSLTITSG 377
Cdd:cd15896   228 --------------DKDLFTETMEAFRIMGIPEDEQIGMLKVVASVLQLGNMSFKK----ERHTDQASMPDNTAAQKVCH 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  378 LLGVDQTELRTALVS-RVMQSKgggfkgTVIMVPLKIYEASNARDALAKAIYSRLFDRIVGLINQSI---PFQASNFyIG 453
Cdd:cd15896   290 LMGMNVTDFTRAILSpRIKVGR------DYVQKAQTQEQAEFAVEALAKATYERMFRWLVMRINKALdktKRQGASF-IG 362
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  454 VLDIAGFEYFTVNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITF-TDNQDIIELIE--AKSNGIFTLLD 530
Cdd:cd15896   363 ILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIEkpASPPGILALLD 442
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  531 EESKLPKPSYSHFTAEVHKSWANHYRLGLPRSsrlkahrtLRDEEGFLVRHFAGAVCYNTEQFIEKNNDALHASLEGLVQ 610
Cdd:cd15896   443 EECWFPKATDKSFVEKVLQEQGTHPKFFKPKK--------LKDEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLN 514
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  611 ECDNPLLQTLFPSGSSTSVRGKLN---------------FISVGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQF 675
Cdd:cd15896   515 QSTDKFVSELWKDVDRIVGLDKVSgmsempgafktrkgmFRTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKL 594
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  676 EGSLALAQLKCSGTISVLELMEHGYPSRVLFADLYSMYKSVLPPELVS--LPARTFCEAMFQSLNLSAKDFKFGITKVFF 753
Cdd:cd15896   595 DPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKgfMDGKQACVLMIKSLELDPNLYRIGQSKVFF 674

                  .
gi 281362442  754 R 754
Cdd:cd15896   675 R 675
MYSc_Myh7 cd14917
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ...
74-754 8.68e-121

class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I cardiac muscle myosin heavy chain 7 (also called CMH1, MPD1, and CMD1S). Muscle myosin is a hexameric protein containing 2 heavy chain subunits, 2 alkali light chain subunits, and 2 regulatory light chain subunits. It is expressed predominantly in normal human ventrical and in skeletal muscle tissues rich in slow-twitch type I muscle fibers. Changes in the relative abundance of this protein and the alpha (or fast) heavy subunit of cardiac myosin correlate with the contractile velocity of cardiac muscle. Its expression is also altered during thyroid hormone depletion and hemodynamic overloading. Mutations in this gene are associated with familial hypertrophic cardiomyopathy, myosin storage myopathy, dilated cardiomyopathy, and Laing early-onset distal myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276881 [Multi-domain]  Cd Length: 668  Bit Score: 390.23  E-value: 8.68e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   74 LDNLKTRYYKDKIYTYVANILIAVNPYREIKeLYAPDTIKKYNGRSLGELPPHVFAIADKAIRDMRVYKLSQSIIVSGES 153
Cdd:cd14917     4 LYNLKERYASWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGES 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  154 GAGKTESTKYLLKYLCY-----------SHDSAGPIETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEVHYDAKCQVVG 222
Cdd:cd14917    83 GAGKTVNTKRVIQYFAViaaigdrskkdQTPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLAS 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  223 GYISHYLLEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSL-GKPDDYRYLSgctqyfanakteqlipgsqksknhqq 301
Cdd:cd14917   163 ADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLItNNPYDYAFIS-------------------------- 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  302 KGPLKDPIIDDYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEIPDDVRGGCQVSEASEQSltitSGLLGV 381
Cdd:cd14917   217 QGETTVASIDDAEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKS----AYLMGL 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  382 DQTELRTALV-SRVMQSKGGGFKGTvimvplKIYEASNARDALAKAIYSRLFDRIVGLINQSIPF-QASNFYIGVLDIAG 459
Cdd:cd14917   293 NSADLLKGLChPRVKVGNEYVTKGQ------NVQQVIYATGALAKAVYEKMFNWMVTRINATLETkQPRQYFIGVLDIAG 366
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  460 FEYFTVNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITF-TDNQDIIELIEaKSNGIFTLLDEESKLPKP 538
Cdd:cd14917   367 FEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKA 445
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  539 SYSHFTAevhKSWANHyrlgLPRSSRLKAHRTLRD--EEGFLVRHFAGAVCYNTEQFIEKNNDALHASLEGLVQECDNPL 616
Cdd:cd14917   446 TDMTFKA---KLFDNH----LGKSNNFQKPRNIKGkpEAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKL 518
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  617 LQTLFP--SGSSTSVRGKLNFISVGSKFKT-------QLGELMEKLEQNGTNFIRCIKPNSKMIDRQFEGSLALAQLKCS 687
Cdd:cd14917   519 LSNLFAnyAGADAPIEKGKGKAKKGSSFQTvsalhreNLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCN 598
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  688 GTISVLELMEHGYPSRVLFADLYSMYKSVLP---PELVSLPARTFCEAMFQSLNLSAKDFKFGITKVFFR 754
Cdd:cd14917   599 GVLEGIRICRKGFPNRILYGDFRQRYRILNPaaiPEGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
MYSc_Myh2_mammals cd14912
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ...
74-754 1.76e-120

class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in mammals. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276877 [Multi-domain]  Cd Length: 673  Bit Score: 389.48  E-value: 1.76e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   74 LDNLKTRYYKDKIYTYVANILIAVNPYREIKeLYAPDTIKKYNGRSLGELPPHVFAIADKAIRDMRVYKLSQSIIVSGES 153
Cdd:cd14912     4 LYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  154 GAGKTESTKYLLKYLCY-------------SHDSAGPIETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEVHYDAKCQV 220
Cdd:cd14912    83 GAGKTVNTKRVIQYFATiavtgekkkeeitSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  221 VGGYISHYLLEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSL-GKPDDYRYLSgctqyfanakteqlipgsqksknh 299
Cdd:cd14912   163 ASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLItTNPYDYPFVS------------------------ 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  300 qqKGPLKDPIIDDYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEIPDDVRGGCQVSEASEQSLTITSgll 379
Cdd:cd14912   219 --QGEISVASIDDQEELMATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQS--- 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  380 gVDQTELRTALV-SRVMQSKGGGFKGTVIMvplkiyEASNARDALAKAIYSRLFDRIVGLINQSIPF-QASNFYIGVLDI 457
Cdd:cd14912   294 -LNSADLLKALCyPRVKVGNEYVTKGQTVE------QVTNAVGALAKAVYEKMFLWMVARINQQLDTkQPRQYFIGVLDI 366
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  458 AGFEYFTVNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITF-TDNQDIIELIEaKSNGIFTLLDEESKLP 536
Cdd:cd14912   367 AGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFP 445
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  537 KPSYSHFTAEVhkswanhYRLGLPRSSRLKAHRTLRD--EEGFLVRHFAGAVCYNTEQFIEKNNDALHASLEGLVQECDN 614
Cdd:cd14912   446 KATDTSFKNKL-------YEQHLGKSANFQKPKVVKGkaEAHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAM 518
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  615 PLLQTLFPSGSSTSVRGK------------LNFISVGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQFEGSLALA 682
Cdd:cd14912   519 KTLAYLFSGAQTAEGASAgggakkggkkkgSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLH 598
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281362442  683 QLKCSGTISVLELMEHGYPSRVLFADLYSMYK---SVLPPELVSLPARTFCEAMFQSLNLSAKDFKFGITKVFFR 754
Cdd:cd14912   599 QLRCNGVLEGIRICRKGFPSRILYADFKQRYKvlnASAIPEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
MYSc_Myh1_mammals cd14910
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ...
74-754 5.91e-120

class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in mammals. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276875 [Multi-domain]  Cd Length: 671  Bit Score: 387.93  E-value: 5.91e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   74 LDNLKTRYYKDKIYTYVANILIAVNPYREIKeLYAPDTIKKYNGRSLGELPPHVFAIADKAIRDMRVYKLSQSIIVSGES 153
Cdd:cd14910     4 LYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  154 GAGKTESTKYLLKYLCY-------------SHDSAGPIETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEVHYDAKCQV 220
Cdd:cd14910    83 GAGKTVNTKRVIQYFATiavtgekkkeeatSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  221 VGGYISHYLLEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSL-GKPDDYRYLSgctqyfanakteqlipgsqksknh 299
Cdd:cd14910   163 ASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLItTNPYDYAFVS------------------------ 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  300 qqKGPLKDPIIDDYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEIPDDVRGGCQVSEASEQSLTITSgll 379
Cdd:cd14910   219 --QGEITVPSIDDQEELMATDSAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQN--- 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  380 gVDQTELRTALV-SRVMQSKGGGFKGTVIMvplKIYeasNARDALAKAIYSRLFDRIVGLINQSIPF-QASNFYIGVLDI 457
Cdd:cd14910   294 -LNSADLLKALCyPRVKVGNEYVTKGQTVQ---QVY---NAVGALAKAVYDKMFLWMVTRINQQLDTkQPRQYFIGVLDI 366
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  458 AGFEYFTVNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITF-TDNQDIIELIEaKSNGIFTLLDEESKLP 536
Cdd:cd14910   367 AGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELIE-KPMGIFSILEEECMFP 445
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  537 KPSYSHFTA---EVHKSWANHYRLGLPRSSRLKAHrtlrdeegFLVRHFAGAVCYNTEQFIEKNNDALHASLEGLVQECD 613
Cdd:cd14910   446 KATDTSFKNklyEQHLGKSNNFQKPKPAKGKVEAH--------FSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSS 517
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  614 NPLLQTLFPSGSSTSVR---GK-------LNFISVGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQFEGSLALAQ 683
Cdd:cd14910   518 MKTLALLFSGAAAAEAEeggGKkggkkkgSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQ 597
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281362442  684 LKCSGTISVLELMEHGYPSRVLFADLYSMYK---SVLPPELVSLPARTFCEAMFQSLNLSAKDFKFGITKVFFR 754
Cdd:cd14910   598 LRCNGVLEGIRICRKGFPSRILYADFKQRYKvlnASAIPEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
MYSc_Myh8 cd14918
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ...
74-754 7.53e-120

class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle myosin heavy chain 8 (also called MyHC-peri, MyHC-pn). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. A mutation in this gene results in trismus-pseudocamptodactyly syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276882 [Multi-domain]  Cd Length: 668  Bit Score: 387.55  E-value: 7.53e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   74 LDNLKTRYYKDKIYTYVANILIAVNPYREIKeLYAPDTIKKYNGRSLGELPPHVFAIADKAIRDMRVYKLSQSIIVSGES 153
Cdd:cd14918     4 LYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  154 GAGKTESTKYLLKYLCY-----------SHDSAGPIETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEVHYDAKCQVVG 222
Cdd:cd14918    83 GAGKTVNTKRVIQYFATiavtgekkkeeSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  223 GYISHYLLEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSL-GKPDDYRYLSgctqyfanakteqlipgsqksknhqq 301
Cdd:cd14918   163 ADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLItTNPYDYAFVS-------------------------- 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  302 KGPLKDPIIDDYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEIPDDVRGGCQVSEASEQSLTITSgllgV 381
Cdd:cd14918   217 QGEITVPSIDDQEELMATDSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQS----L 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  382 DQTELRTALV-SRVMQSKGGGFKGTVIMvplKIYeasNARDALAKAIYSRLFDRIVGLINQSIPF-QASNFYIGVLDIAG 459
Cdd:cd14918   293 NSADLLKALCyPRVKVGNEYVTKGQTVQ---QVY---NAVGALAKAVYEKMFLWMVTRINQQLDTkQPRQYFIGVLDIAG 366
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  460 FEYFTVNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITF-TDNQDIIELIEaKSNGIFTLLDEESKLPKP 538
Cdd:cd14918   367 FEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPLGIFSILEEECMFPKA 445
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  539 SYSHFTAEVhkswanhYRLGLPRSSRLKAHRTLRD--EEGFLVRHFAGAVCYNTEQFIEKNNDALHASLEGLVQECDNPL 616
Cdd:cd14918   446 TDTSFKNKL-------YDQHLGKSANFQKPKVVKGkaEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKT 518
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  617 LQTLFPS-----GSSTSVRGK----LNFISVGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQFEGSLALAQLKCS 687
Cdd:cd14918   519 LASLFSTyasaeADSGAKKGAkkkgSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCN 598
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  688 GTISVLELMEHGYPSRVLFADLYSMYK---SVLPPELVSLPARTFCEAMFQSLNLSAKDFKFGITKVFFR 754
Cdd:cd14918   599 GVLEGIRICRKGFPSRILYGDFKQRYKvlnASAIPEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
MYSc_Myh14_mammals cd14930
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ...
71-754 2.73e-119

class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy chain 14 (also called FLJ13881, KIAA2034, MHC16, MYH17). Its members include mammals, chickens, and turtles. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.


Pssm-ID: 276893 [Multi-domain]  Cd Length: 670  Bit Score: 385.99  E-value: 2.73e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   71 ATFLDNLKTRYYKDKIYTYVANILIAVNPYREIKeLYAPDTIKKYNGRSLGELPPHVFAIADKAIRDMRVYKLSQSIIVS 150
Cdd:cd14930     1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  151 GESGAGKTESTKYLLKYLCYSHDSA---------GPIETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEVHYDAKCQVV 221
Cdd:cd14930    80 GESGAGKTENTKKVIQYLAHVASSPkgrkepgvpGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  222 GGYISHYLLEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSLGKPDDYRYLSgctqyfanakteqlipgsqksknhqq 301
Cdd:cd14930   160 GANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLT-------------------------- 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  302 KGPLKDPiIDDYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEipddVRGGCQVSEASEQSLTITSGLLGV 381
Cdd:cd14930   214 NGPSSSP-GQERELFQETLESLRVLGFSHEEITSMLRMVSAVLQFGNIVLKR----ERNTDQATMPDNTAAQKLCRLLGL 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  382 DQTELRTALVS-RVMQSKgggfkgTVIMVPLKIYEASNARDALAKAIYSRLFDRIVGLINQSI---PFQASNFyIGVLDI 457
Cdd:cd14930   289 GVTDFSRALLTpRIKVGR------DYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALdrsPRQGASF-LGILDI 361
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  458 AGFEYFTVNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITF-TDNQDIIELIEAKSN--GIFTLLDEESK 534
Cdd:cd14930   362 AGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPANppGLLALLDEECW 441
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  535 LPKPSYSHFTAEVHKSWANHYRLGLPRSsrlkahrtLRDEEGFLVRHFAGAVCYNTEQFIEKNNDALHASLEGLVQECDN 614
Cdd:cd14930   442 FPKATDKSFVEKVAQEQGGHPKFQRPRH--------LRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTD 513
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  615 PLLQTLF------------------PSGSSTSvRGKlnFISVGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQFE 676
Cdd:cd14930   514 RLTAEIWkdvegivgleqvsslgdgPPGGRPR-RGM--FRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLE 590
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  677 GSLALAQLKCSGTISVLELMEHGYPSRVLFADLYSMYKSVLPPELVS--LPARTFCEAMFQSLNLSAKDFKFGITKVFFR 754
Cdd:cd14930   591 PRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKgfMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
MYSc_Myh6 cd14916
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ...
74-754 2.10e-118

class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac muscle myosin heavy chain 6. Cardiac muscle myosin is a hexamer consisting of two heavy chain subunits, two light chain subunits, and two regulatory subunits. This gene encodes the alpha heavy chain subunit of cardiac myosin. Mutations in this gene cause familial hypertrophic cardiomyopathy and atrial septal defect. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276880 [Multi-domain]  Cd Length: 670  Bit Score: 383.64  E-value: 2.10e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   74 LDNLKTRYYKDKIYTYVANILIAVNPYREIKeLYAPDTIKKYNGRSLGELPPHVFAIADKAIRDMRVYKLSQSIIVSGES 153
Cdd:cd14916     4 LYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGES 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  154 GAGKTESTKYLLKYLC------------YSHDSAGPIETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEVHYDAKCQVV 221
Cdd:cd14916    83 GAGKTVNTKRVIQYFAsiaaigdrskkeNPNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  222 GGYISHYLLEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSL-GKPDDYRYLSgctqyfanakteqlipgsqksknhq 300
Cdd:cd14916   163 SADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVtNNPYDYAFVS------------------------- 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  301 qKGPLKDPIIDDYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEIPDDVRGGCQVSEASEQSltitSGLLG 380
Cdd:cd14916   218 -QGEVSVASIDDSEELLATDSAFDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKS----AYLMG 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  381 VDQTELRTALV-SRVMQSKGGGFKGTVIMvplKIYEASNardALAKAIYSRLFDRIVGLINQSIPF-QASNFYIGVLDIA 458
Cdd:cd14916   293 LNSADLLKGLChPRVKVGNEYVTKGQSVQ---QVYYSIG---ALAKSVYEKMFNWMVTRINATLETkQPRQYFIGVLDIA 366
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  459 GFEYFTVNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITF-TDNQDIIELIEaKSNGIFTLLDEESKLPK 537
Cdd:cd14916   367 GFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPK 445
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  538 PSYSHFTAevhKSWANHyrlgLPRSSRLKAHRTL--RDEEGFLVRHFAGAVCYNTEQFIEKNNDALHASLEGLVQECDNP 615
Cdd:cd14916   446 ASDMTFKA---KLYDNH----LGKSNNFQKPRNVkgKQEAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLK 518
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  616 LLQTLFPS--GSSTSVRGK--------LNFISVGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQFEGSLALAQLK 685
Cdd:cd14916   519 LMATLFSTyaSADTGDSGKgkggkkkgSSFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLR 598
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 281362442  686 CSGTISVLELMEHGYPSRVLFADLYSMYKSVLP---PELVSLPARTFCEAMFQSLNLSAKDFKFGITKVFFR 754
Cdd:cd14916   599 CNGVLEGIRICRKGFPNRILYGDFRQRYRILNPaaiPEGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
MYSc_Myh13 cd14923
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ...
74-754 3.13e-117

class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 13 (also called MyHC-eo) in mammals, chicken, and green anole. Myh13 is a myosin whose expression is restricted primarily to the extrinsic eye muscles which are specialized for function in eye movement. Class II myosins, also called conventional myosins, are the myosin type responsible for producing muscle contraction in muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276887 [Multi-domain]  Cd Length: 671  Bit Score: 380.57  E-value: 3.13e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   74 LDNLKTRYYKDKIYTYVANILIAVNPYREIKeLYAPDTIKKYNGRSLGELPPHVFAIADKAIRDMRVYKLSQSIIVSGES 153
Cdd:cd14923     4 LYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGES 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  154 GAGKTESTKYLLKYLC------------YSHDSAGPIETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEVHYDAKCQVV 221
Cdd:cd14923    83 GAGKTVNTKRVIQYFAtiavtgdkkkeqQPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  222 GGYISHYLLEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSLG-KPDDYRYLSgctqyfanakteqlipgsqksknhq 300
Cdd:cd14923   163 SADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLIStNPFDFPFVS------------------------- 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  301 qKGPLKDPIIDDYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEIPDDVRGGCQVSEASEQSltitSGLLG 380
Cdd:cd14923   218 -QGEVTVASIDDSEELLATDNAIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKA----GYLMG 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  381 VDQTELRTALV-SRVMQSKGGGFKGTvimvplKIYEASNARDALAKAIYSRLFDRIVGLINQSIPF-QASNFYIGVLDIA 458
Cdd:cd14923   293 LNSAEMLKGLCcPRVKVGNEYVTKGQ------NVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTkQPRQYFIGVLDIA 366
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  459 GFEYFTVNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITF-TDNQDIIELIEaKSNGIFTLLDEESKLPK 537
Cdd:cd14923   367 GFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELIE-KPMGIFSILEEECMFPK 445
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  538 PSYSHFTAEV---HKSWANHYRLGLPRSSRLKAHrtlrdeegFLVRHFAGAVCYNTEQFIEKNNDALHASLEGLVQECDN 614
Cdd:cd14923   446 ATDTSFKNKLydqHLGKSNNFQKPKPAKGKAEAH--------FSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSL 517
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  615 PLLQTLFPSGSSTSV-----------RGKLNFISVGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQFEGSLALAQ 683
Cdd:cd14923   518 KLLSFLFSNYAGAEAgdsggskkggkKKGSSFQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQ 597
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281362442  684 LKCSGTISVLELMEHGYPSRVLFADLYSMYK---SVLPPELVSLPARTFCEAMFQSLNLSAKDFKFGITKVFFR 754
Cdd:cd14923   598 LRCNGVLEGIRICRKGFPSRILYADFKQRYRilnASAIPEGQFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
MYSc_Myo17 cd14879
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ...
68-753 1.17e-109

class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase uses its motor domain to tether its vesicular cargo to peripheral actin. It works in opposition to dynein, contributing to the retention of Mcs1 vesicles at the site of cell growth and increasing vesicle fusion necessary for polarized growth. Class 17 myosins consist of a N-terminal myosin motor domain with Cyt-b5, chitin synthase 2, and a DEK_C domains at it C-terminus. The chitin synthase region contains several transmembrane domains by which myosin 17 is thought to bind secretory vesicles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276845 [Multi-domain]  Cd Length: 647  Bit Score: 359.17  E-value: 1.17e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   68 LNEATFLDNLKTRYYKDKIYTYV-ANILIAVNPY-----------REIKELYAPDTikkynGRSLGELPPHVFAIADKAI 135
Cdd:cd14879     1 PSDDAITSHLASRFRSDLPYTRLgSSALVAVNPYkylssnsdaslGEYGSEYYDTT-----SGSKEPLPPHAYDLAARAY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  136 RDMRVYKLSQSIIVSGESGAGKTESTKYLLKYLC-YShdSAGPIETK----ILDANPVLEAFGNAKTTRNNNSSRFGKFI 210
Cdd:cd14879    76 LRMRRRSEDQAVVFLGETGSGKSESRRLLLRQLLrLS--SHSKKGTKlssqISAAEFVLDSFGNAKTLTNPNASRFGRYT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  211 EVHYDAKCQVVGGYISHYLLEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSLGKPDDYRYL--SGCTQyfanaktEQ 288
Cdd:cd14879   154 ELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLasYGCHP-------LP 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  289 LIPGSqksknhqqkgplkdpiiDDYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEIPDDVRGGCQVseAS 368
Cdd:cd14879   227 LGPGS-----------------DDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFTYDHEGGEESAVV--KN 287
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  369 EQSLTITSGLLGVDQTELRTALVSR----------VM-QSKGggfkgtvimvplkiyeASNARDALAKAIYSRLFDRIVG 437
Cdd:cd14879   288 TDVLDIVAAFLGVSPEDLETSLTYKtklvrkelctVFlDPEG----------------AAAQRDELARTLYSLLFAWVVE 351
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  438 LINQSIPFQASNF--YIGVLDIAGFEYFT---VNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITFTDNQ 512
Cdd:cd14879   352 TINQKLCAPEDDFatFISLLDFPGFQNRSstgGNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSYFDNS 431
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  513 DIIELIEAKSNGIFTLLDEESK-LPKPSYSHFTAEVHKSWANH--YRLGLPRSSRlkahrtlRDEEGFLVRHFAGAVCYN 589
Cdd:cd14879   432 DCVRLLRGKPGGLLGILDDQTRrMPKKTDEQMLEALRKRFGNHssFIAVGNFATR-------SGSASFTVNHYAGEVTYS 504
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  590 TEQFIEKNNDALhasleglvqecdNPLLQTLFpsGSSTSVRGKLNfisvgskfktqlgELMEKLEQNGTNFIRCIKPNSK 669
Cdd:cd14879   505 VEGFLERNGDVL------------SPDFVNLL--RGATQLNAALS-------------ELLDTLDRTRLWSVFCIRPNDS 557
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  670 MIDRQFEGSLALAQLKCSGTISVLELMEHGYPSRVLFADLYSMYKSVLPPELVSlPARTFCEAMfqsLNLSAKDFKFGIT 749
Cdd:cd14879   558 QLPNSFDKRRVKAQIRSLGLPELAARLRVEYVVSLEHAEFCERYKSTLRGSAAE-RIRQCARAN---GWWEGRDYVLGNT 633

                  ....
gi 281362442  750 KVFF 753
Cdd:cd14879   634 KVFL 637
MYSc_Myo26 cd14887
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ...
71-754 2.04e-105

class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the other myosins that have a MyTH4 domain such as class III, VII, IX, X , XV, XVI, XVII, XX, XXII, XXV, and XXXIV. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276852  Cd Length: 725  Bit Score: 350.10  E-value: 2.04e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   71 ATFLDNLKTRYYK--------DKIYTYVANILIAVNPYREIkELYAPDTIKKYNGRSLGELPPHVFAIADKAIRDMRVYK 142
Cdd:cd14887     1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFF-NLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  143 LSQSIIVSGESGAGKTESTKYLLKYLCYSHD-----SAGPIETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEVHYDAK 217
Cdd:cd14887    80 RSQSILISGESGAGKTETSKHVLTYLAAVSDrrhgaDSQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  218 CQVVGGYISHYLLEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSLGKPDDYRYlsgctqyfanakteqlipgsqksk 297
Cdd:cd14887   160 GKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSSAGEGDPEST------------------------ 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  298 nhqqkgplkdpiiddyqHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEIPDD----------VRGGC----- 362
Cdd:cd14887   216 -----------------DLRRITAAMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPetskkrkltsVSVGCeetaa 278
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  363 ---------------QVSEASEQSLTITSGLLGV-----DQTELRTALVSRVMQSKGGGFkgtvimvplKIYEASNARDA 422
Cdd:cd14887   279 drshssevkclssglKVTEASRKHLKTVARLLGLppgveGEEMLRLALVSRSVRETRSFF---------DLDGAAAARDA 349
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  423 LAKAIYSRLFDRIVGLINQSIPFQASNFY---------------IGVLDIAGFEYF---TVNSFEQFCINYCNEKLQKFF 484
Cdd:cd14887   350 ACKNLYSRAFDAVVARINAGLQRSAKPSEsdsdedtpsttgtqtIGILDLFGFEDLrnhSKNRLEQLCINYANERLHCFL 429
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  485 NDNILKNEQELYKREGLNVPEITFTDNQDI---IELIEAKSN-----------------------GIFTLLDEESKLPKP 538
Cdd:cd14887   430 LEQLILNEHMLYTQEGVFQNQDCSAFPFSFplaSTLTSSPSStspfsptpsfrsssafatspslpSSLSSLSSSLSSSPP 509
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  539 SYS-HFTAEVHKSWANHYRLGLPRSSRLKAHRTlRDEEGFLVRHFAGAVCYNTEQFIEKNNDALHASLEGLVQECDNplL 617
Cdd:cd14887   510 VWEgRDNSDLFYEKLNKNIINSAKYKNITPALS-RENLEFTVSHFACDVTYDARDFCRANREATSDELERLFLACST--Y 586
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  618 QTLFPSGSSTSVRGKLNFIS-VGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQFEGSLALAQLKCSGTISVLELM 696
Cdd:cd14887   587 TRLVGSKKNSGVRAISSRRStLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVM 666
                         730       740       750       760       770
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 281362442  697 EHGYPSRVLFADLYSMYKSVLPPELV-SLPARTFCEAMFQSLNLSAKDFKFGITKVFFR 754
Cdd:cd14887   667 ADGFPCRLPYVELWRRYETKLPMALReALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
MYSc_Myo38 cd14899
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ...
71-717 1.75e-103

class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276864 [Multi-domain]  Cd Length: 717  Bit Score: 344.77  E-value: 1.75e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   71 ATFLDNLKTRYYKDKIYTYVANILIAVNPYREIKELYAPDTIKKY---NGRSLGE-------LPPHVFAIADKAIRDMRV 140
Cdd:cd14899     1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPQLYGDEILRGYaydHNSQFGDrvtstdpREPHLFAVARAAYIDIVQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  141 YKLSQSIIVSGESGAGKTESTKYLLKYLCYSHDSAGP------------------IETKILDANPVLEAFGNAKTTRNNN 202
Cdd:cd14899    81 NGRSQSILISGESGAGKTEATKIIMTYFAVHCGTGNNnltnsesisppaspsrttIEEQVLQSNPILEAFGNARTVRNDN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  203 SSRFGKFIEVHY-DAKCQVVGGYISHYLLEKSRICTQSAEERNYHVFYMLLAG----APQQLRDKLSL-GKPDDYRYLSg 276
Cdd:cd14899   161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncVSKEQKQVLALsGGPQSFRLLN- 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  277 ctqyfanakteqlipgsqKSKNHQQKGPLKDPIiddyqHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEIPD 356
Cdd:cd14899   240 ------------------QSLCSKRRDGVKDGV-----QFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQIPH 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  357 DVRGGCQVSEASEQS--------LTITSGLLGVDQTELRTALVSRVMQSKGggfkgTVIMVPLKIYEASNARDALAKAIY 428
Cdd:cd14899   297 KGDDTVFADEARVMSsttgafdhFTKAAELLGVSTEALDHALTKRWLHASN-----ETLVVGVDVAHARNTRNALTMECY 371
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  429 SRLFDRIVGLINQSIPFQAS----------------NFYIGVLDIAGFEYFTVNSFEQFCINYCNEKLQKFFNDNILKNE 492
Cdd:cd14899   372 RLLFEWLVARVNNKLQRQASapwgadesdvddeedaTDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEE 451
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  493 QELYKREGLNVPEITFTDNQDIIELIEAKSNGIFTLLDEESKLPKPSYSHFTAEVHKSWANHYRLGLPRSSRLKAHRTlr 572
Cdd:cd14899   452 QRLYRDEGIRWSFVDFPNNRACLELFEHRPIGIFSLTDQECVFPQGTDRALVAKYYLEFEKKNSHPHFRSAPLIQRTT-- 529
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  573 deeGFLVRHFAGAVCYNTEQFIEKNNDALHASLEGLVQECDNPLLQTLFPSGSSTSVRGKLNF----------------- 635
Cdd:cd14899   530 ---QFVVAHYAGCVTYTIDGFLAKNKDSFCESAAQLLAGSSNPLIQALAAGSNDEDANGDSELdgfggrtrrraksaiaa 606
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  636 ISVGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQFEGSLALAQLKCSGTISVLELMEHGYPSRVLFADLYSMYKS 715
Cdd:cd14899   607 VSVGTQFKIQLNELLSTVRATTPRYVRCIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRYRR 686

                  ..
gi 281362442  716 VL 717
Cdd:cd14899   687 VL 688
MYSc_Myo16 cd14878
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ...
71-754 2.55e-101

class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 3/NYAP3. Myo16 is thought to play a regulatory role in cell cycle progression and has been recently implicated in Schizophrenia. Class XVI myosins are characterized by an N-terminal ankyrin repeat domain and some with chitin synthase domains that arose independently from the ones in the class XVII fungal myosins. They bind protein phosphatase 1 catalytic subunits 1alpha/PPP1CA and 1gamma/PPP1CC. Human Myo16 interacts with ACOT9, ARHGAP26 and PIK3R2 and with components of the WAVE1 complex, CYFIP1 and NCKAP1. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276844 [Multi-domain]  Cd Length: 656  Bit Score: 336.79  E-value: 2.55e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   71 ATFLDNLKTRYYKDKIYTYVANILIAVNPYREIKeLYAPDTIKKYN---GRSLGELPPHVFAIADKAIRDMRVYKLSQSI 147
Cdd:cd14878     1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  148 IVSGESGAGKTESTKYLLKYL-CYSHDSAGPIETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEVHY-DAKCQVVGGYI 225
Cdd:cd14878    80 ILSGERGSGKTEASKQIMKHLtCRASSSRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKKHLTGARI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  226 SHYLLEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSLGKPDDYRYLSgctqyfanakteQLIPGSQKSKNHQQkgpl 305
Cdd:cd14878   160 YTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLN------------QTMREDVSTAERSL---- 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  306 kdpiidDYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEIPDDvrGGCQVSEAseQSLTITSGLLGVDQTE 385
Cdd:cd14878   224 ------NREKLAVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEA--DSAFVSDL--QLLEQVAGMLQVSTDE 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  386 LRTALVSRVMQskgggFKGTVIMVPLKIYEASNARDALAKAIYSRLFDRIVGLIN-----QSIPFQASNFYIGVLDIAGF 460
Cdd:cd14878   294 LASALTTDIQY-----FKGDMIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNcclqsQDEQKSMQTLDIGILDIFGF 368
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  461 EYFTVNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITFTDNQD-IIELIEAKSNGIFTLLDEESKLPKPS 539
Cdd:cd14878   369 EEFQKNEFEQLCVNMTNEKMHHYINEVLFLQEQTECVQEGVTMETAYSPGNQTgVLDFFFQKPSGFLSLLDEESQMIWSV 448
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  540 YSHFTAEVHkswanhyrlGLPRSSRLKA-HRTLRDEEG----------FLVRHFAGAVCYNTEQFIEKNNDALHASLEGL 608
Cdd:cd14878   449 EPNLPKKLQ---------SLLESSNTNAvYSPMKDGNGnvalkdqgtaFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFV 519
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  609 VQECDNPLLQTLFPSgsstsvrgKLnfISVGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQFEGSLALAQLKCSG 688
Cdd:cd14878   520 MKTSENVVINHLFQS--------KL--VTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIG 589
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281362442  689 TISVLELMEHGYPSRVLFADLYSMYK---SVLPPELVSLPARTFCEAMFQSLNLSAkdFKFGITKVFFR 754
Cdd:cd14878   590 VLEMVKIFRYGYPVRLSFSDFLSRYKplaDTLLGEKKKQSAEERCRLVLQQCKLQG--WQMGVRKVFLK 656
MYSc_Myo24A cd14937
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ...
71-754 1.21e-98

class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The function of the class XXIV myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276897  Cd Length: 637  Bit Score: 328.90  E-value: 1.21e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   71 ATFLDNLKTRYYKDKIYTYVANILIAVNPYREIkelyapDT-IKKYNGRSLGELPPHVFAIADKAIRDMRVYKLSQSIIV 149
Cdd:cd14937     1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVI------DVdINEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIII 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  150 SGESGAGKTESTKYLLKYLCYSHDSAGPIETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEVHYDAKCQVVGGYISHYL 229
Cdd:cd14937    75 SGESGSGKTEASKLVIKYYLSGVKEDNEISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSIEIFL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  230 LEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSLGKPDDYRYLSgctqyfanakteqlipgsqkSKNhqqkgpLKDPI 309
Cdd:cd14937   155 LENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIV--------------------NKN------VVIPE 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  310 IDDYQHFHNLDKALGRLGLSDTeKLGIYSLVAAVLHLGNIAFEEIPDDVRGGCqvSEASEQSLTIT---SGLLGVDQTEL 386
Cdd:cd14937   209 IDDAKDFGNLMISFDKMNMHDM-KDDLFLTLSGLLLLGNVEYQEIEKGGKTNC--SELDKNNLELVneiSNLLGINYENL 285
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  387 RTALV---SRVMQSKgggfkgtvIMVPLKIYEASNARDALAKAIYSRLFDRIVGLINQSIPFQAS-NFYIGVLDIAGFEY 462
Cdd:cd14937   286 KDCLVfteKTIANQK--------IEIPLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNKElNNYIGILDIFGFEI 357
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  463 FTVNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITFTDNQDIIELIEAKSNgIFTLLDEESKLPKPSYSH 542
Cdd:cd14937   358 FSKNSLEQLLINIANEEIHSIYLYIVYEKETELYKAEDILIESVKYTTNESIIDLLRGKTS-IISILEDSCLGPVKNDES 436
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  543 FTAEVHKSWANHYRLGLPRSSRlkahrtlrdEEGFLVRHFAGAVCYNTEQFIEKNNDALHASLEGLVQECDNPLLQTLFP 622
Cdd:cd14937   437 IVSVYTNKFSKHEKYASTKKDI---------NKNFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYE 507
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  623 SGSSTSVRGKLNFISVgsKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQFEGSLALAQLKCSGTISVLEL---MEHG 699
Cdd:cd14937   508 DVEVSESLGRKNLITF--KYLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNIsffFQYK 585
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 281362442  700 YPSRVLFAdlYSMYKSVLPPELVSLPARTFCEAMFQSlNLSAKDFKFGITKVFFR 754
Cdd:cd14937   586 YTFDVFLS--YFEYLDYSTSKDSSLTDKEKVSMILQN-TVDPDLYKVGKTMVFLK 637
MYSc_Myo23 cd14884
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ...
71-722 2.67e-92

class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 IQ motifs and a single MyTH4 domain in its C-terminal tail. The lack of a FERM domain here is odd since MyTH4 domains are usually found alongside FERM domains where they bind to microtubules. At any rate these Class XXIII myosins are still proposed to function in the apicomplexan microtubule cytoskeleton. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276850 [Multi-domain]  Cd Length: 685  Bit Score: 312.61  E-value: 2.67e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   71 ATFLDNLKTRYYKDKIYTYVANILIAVNPYREIKELYAPDTIKKY-------NGRSLGELPPHVFAIADKAIRDMRVYKL 143
Cdd:cd14884     1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKELYDQDVMNVYlhkksnsAASAAPFPKAHIYDIANMAYKNMRGKLK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  144 SQSIIVSGESGAGKTESTKYLLKYLCYSHDSAGPIE--TKILDANPVLEAFGNAKTTRNNNSSRFGKFIEVHYDAKCQVV 221
Cdd:cd14884    81 RQTIVVSGHSGSGKTENCKFLFKYFHYIQTDSQMTEriDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFEEVENTQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  222 GGYISH---------YLLEKSRICTQSAEERNYHVFYMLLAG-APQQLRDKLSLGKPDDYRYLSGCTQYFANAKTEQLIP 291
Cdd:cd14884   161 KNMFNGcfrnikikiLLLEINRCIAHNFGERNFHVFYQVLRGlSDEDLARRNLVRNCGVYGLLNPDESHQKRSVKGTLRL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  292 GSQKSKnhqqkgPLKDPIIDDYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNiafeeipddvrggcqvseaseQS 371
Cdd:cd14884   241 GSDSLD------PSEEEKAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGN---------------------RA 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  372 LTITSGLLGVDQTELRTALVSRVMQSKGggfkgTVIMVPLKIYEASNARDALAKAIYSRLFDRIVGLIN----------- 440
Cdd:cd14884   294 YKAAAECLQIEEEDLENVIKYKNIRVSH-----EVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINrnvlkckekde 368
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  441 ---QSIPFQASNFyIGVLDIAGFEYFTVNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITFTDNQDIIEL 517
Cdd:cd14884   369 sdnEDIYSINEAI-ISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAPSYSDTLIF 447
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  518 IEAksngIFTLLDEESKLP----KPSYSHF-------TAEVHKSWANHYRLGLPRSSRLKAHRTLRDEEGFLVRHFAGAV 586
Cdd:cd14884   448 IAK----IFRRLDDITKLKnqgqKKTDDHFfryllnnERQQQLEGKVSYGFVLNHDADGTAKKQNIKKNIFFIRHYAGLV 523
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  587 CYNTEQFIEKNNDALHASLEGLVQECDNPLLqtlfpsgSSTSVRG-KLNFISVGSKFKTQLGELMEKLEQNGTNFIRCIK 665
Cdd:cd14884   524 TYRINNWIDKNSDKIETSIETLISCSSNRFL-------REANNGGnKGNFLSVSKKYIKELDNLFTQLQSTDMYYIRCFL 596
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 281362442  666 PNSKMIDRQFEGSLALAQLKCSGTISVLELMEHGYPSRVLFADLYSMYKSVLPPELV 722
Cdd:cd14884   597 PNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKETAAALKEQIAKELE 653
MYSc_Myo37 cd14898
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ...
74-718 5.62e-89

class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276863  Cd Length: 578  Bit Score: 300.28  E-value: 5.62e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   74 LDNLKTRYYKDKIYTYVANILIAVNPYREIkelYAPDTIKKYNgRSLGELPPHVFAIADKAIRDMRVYKlSQSIIVSGES 153
Cdd:cd14898     4 LEILEKRYASGKIYTKSGLVFLALNPYETI---YGAGAMKAYL-KNYSHVEPHVYDVAEASVQDLLVHG-NQTIVISGES 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  154 GAGKTESTKYLLKYLCYSHDSAGPIETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEVHYDAKcqVVGGYISHYLLEKS 233
Cdd:cd14898    79 GSGKTENAKLVIKYLVERTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFDGK--ITGAKFETYLLEKS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  234 RICTQSAEERNYHVFYMLLAGAPQQLRDKLSlgkpdDYRYLSGctqyfanaKTEQLIPGSQKSKnhqqkgplkdpiiddy 313
Cdd:cd14898   157 RVTHHEKGERNFHIFYQFCASKRLNIKNDFI-----DTSSTAG--------NKESIVQLSEKYK---------------- 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  314 qhfhNLDKALGRLGLSDTEKlgIYSLVAAVLHLGNIAFeeipddVRGGCQVSEASEqSLTITSGLLGVDQTELRTALVSR 393
Cdd:cd14898   208 ----MTCSAMKSLGIANFKS--IEDCLLGILYLGSIQF------VNDGILKLQRNE-SFTEFCKLHNIQEEDFEESLVKF 274
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  394 VMQskgggFKGTVIMVPLKIYEASNARDALAKAIYSRLFDRIVGLINQSIPfQASNFYIGVLDIAGFEYFTVNSFEQFCI 473
Cdd:cd14898   275 SIQ-----VKGETIEVFNTLKQARTIRNSMARLLYSNVFNYITASINNCLE-GSGERSISVLDIFGFEIFESNGLDQLCI 348
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  474 NYCNEKLQKFFNDNILKNEQELYKREGLNVPEITFTDNQDIIELIEaKSNGIFTLLDEESKLPKPSYSHFTAEVHKsWAN 553
Cdd:cd14898   349 NWTNEKIQNDFIKKMFRAKQGMYKEEGIEWPDVEFFDNNQCIRDFE-KPCGLMDLISEESFNAWGNVKNLLVKIKK-YLN 426
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  554 HYrlglprsSRLKAHRTLrdeegfLVRHFAGAVCYNTEQFIEKNNDalhaslEGLVQECDNPLLQTlfpSGSstsvrgKL 633
Cdd:cd14898   427 GF-------INTKARDKI------KVSHYAGDVEYDLRDFLDKNRE------KGQLLIFKNLLIND---EGS------KE 478
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  634 NFISVgskFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQFEGSLALAQLKCSGTISVLELMEHGYPSRVLFADLYSMY 713
Cdd:cd14898   479 DLVKY---FKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERY 555

                  ....*
gi 281362442  714 KSVLP 718
Cdd:cd14898   556 RILGI 560
MYSc_Myo20 cd14881
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ...
77-718 1.64e-82

class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such members as Drosophila, Daphnia, and mosquitoes. These myosins contain a single IQ motif in the neck region. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276847 [Multi-domain]  Cd Length: 633  Bit Score: 283.54  E-value: 1.64e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   77 LKTRYYKDKIYTYVANILIAVNPYREIKE---LYAPDTIKKYngrslgelpPHVFAIADKAIRDMRVYKLSQSIIVSGES 153
Cdd:cd14881     7 LQARFYAKEFFTNVGPILLSVNPYRDVGNpltLTSTRSSPLA---------PQLLKVVQEAVRQQSETGYPQAIILSGTS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  154 GAGKTESTKYLLKYLcYSHDSAGPiET---KILDAN-PVLEAFGNAKTTRNNNSSRFGKFIEVhydakcQVVGG--Y--- 224
Cdd:cd14881    78 GSGKTYASMLLLRQL-FDVAGGGP-ETdafKHLAAAfTVLRSLGSAKTATNSESSRIGHFIEV------QVTDGalYrtk 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  225 ISHYLLEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSLG--KPDDYRYLsgctqyfanakteqlipgsqksknhqQK 302
Cdd:cd14881   150 IHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDgySPANLRYL--------------------------SH 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  303 GPLKDPIIDDYQHFHNLDKALGRLGLSDTEKLGIyslVAAVLHLGNIAFEEipddvRGGCQVSEASEQSLTITSGLLGVD 382
Cdd:cd14881   204 GDTRQNEAEDAARFQAWKACLGILGIPFLDVVRV---LAAVLLLGNVQFID-----GGGLEVDVKGETELKSVAALLGVS 275
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  383 QTELRTALVSRVMQSKGggfkgTVIMVPLKIYEASNARDALAKAIYSRLFDRIVGLINQ------SIPFQASNFYIGVLD 456
Cdd:cd14881   276 GAALFRGLTTRTHNARG-----QLVKSVCDANMSNMTRDALAKALYCRTVATIVRRANSlkrlgsTLGTHATDGFIGILD 350
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  457 IAGFEYFTVNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVP-EITFTDNQDIIELIEAKSNGIFTLLDEESKl 535
Cdd:cd14881   351 MFGFEDPKPSQLEHLCINLCAETMQHFYNTHIFKSSIESCRDEGIQCEvEVDYVDNVPCIDLISSLRTGLLSMLDVECS- 429
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  536 PKPSYSHFTAEVHKSWANHYRLGLPRSSrlkahrtlrDEEGFLVRHFAGAVCYNTEQFIEKNNDALHASLEGLV--QECD 613
Cdd:cd14881   430 PRGTAESYVAKIKVQHRQNPRLFEAKPQ---------DDRMFGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFykQNCN 500
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  614 npllqtlfpsgsstsvrgkLNFISVGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQFEGSLALAQLKcsgTISVL 693
Cdd:cd14881   501 -------------------FGFATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIR---SLQVL 558
                         650       660
                  ....*....|....*....|....*...
gi 281362442  694 E---LMEHGYPSRVLFADLYSMYKSVLP 718
Cdd:cd14881   559 EtvnLMAGGYPHRMRFKAFNARYRLLAP 586
MYSc_Myo32 cd14893
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ...
74-753 1.27e-77

class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but possess tandem MyTH4 and FERM domains. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276858  Cd Length: 741  Bit Score: 272.61  E-value: 1.27e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   74 LDNLKTRYYKDKIYTYVANILIAVNPYREIKeLYAPDTIKKYNGR----------SLGELPPHVFAIADKAIRDMRVYKL 143
Cdd:cd14893     4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLP-IYTPDHMQAYNKSreqtplyekdTVNDAPPHVFALAQNALRCMQDAGE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  144 SQSIIVSGESGAGKTESTKYLLKYLCY-------SHDSAG------PIETKILDANPVLEAFGNAKTTRNNNSSRFGKFI 210
Cdd:cd14893    83 DQAVILLGGMGAGKSEAAKLIVQYLCEigdetepRPDSEGasgvlhPIGQQILHAFTILEAFGNAATRQNRNSSRFAKMI 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  211 EVHYDAKCQVVGG-YISHYLlEKSRICTQSAEERNYHVFYMLLAGAPQQ--LRDKLSLGKpddyrylsgCTQYFANAKte 287
Cdd:cd14893   163 SVEFSKHGHVIGGgFTTHYF-EKSRVIDCRSHERNFHVFYQVLAGVQHDptLRDSLEMNK---------CVNEFVMLK-- 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  288 qlipgsqksknhqQKGPLKDPIIDDYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFeeIPD-----DVRGGC 362
Cdd:cd14893   231 -------------QADPLATNFALDARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDF--VPDpeggkSVGGAN 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  363 QVSEASEQS--------LTITSGLLGVDQTELRTALVSRVMQSKGGGfKGTVIMVPLKIYEASNARDALAKAIYSRLFDR 434
Cdd:cd14893   296 STTVSDAQScalkdpaqILLAAKLLEVEPVVLDNYFRTRQFFSKDGN-KTVSSLKVVTVHQARKARDTFVRSLYESLFNF 374
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  435 IVGLINQSI-----PFQASNFYIG-----VLDIAGFEYFT--VNSFEQFCINYCNEKLQKFFNDNILK-NEQELYKREGL 501
Cdd:cd14893   375 LVETLNGILggifdRYEKSNIVINsqgvhVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYVQNTLAiNFSFLEDESQQ 454
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  502 NVPEITFTDNQDI-------IELIEAKSNGIFTLLDEESKLPKPSYSHFTAEVHKswANHYRLGLPR--------SSRLK 566
Cdd:cd14893   455 VENRLTVNSNVDItseqekcLQLFEDKPFGIFDLLTENCKVRLPNDEDFVNKLFS--GNEAVGGLSRpnmgadttNEYLA 532
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  567 AHRTLRdeEGFLVRHFAGAVCYNTEQFIEKNNDALHASLEGLVQECDNPLLQTL-------------------------- 620
Cdd:cd14893   533 PSKDWR--LLFIVQHHCGKVTYNGKGLSSKNMLSISSTCAAIMQSSKNAVLHAVgaaqmaaassekaakqteergstssk 610
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  621 FPSGSSTSVRGKLNFISVGSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMIDRQFEGSLALAQLKCSGTISVLELMEHGY 700
Cdd:cd14893   611 FRKSASSARESKNITDSAATDVYNQADALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIF 690
                         730       740       750       760       770
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 281362442  701 PSRVLFADLYSMYKSVlppelvsLPARTFCEAMFQSLN----LSAKDFKFGITKVFF 753
Cdd:cd14893   691 TVHLTYGHFFRRYKNV-------CGHRGTLESLLRSLSaigvLEEEKFVVGKTKVYL 740
MYSc_Myo12 cd14874
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ...
71-754 4.75e-77

class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They are found predominately in nematodes. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276841 [Multi-domain]  Cd Length: 628  Bit Score: 267.89  E-value: 4.75e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   71 ATFLDNLKTRYYKDKIYTYVANILIAVNPYrEIKELYAPDTIKKYngrslgelppHVFAIADKAIRDMRVYKL-SQSIIV 149
Cdd:cd14874     1 AGIAQNLHERFKKGQTYTKASNVLVFVNDF-NKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSnAESIVF 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  150 SGESGAGKTESTKYLLKYLCYSHDSAgpIETKILDA-NPVLEAFGNAKTTRNNNSSRFGKFIEVHYdaKCQVVGGYISHY 228
Cdd:cd14874    70 GGESGSGKSYNAFQVFKYLTSQPKSK--VTTKHSSAiESVFKSFGCAKTLKNDEATRFGCSIDLLY--KRNVLTGLNLKY 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  229 L--LEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSLGKPDDYRYLSgctqyfanakteqlipgsqksknhqqKGPLK 306
Cdd:cd14874   146 TvpLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYIN--------------------------QGNST 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  307 DPIIDDYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAF--EEIPDDVRGGCQVSEASEqsLTITSGLLGVDQT 384
Cdd:cd14874   200 ENIQSDVNHFKHLEDALHVLGFSDDHCISIYKIISTILHIGNIYFrtKRNPNVEQDVVEIGNMSE--VKWVAFLLEVDFD 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  385 ELRTALVSRvmqskgggfkgTVIMVPLKIYEASNARDALAKAIYSRLFDRIVGLINQSIPFQASNFYIGVLDIAGFEYFT 464
Cdd:cd14874   278 QLVNFLLPK-----------SEDGTTIDLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGVISILDHYGFEKYN 346
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  465 VNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNV----PeiTFTDNQDIIELIEAKSNGIFTLLDEESKLPKPSy 540
Cdd:cd14874   347 NNGVEEFLINSVNERIENLFVKHSFHDQLVDYAKDGISVdykvP--NSIENGKTVELLFKKPYGLLPLLTDECKFPKGS- 423
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  541 shftaevHKSWANHYRLG-LPRSSRLKAHRTLRDEegFLVRHFAGAVCYNTEQFIEKNNDALHASLEGLVQECDNPLLQT 619
Cdd:cd14874   424 -------HESYLEHCNLNhTDRSSYGKARNKERLE--FGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGL 494
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  620 LFPSGSSTS---VRGKLNFISVGSKfktqlgELMEKLEQNGTNFIRCIKPNSKMIDRQFEGSLALAQLKCSGTISVLELM 696
Cdd:cd14874   495 LFESYSSNTsdmIVSQAQFILRGAQ------EIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFR 568
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  697 EHGYPSRVLFADLYSMYKSVLPPELVSL--PARTFCEAMFQSLNLSAKDFKFGITKVFFR 754
Cdd:cd14874   569 IKGYPVKISKTTFARQYRCLLPGDIAMCqnEKEIIQDILQGQGVKYENDFKIGTEYVFLR 628
MYSc_Myo18 cd01386
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ...
77-754 5.82e-76

class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain which is commonly found in proteins establishing molecular complexes. The motor domain itself does not exhibit ATPase activity, suggesting that it functions as an actin tether protein. It also has two IQ domains that probably bind light chains or related calmodulins and a C-terminal tail with two sections of coiled-coil domains, which are thought to mediate homodimerization. The function of these myosins are largely unknown. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276837 [Multi-domain]  Cd Length: 689  Bit Score: 266.48  E-value: 5.82e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   77 LKTRYYKDKIYTYVANILIAVNPyREIKELYAPDTIKKYNGRSLGELPPHVFAIADKAIRDMRVYKLSQSIIVSGESGAG 156
Cdd:cd01386     7 LRQRYGANLIHTYAGPSLIVINP-RHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLGRSGSG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  157 KTESTKYLLKYLCYSHDSAGPIET--KILDANPVLEAFGNAKTTRNNNSSRFGKFIEVHYDAKCQVVGGYISHYLLEKSR 234
Cdd:cd01386    86 KTTNCRHILEYLVTAAGSVGGVLSveKLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASIQTLLLERSR 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  235 ICTQSAEERNYHVFYMLLAGAPQQLRDKLSLgkpddyrylsgctqyfaNAKTEQLIPGSQKSKNHQQKGplkdpiiDDYQ 314
Cdd:cd01386   166 VARRPEGESNFNVFYYLLAGADAALRTELHL-----------------NQLAESNSFGIVPLQKPEDKQ-------KAAA 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  315 HFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIafeeipddvrGGCQVSEASE------QSLTITSGLLGVDQTELRT 388
Cdd:cd01386   222 AFSKLQAAMKTLGISEEEQRAIWSILAAIYHLGAA----------GATKAASAGRkqfarpEWAQRAAYLLGCTLEELSS 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  389 A-----LVSRVMQSKGGGFKGTVIMVPL--KIYEASNARDALAKAIYSRLFDRIVGLINQSI-PFQASNFYIGVLDIAGF 460
Cdd:cd01386   292 AifkhhLSGGPQQSTTSSGQESPARSSSggPKLTGVEALEGFAAGLYSELFAAVVSLINRSLsSSHHSTSSITIVDTPGF 371
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  461 EY------FTVNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITFTDN-QDIIELI--------------- 518
Cdd:cd01386   372 QNpahsgsQRGATFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSpGALVALIdqapqqalvrsdlrd 451
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  519 -EAKsnGIFTLLDEESKLPKPSYSHFTAEVHkswaNHYrlGLPRSSrlKAHRTLRDEEG---FLVRHFAGA--VCYNTEQ 592
Cdd:cd01386   452 eDRR--GLLWLLDEEALYPGSSDDTFLERLF----SHY--GDKEGG--KGHSLLRRSEGplqFVLGHLLGTnpVEYDVSG 521
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  593 FieknndaLHASLEGLVQECDNPLLQtlfpsgSSTSVRGKLNFISVGSKFKTQLGELMEKLEQNGTNFIRCIKPNSK--- 669
Cdd:cd01386   522 W-------LKAAKENPSAQNATQLLQ------ESQKETAAVKRKSPCLQIKFQVDALIDTLRRTGLHFVHCLLPQHNagk 588
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  670 ---------MIDRQFEGSLALAQLKCSGTISVLELMEHGYPSRVLFADLYSMYKSVLPPELVSLPA-------RTFCEAM 733
Cdd:cd01386   589 derstsspaAGDELLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGLnsevadeRKAVEEL 668
                         730       740
                  ....*....|....*....|.
gi 281362442  734 FQSLNLSAKDFKFGITKVFFR 754
Cdd:cd01386   669 LEELDLEKSSYRIGLSQVFFR 689
MYSc_Myo44 cd14905
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ...
72-601 1.48e-67

class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV class. Members here include cellular slime mold Polysphondylium and soil-living amoeba Dictyostelium. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276870  Cd Length: 673  Bit Score: 241.54  E-value: 1.48e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   72 TFLDNLKTRYYKDKIYTYVANILIAVNPYREIKELYAPDTIKKYNGRSlgELPPHVFAIADKAIRDMRVYKLSQSIIVSG 151
Cdd:cd14905     2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPFLHSQELVRNYNQRR--GLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  152 ESGAGKTESTKYLLKYLCYSHDSAGP-IETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEVHYDAKCQVVGGYISHYLL 230
Cdd:cd14905    80 ESGSGKSENTKIIIQYLLTTDLSRSKyLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKLYSYFL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  231 EKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSLGKPDDYRYLSgctqyfanakteqlipgsqksknhqQKGPLKDPII 310
Cdd:cd14905   160 DENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLN-------------------------QGGSISVESI 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  311 DDYQHFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEipddvRGGcqVSEASEQSLTIT-SGLLGVDQTELRTA 389
Cdd:cd14905   215 DDNRVFDRLKMSFVFFDFPSEKIDLIFKTLSFIIILGNVTFFQ-----KNG--KTEVKDRTLIESlSHNITFDSTKLENI 287
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  390 LVS-RVMqskgggfkgtvimvplKIYEASNARDALAKAIYSRLFDRIVGLINQSIPFQASNFYIGVLDIAGFEYFTVNSF 468
Cdd:cd14905   288 LISdRSM----------------PVNEAVENRDSLARSLYSALFHWIIDFLNSKLKPTQYSHTLGILDLFGQESSQLNGY 351
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  469 EQFCINYCNEKLQKFFNDNILKNEQELYKREGLN-VPEITFTDNQDIIELIEAksngIFTLLDEESKLPKPSYSHFTAEV 547
Cdd:cd14905   352 EQFSINFLEERLQQIYLQTVLKQEQREYQTERIPwMTPISFKDNEESVEMMEK----IINLLDQESKNINSSDQIFLEKL 427
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 281362442  548 HKSWANHYRLGlprssrlkahrtlRDEEGFLVRHFAGAVCYNTEQFIEKNNDAL 601
Cdd:cd14905   428 QNFLSRHHLFG-------------KKPNKFGIEHYFGQFYYDVRGFIIKNRDEI 468
MYSc_Myo21 cd14882
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ...
72-714 2.44e-65

class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class XXI myosins do not group with them. Myo21, unlike other myosin proteins, contains UBA-like protein domains and has no structural or functional relationship with the myosins present in other organisms possessing cilia or flagella. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They have diverse tails with IQ, WW, PX, and Tub domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276848  Cd Length: 642  Bit Score: 234.25  E-value: 2.44e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   72 TFLDNLKTRYYKDKIYTYVANILIAVNPyREIKELYAPDTIKKYNGRSLGELPPHVFAIADKAIRDMRVYKLSQSIIVSG 151
Cdd:cd14882     2 NILEELRHRYLMGESYTFIGDILLSLNP-NEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  152 ESGAGKTESTKYLLKYLCYSHDSAGPIETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEVHYDAKCQVVGGYISHYLLE 231
Cdd:cd14882    81 ESYSGKTTNARLLIKHLCYLGDGNRGATGRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFWMYQLE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  232 KSRICTQSAEERNYHVFYMLLAG--APQQLRDkLSLGKPDDYRYLsgctqyfanakteQLIPGSQKSKNHQQKgplkdpi 309
Cdd:cd14882   161 KLRVSTTDGNQSNFHIFYYFYDFieAQNRLKE-YNLKAGRNYRYL-------------RIPPEVPPSKLKYRR------- 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  310 iDDYQH----FHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNIAFEEipddvRGGCQVSEASEQSLTITSgLLGVDQTE 385
Cdd:cd14882   220 -DDPEGnverYKEFEEILKDLDFNEEQLETVRKVLAAILNLGEIRFRQ-----NGGYAELENTEIASRVAE-LLRLDEKK 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  386 LRTALVSRVMQSkgggfKGTVIMVPLKIYEASNARDALAKAIYSRLFDRIVGLINQSIPFQAS----NFYIGVLDIAGFE 461
Cdd:cd14882   293 FMWALTNYCLIK-----GGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSFPRAvfgdKYSISIHDMFGFE 367
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  462 YFTVNSFEQFCINYCNEKLQKFFNDNILKNEQELYKREGLNVPEITFTDNQDIIELIEAKSNGIFTLLDEESK-LPKPSY 540
Cdd:cd14882   368 CFHRNRLEQLMVNTLNEQMQYHYNQRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPDGLFYIIDDASRsCQDQNY 447
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  541 SHFTAEVHKSwanhyrlglPRSSRLKAHRtlrdeegFLVRHFAGAVCYNTEQFIEKNNDALHASLEGLVQECDNPLLQTL 620
Cdd:cd14882   448 IMDRIKEKHS---------QFVKKHSAHE-------FSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLM 511
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  621 FpsgSSTSVRgklNFISVGSKFKTQLGELMEKLEQN----GTNFIRCIKPNSKMIDRQFEGSLALAQLKCSGTISVLELM 696
Cdd:cd14882   512 F---TNSQVR---NMRTLAATFRATSLELLKMLSIGansgGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKAR 585
                         650
                  ....*....|....*...
gi 281362442  697 EHGYPSRVLFADLYSMYK 714
Cdd:cd14882   586 QKGFSYRIPFQEFLRRYQ 603
CBD_MYO6-like cd21759
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, ...
765-913 1.74e-59

calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, which are actin-based motor molecules with ATPase activity, include unconventional myosins that serve in intracellular movements. Myosin-VI, also called unconventional myosin-6 (MYO6), is a reverse-direction motor protein that moves towards the minus-end of actin filaments. It is required for the structural integrity of the Golgi apparatus via the p53-dependent pro-survival pathway. Myosin-VI appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells. It modulates RNA polymerase II-dependent transcription. As part of the DISP (DOCK7-Induced Septin disPlacement) complex, Myosin-VI may regulate the association of septins with actin and thereby regulate the actin cytoskeleton. Myosin-VI is encoded by gene MYO6, the human homolog of the gene responsible for deafness in Snell's waltzer mice. It is mutated in autosomal dominant non-syndromic hearing loss. This family also includes Drosophila melanogaster unconventional myosin VI Jaguar (Jar; also called myosin heavy chain 95F (Mhc95F), or 95F MHC), which is a motor protein necessary for the morphogenesis of epithelial tissues during Drosophila development. Jar is required for basal protein targeting and correct spindle orientation in mitotic neuroblasts. It contributes to synaptic transmission and development at the Drosophila neuromuscular junction. Together with CLIP-190 (CAP-Gly domain-containing/cytoplasmic linker protein 190), Jar may coordinate the interaction between the actin and microtubule cytoskeleton. Jar may link endocytic vesicles to microtubules and possibly be involved in transport in the early embryo and in the dynamic process of dorsal closure; its function is believed to change during the life cycle. This model corresponds to the calmodulin (CaM) binding domain (CBD), which consists of three subdomains: a unique insert (Insert 2 or Ins2), an IQ motif, and a proximal tail domain (PTD, also known as lever arm extension or LAE).


Pssm-ID: 409646 [Multi-domain]  Cd Length: 149  Bit Score: 200.81  E-value: 1.74e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  765 MRSDPENMLAIVAKVKKWLIRSRWVKSALGALCVIKLRNRIIYRNKCVLIAQRIARGFLARKQHRPRYQGIGKINKIRTN 844
Cdd:cd21759     1 MKSDPENLKELVKKVKKWLIRSRWRKAQWCALSVIKLKNKILYRREALIKIQKTVRGYLARKKHRPRIKGLRKIRALEKQ 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 281362442  845 TLKTIEIASGLKMGREEIISGVNDIYRQIDDAIKKIKMNPRITQREMDSMYTVVMANMNKLTVDLNTKL 913
Cdd:cd21759    81 LKEMEEIASQLKKDKDKWTKQVKELKKEIDALIKKIKTNDMITRKEIDKLYNALVKKVDKQLAELQKKL 149
Myosin-VI_CBD pfam16521
Myosin VI cargo binding domain; Myosin-VI_CBD is a C-terminal family that allows ...
1160-1246 9.14e-57

Myosin VI cargo binding domain; Myosin-VI_CBD is a C-terminal family that allows unconventional myosin-VI to recognize and select its binding cargoes. Several adaptor proteins have been reported to interact specifically with the CBD, thus defining the specific subcellular functions of myosin VI. The crystal structure determination of the myosin VI CBD/Dab2 (an endocytic adaptor protein Disabled-2 that is a cargo) complex shows that the Myosin-VI_CBD forms a cargo-induced dimer, suggesting that the motor undergoes monomer-to-dimer conversion that is dependent upon cargo binding. In the absence of cargo myosin VI exists as a stable monomer. This cargo binding-mediated monomer-to-dimer conversion mechanism adopted by myosin VI may be shared by other unconventional myosins, such as myosin VII and myosin X.


Pssm-ID: 465157  Cd Length: 90  Bit Score: 190.57  E-value: 9.14e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  1160 HRYFRIPFMRANAPDNT---KRGLWYAHFDGQWIARQMELHADKPPILLVAGTDDMQMCELSLEETGLTRKRGAEILEHE 1236
Cdd:pfam16521    1 QRYFRIPFVRPSDKKRDggrKKGWWYAHFDGQWIARQMELHPDKPPVLLVAGKDDMQMCELSLEETGLTRKRGAEILEEE 80
                           90
                   ....*....|
gi 281362442  1237 FNREWERNGG 1246
Cdd:pfam16521   81 FEEEWKKHGG 90
MYSc_Myo24B cd14938
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ...
72-752 5.00e-50

class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The functions of these myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276898 [Multi-domain]  Cd Length: 713  Bit Score: 190.05  E-value: 5.00e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   72 TFLDNLKTRYYKDKIYTYVANILIAVNPyREIKELYAPDTIKKYN-GRSLGELPPHVFAIADKAIRDMRVYKLSQSIIVS 150
Cdd:cd14938     2 SVLYHLKERFKNNKFYTKMGPLLIFINP-KINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIIS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  151 GESGAGKTESTKYLLKYLCYSHDSAGPIETKILDANP------------------------VLEAFGNAKTTRNNNSSRF 206
Cdd:cd14938    81 GESGSGKSEIAKNIINFIAYQVKGSRRLPTNLNDQEEdnihneentdyqfnmsemlkhvnvVMEAFGNAKTVKNNNSSRF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  207 GKFIEVHYDAKcQVVGGYISHYLLEKSRICTQSAEERNYHVFYMLLAGAPQQLRDKLSLGKPDDYRYLSgctqyfaNAKt 286
Cdd:cd14938   161 SKFCTIHIENE-EIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLN-------NEK- 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  287 eqlipGSQKSKNHQQKgplkdpiiddyqhFHNLDKALGRLGLSDTEKLGIYSLVAAVLHLGNI----AFEEIPDDV-RGG 361
Cdd:cd14938   232 -----GFEKFSDYSGK-------------ILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTeivkAFRKKSLLMgKNQ 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  362 CQVSEASE------------------QSLTITSGLLGVDQTELRTALVSRVMqskgggFKGTVIMVPLKIYEASNARDAL 423
Cdd:cd14938   294 CGQNINYEtilselensedigldenvKNLLLACKLLSFDIETFVKYFTTNYI------FNDSILIKVHNETKIQKKLENF 367
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  424 AKAIYSRLFDRIVGLINQSI-PFQASNF---YIGVLDIAGFEYFTVNSFEQFCINYCNEKLQKFFNDNILKNEQELYKRE 499
Cdd:cd14938   368 IKTCYEELFNWIIYKINEKCtQLQNINIntnYINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNED 447
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  500 GLNVP-EITFTDNQDIIELIEAKSNG-IFTLLDEESKLPKPSYSHFTAEVHKSWANHyrlglprSSRLKAHRTLRDEEGF 577
Cdd:cd14938   448 GIFCEyNSENIDNEPLYNLLVGPTEGsLFSLLENVSTKTIFDKSNLHSSIIRKFSRN-------SKYIKKDDITGNKKTF 520
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  578 LVRHFAGAVCYNTEQFIEKNNDALHASLEGLVQECDNPLLQTLFPS----GSSTSVRGKLNFiSVGSKFK---------- 643
Cdd:cd14938   521 VITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSENEYMRQFCMFynydNSGNIVEEKRRY-SIQSALKlfkrrydtkn 599
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  644 --------TQLGELMEKLEQNGTNFIRCIKPN-SKMIDRQFEGSLALAQLKCSGTISVLELMEHGYPSRVLFADLYSMYK 714
Cdd:cd14938   600 qmavsllrNNLTELEKLQETTFCHFIVCMKPNeSKRELCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFD 679
                         730       740       750
                  ....*....|....*....|....*....|....*...
gi 281362442  715 svlppeLVSLPARTFCEAMFQSLNLSAKDFKFGITKVF 752
Cdd:cd14938   680 ------IKNEDLKEKVEALIKSYQISNYEWMIGNNMIF 711
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
93-212 1.19e-41

Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.


Pssm-ID: 276814 [Multi-domain]  Cd Length: 170  Bit Score: 150.57  E-value: 1.19e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   93 ILIAVNPYREIKELYAPDTIKKYNGRSLGELPPHVFAIADKAIRDMRVYKLSQSIIVSGESGAGKTESTKYLLKYLC--- 169
Cdd:cd01363     1 VLVRVNPFKELPIYRDSKIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLAsva 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 281362442  170 -------------YSHDSAGPIETKILDANPVLEAFGNAKTTRNNNSSRFGKFIEV 212
Cdd:cd01363    81 fnginkgetegwvYLTEITVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEI 136
MYSc_Myo33 cd14894
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ...
73-702 1.71e-30

class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276859 [Multi-domain]  Cd Length: 871  Bit Score: 130.63  E-value: 1.71e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   73 FLDNLKTRYYKDKIYTYVANILIAV-NPYREIK-----ELYAPDTIKKYNGRSLGE--LPPHVFAIADKAI--------- 135
Cdd:cd14894     3 LVDALTSRFDDDRIYTYINHHTMAVmNPYRLLQtarftSIYDEQVVLTYADTANAEtvLAPHPFAIAKQSLvrlffdneh 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  136 -----------RDMRVYKlSQSIIVSGESGAGKTESTKYLLKYLC----------------------------YSHDSAG 176
Cdd:cd14894    83 tmplpstissnRSMTEGR-GQSLFLCGESGSGKTELAKDLLKYLVlvaqpalskgseetckvsgstrqpkiklFTSSTKS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  177 PIETK--------------------------------------------------------------------------- 181
Cdd:cd14894   162 TIQMRteeartialleakgvekyeivlldlhperwdemtsvsrskrlpqvhvdglffgfyeklehledeeqlrmyfknph 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  182 -------ILDANPVLEAFGNAKTTRNNNSSRFGKFIEVH-----YDAKCQVVGGYISHYLLEKSRICTQSAEER------ 243
Cdd:cd14894   242 aakklsiVLDSNIVLEAFGHATTSMNLNSSRFGKMTTLQvafglHPWEFQICGCHISPFLLEKSRVTSERGRESgdqnel 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  244 NYHVFYMLLAGAP-----QQLRDKLSLGKPDdyrylsgCTQYFANAKTEQLIPGSQKSKNHQQKgplkdpiidDYQHFHN 318
Cdd:cd14894   322 NFHILYAMVAGVNafpfmRLLAKELHLDGID-------CSALTYLGRSDHKLAGFVSKEDTWKK---------DVERWQQ 385
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  319 LDKALGRLGLSDTEKLGIYSLVAAVLHLGNIA--FEEIPDDVRGGCQVSEASEQSLTITSGLLGVDQTELRTALVSRVMQ 396
Cdd:cd14894   386 VIDGLDELNVSPDEQKTIFKVLSAVLWLGNIEldYREVSGKLVMSSTGALNAPQKVVELLELGSVEKLERMLMTKSVSLQ 465
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  397 SKGGGFKgtvimVPLKIYEASNARDALAKAIYSRLFDRIVGLINQSIPFQA-----------SNF-------YIGVLDIA 458
Cdd:cd14894   466 STSETFE-----VTLEKGQVNHVRDTLARLLYQLAFNYVVFVMNEATKMSAlstdgnkhqmdSNAsapeavsLLKIVDVF 540
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  459 GFEYFTVNSFEQFCINYCNEKLqkffndniLKNEQELYKREGLNVPEITFTDNQDIIELIEAKSNGIFTLLDEESKLPKP 538
Cdd:cd14894   541 GFEDLTHNSLDQLCINYLSEKL--------YAREEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASLEELTILHQS 612
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  539 SYSHFTAEVHKSW--------ANHYRLGLPRSSRLKAHR---TLRDEEGFLVRHFAGAVCYNTEQFIEKNNDALHAS-LE 606
Cdd:cd14894   613 ENMNAQQEEKRNKlfvrniydRNSSRLPEPPRVLSNAKRhtpVLLNVLPFVIPHTRGNVIYDANDFVKKNSDFVYANlLV 692
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442  607 GLVQECDNPLLQTLFPS--------------GSSTS-VRGKLNFIsvgSKFKTQLGELMEKLEQNGTNFIRCIKPNSKMI 671
Cdd:cd14894   693 GLKTSNSSHFCRMLNESsqlgwspntnrsmlGSAESrLSGTKSFV---GQFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQ 769
                         810       820       830
                  ....*....|....*....|....*....|.
gi 281362442  672 DRQFEGSLALAQLKCSGTISVLELMEHGYPS 702
Cdd:cd14894   770 PSLVNNDLVEQQCRSQRLIRQMEICRNSSSS 800
MyUb_Myo6 cd21958
myosin VI ubiquitin-binding domain (MyUb) found in unconventional myosin-VI and similar ...
1076-1116 9.82e-25

myosin VI ubiquitin-binding domain (MyUb) found in unconventional myosin-VI and similar proteins; Unconventional myosin VI, also called Myo6, or unconventional myosin-6, is a monomeric myosin, which moves towards the minus-end of actin filaments, in contrast to most other myosins which moves towards the plus-end of actin filaments. It is thought that myosin VI, unlike plus-end directed myosins, does not use a pure lever arm mechanism, but instead steps with a mechanism analogous to the kinesin neck-linker uncoupling model. It has been implicated in a myriad of functions including the transport of cytoplasmic organelles, maintenance of normal Golgi morphology, endocytosis, secretion, cell migration, border cell migration during development, cancer metastasis, deafness, and retinal development, among others. For example, the GIPC1 (GAIP interacting protein, C-terminus 1) adaptor protein mediates endocytosis by tethering PlexinD1, a transmembrane receptor that regulates neuronal and cardiovascular development and cargo protein of GIPC1, to myosin VI motor through a regulated oligomerization mechanism, forming a PlexinD1/GIPC/myosin VI complex. This model corresponds to the myosin VI ubiquitin-binding domain (MyUb) that binds to ubiquitin chains, especially those linked via K63, K11, and K29.


Pssm-ID: 439319 [Multi-domain]  Cd Length: 41  Bit Score: 97.44  E-value: 9.82e-25
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 281362442 1076 QKYDLSKWKYSELRDAINTSCDIELLEACRQEFHRRLKVYH 1116
Cdd:cd21958     1 KKYDLSKWKYAELRDTINTSCDIELLEACREEFHRRLKVYH 41
Myosin_N pfam02736
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ...
7-49 1.14e-07

Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the N-terminus of many but not all myosins. The function of this domain is unknown.


Pssm-ID: 460670  Cd Length: 45  Bit Score: 49.35  E-value: 1.14e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 281362442     7 LVWVRDAAEGYIQGRITEIGAKEFEVTPTDRKypKRTCHFDDI 49
Cdd:pfam02736    5 LVWVPDPKEGFVKGEIKEEEGDKVTVETEDGK--TVTVKKDDV 45
MYO6_MIU_linker cd22294
MIU-linker domain found in unconventional myosin-VI; Myosins are actin-based motor molecules ...
1002-1093 4.05e-07

MIU-linker domain found in unconventional myosin-VI; Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins function in intracellular movements. Myosin-VI, also called unconventional myosin-6 (MYO6), is a reverse-direction motor protein that moves towards the minus-end of actin filaments. It is required for the structural integrity of the Golgi apparatus via the p53-dependent pro-survival pathway. It appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells. It modulates RNA polymerase II-dependent transcription. As part of the DISP complex, Myosin-VI may regulate the association of septins with actin and thereby regulate the actin cytoskeleton. Myosin-VI is encoded by the MYO6 gene, the human homologue of the gene responsible for deafness in Snell's waltzer mice. It is mutated in autosomal dominant nonsyndromic hearing loss. This model corresponds to a conserved region of myosin-VI, which consist of three helices: MIU (Motif Interacting with Ubiquitin), a common linker helix (linker-alpha1) and an isoform-specific helix (linker-alpha2).


Pssm-ID: 412090 [Multi-domain]  Cd Length: 69  Bit Score: 48.36  E-value: 4.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442 1002 LEQERRDHELALRLAnESNGQ--VEDSPPVIRngvndaspmgpnklisfsqvvsniasryLNKSENVRAQQQALGKQKYD 1079
Cdd:cd22294     5 LEQERRDRELAMRIA-QSEAEliSEETQPDLA----------------------------LRRSAGTQAVSAGGGKKKMT 55
                          90
                  ....*....|....
gi 281362442 1080 LSKWKYSELRDAIN 1093
Cdd:cd22294    56 MEEMAKEMSEDLSR 69
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
954-1020 2.00e-05

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 45.29  E-value: 2.00e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281362442   954 RLKAEMETRRKAAEAQRLRQEEEdRRAALALQEQLEKEAKDDAKYRQQLEQERRDH-ELALRLANESN 1020
Cdd:pfam20492   34 ETAEELEEERRQAEEEAERLEQK-RQEAEEEKERLEESAEMEAEEKEQLEAELAEAqEEIARLEEEVE 100
UDM1_RNF168_RNF169-like cd22249
UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, ...
955-1015 2.11e-05

UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, RNF169 and similar proteins; This model represents the UDM1 (ubiquitin-dependent double-strand break [DSB] recruitment module 1) found in RING finger proteins, RNF168 and RNF169. RNF168 is an E3 ubiquitin-protein ligase that promotes non-canonical K27 ubiquitination to signal DNA damage. It functions, together with RNF8, as a DNA damage response (DDR) factor that promotes a series of ubiquitylation events on substrates such as H2A and H2AX. With H2AK13/15 ubiquitylation, it facilitates recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of double-strand breaks (DSBs), and inhibits homologous recombination (HR) in cells deficient in the tumor suppressor BRCA1. RNF168 also promotes H2A neddylation, which antagonizes ubiquitylation of H2A and regulates DNA damage repair. In addition, RNF168 forms a functional complex with RAD6A or RAD6B during the DNA damage response. RNF169 is an uncharacterized E3 ubiquitin-protein ligase paralogous to RNF168. It functions as a negative regulator of the DNA damage signaling cascade. RNF169 recognizes polyubiquitin structures but does not itself contribute to double-strand break (DSB)-induced chromatin ubiquitylation. It contributes to the regulation of DSB repair pathway utilization via functionally competing with recruiting repair factors, 53BP1 and RAP80-BRCA1, for association with RNF168-modified chromatin, independent of its catalytic activity, limiting the magnitude of the RNF8/RNF168-dependent signaling response to DSBs. The UDM1 domain comprises LRM1 (LR motif 1), UMI (ubiquitin-interacting motif [UIM]- and MIU-related UBD) and MIU1 (motif interacting with ubiquitin 1). Mutations of Ub-interacting residues in UDM1 have little effect on the accumulation of RNF168 to DSB sites, suggesting that it may not be the main site of binding ubiquitylated and polyubiquitylated targets.


Pssm-ID: 409016 [Multi-domain]  Cd Length: 66  Bit Score: 43.41  E-value: 2.11e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281362442  955 LKAEMETRRKAAEAQRLRQEEEDRRAALALQEQLEKEAKDDAKyRQQLEQERRDHELALRL 1015
Cdd:cd22249     7 IREEYEAQLKKLEEERRKEREEEEKASEELIRKLQEEEERQRK-REREEQLKQDEELAKQL 66
MIU2_RNF168-like cd21932
second motif interacting with ubiquitin domain found in RING finger protein 168 and similar ...
969-993 7.28e-04

second motif interacting with ubiquitin domain found in RING finger protein 168 and similar domains; The domain family includes motif interacting with ubiquitin (MIU) domains of RING finger protein, RNF168 and RNF169. RNF168 is an E3 ubiquitin-protein ligase that promotes noncanonical K27 ubiquitination to signal DNA damage. It, together with RNF8, functions as a DNA damage response (DDR) factor that promotes monoubiquitination of H2A/H2AX at K13/15, facilitates recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of double-strand breaks (DSBs), and inhibits homologous recombination (HR) in cells deficient in the tumor suppressor BRCA1. RNF168 also promotes H2A neddylation, which antagonizes ubiquitylation of H2A and regulates DNA damage repair. RNF169 is an uncharacterized E3 ubiquitin-protein ligase paralogous to RNF168. It functions as a negative regulator of the DNA damage signaling cascade. RNF169 recognizes polyubiquitin structures but does not itself contribute to double-strand break (DSB)-induced chromatin ubiquitylation. It contributes to the regulation of the DSB repair pathway by competing with repair factors, 53BP1 and RAP80-BRCA1, for association with RNF168-modified chromatin, limiting the magnitude of the RNF8/RNF168-dependent signaling response to DSBs. RNF168 contains an N-terminal C3HC4-type RING-HC finger that catalyzes H2A-K15ub modification and interacts with H2A, and two MIU (motif interacting with ubiquitin) domains responsible for interaction with K63 linked poly-ubiquitin. RNF169 contains an N-terminal C3HC4-type RING-HC finger and a C-terminal MIU domain. This model corresponds to the second MIU (MIU2) domain of RNF168 and the C-terminal MIU domain of RNF169, which is responsible for bridging histone and ubiquitin surfaces.


Pssm-ID: 409264  Cd Length: 42  Bit Score: 38.38  E-value: 7.28e-04
                          10        20
                  ....*....|....*....|....*
gi 281362442  969 QRLRQEEEDRRAALALQEQLEKEAK 993
Cdd:cd21932     3 ERLTQEEEDRLLALKLQRQFDLEDK 27
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
958-1016 9.24e-04

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 43.57  E-value: 9.24e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281362442   958 EMETRRKAAEAQRLRQEEEDRRAAL-ALQEQLEKEAKDDAKYRQQLEQER-----RDHELALRLA 1016
Cdd:pfam17380  311 EVERRRKLEEAEKARQAEMDRQAAIyAEQERMAMERERELERIRQEERKReleriRQEEIAMEIS 375
Caldesmon pfam02029
Caldesmon;
955-1079 1.14e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 42.93  E-value: 1.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281362442   955 LKAEMETRRKaaeaqrLRQEEEDRRAalalQEQLEKEAKDDAKYRQQLEQ-ERRDHELA-LRLANESNGQVEDSPPvirn 1032
Cdd:pfam02029  282 LKKKREERRK------LLEEEEQRRK----QEEAERKLREEEEKRRMKEEiERRRAEAAeKRQKLPEDSSSEGKKP---- 347
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 281362442  1033 gVNDASPMGPNKLISFSqvvSNIASRYLNKSENVRAQQQALGKQKYD 1079
Cdd:pfam02029  348 -FKCFSPKGSSLKITER---AEFLNKSLQKSSSVKKTHPPAVVSKID 390
MIU2_RNF168 cd21952
second motif interacting with ubiquitin domain found in RING finger protein 168; RNF168 is an ...
969-991 1.66e-03

second motif interacting with ubiquitin domain found in RING finger protein 168; RNF168 is an E3 ubiquitin-protein ligase that promotes noncanonical K27 ubiquitination to signal DNA damage. It, together with RNF8, functions as a DNA damage response (DDR) factor that promotes monoubiquitination of H2A/H2AX at K13/15, facilitates recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of double-strand breaks (DSBs), and inhibits homologous recombination (HR) in cells deficient in the tumor suppressor BRCA1. RNF168 also promotes H2A neddylation, which antagonizes ubiquitylation of H2A and regulates DNA damage repair. Moreover, RNF168 forms a functional complex with RAD6A or RAD6B during the DNA damage response. RNF168 contains an N-terminal C3HC4-type RING-HC finger that catalyzes H2A-K15ub modification and interacts with H2A, and two MIU (motif interacting with ubiquitin) domains responsible for the interaction with K63 linked poly-ubiquitin. This model corresponds to the second MIU (MIU2) domain of RNF168. The first MIU belongs to a different domain family and is not included here.


Pssm-ID: 409266  Cd Length: 51  Bit Score: 37.72  E-value: 1.66e-03
                          10        20
                  ....*....|....*....|...
gi 281362442  969 QRLRQEEEDRRAALALQEQLEKE 991
Cdd:cd21952     8 ERLRQEEQDRQLALKLQKQLDKE 30
UDM1_RNF168 cd22265
UDM1 (ubiquitin-dependent DSB recruitment module 1) domain found in RING finger protein 168; ...
955-1015 4.17e-03

UDM1 (ubiquitin-dependent DSB recruitment module 1) domain found in RING finger protein 168; RING finger protein 168 (RNF168) is an E3 ubiquitin-protein ligase that promotes noncanonical K27 ubiquitination to signal DNA damage. Together with RNF8, RNF168 functions as a DNA damage response (DDR) factor that promotes a series of ubiquitylation events on substrates such as H2A and H2AX. With H2AK13/15 ubiquitylation, it facilitates recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of double-strand breaks (DSBs), and inhibits homologous recombination (HR) in cells deficient in the tumor suppressor BRCA1. RNF168 also promotes H2A neddylation, which antagonizes ubiquitylation of H2A and regulates DNA damage repair. In addition, RNF168 forms a functional complex with RAD6A or RAD6B during the DNA damage response. This model corresponds to the UDM1 (ubiquitin-dependent double-strand break [DSB] recruitment module 1) domain of RNF168, which comprises LRM1 (LR motif 1), UMI (ubiquitin-interacting motif [UIM]- and MIU-related UBD) and MIU1 (motif interacting with ubiquitin 1). Mutations of Ub-interacting residues in UDM1 have little effect on the accumulation of RNF168 to DSB sites, suggesting that it may not be the main site of binding ubiquitylated and polyubiquitylated targets.


Pssm-ID: 409018 [Multi-domain]  Cd Length: 73  Bit Score: 37.15  E-value: 4.17e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 281362442  955 LKAEMETRRKAAEAQRLRQEEEDRRAALA-----LQEQLEKEAKDDAKYRQQLEQERRDHELALRL 1015
Cdd:cd22265     7 LRQEYEEEISKLEAERRALEEEENRASEEyiqklLAEEEEEEKLAEERRRAEEEQLKEDEELARKL 72
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
953-1018 6.02e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 40.71  E-value: 6.02e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281362442   953 KRLKAEMETRRKAAEAQRLRQ------EEEDRRAALALQEQLE---KEAKDDAKYRQQLEQERRDHELALRLANE 1018
Cdd:pfam15709  436 QRKKQQEEAERAEAEKQRQKElemqlaEEQKRLMEMAEEERLEyqrQKQEAEEKARLEAEERRQKEEEAARLALE 510
Casc1_N pfam15927
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ...
962-1013 7.00e-03

Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is approximately 200 amino acids in length. The family is found in association with pfam12366. There are two completely conserved residues (N and W) that may be functionally important.


Pssm-ID: 464947 [Multi-domain]  Cd Length: 201  Bit Score: 39.27  E-value: 7.00e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 281362442   962 RRKAAEAQRLRQEEEDRRAalalqeqLEKEAKDDAKYRQQL-EQERRDHELAL 1013
Cdd:pfam15927    2 RLREEEEERLRAEEEEAER-------LEEERREEEEEERLAaEQDRRAEELEE 47
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
956-1018 7.40e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 40.17  E-value: 7.40e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281362442  956 KAEMETRRKAAEAQRLRQEEEDRRAALALQEQLEKEAKDDAKYRQQLEQERRDHELALRLANE 1018
Cdd:PRK09510   88 QAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAE 150
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
953-1026 8.92e-03

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 40.02  E-value: 8.92e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281362442  953 KRLKAEMETRRKAAEAQRLRQEEEDRRAALALQEQLEKE-AKDDAKYRQQLEQERRDHELALRLANESNGQVEDS 1026
Cdd:COG3064    58 REAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEkAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEE 132
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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