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Conserved domains on  [gi|808358096|ref|NP_001294574|]
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Myosin motor domain-containing protein [Caenorhabditis elegans]

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 ...
 143-825 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: 1228.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  143 ATLLNNIRLRYQNGKIYSYVANILISINPYQTIDGFYSLQKIKEYRGKSLGQKEPHIFAIADKSYREMIRHRKSQSIIVS 222
Cdd:cd01382     1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPKLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  223 GESGAGKTESQKAVLRYLCENWGSGAGEIQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFADTGNVAGGYVSHYL 302
Cdd:cd01382    81 GESGAGKTESTKYILRYLTESWGSGAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  303 LETSRICRQAAGERNYHIFYQLIAGSSPELFKflalgqpnqfnylkrgfigffthpssgttskipknrlsdpKFTQDSMV 382
Cdd:cd01382   161 LEKSRICVQSKEERNYHIFYRLCAGAPEDLRE----------------------------------------KLLKDPLL 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  383 DDFSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEESLDDSRGGCKVFNGSEQDLIQAARLLGLETMELKMGL 462
Cdd:cd01382   201 DDVGDFIRMDKAMKKIGLSDEEKLDIFRVVAAVLHLGNIEFEENGSDSGGGCNVKPKSEQSLEYAAELLGLDQDELRVSL 280

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  463 CARIMQTTKGGARGTLIRVPLKPHEACSGRDALSKAIYSKLFDWLVSRINDSIPFEKSTNFVGVLDVAGFEFYAKNSFEQ 542
Cdd:cd01382   281 TTRVMQTTRGGAKGTVIKVPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFETSSYFIGVLDIAGFEYFEVNSFEQ 360

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  543 FCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEFIDNQDCIELFELKGNGLFDLLDEEAKFPTSNYKSFTKRAHEE 622
Cdd:cd01382   361 FCINYCNEKLQQFFNERILKEEQELYEKEGLGVKEVEYVDNQDCIDLIEAKLVGILDLLDEESKLPKPSDQHFTSAVHQK 440

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  623 NRKHFRLDTPRKSKVKSHRELRDDEGLLIRHYAGSVCYETKHFVEKNDDLLHNSLQILIEQSTIRLLVSLF------GST 696
Cdd:cd01382   441 HKNHFRLSIPRKSKLKIHRNLRDDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFesstnnNKD 520

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  697 AYPTKSKLKALSVGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGSAILSQLQCAGMTSVLKLMQDGFPSRTG 776
Cdd:cd01382   521 SKQKAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTS 600

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*....
gi 808358096  777 FGDLYACYQKKLPPKLSKLDPRMFCKCLFRALGLDQHDFQFGLTKVFFR 825
Cdd:cd01382   601 FHDLYNMYKKYLPPKLARLDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
CBD_MYO6-like cd21759
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, ...
 836-987 3.72e-46

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: 162.68  E-value: 3.72e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  836 MKQDPETMTSLIQKVNEWLVGARWKQSQYAVWSVIKLKNKIAWRSAQVTRLQSIARGYLTRQRFSRQIALYRKSVALLKN 915
Cdd:cd21759     1 MKSDPENLKELVKKVKKWLIRSRWRKAQWCALSVIKLKNKILYRREALIKIQKTVRGYLARKKHRPRIKGLRKIRALEKQ 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808358096  916 SKEIEKILFRLNEhSRAKYTSSAHSTIRDLEKLVSHIKltTSANDHFEKAENAYEHYVKRVDSMIADLKKQQ 987
Cdd:cd21759    81 LKEMEEIASQLKK-DKDKWTKQVKELKKEIDALIKKIK--TNDMITRKEIDKLYNALVKKVDKQLAELQKKL 149
Myosin-VI_CBD super family cl24928
Myosin VI cargo binding domain; Myosin-VI_CBD is a C-terminal family that allows ...
 1180-1276 1.56e-42

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.


The actual alignment was detected with superfamily member pfam16521:

Pssm-ID: 465157  Cd Length: 90  Bit Score: 150.12  E-value: 1.56e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  1180 QRYFKCEFKENNQKGTcswgssikcEDLDQVSMWFVHFSGQQIQRQLTFTSSRPPQTLIAGRDDAQMCTLALQETLLVGK 1259
Cdd:pfam16521    1 QRYFRIPFVRPSDKKR---------DGGRKKGWWYAHFDGQWIARQMELHPDKPPVLLVAGKDDMQMCELSLEETGLTRK 71

                           90
                   ....*....|....*..
gi 808358096  1260 RGAEISEDEFESHWKLG 1276
Cdd:pfam16521   72 RGAEILEEEFEEEWKKH 88
MyUb_Myo6 super family cl45552
myosin VI ubiquitin-binding domain (MyUb) found in unconventional myosin-VI and similar ...
 1099-1139 8.04e-18

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.


The actual alignment was detected with superfamily member cd21958:

Pssm-ID: 439319 [Multi-domain]  Cd Length: 41  Bit Score: 77.80  E-value: 8.04e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 808358096 1099 GKYDVGGCSFAYLRDTINTSMDINLLKACEEEFRRRLRIYN 1139
Cdd:cd21958     1 KKYDLSKWKYAELRDTINTSCDIELLEACREEFHRRLKVYH 41
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 983-1076 2.24e-08

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


:

Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 57.55  E-value: 2.24e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   983 LKKQQKSDELAEIERKRRESEEKERLEIEAKKEAERQREIKRKLEEQQQNAQKEHENYLISEIHKAAEEtEKKRQNEEKE 1062
Cdd:TIGR02794   55 IQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEE-AKAKQAAEAK 133

                           90
                   ....*....|....
gi 808358096  1063 KLDKMVSNRLAEAD 1076
Cdd:TIGR02794  134 AKAEAEAERKAKEE 147
 
Name Accession Description Interval E-value
MYSc_Myo6 cd01382
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ...
 143-825 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: 1228.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  143 ATLLNNIRLRYQNGKIYSYVANILISINPYQTIDGFYSLQKIKEYRGKSLGQKEPHIFAIADKSYREMIRHRKSQSIIVS 222
Cdd:cd01382     1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPKLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  223 GESGAGKTESQKAVLRYLCENWGSGAGEIQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFADTGNVAGGYVSHYL 302
Cdd:cd01382    81 GESGAGKTESTKYILRYLTESWGSGAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  303 LETSRICRQAAGERNYHIFYQLIAGSSPELFKflalgqpnqfnylkrgfigffthpssgttskipknrlsdpKFTQDSMV 382
Cdd:cd01382   161 LEKSRICVQSKEERNYHIFYRLCAGAPEDLRE----------------------------------------KLLKDPLL 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  383 DDFSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEESLDDSRGGCKVFNGSEQDLIQAARLLGLETMELKMGL 462
Cdd:cd01382   201 DDVGDFIRMDKAMKKIGLSDEEKLDIFRVVAAVLHLGNIEFEENGSDSGGGCNVKPKSEQSLEYAAELLGLDQDELRVSL 280

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  463 CARIMQTTKGGARGTLIRVPLKPHEACSGRDALSKAIYSKLFDWLVSRINDSIPFEKSTNFVGVLDVAGFEFYAKNSFEQ 542
Cdd:cd01382   281 TTRVMQTTRGGAKGTVIKVPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFETSSYFIGVLDIAGFEYFEVNSFEQ 360

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  543 FCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEFIDNQDCIELFELKGNGLFDLLDEEAKFPTSNYKSFTKRAHEE 622
Cdd:cd01382   361 FCINYCNEKLQQFFNERILKEEQELYEKEGLGVKEVEYVDNQDCIDLIEAKLVGILDLLDEESKLPKPSDQHFTSAVHQK 440

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  623 NRKHFRLDTPRKSKVKSHRELRDDEGLLIRHYAGSVCYETKHFVEKNDDLLHNSLQILIEQSTIRLLVSLF------GST 696
Cdd:cd01382   441 HKNHFRLSIPRKSKLKIHRNLRDDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFesstnnNKD 520

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  697 AYPTKSKLKALSVGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGSAILSQLQCAGMTSVLKLMQDGFPSRTG 776
Cdd:cd01382   521 SKQKAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTS 600

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*....
gi 808358096  777 FGDLYACYQKKLPPKLSKLDPRMFCKCLFRALGLDQHDFQFGLTKVFFR 825
Cdd:cd01382   601 FHDLYNMYKKYLPPKLARLDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
MYSc smart00242
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...
 131-837 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: 848.37  E-value: 0e+00
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096    131 VEDNCQLMHLNEATLLNNIRLRYQNGKIYSYVANILISINPYQTIdGFYSLQKIKEYRGKSLGQKEPHIFAIADKSYREM 210
Cdd:smart00242    8 VEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQL-PIYTDEVIKKYRGKSRGELPPHVFAIADNAYRNM 86

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096    211 IRHRKSQSIIVSGESGAGKTESQKAVLRYLCENWGSG--AGEIQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFA 288
Cdd:smart00242   87 LNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNteVGSVEDQILESNPILEAFGNAKTLRNNNSSRFGKFIEIHFD 166

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096    289 DTGNVAGGYVSHYLLETSRICRQAAGERNYHIFYQLIAGSSPELFKFLALGQPNQFNYLkrgfigffthpSSGTTSKIPk 368
Cdd:smart00242  167 AKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYL-----------NQGGCLTVD- 234

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096    369 nrlsdpkftqdsMVDDFSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEESLDDSRGGCkvfNGSEQDLIQAA 448
Cdd:smart00242  235 ------------GIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAAST---VKDKEELSNAA 299

                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096    449 RLLGLETMELKMGLCARIMQTTKGgargtLIRVPLKPHEACSGRDALSKAIYSKLFDWLVSRINDSIPF-EKSTNFVGVL 527
Cdd:smart00242  300 ELLGVDPEELEKALTKRKIKTGGE-----VITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFkDGSTYFIGVL 374

                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096    528 DVAGFEFYAKNSFEQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEFIDNQDCIELFELKGNGLFDLLDEEAKF 607
Cdd:smart00242  375 DIYGFEIFEVNSFEQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFFDNQDCIDLIEKKPPGILSLLDEECRF 454

                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096    608 PTSNYKSFTKRAHEENRKHFRLDTPRKskvkshrelRDDEGLLIRHYAGSVCYETKHFVEKNDDLLHNSLQILIEQSTIR 687
Cdd:smart00242  455 PKGTDQTFLEKLNQHHKKHPHFSKPKK---------KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNP 525

                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096    688 LLVSLFGSTAYPTKSKLKALSVGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGSAILSQLQCAGMTSVLKLM 767
Cdd:smart00242  526 LIASLFPSGVSNAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIR 605

                           650       660       670       680       690       700       710
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808358096    768 QDGFPSRTGFGDLYACYQKKLPPKLSKLDPRM--FCKCLFRALGLDQHDFQFGLTKVFFRAGKFAEFDQMMK 837
Cdd:smart00242  606 RAGFPYRLPFDEFLQRYRVLLPDTWPPWGGDAkkACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
Myosin_head pfam00063
Myosin head (motor domain);
131-825 0e+00

Myosin head (motor domain);


Pssm-ID: 395017 [Multi-domain]  Cd Length: 674  Bit Score: 741.40  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   131 VEDNCQLMHLNEATLLNNIRLRYQNGKIYSYVANILISINPYQTIDgFYSLQKIKEYRGKSLGQKEPHIFAIADKSYREM 210
Cdd:pfam00063    1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLP-IYSEDMIKAYRGKRRGELPPHIFAIADEAYRSM 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   211 IRHRKSQSIIVSGESGAGKTESQKAVLRYLCENWGSGA----GEIQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIH 286
Cdd:pfam00063   80 LQDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSagnvGRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQ 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   287 FADTGNVAGGYVSHYLLETSRICRQAAGERNYHIFYQLIAGSSPELFKFLALGQPNQFNYLKRgfigffthpssGTTSKI 366
Cdd:pfam00063  160 FDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQ-----------SGCYTI 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   367 PKnrlsdpkftqdsmVDDFSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEESLDDSRGgckVFNGSEqDLIQ 446
Cdd:pfam00063  229 DG-------------IDDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQA---VPDDTE-NLQK 291

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   447 AARLLGLETMELKMGLCARIMQTtkggaRGTLIRVPLKPHEACSGRDALSKAIYSKLFDWLVSRINDSIPFEKST--NFV 524
Cdd:pfam00063  292 AASLLGIDSTELEKALCKRRIKT-----GRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEkaSFI 366

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   525 GVLDVAGFEFYAKNSFEQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEFIDNQDCIELFELKGNGLFDLLDEE 604
Cdd:pfam00063  367 GVLDIYGFEIFEKNSFEQLCINYVNEKLQQFFNHHMFKLEQEEYVREGIEWTFIDFGDNQPCIDLIEKKPLGILSLLDEE 446

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   605 AKFPTSNYKSFTKRAHEENRKHFRLDTPRkskvkshreLRDDEGLLIRHYAGSVCYETKHFVEKNDDLLHNSLQILIEQS 684
Cdd:pfam00063  447 CLFPKATDQTFLDKLYSTFSKHPHFQKPR---------LQGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSS 517

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   685 TIRLLVSLF---------------GSTAYPTKSKLKAlSVGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGS 749
Cdd:pfam00063  518 SDPLLAELFpdyetaesaaanesgKSTPKRTKKKRFI-TVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNS 596

                          650       660       670       680       690       700       710
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 808358096   750 AILSQLQCAGMTSVLKLMQDGFPSRTGFGDLYACYQKKLPPKLSK--LDPRMFCKCLFRALGLDQHDFQFGLTKVFFR 825
Cdd:pfam00063  597 LVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRYRILAPKTWPKwkGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
COG5022 COG5022
Myosin heavy chain [General function prediction only];
76-1070 0e+00

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 629.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   76 GRTVWITDATDGFRAARIIDLSATG--FTLrLLDNTGDTVTRVFEDVLACEDDSRRH---VEDNCQLMHLNEATLLNNIR 150
Cdd:COG5022     9 GSGCWIPDEEKGWIWAEIIKEAFNKgkVTE-EGKKEDGESVSVKKKVLGNDRIKLPKfdgVDDLTELSYLNEPAVLHNLE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  151 LRYQNGKIYSYVANILISINPYQTIdGFYSLQKIKEYRGKSLGQKEPHIFAIADKSYREMIRHRKSQSIIVSGESGAGKT 230
Cdd:COG5022    88 KRYNNGQIYTYSGLVLIAVNPYRDL-GIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKT 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  231 ESQKAVLRYLCENWGS---GAGEIQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFADTGNVAGGYVSHYLLETSR 307
Cdd:COG5022   167 ENAKRIMQYLASVTSSstvEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSR 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  308 ICRQAAGERNYHIFYQLIAGSSPELFKFLALGQPNQFNYLKrgfigffthpsSGTTSKIPKnrlsdpkftqdsmVDDFSD 387
Cdd:COG5022   247 VVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLS-----------QGGCDKIDG-------------IDDAKE 302

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  388 FQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEESLDdsrGGCKVfnGSEQDLIQAARLLGLETMELKMGLCARIM 467
Cdd:COG5022   303 FKITLDALKTIGIDEEEQDQIFKILAAILHIGNIEFKEDRN---GAAIF--SDNSVLDKACYLLGIDPSLFVKWLVKRQI 377

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  468 QTtkggaRGTLIRVPLKPHEACSGRDALSKAIYSKLFDWLVSRINDSI-PFEKSTNFVGVLDVAGFEFYAKNSFEQFCIN 546
Cdd:COG5022   378 KT-----GGEWIVVPLNLEQALAIRDSLAKALYSNLFDWIVDRINKSLdHSAAASNFIGVLDIYGFEIFEKNSFEQLCIN 452

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  547 FCNEKLQNFFNQRILREEQELYEKEGLNVRKIEFIDNQDCIELFELKGN-GLFDLLDEEAKFPTSNYKSFTKRAHEenrk 625
Cdd:COG5022   453 YTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFIDYFDNQPCIDLIEKKNPlGILSLLDEECVMPHATDESFTSKLAQ---- 528

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  626 hfRLDTPRKSKVKSHReLRDDeGLLIRHYAGSVCYETKHFVEKNDDLLHNSLQILIEQSTIRLLVSLFGSTAyPTKSKLK 705
Cdd:COG5022   529 --RLNKNSNPKFKKSR-FRDN-KFVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEE-NIESKGR 603

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  706 ALSVGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGSAILSQLQCAGMTSVLKLMQDGFPSRTGFGDLYACYQ 785
Cdd:COG5022   604 FPTLGSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYR 683

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  786 KKLPPKL------SKLDPRMFCKCLFRALGLDQHDFQFGLTKVFFRAGKFAEFDQMMKQDPETMTSLIQKvnEWLVGARW 859
Cdd:COG5022   684 ILSPSKSwtgeytWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQR--AIRGRYLR 761

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  860 KQSQYAVWSVIKLKNKIA-WRSAQVT----------RLQSIARGYLTRQRFSRQIALYRKsvalLKNSKEIEKIL----- 923
Cdd:COG5022   762 RRYLQALKRIKKIQVIQHgFRLRRLVdyelkwrlfiKLQPLLSLLGSRKEYRSYLACIIK----LQKTIKREKKLretee 837

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  924 --FRLNE---HSRAKYTSSAHSTIRDLEKLVSHIKLTTsandHFEKAENAYEHY---VKRV----------DSMIADLKK 985
Cdd:COG5022   838 veFSLKAevlIQKFGRSLKAKKRFSLLKKETIYLQSAQ----RVELAERQLQELkidVKSIsslklvnlelESEIIELKK 913

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  986 QQKSDELAEIERKRRESEEKERL--EIEAKKEAERQREIKRKLEE-QQQNAQKEHENYLISEIHKaaEETEKKRQ-NEEK 1061
Cdd:COG5022   914 SLSSDLIENLEFKTELIARLKKLlnNIDLEEGPSIEYVKLPELNKlHEVESKLKETSEEYEDLLK--KSTILVREgNKAN 991


                  ....*....
gi 808358096 1062 EKLDKMVSN 1070
Cdd:COG5022   992 SELKNFKKE 1000
PTZ00014 PTZ00014
myosin-A; Provisional
 137-894 3.49e-138

myosin-A; Provisional


Pssm-ID: 240229 [Multi-domain]  Cd Length: 821  Bit Score: 441.78  E-value: 3.49e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  137 LMHLNEATLLNNIRLRYQNGKIYSYVANILISINPYQTIdGFYSLQKIKEYR-GKSLGQKEPHIFAIADKSYREMIRHRK 215
Cdd:PTZ00014  104 LPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDL-GNTTNDWIRRYRdAKDSDKLPPHVFTTARRALENLHGVKK 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  216 SQSIIVSGESGAGKTESQKAVLRYLcenwGSGAGE-----IQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFADT 290
Cdd:PTZ00014  183 SQTIIVSGESGAGKTEATKQIMRYF----ASSKSGnmdlkIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEE 258

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  291 GNVAGGYVSHYLLETSRICRQAAGERNYHIFYQLIAGSSPELFKFLALGQPNQFNYLkrgfigffthpssgttskipknr 370
Cdd:PTZ00014  259 GGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYI----------------------- 315

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  371 lsDPKFTQDSMVDDFSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEESLDDSRGGCKVF-NGSEQDLIQAAR 449
Cdd:PTZ00014  316 --NPKCLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEGGLTDAAAIsDESLEVFNEACE 393

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  450 LLGLETMELKMGLcarIMQTTKGGarGTLIRVPLKPHEACSGRDALSKAIYSKLFDWLVSRINDSI-PFEKSTNFVGVLD 528
Cdd:PTZ00014  394 LLFLDYESLKKEL---TVKVTYAG--NQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIePPGGFKVFIGMLD 468

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  529 VAGFEFYAKNSFEQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEFIDNQDCIELFELKGNGLFDLLDEEAKFP 608
Cdd:PTZ00014  469 IFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGKSVLSILEDQCLAP 548

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  609 TSNYKSFTKRAHEENRKHFRLDTPRKSKVKShrelrddegLLIRHYAGSVCYETKHFVEKNDDLLHNSLQILIEQSTIRL 688
Cdd:PTZ00014  549 GGTDEKFVSSCNTNLKNNPKYKPAKVDSNKN---------FVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPL 619

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  689 LVSLFgSTAYPTKSKL-KALSVGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGSAILSQLQCAGMTSVLKLM 767
Cdd:PTZ00014  620 VRDLF-EGVEVEKGKLaKGQLIGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLR 698

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  768 QDGFPSRTGFGDLyaCYQKK---LP-PKLSKLDPRMFCKCLFRALGLDQHDFQFGLTKVFfragkfaefdqmMKQDP-ET 842
Cdd:PTZ00014  699 QLGFSYRRTFAEF--LSQFKyldLAvSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVF------------LKKDAaKE 764

                         730       740       750       760       770
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 808358096  843 MTSLI-QKVNEW--LVGArwkqsQYAVWSVIKLKNKIAWRSAQVTRLQSIARGYL 894
Cdd:PTZ00014  765 LTQIQrEKLAAWepLVSV-----LEALILKIKKKRKVRKNIKSLVRIQAHLRRHL 814
CBD_MYO6-like cd21759
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, ...
 836-987 3.72e-46

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: 162.68  E-value: 3.72e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  836 MKQDPETMTSLIQKVNEWLVGARWKQSQYAVWSVIKLKNKIAWRSAQVTRLQSIARGYLTRQRFSRQIALYRKSVALLKN 915
Cdd:cd21759     1 MKSDPENLKELVKKVKKWLIRSRWRKAQWCALSVIKLKNKILYRREALIKIQKTVRGYLARKKHRPRIKGLRKIRALEKQ 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808358096  916 SKEIEKILFRLNEhSRAKYTSSAHSTIRDLEKLVSHIKltTSANDHFEKAENAYEHYVKRVDSMIADLKKQQ 987
Cdd:cd21759    81 LKEMEEIASQLKK-DKDKWTKQVKELKKEIDALIKKIK--TNDMITRKEIDKLYNALVKKVDKQLAELQKKL 149
Myosin-VI_CBD pfam16521
Myosin VI cargo binding domain; Myosin-VI_CBD is a C-terminal family that allows ...
 1180-1276 1.56e-42

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: 150.12  E-value: 1.56e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  1180 QRYFKCEFKENNQKGTcswgssikcEDLDQVSMWFVHFSGQQIQRQLTFTSSRPPQTLIAGRDDAQMCTLALQETLLVGK 1259
Cdd:pfam16521    1 QRYFRIPFVRPSDKKR---------DGGRKKGWWYAHFDGQWIARQMELHPDKPPVLLVAGKDDMQMCELSLEETGLTRK 71

                           90
                   ....*....|....*..
gi 808358096  1260 RGAEISEDEFESHWKLG 1276
Cdd:pfam16521   72 RGAEILEEEFEEEWKKH 88
MyUb_Myo6 cd21958
myosin VI ubiquitin-binding domain (MyUb) found in unconventional myosin-VI and similar ...
 1099-1139 8.04e-18

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: 77.80  E-value: 8.04e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 808358096 1099 GKYDVGGCSFAYLRDTINTSMDINLLKACEEEFRRRLRIYN 1139
Cdd:cd21958     1 KKYDLSKWKYAELRDTINTSCDIELLEACREEFHRRLKVYH 41
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 983-1076 2.24e-08

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 57.55  E-value: 2.24e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   983 LKKQQKSDELAEIERKRRESEEKERLEIEAKKEAERQREIKRKLEEQQQNAQKEHENYLISEIHKAAEEtEKKRQNEEKE 1062
Cdd:TIGR02794   55 IQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEE-AKAKQAAEAK 133

                           90
                   ....*....|....
gi 808358096  1063 KLDKMVSNRLAEAD 1076
Cdd:TIGR02794  134 AKAEAEAERKAKEE 147
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 983-1075 5.11e-08

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 56.74  E-value: 5.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  983 LKKQQKSDELAEIERKRRESEEKERLEIEAKKEAERQREI-KRKLEEQQQNAQKEHENYLISEIHKAAEETEKKRQNEEK 1061
Cdd:PRK09510   67 QQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLeKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAK 146

                          90
                  ....*....|....
gi 808358096 1062 EKLDKMvSNRLAEA 1075
Cdd:PRK09510  147 AKAEAE-AKRAAAA 159
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 991-1075 1.05e-06

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 49.65  E-value: 1.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   991 ELAEIERKRRESEEKERLEIEAKKEAE---RQREIKRKLEEQQQNAQKEHEnyliseiHKAAEETEKKRQNEEKEKLDKM 1067
Cdd:pfam05672   28 EREEQERLEKEEEERLRKEELRRRAEEeraRREEEARRLEEERRREEEERQ-------RKAEEEAEEREQREQEEQERLQ 100


                   ....*...
gi 808358096  1068 VSNRLAEA 1075
Cdd:pfam05672  101 KQKEEAEA 108
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
980-1063 1.33e-05

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 49.10  E-value: 1.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  980 IADLKKQQKSDElAEIERKRR-ESEEKERLEIEAKKEAERQREIKRKLEEQQQNAQKEHENYLISEIHKAAEETEKKRQN 1058
Cdd:COG2268   194 IAEIIRDARIAE-AEAERETEiAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAEAAYEIAE 272


                  ....*
gi 808358096 1059 EEKEK 1063
Cdd:COG2268   273 ANAER 277
PTZ00121 PTZ00121
MAEBL; Provisional
 907-1067 1.58e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.75  E-value: 1.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  907 RKSVALLKNSKEIEKILFRLNEHSRAKYTSSAHSTIRDLEKLVSHIKLTTSANDHFEKAENAYEHyVKRVDSMIADLKKQ 986
Cdd:PTZ00121 1365 KAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEE-KKKADEAKKKAEEA 1443

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  987 QKSDEL---AEIERK----RRESEEKERLEiEAKKEAERQR---EIKRKLEEQQQNA----QKEHENYLISEIHKAAE-- 1050
Cdd:PTZ00121 1444 KKADEAkkkAEEAKKaeeaKKKAEEAKKAD-EAKKKAEEAKkadEAKKKAEEAKKKAdeakKAAEAKKKADEAKKAEEak 1522

                         170
                  ....*....|....*..
gi 808358096 1051 ETEKKRQNEEKEKLDKM 1067
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEA 1539
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 881-1067 2.94e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 2.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  881 AQVTRLQ---SIARGYltrQRFSRQIALYRKSVALLK---NSKEIEKILFRLNEHSRAKytSSAHSTIRDLEKLVSHIKL 954
Cdd:COG1196   200 RQLEPLErqaEKAERY---RELKEELKELEAELLLLKlreLEAELEELEAELEELEAEL--EELEAELAELEAELEELRL 274

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  955 T-TSANDHFEKAENAYEHYVKRVDSMIADLK--KQQKSDELAEIERKRRESEEKERLEIEAKKEAERQREIKRKLEEQQQ 1031
Cdd:COG1196   275 ElEELELELEEAQAEEYELLAELARLEQDIArlEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 808358096 1032 NAQKEHENYL--ISEIHKAAEETEKKRQNEEKEKLDKM 1067
Cdd:COG1196   355 EAEAELAEAEeaLLEAEAELAEAEEELEELAEELLEAL 392
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 964-1074 3.77e-04

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 44.11  E-value: 3.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  964 KAENAYEHYVKRVDSMIADLKKQQKSdeLAEIERKRRESEEKERLeieAKKEAERQREIKRKLEEQQQNAQKEHENYlis 1043
Cdd:cd16269   167 KAEEVLQEFLQSKEAEAEAILQADQA--LTEKEKEIEAERAKAEA---AEQERKLLEEQQRELEQKLEDQERSYEEH--- 238

                          90       100       110
                  ....*....|....*....|....*....|.
gi 808358096 1044 eIHKAAEETEKKRQNEEKEKlDKMVSNRLAE 1074
Cdd:cd16269   239 -LRQLKEKMEEERENLLKEQ-ERALESKLKE 267
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 896-1076 5.20e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 44.58  E-value: 5.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   896 RQRFSRQIALYRKSVALLKNSKEIEKILFRLNEHSRAKYTSSAHSTIRDLEKLVSHIKLTTSAndhFEKAENAYEHYVKR 975
Cdd:pfam02463  232 LKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKE---EEELKSELLKLERR 308

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   976 VDSMIADLKKQQKSDELAEIERKRrESEEKERLEIEaKKEAERQR-----EIKRKLEEQQQNAQKEHENYLISEIHKAAE 1050
Cdd:pfam02463  309 KVDDEEKLKESEKEKKKAEKELKK-EKEEIEELEKE-LKELEIKReaeeeEEEELEKLQEKLEQLEEELLAKKKLESERL 386

                          170       180
                   ....*....|....*....|....*.
gi 808358096  1051 ETEKKRQNEEKEKLDKMVSNRLAEAD 1076
Cdd:pfam02463  387 SSAAKLKEEELELKSEEEKEAQLLLE 412
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 868-1075 3.20e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.97  E-value: 3.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   868 SVIKLKNKIAWRSAQVTRLQsIARGYLTRQRFSRQIALYRKSVALLKNSKEIEKilfrlNEHSRAKYTSSAHSTIRDLEK 947
Cdd:TIGR02168  734 DLARLEAEVEQLEERIAQLS-KELTELEAEIEELEERLEEAEEELAEAEAEIEE-----LEAQIEQLKEELKALREALDE 807

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   948 LVSHIKLTtsaNDHFEKAENAYEHYVKRVDSMIADLK--KQQKSDELAEIERKRRESEEKERLEIEAKKEAERQREIKRK 1025
Cdd:TIGR02168  808 LRAELTLL---NEEAANLRERLESLERRIAATERRLEdlEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS 884

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 808358096  1026 LEEQQQNAQKEHENyLISEIHKAaeETEKKRQNEEKEKLDKMVS---NRLAEA 1075
Cdd:TIGR02168  885 LEEALALLRSELEE-LSEELREL--ESKRSELRRELEELREKLAqleLRLEGL 934
 
Name Accession Description Interval E-value
MYSc_Myo6 cd01382
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ...
 143-825 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: 1228.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  143 ATLLNNIRLRYQNGKIYSYVANILISINPYQTIDGFYSLQKIKEYRGKSLGQKEPHIFAIADKSYREMIRHRKSQSIIVS 222
Cdd:cd01382     1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPKLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  223 GESGAGKTESQKAVLRYLCENWGSGAGEIQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFADTGNVAGGYVSHYL 302
Cdd:cd01382    81 GESGAGKTESTKYILRYLTESWGSGAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  303 LETSRICRQAAGERNYHIFYQLIAGSSPELFKflalgqpnqfnylkrgfigffthpssgttskipknrlsdpKFTQDSMV 382
Cdd:cd01382   161 LEKSRICVQSKEERNYHIFYRLCAGAPEDLRE----------------------------------------KLLKDPLL 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  383 DDFSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEESLDDSRGGCKVFNGSEQDLIQAARLLGLETMELKMGL 462
Cdd:cd01382   201 DDVGDFIRMDKAMKKIGLSDEEKLDIFRVVAAVLHLGNIEFEENGSDSGGGCNVKPKSEQSLEYAAELLGLDQDELRVSL 280

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  463 CARIMQTTKGGARGTLIRVPLKPHEACSGRDALSKAIYSKLFDWLVSRINDSIPFEKSTNFVGVLDVAGFEFYAKNSFEQ 542
Cdd:cd01382   281 TTRVMQTTRGGAKGTVIKVPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFETSSYFIGVLDIAGFEYFEVNSFEQ 360

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  543 FCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEFIDNQDCIELFELKGNGLFDLLDEEAKFPTSNYKSFTKRAHEE 622
Cdd:cd01382   361 FCINYCNEKLQQFFNERILKEEQELYEKEGLGVKEVEYVDNQDCIDLIEAKLVGILDLLDEESKLPKPSDQHFTSAVHQK 440

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  623 NRKHFRLDTPRKSKVKSHRELRDDEGLLIRHYAGSVCYETKHFVEKNDDLLHNSLQILIEQSTIRLLVSLF------GST 696
Cdd:cd01382   441 HKNHFRLSIPRKSKLKIHRNLRDDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFesstnnNKD 520

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  697 AYPTKSKLKALSVGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGSAILSQLQCAGMTSVLKLMQDGFPSRTG 776
Cdd:cd01382   521 SKQKAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTS 600

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*....
gi 808358096  777 FGDLYACYQKKLPPKLSKLDPRMFCKCLFRALGLDQHDFQFGLTKVFFR 825
Cdd:cd01382   601 FHDLYNMYKKYLPPKLARLDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
MYSc smart00242
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...
 131-837 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: 848.37  E-value: 0e+00
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096    131 VEDNCQLMHLNEATLLNNIRLRYQNGKIYSYVANILISINPYQTIdGFYSLQKIKEYRGKSLGQKEPHIFAIADKSYREM 210
Cdd:smart00242    8 VEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQL-PIYTDEVIKKYRGKSRGELPPHVFAIADNAYRNM 86

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096    211 IRHRKSQSIIVSGESGAGKTESQKAVLRYLCENWGSG--AGEIQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFA 288
Cdd:smart00242   87 LNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNteVGSVEDQILESNPILEAFGNAKTLRNNNSSRFGKFIEIHFD 166

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096    289 DTGNVAGGYVSHYLLETSRICRQAAGERNYHIFYQLIAGSSPELFKFLALGQPNQFNYLkrgfigffthpSSGTTSKIPk 368
Cdd:smart00242  167 AKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYL-----------NQGGCLTVD- 234

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096    369 nrlsdpkftqdsMVDDFSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEESLDDSRGGCkvfNGSEQDLIQAA 448
Cdd:smart00242  235 ------------GIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAAST---VKDKEELSNAA 299

                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096    449 RLLGLETMELKMGLCARIMQTTKGgargtLIRVPLKPHEACSGRDALSKAIYSKLFDWLVSRINDSIPF-EKSTNFVGVL 527
Cdd:smart00242  300 ELLGVDPEELEKALTKRKIKTGGE-----VITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFkDGSTYFIGVL 374

                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096    528 DVAGFEFYAKNSFEQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEFIDNQDCIELFELKGNGLFDLLDEEAKF 607
Cdd:smart00242  375 DIYGFEIFEVNSFEQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFFDNQDCIDLIEKKPPGILSLLDEECRF 454

                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096    608 PTSNYKSFTKRAHEENRKHFRLDTPRKskvkshrelRDDEGLLIRHYAGSVCYETKHFVEKNDDLLHNSLQILIEQSTIR 687
Cdd:smart00242  455 PKGTDQTFLEKLNQHHKKHPHFSKPKK---------KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNP 525

                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096    688 LLVSLFGSTAYPTKSKLKALSVGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGSAILSQLQCAGMTSVLKLM 767
Cdd:smart00242  526 LIASLFPSGVSNAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIR 605

                           650       660       670       680       690       700       710
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808358096    768 QDGFPSRTGFGDLYACYQKKLPPKLSKLDPRM--FCKCLFRALGLDQHDFQFGLTKVFFRAGKFAEFDQMMK 837
Cdd:smart00242  606 RAGFPYRLPFDEFLQRYRVLLPDTWPPWGGDAkkACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
Myosin_head pfam00063
Myosin head (motor domain);
131-825 0e+00

Myosin head (motor domain);


Pssm-ID: 395017 [Multi-domain]  Cd Length: 674  Bit Score: 741.40  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   131 VEDNCQLMHLNEATLLNNIRLRYQNGKIYSYVANILISINPYQTIDgFYSLQKIKEYRGKSLGQKEPHIFAIADKSYREM 210
Cdd:pfam00063    1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLP-IYSEDMIKAYRGKRRGELPPHIFAIADEAYRSM 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   211 IRHRKSQSIIVSGESGAGKTESQKAVLRYLCENWGSGA----GEIQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIH 286
Cdd:pfam00063   80 LQDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSagnvGRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQ 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   287 FADTGNVAGGYVSHYLLETSRICRQAAGERNYHIFYQLIAGSSPELFKFLALGQPNQFNYLKRgfigffthpssGTTSKI 366
Cdd:pfam00063  160 FDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQ-----------SGCYTI 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   367 PKnrlsdpkftqdsmVDDFSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEESLDDSRGgckVFNGSEqDLIQ 446
Cdd:pfam00063  229 DG-------------IDDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQA---VPDDTE-NLQK 291

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   447 AARLLGLETMELKMGLCARIMQTtkggaRGTLIRVPLKPHEACSGRDALSKAIYSKLFDWLVSRINDSIPFEKST--NFV 524
Cdd:pfam00063  292 AASLLGIDSTELEKALCKRRIKT-----GRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEkaSFI 366

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   525 GVLDVAGFEFYAKNSFEQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEFIDNQDCIELFELKGNGLFDLLDEE 604
Cdd:pfam00063  367 GVLDIYGFEIFEKNSFEQLCINYVNEKLQQFFNHHMFKLEQEEYVREGIEWTFIDFGDNQPCIDLIEKKPLGILSLLDEE 446

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   605 AKFPTSNYKSFTKRAHEENRKHFRLDTPRkskvkshreLRDDEGLLIRHYAGSVCYETKHFVEKNDDLLHNSLQILIEQS 684
Cdd:pfam00063  447 CLFPKATDQTFLDKLYSTFSKHPHFQKPR---------LQGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSS 517

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   685 TIRLLVSLF---------------GSTAYPTKSKLKAlSVGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGS 749
Cdd:pfam00063  518 SDPLLAELFpdyetaesaaanesgKSTPKRTKKKRFI-TVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNS 596

                          650       660       670       680       690       700       710
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 808358096   750 AILSQLQCAGMTSVLKLMQDGFPSRTGFGDLYACYQKKLPPKLSK--LDPRMFCKCLFRALGLDQHDFQFGLTKVFFR 825
Cdd:pfam00063  597 LVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRYRILAPKTWPKwkGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
MYSc cd00124
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ...
 143-825 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: 720.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  143 ATLLNNIRLRYQNGKIYSYVANILISINPYQTIDgFYSLQKIKEYRGKSLGQK-EPHIFAIADKSYREMIRHRKSQSIIV 221
Cdd:cd00124     1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLP-LYSEEVMEKYRGKGRSADlPPHVFAVADAAYRAMLRDGQNQSILI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  222 SGESGAGKTESQKAVLRYLCE-------NWGSGAGEIQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFADTGNVA 294
Cdd:cd00124    80 SGESGAGKTETTKLVLKYLAAlsgsgssKSSSSASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  295 GGYVSHYLLETSRICRQAAGERNYHIFYQLIAGSSPELFKFLALGQPNQFNYLkrgfigffthpssgttskipKNRLSDP 374
Cdd:cd00124   160 GASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYL--------------------NDYLNSS 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  375 KFTQDSMVDDFSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEESLDDSRGGCKVfnGSEQDLIQAARLLGLE 454
Cdd:cd00124   220 GCDRIDGVDDAEEFQELLDALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEDSSAEV--ADDESLKAAAKLLGVD 297

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  455 TMELKMGLCARIMQTtkggaRGTLIRVPLKPHEACSGRDALSKAIYSKLFDWLVSRINDSI---PFEKSTNFVGVLDVAG 531
Cdd:cd00124   298 AEDLEEALTTRTIKV-----GGETITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALsptDAAESTSFIGILDIFG 372

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  532 FEFYAKNSFEQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEFIDNQDCIELFELKGNGLFDLLDEEAKFPTSN 611
Cdd:cd00124   373 FENFEVNSFEQLCINYANEKLQQFFNQHVFKLEQEEYEEEGIDWSFIDFPDNQDCLDLIEGKPLGILSLLDEECLFPKGT 452

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  612 YKSFTKRAHEENRKHFRLDTPRKSKVKShrelrddegLLIRHYAGSVCYETKHFVEKNDDLLHNSLQILieqstirllvs 691
Cdd:cd00124   453 DATFLEKLYSAHGSHPRFFSKKRKAKLE---------FGIKHYAGDVTYDADGFLEKNKDTLPPDLVDL----------- 512

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  692 lfgstayptksklkaLSVGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGSAILSQLQCAGMTSVLKLMQDGF 771
Cdd:cd00124   513 ---------------LRSGSQFRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGY 577

                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 808358096  772 PSRTGFGDLYACYQKKLPP--KLSKLDPRMFCKCLFRALGLDQHDFQFGLTKVFFR 825
Cdd:cd00124   578 PVRLPFDEFLKRYRILAPGatEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
COG5022 COG5022
Myosin heavy chain [General function prediction only];
76-1070 0e+00

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 629.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   76 GRTVWITDATDGFRAARIIDLSATG--FTLrLLDNTGDTVTRVFEDVLACEDDSRRH---VEDNCQLMHLNEATLLNNIR 150
Cdd:COG5022     9 GSGCWIPDEEKGWIWAEIIKEAFNKgkVTE-EGKKEDGESVSVKKKVLGNDRIKLPKfdgVDDLTELSYLNEPAVLHNLE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  151 LRYQNGKIYSYVANILISINPYQTIdGFYSLQKIKEYRGKSLGQKEPHIFAIADKSYREMIRHRKSQSIIVSGESGAGKT 230
Cdd:COG5022    88 KRYNNGQIYTYSGLVLIAVNPYRDL-GIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKT 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  231 ESQKAVLRYLCENWGS---GAGEIQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFADTGNVAGGYVSHYLLETSR 307
Cdd:COG5022   167 ENAKRIMQYLASVTSSstvEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSR 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  308 ICRQAAGERNYHIFYQLIAGSSPELFKFLALGQPNQFNYLKrgfigffthpsSGTTSKIPKnrlsdpkftqdsmVDDFSD 387
Cdd:COG5022   247 VVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLS-----------QGGCDKIDG-------------IDDAKE 302

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  388 FQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEESLDdsrGGCKVfnGSEQDLIQAARLLGLETMELKMGLCARIM 467
Cdd:COG5022   303 FKITLDALKTIGIDEEEQDQIFKILAAILHIGNIEFKEDRN---GAAIF--SDNSVLDKACYLLGIDPSLFVKWLVKRQI 377

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  468 QTtkggaRGTLIRVPLKPHEACSGRDALSKAIYSKLFDWLVSRINDSI-PFEKSTNFVGVLDVAGFEFYAKNSFEQFCIN 546
Cdd:COG5022   378 KT-----GGEWIVVPLNLEQALAIRDSLAKALYSNLFDWIVDRINKSLdHSAAASNFIGVLDIYGFEIFEKNSFEQLCIN 452

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  547 FCNEKLQNFFNQRILREEQELYEKEGLNVRKIEFIDNQDCIELFELKGN-GLFDLLDEEAKFPTSNYKSFTKRAHEenrk 625
Cdd:COG5022   453 YTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFIDYFDNQPCIDLIEKKNPlGILSLLDEECVMPHATDESFTSKLAQ---- 528

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  626 hfRLDTPRKSKVKSHReLRDDeGLLIRHYAGSVCYETKHFVEKNDDLLHNSLQILIEQSTIRLLVSLFGSTAyPTKSKLK 705
Cdd:COG5022   529 --RLNKNSNPKFKKSR-FRDN-KFVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEE-NIESKGR 603

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  706 ALSVGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGSAILSQLQCAGMTSVLKLMQDGFPSRTGFGDLYACYQ 785
Cdd:COG5022   604 FPTLGSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYR 683

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  786 KKLPPKL------SKLDPRMFCKCLFRALGLDQHDFQFGLTKVFFRAGKFAEFDQMMKQDPETMTSLIQKvnEWLVGARW 859
Cdd:COG5022   684 ILSPSKSwtgeytWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQR--AIRGRYLR 761

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  860 KQSQYAVWSVIKLKNKIA-WRSAQVT----------RLQSIARGYLTRQRFSRQIALYRKsvalLKNSKEIEKIL----- 923
Cdd:COG5022   762 RRYLQALKRIKKIQVIQHgFRLRRLVdyelkwrlfiKLQPLLSLLGSRKEYRSYLACIIK----LQKTIKREKKLretee 837

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  924 --FRLNE---HSRAKYTSSAHSTIRDLEKLVSHIKLTTsandHFEKAENAYEHY---VKRV----------DSMIADLKK 985
Cdd:COG5022   838 veFSLKAevlIQKFGRSLKAKKRFSLLKKETIYLQSAQ----RVELAERQLQELkidVKSIsslklvnlelESEIIELKK 913

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  986 QQKSDELAEIERKRRESEEKERL--EIEAKKEAERQREIKRKLEE-QQQNAQKEHENYLISEIHKaaEETEKKRQ-NEEK 1061
Cdd:COG5022   914 SLSSDLIENLEFKTELIARLKKLlnNIDLEEGPSIEYVKLPELNKlHEVESKLKETSEEYEDLLK--KSTILVREgNKAN 991


                  ....*....
gi 808358096 1062 EKLDKMVSN 1070
Cdd:COG5022   992 SELKNFKKE 1000
MYSc_Myo11 cd01384
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ...
 146-825 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: 626.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  146 LNNIRLRYQNGKIYSYVANILISINPYQTIDGFYSLQKIKEYRGKSLGQKEPHIFAIADKSYREMIRHRKSQSIIVSGES 225
Cdd:cd01384     4 LHNLKVRYELDEIYTYTGNILIAVNPFKRLPHLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVSGES 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  226 GAGKTESQKAVLRYLCENWGSGAGE---IQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFADTGNVAGGYVSHYL 302
Cdd:cd01384    84 GAGKTETTKMLMQYLAYMGGRAVTEgrsVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAAIRTYL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  303 LETSRICRQAAGERNYHIFYQLIAGSSPELFKFLALGQPNQFNYLKRgfigffthpssgttSKIPKnrLSDpkftqdsmV 382
Cdd:cd01384   164 LERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNQ--------------SKCFE--LDG--------V 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  383 DDFSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEESLDDSRGGCKVfNGSEQDLIQAARLLGLETMELKMGL 462
Cdd:cd01384   220 DDAEEYRATRRAMDVVGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKD-EKSEFHLKAAAELLMCDEKALEDAL 298

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  463 CARIMQTTKGgargtLIRVPLKPHEACSGRDALSKAIYSKLFDWLVSRINDSIPFEK-STNFVGVLDVAGFEFYAKNSFE 541
Cdd:cd01384   299 CKRVIVTPDG-----IITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPnSKRLIGVLDIYGFESFKTNSFE 373

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  542 QFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEFIDNQDCIELFELKGNGLFDLLDEEAKFPTSNYKSFTKRAHE 621
Cdd:cd01384   374 QFCINLANEKLQQHFNQHVFKMEQEEYTKEEIDWSYIEFVDNQDVLDLIEKKPGGIIALLDEACMFPRSTHETFAQKLYQ 453

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  622 ENRKHFRLDTPRKSKVKshrelrddegLLIRHYAGSVCYETKHFVEKNDDLLHNSLQILIEQSTIRLLVSLFGSTAYP-T 700
Cdd:cd01384   454 TLKDHKRFSKPKLSRTD----------FTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPREgT 523

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  701 KSKLKALSVGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGSAILSQLQCAGMTSVLKLMQDGFPSRTGFGDL 780
Cdd:cd01384   524 SSSSKFSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEF 603

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*.
gi 808358096  781 YACYQKKLPPKLSKLDPR-MFCKCLFRALGLDqhDFQFGLTKVFFR 825
Cdd:cd01384   604 LDRFGLLAPEVLKGSDDEkAACKKILEKAGLK--GYQIGKTKVFLR 647
MYSc_Myo22 cd14883
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ...
 144-825 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: 618.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  144 TLLNNIRLRYQNGKIYSYVANILISINPYQTIDgFYSLQKIKEYRGKSLGQKEPHIFAIADKSYREMIRHRKSQSIIVSG 223
Cdd:cd14883     2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELP-IYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  224 ESGAGKTESQKAVLRYLCENwGSGAGEIQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFADTGNVAGGYVSHYLL 303
Cdd:cd14883    81 ESGAGKTETTKLILQYLCAV-TNNHSWVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGAIIQDYLL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  304 ETSRICRQAAGERNYHIFYQLIAG--SSPELFKFLALGQPNQFNYLkrgfigffthPSSGTtSKIPKnrlsdpkftqdsm 381
Cdd:cd14883   160 EQSRITFQAPGERNYHVFYQLLAGakHSKELKEKLKLGEPEDYHYL----------NQSGC-IRIDN------------- 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  382 VDDFSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEESlDDSRGGCKVFNGSEQDLIqaARLLGLETMELKMG 461
Cdd:cd14883   216 INDKKDFDHLRLAMNVLGIPEEMQEGIFSVLSAILHLGNLTFEDI-DGETGALTVEDKEILKIV--AKLLGVDPDKLKKA 292

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  462 LCARIMQTtkggaRGTLIRVPLKPHEACSGRDALSKAIYSKLFDWLVSRINDSI-PFEKSTNFVGVLDVAGFEFYAKNSF 540
Cdd:cd14883   293 LTIRQINV-----RGNVTEIPLKVQEARDNRDAMAKALYSRTFAWLVNHINSCTnPGQKNSRFIGVLDIFGFENFKVNSF 367

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  541 EQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEFIDNQDCIELFELKGNGLFDLLDEEAKFPTSNYKSFTKRAH 620
Cdd:cd14883   368 EQLCINYTNEKLHKFFNHYVFKLEQEEYEKEGINWSHIVFTDNQECLDLIEKPPLGILKLLDEECRFPKGTDLTYLEKLH 447

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  621 EENRKHfrldtprKSKVKSHRELRDDEgLLIRHYAGSVCYETKHFVEKNDDLLHNSLQILIEQSTIRLLVSLF------- 693
Cdd:cd14883   448 AAHEKH-------PYYEKPDRRRWKTE-FGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFtypdlla 519

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  694 --------GSTAYPTKSKLKALSVGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGSAILSQLQCAGMTSVLK 765
Cdd:cd14883   520 ltglsislGGDTTSRGTSKGKPTVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIR 599

                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 808358096  766 LMQDGFPSRTGFGDLYACYqKKLPPKLSKLDPRMFCKC---LFRALGLDQHDFQFGLTKVFFR 825
Cdd:cd14883   600 IRKEGFPIHLTFKEFVDRY-LCLDPRARSADHKETCGAvraLMGLGGLPEDEWQVGKTKVFLR 661
MYSc_Myo5 cd01380
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ...
 146-825 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: 611.85  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  146 LNNIRLRYQNGK-IYSYVANILISINPYQTIDgFYSLQKIKEYRGKSLGQKEPHIFAIADKSYREMIRHRKSQSIIVSGE 224
Cdd:cd01380     4 LHNLKVRFCQRNaIYTYCGIVLVAINPYEDLP-IYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSGE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  225 SGAGKTESQKAVLRYLCENWGSGAGE--IQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFADTGNVAGGYVSHYL 302
Cdd:cd01380    83 SGAGKTVSAKYAMRYFATVGGSSSGEtqVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANMRTYL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  303 LETSRICRQAAGERNYHIFYQLIAGSSPELFKFLALGQPNQFNYLkrgfigffthpSSGTTSKIPKnrlsdpkftqdsmV 382
Cdd:cd01380   163 LEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYT-----------NQGGSPVIDG-------------V 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  383 DDFSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEEslddSRGGCKVFNGSEQDLIQAARLLGLETMELKMGL 462
Cdd:cd01380   219 DDAAEFEETRKALTLLGISEEEQMEIFRILAAILHLGNVEIKA----TRNDSASISPDDEHLQIACELLGIDESQLAKWL 294

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  463 CARIMQTtkggaRGTLIRVPLKPHEACSGRDALSKAIYSKLFDWLVSRINDSIPF---EKSTNFVGVLDVAGFEFYAKNS 539
Cdd:cd01380   295 CKRKIVT-----RSEVIVKPLTLQQAIVARDALAKHIYAQLFDWIVDRINKALASpvkEKQHSFIGVLDIYGFETFEVNS 369

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  540 FEQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEFIDNQDCIELFELKgNGLFDLLDEEAKFPTSNYKSFTKRA 619
Cdd:cd01380   370 FEQFCINYANEKLQQQFNQHVFKLEQEEYVKEEIEWSFIDFYDNQPCIDLIEGK-LGILDLLDEECRLPKGSDENWAQKL 448

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  620 HEE----NRKHFRLdtPRKSKvkshrelrddEGLLIRHYAGSVCYETKHFVEKNDDllhnslQILIEQstIRLLVSlfgs 695
Cdd:cd01380   449 YNQhlkkPNKHFKK--PRFSN----------TAFIVKHFADDVEYQVEGFLEKNRD------TVSEEH--LNVLKA---- 504

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  696 tayptkSKLKALSVGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGSAILSQLQCAGMTSVLKLMQDGFPSRT 775
Cdd:cd01380   505 ------SKNRKKTVGSQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRW 578

                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|.
gi 808358096  776 GFGDLYACYQKKLPPK-LSKLDPRMFCKCLFRALGLDQHDFQFGLTKVFFR 825
Cdd:cd01380   579 TYEEFFSRYRVLLPSKeWLRDDKKKTCENILENLILDPDKYQFGKTKIFFR 629
MYSc_Myo1 cd01378
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ...
 145-825 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: 596.06  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  145 LLNNIRLRYQNGKIYSYVANILISINPYQTIdGFYSLQKIKEYRGKSLGQKEPHIFAIADKSYREMIRHRKSQSIIVSGE 224
Cdd:cd01378     3 INENLKKRFENDEIYTYIGHVLISVNPFKDL-GIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  225 SGAGKTESQKAVLRYLCENWGSGAGEIQK---RLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFADTGNVAGGYVSHY 301
Cdd:cd01378    82 SGAGKTEASKRIMQYIAAVSGGSESEVERvkdMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGHITNY 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  302 LLETSRICRQAAGERNYHIFYQLIAGSSPELFKFLALGQPNQFNYLKRgfigffthpsSGTtskipknrlsdpkFTQDSM 381
Cdd:cd01378   162 LLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSK----------SGC-------------FDVDGI 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  382 vDDFSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEEsldDSRGGCKVFNGSEQDLIqaARLLGLETMELKMG 461
Cdd:cd01378   219 -DDAADFKEVLNAMKVIGFTEEEQDSIFRILAAILHLGNIQFAE---DEEGNAAISDTSVLDFV--AYLLGVDPDQLEKA 292

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  462 LCARIMQTTKGGArgTLIRVPLKPHEACSGRDALSKAIYSKLFDWLVSRINDSIPFEKST--NFVGVLDVAGFEFYAKNS 539
Cdd:cd01378   293 LTHRTIETGGGGR--SVYEVPLNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGkkKVIGVLDIYGFEIFEKNS 370

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  540 FEQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEFIDNQDCIELFELKGNGLFDLLDEEAKFP-TSNYKSFTKR 618
Cdd:cd01378   371 FEQFCINYVNEKLQQIFIELTLKAEQEEYVREGIEWTPIKYFNNKIICDLIEEKPPGIFAILDDACLTAgDATDQTFLQK 450

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  619 AHEENRKHfrldtPRKSKVKSHRELRDDEgLLIRHYAGSVCYETKHFVEKNDDLLHNSLQILIEQSTIRLLVSLFGSTAy 698
Cdd:cd01378   451 LNQLFSNH-----PHFECPSGHFELRRGE-FRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGV- 523

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  699 PTKSKLKALSVGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGSAILSQLQCAGMTSVLKLMQDGFPSRTGFg 778
Cdd:cd01378   524 DLDSKKRPPTAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTY- 602

                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|
gi 808358096  779 DLYACYQKKLPPKLS---KLDPRMFCKCLFRALGLDQHDFQFGLTKVFFR 825
Cdd:cd01378   603 EKFLERYKLLSPKTWpawDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
MYSc_Myo8 cd01383
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ...
 145-825 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: 583.89  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  145 LLNNIRLRYQNGKIYSYVANILISINPYQTIDgFYSLQKIKEYRGKSLGqkEPHIFAIADKSYREMIRHRKSQSIIVSGE 224
Cdd:cd01383     3 VLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVP-LYGNEFITAYRQKLLD--SPHVYAVADTAYREMMRDEINQSIIISGE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  225 SGAGKTESQKAVLRYLcENWGSGAGEIQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFADTGNVAGGYVSHYLLE 304
Cdd:cd01383    80 SGAGKTETAKIAMQYL-AALGGGSSGIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQTYLLE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  305 TSRICRQAAGERNYHIFYQLIAGSSPELFKFLALGQPNQFNYLkrgfigffthpSSGTTSKIPKnrlsdpkftqdsmVDD 384
Cdd:cd01383   159 KSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYL-----------NQSNCLTIDG-------------VDD 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  385 FSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEEslddsRGGCKVFNGSEQD-LIQAARLLGLETMELKMGLC 463
Cdd:cd01383   215 AKKFHELKEALDTVGISKEDQEHIFQMLAAVLWLGNISFQV-----IDNENHVEVVADEaVSTAASLLGCNANDLMLALS 289

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  464 ARIMQttkggARGTLIRVPLKPHEACSGRDALSKAIYSKLFDWLVSRINDSIPFEKSTN--FVGVLDVAGFEFYAKNSFE 541
Cdd:cd01383   290 TRKIQ-----AGGDKIVKKLTLQQAIDARDALAKAIYASLFDWLVEQINKSLEVGKRRTgrSISILDIYGFESFQKNSFE 364

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  542 QFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEFIDNQDCIELFELKGNGLFDLLDEEAKFPTSNYKSFTKRAHE 621
Cdd:cd01383   365 QLCINYANERLQQHFNRHLFKLEQEEYELDGIDWTKVDFEDNQECLDLIEKKPLGLISLLDEESNFPKATDLTFANKLKQ 444

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  622 ENRKHfrldtprkskvkSHRELRDDEGLLIRHYAGSVCYETKHFVEKNDDLLH-NSLQILieQSTIRLLVSLFGS----- 695
Cdd:cd01383   445 HLKSN------------SCFKGERGGAFTIRHYAGEVTYDTSGFLEKNRDLLHsDLIQLL--SSCSCQLPQLFASkmlda 510

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  696 ------TAYPTKSKLKALSVGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGSAILSQLQCAGMTSVLKLMQD 769
Cdd:cd01383   511 srkalpLTKASGSDSQKQSVATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRS 590

                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 808358096  770 GFPSRTGFGDLYACYQKKLPPKLS-KLDPRMFCKCLFRALGLDQHDFQFGLTKVFFR 825
Cdd:cd01383   591 GYPTRMTHQEFARRYGFLLPEDVSaSQDPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
MYSc_class_II cd01377
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ...
 143-825 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: 570.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  143 ATLLNNIRLRYQNGKIYSYVANILISINPYQTIDgFYSLQKIKEYRGKSLGQKEPHIFAIADKSYREMIRHRKSQSIIVS 222
Cdd:cd01377     1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLP-IYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILIT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  223 GESGAGKTESQKAVLRYL---------CENWGSGAGEIQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFADTGNV 293
Cdd:cd01377    80 GESGAGKTENTKKVIQYLasvaasskkKKESGKKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  294 AGGYVSHYLLETSRICRQAAGERNYHIFYQLIAGSSPEL-FKFLALGQPNQFNYLKRGfigffthpssgttskipknRLS 372
Cdd:cd01377   160 AGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELkEKLLLTGDPSYYFFLSQG-------------------ELT 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  373 DPkftqdsMVDDFSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEEsldDSRGGCKVFNGSEqDLIQAARLLG 452
Cdd:cd01377   221 ID------GVDDAEEFKLTDEAFDILGFSEEEKMSIFKIVAAILHLGNIKFKQ---RRREEQAELDGTE-EADKAAHLLG 290

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  453 LETMELKMGLC-ARIMQ----TTKGgargtlirvpLKPHEACSGRDALSKAIYSKLFDWLVSRINDSIPF-EKSTNFVGV 526
Cdd:cd01377   291 VNSSDLLKALLkPRIKVgrewVTKG----------QNKEQVVFSVGALAKALYERLFLWLVKRINKTLDTkSKRQYFIGV 360

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  527 LDVAGFEFYAKNSFEQFCINFCNEKLQNFFNQR--ILreEQELYEKEGlnvrkIE--FI----DNQDCIELFELKGNGLF 598
Cdd:cd01377   361 LDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHmfVL--EQEEYKKEG-----IEwtFIdfglDLQPTIDLIEKPNMGIL 433

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  599 DLLDEEAKFPTSNYKSFTKRAHEENRKHFRLDTPRKSKvkshrelRDDEGLLIRHYAGSVCYETKHFVEKNDDLLHNSLQ 678
Cdd:cd01377   434 SILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKPKPK-------KSEAHFILKHYAGDVEYNIDGWLEKNKDPLNENVV 506

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  679 ILIEQSTIRLLVSLF----GSTAYPTKSKLKA---LSVGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGSAI 751
Cdd:cd01377   507 ALLKKSSDPLVASLFkdyeESGGGGGKKKKKGgsfRTVSQLHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLV 586

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  752 LSQLQCAGmtsVL---KLMQDGFPSRTGFGDLYACYQ---KKLPPKlSKLDPRMFCKCLFRALGLDQHDFQFGLTKVFFR 825
Cdd:cd01377   587 LHQLRCNG---VLegiRICRKGFPNRIIFAEFKQRYSilaPNAIPK-GFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
MYSc_Myo7 cd01381
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ...
 143-825 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: 568.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  143 ATLLNNIRLRYQNGKIYSYVANILISINPYQTIDgFYSLQKIKEYRGKSLGQKEPHIFAIADKSYREMIRHRKSQSIIVS 222
Cdd:cd01381     1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILP-IYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVIS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  223 GESGAGKTESQKAVLRYLCENwgSGAGE-IQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFADTGNVAGGYVSHY 301
Cdd:cd01381    80 GESGAGKTESTKLILQYLAAI--SGQHSwIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKIEQY 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  302 LLETSRICRQAAGERNYHIFYQLIAGSSPELFKFLALGQPNQFNYLKRGfigffthpssgttskipknrlsdpKFTQDSM 381
Cdd:cd01381   158 LLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQG------------------------NCLTCEG 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  382 VDDFSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEESLDDSRGGCKVFNGSEqdLIQAARLLGLETMELKMG 461
Cdd:cd01381   214 RDDAAEFADIRSAMKVLMFTDEEIWDIFKLLAAILHLGNIKFEATVVDNLDASEVRDPPN--LERAAKLLEVPKQDLVDA 291

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  462 LCARIMQTtkggaRGTLIRVPLKPHEACSGRDALSKAIYSKLFDWLVSRINDSI----PFEKSTNFVGVLDVAGFEFYAK 537
Cdd:cd01381   292 LTTRTIFT-----RGETVVSPLSAEQALDVRDAFVKGIYGRLFIWIVNKINSAIykprGTDSSRTSIGVLDIFGFENFEV 366

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  538 NSFEQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEFIDNQDCIELFELKGNGLFDLLDEEAKFPTSNYKSFTK 617
Cdd:cd01381   367 NSFEQLCINFANENLQQFFVRHIFKLEQEEYDKEGINWQHIEFVDNQDVLDLIALKPMNIMSLIDEESKFPKGTDQTMLE 446

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  618 RAHEENRKHfrldtprKSKVKSHRELRDDEGllIRHYAGSVCYETKHFVEKNDDLLHNSLQILIEQSTIRLLVSLFGST- 696
Cdd:cd01381   447 KLHSTHGNN-------KNYLKPKSDLNTSFG--INHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDi 517

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  697 AYPTKSKLKALSVGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGSAILSQLQCAGMTSVLKLMQDGFPSRTG 776
Cdd:cd01381   518 SMGSETRKKSPTLSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHT 597

                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|.
gi 808358096  777 FGDLYACYQKKLP--PKLSKLDPRMFCKCLFRALGLDQHDFQFGLTKVFFR 825
Cdd:cd01381   598 FEEFVERYRVLVPgiPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
MYSc_Myo29 cd14890
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ...
 143-825 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: 549.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  143 ATLLNNIRLRYQNGKIYSYVANILISINPYQTIDGFYSLQKIKEYRGKSLGQKEPHIFAIADKSYREMIRHRKS----QS 218
Cdd:cd14890     1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPDLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQSGVLdpsnQS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  219 IIVSGESGAGKTESQKAVLRYLC------------------ENWGSGAGEIQKRLLETNPILEAFGNAKTLRNNNSSRFG 280
Cdd:cd14890    81 IIISGESGAGKTEATKIIMQYLAritsgfaqgasgegeaasEAIEQTLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  281 KFVQIHFADTGNVAGGYVSHYLLETSRICRQAAGERNYHIFYQLIAGSSPELFKFLALGQPNQFNYLKrgfigffthpss 360
Cdd:cd14890   161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLR------------ 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  361 gttskipKNRLSDPKftqdsmVDDFSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEESLDDSRGGCKVfngS 440
Cdd:cd14890   229 -------GECSSIPS------CDDAKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLEDAT---T 292

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  441 EQDLIQAARLLGLETMELKMGLCARIMQTtkggaRGTLIRVPLKPHEACSGRDALSKAIYSKLFDWLVSRINDSIPF-EK 519
Cdd:cd14890   293 LQSLKLAAELLGVNEDALEKALLTRQLFV-----GGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSpDD 367

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  520 STNFVGVLDVAGFEFYAKNSFEQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEFIDNQDCIELFELKGN---G 596
Cdd:cd14890   368 KWGFIGVLDIYGFEKFEWNTFEQLCINYANEKLQRHFNQHMFEVEQVEYSNEGIDWQYITFNDNQACLELIEGKVNgkpG 447

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  597 LFDLLD-------EEA--KFPTSNYKSF-------TKRAHEENRKHFRldTPrksKVKSHRElrddegLLIRHYAGSVCY 660
Cdd:cd14890   448 IFITLDdcwrfkgEEAnkKFVSQLHASFgrksgsgGTRRGSSQHPHFV--HP---KFDADKQ------FGIKHYAGDVIY 516

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  661 ETKHFVEKNDDLLHNSLQILIEQSTirllvslfgstayptkSKLKALSVGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQ 740
Cdd:cd14890   517 DASGFNEKNNETLNAEMKELIKQSR----------------RSIREVSVGAQFRTQLQELMAKISLTNPRYVRCIKPNET 580

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  741 MIPFEFDGSAILSQLQCAGMTSVLKLMQDGFPSRTGFGDLYACYQKKLPpklSKLDPRMFCKCLFRALGLDQHDFQFGLT 820
Cdd:cd14890   581 KAPGKFDGLDCLRQLKYSGMMEAIQIRQQGFALREEHDSFFYDFQVLLP---TAENIEQLVAVLSKMLGLGKADWQIGSS 657


                  ....*
gi 808358096  821 KVFFR 825
Cdd:cd14890   658 KIFLK 662
MYSc_Myo4 cd14872
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ...
 143-825 1.15e-177

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: 539.75  E-value: 1.15e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  143 ATLLNNIRLRYQNGKIYSYVANILISINPYQTIDgFYSLQKIKEYRGKSLGQKEPHIFAIADKSYREMIRHRKSQSIIVS 222
Cdd:cd14872     1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLP-LYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILIS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  223 GESGAGKTESQKAVLRYLCENWGSGAGeIQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFADTGNVAGGYVSHYL 302
Cdd:cd14872    80 GESGAGKTEATKQCLSFFAEVAGSTNG-VEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGASTENYL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  303 LETSRICRQAAGERNYHIFYQLIAGSSPElfkflalgqpnqfnylkrgfigffthPSSGTTSKIPKNRLSDPKFTQDSMV 382
Cdd:cd14872   159 LEKSRVVYQIKGERNFHIFYQLLASPDPA--------------------------SRGGWGSSAAYGYLSLSGCIEVEGV 212

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  383 DDFSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEESLDDSrGGCKVFNGSEQDLIQAARLLGLETMELKMGL 462
Cdd:cd14872   213 DDVADFEEVVLAMEQLGFDDADINNVMSLIAAILKLGNIEFASGGGKS-LVSGSTVANRDVLKEVATLLGVDAATLEEAL 291

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  463 CARIMqTTKGGaRGTliRVPLKPHEACSGRDALSKAIYSKLFDWLVSRINDSIPFEKS--TNFVGVLDVAGFEFYAKNSF 540
Cdd:cd14872   292 TSRLM-EIKGC-DPT--RIPLTPAQATDACDALAKAAYSRLFDWLVKKINESMRPQKGakTTFIGVLDIFGFEIFEKNSF 367

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  541 EQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEFIDNQDCIELFELKGNGLFDLLDEEAKFPTSNYKSFTKRAH 620
Cdd:cd14872   368 EQLCINFTNEKLQQHFNQYTFKLEEALYQSEGVKFEHIDFIDNQPVLDLIEKKQPGLMLALDDQVKIPKGSDATFMIAAN 447

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  621 EENRKhfrldtpRKSKVKSHRElRDDEGLLIRHYAGSVCYETKHFVEKNDDLLHNSLQILIEQSTIRLLVSLFgsTAYPT 700
Cdd:cd14872   448 QTHAA-------KSTFVYAEVR-TSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLF--PPSEG 517

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  701 KSKLKALSVGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGSAILSQLQCAGMTSVLKLMQDGFPSR---TGF 777
Cdd:cd14872   518 DQKTSKVTLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRyshERF 597

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*...
gi 808358096  778 GDLYACYQKKLPPKLSKLDpRMFCKCLFRALGLDQHDFQFGLTKVFFR 825
Cdd:cd14872   598 LKRYRFLVKTIAKRVGPDD-RQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
MYSc_Myo27 cd14888
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ...
 143-825 1.36e-174

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: 532.35  E-value: 1.36e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  143 ATLLNNIRLRYQNGKIYSYVANILISINPYQTIDGFYSLQKIKEYRGKSlGQKEPHIFAIADKSYREMIRHRKSQSIIVS 222
Cdd:cd14888     1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPGLYSDEMLLKFIQPS-ISKSPHVFSTASSAYQGMCNNKKSQTILIS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  223 GESGAGKTESQKAVLRYLCenwGSGAGEIQKR------LLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFA-------- 288
Cdd:cd14888    80 GESGAGKTESTKYVMKFLA---CAGSEDIKKRslveaqVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSklkskrms 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  289 -DTGNVAGGYVSHYLLETSRICRQAAGERNYHIFYQLIAGSspELFKFLALGQPNQFNYLKRG---------FIGFFTHP 358
Cdd:cd14888   157 gDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAA--REAKNTGLSYEENDEKLAKGadakpisidMSSFEPHL 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  359 SSGTTSKIPKNRLSDpkftqdsmVDDFSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEESlDDSRGGCKVFN 438
Cdd:cd14888   235 KFRYLTKSSCHELPD--------VDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENN-EACSEGAVVSA 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  439 GSEQDLIQAARLLGLETMELKMGLCARIMQTTKGgargtLIRVPLKPHEACSGRDALSKAIYSKLFDWLVSRINDSIPFE 518
Cdd:cd14888   306 SCTDDLEKVASLLGVDAEDLLNALCYRTIKTAHE-----FYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYS 380

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  519 KSTN--FVGVLDVAGFEFYAKNSFEQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEFIDNQDCIELFELKGNG 596
Cdd:cd14888   381 KDNSllFCGVLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFPDNQDCVDLLQEKPLG 460

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  597 LFDLLDEEAKFPTSNYKSFTKRAHEENRKHFRLDtprksKVKShrelrDDEGLLIRHYAGSVCYETKHFVEKNDDLLHNS 676
Cdd:cd14888   461 IFCMLDEECFVPGGKDQGLCNKLCQKHKGHKRFD-----VVKT-----DPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVD 530

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  677 LQILIEQSTIRLLVSLF------GSTAYPTKSKLKalSVGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGSA 750
Cdd:cd14888   531 AQEVIKNSKNPFISNLFsaylrrGTDGNTKKKKFV--TVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRIS 608

                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 808358096  751 ILSQLQCAGMTSVLKLMQDGFPSRTGFGDLYACYqkklppklskldprmfcKCLFRALGLDQHD-FQFGLTKVFFR 825
Cdd:cd14888   609 VNEQLKYGGVLQAVQVSRAGYPVRLSHAEFYNDY-----------------RILLNGEGKKQLSiWAVGKTLCFFK 667
MYSc_Myo10 cd14873
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ...
 143-825 5.12e-167

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: 512.03  E-value: 5.12e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  143 ATLLNNIRLRYQNGKIYSYVANILISINPYQTIDGFYSLQKIKEYRGKSLGQKEPHIFAIADKSYREMIRHRKSQSIIVS 222
Cdd:cd14873     1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAGLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  223 GESGAGKTESQKAVLRYLCE----NWGSGAGEIQKR----LLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFADTGNVA 294
Cdd:cd14873    81 GESGAGKTESTKLILKFLSVisqqSLELSLKEKTSCveqaILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  295 GGYVSHYLLETSRICRQAAGERNYHIFYQLIAGSSPELFKFLALGQPNQFNYLKRgfigffthpsSGTTSkipknrlsdp 374
Cdd:cd14873   161 GGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNQ----------SGCVE---------- 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  375 kftqDSMVDDFSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEeslddSRGGCKVfnGSEQDLIQAARLLGLE 454
Cdd:cd14873   221 ----DKTISDQESFREVITAMEVMQFSKEEVREVSRLLAGILHLGNIEFI-----TAGGAQV--SFKTALGRSAELLGLD 289

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  455 TMELKMGLCARIMQTtkggaRGTLIRVPLKPHEACSGRDALSKAIYSKLFDWLVSRINDSIPFEKSTNFVGVLDVAGFEF 534
Cdd:cd14873   290 PTQLTDALTQRSMFL-----RGEEILTPLNVQQAVDSRDSLAMALYARCFEWVIKKINSRIKGKEDFKSIGILDIFGFEN 364

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  535 YAKNSFEQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEFIDNQDCIELFELKgNGLFDLLDEEAKFPTSNYKS 614
Cdd:cd14873   365 FEVNHFEQFNINYANEKLQEYFNKHIFSLEQLEYSREGLVWEDIDWIDNGECLDLIEKK-LGLLALINEESHFPQATDST 443

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  615 FTKRAHEEnrkHFRLDTPRKSKVKSHRelrddegLLIRHYAGSVCYETKHFVEKNDDLLHNSLQILIEQSTIRLLVSLFG 694
Cdd:cd14873   444 LLEKLHSQ---HANNHFYVKPRVAVNN-------FGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFE 513

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  695 STAY-------PTKSKLKALSVGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGSAILSQLQCAGMTSVLKLM 767
Cdd:cd14873   514 HVSSrnnqdtlKCGSKHRRPTVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIR 593

                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 808358096  768 QDGFPSRTGFGDLYACYQKKLPPKLSKLDPRMFCKCLFRALGLDQHDFQFGLTKVFFR 825
Cdd:cd14873   594 KAGYAVRRPFQDFYKRYKVLMRNLALPEDVRGKCTSLLQLYDASNSEWQLGKTKVFLR 651
MYSc_Myo36 cd14897
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ...
 143-825 1.17e-164

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: 505.38  E-value: 1.17e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  143 ATLLNNIRLRYQNGKIYSYVANILISINPYQTIDgFYSLQKIKEYRGKSL-GQKEPHIFAIADKSYREMIRHRKSQSIIV 221
Cdd:cd14897     1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLP-IFDKKHHEEYSNLSVrSQRPPHLFWIADQAYRRLLETGRNQCILV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  222 SGESGAGKTESQKAVLRYLCENWGSGAGEIQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFADTGNVAGGYVSHY 301
Cdd:cd14897    80 SGESGAGKTESTKYMIKHLMKLSPSDDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAKIDDY 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  302 LLETSRICRQAAGERNYHIFYQLIAGSSPELFKFLALGQPNQFNYLKRGFIgffTHPSSGTTSKIPKNRLSdpkftqdsm 381
Cdd:cd14897   160 LLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILRDDNR---NRPVFNDSEELEYYRQM--------- 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  382 vddfsdFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEEslDDSRGGCKVFNgsEQDLIQAARLLGLETMELKMG 461
Cdd:cd14897   228 ------FHDLTNIMKLIGFSEEDISVIFTILAAILHLTNIVFIP--DEDTDGVTVAD--EYPLHAVAKLLGIDEVELTEA 297

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  462 LCARIMQTtkggaRGTLIRVPLKPHEACSGRDALSKAIYSKLFDWLVSRINDSIPFEKSTNF------VGVLDVAGFEFY 535
Cdd:cd14897   298 LISNVNTI-----RGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDFQImtrgpsIGILDMSGFENF 372

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  536 AKNSFEQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEFIDNQDCIELFELKGNGLFDLLDEEAKFPTSNYKSF 615
Cdd:cd14897   373 KINSFDQLCINLSNERLQQYFNDYVFPRERSEYEIEGIEWRDIEYHDNDDVLELFFKKPLGILPLLDEESTFPQSTDSSL 452

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  616 TKRAHeenrKHFRlDTPRKSKVKShrelrDDEGLLIRHYAGSVCYETKHFVEKNDDLLHNSLQILIEQSTIRLLVSLFgs 695
Cdd:cd14897   453 VQKLN----KYCG-ESPRYVASPG-----NRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLF-- 520

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  696 TAYptksklkalsvgakFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGSAILSQLQCAGMTSVLKLMQDGFPSRT 775
Cdd:cd14897   521 TSY--------------FKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRI 586

                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|
gi 808358096  776 GFGDLYACYqKKLPPKLSKLDPRMFCKCLFRALGLDQHDFQFGLTKVFFR 825
Cdd:cd14897   587 KYEDFVKRY-KEICDFSNKVRSDDLGKCQKILKTAGIKGYQFGKTKVFLK 635
MYSc_Myo15 cd01387
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ...
 143-825 1.67e-163

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: 503.13  E-value: 1.67e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  143 ATLLNNIRLRYQNGKIYSYVANILISINPYQTIDgFYSLQKIKEYRGKSLGQKEPHIFAIADKSYREMIRHRKSQSIIVS 222
Cdd:cd01387     1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFD-IYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVIS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  223 GESGAGKTESQKAVLRYLCENWGSGAGEIQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFADtGNVAGGYVSHYL 302
Cdd:cd01387    80 GESGSGKTEATKLIMQYLAAVNQRRNNLVTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFFEG-GVIVGAITSQYL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  303 LETSRICRQAAGERNYHIFYQLIAGSSPELFKFLALGQPNQFNYLKRgfigffthpssGTTSKIPKNrlsdpkftqdsmv 382
Cdd:cd01387   159 LEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQ-----------GGNCEIAGK------------- 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  383 DDFSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEE-SLDDSRGGCKVfnGSEQDLIQAARLLGLETMELKMG 461
Cdd:cd01387   215 SDADDFRRLLAAMQVLGFSSEEQDSIFRILASVLHLGNVYFHKrQLRHGQEGVSV--GSDAEIQWVAHLLQISPEGLQKA 292

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  462 LCARIMQTtkggaRGTLIRVPLKPHEACSGRDALSKAIYSKLFDWLVSRINDSIPFE-KSTNFVGVLDVAGFEFYAKNSF 540
Cdd:cd01387   293 LTFKVTET-----RRERIFTPLTIDQALDARDAIAKALYALLFSWLVTRVNAIVYSGtQDTLSIAILDIFGFEDLSENSF 367

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  541 EQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEFIDNQDCIELFELKGNGLFDLLDEEAKFPTSNYKSFTKRAH 620
Cdd:cd01387   368 EQLCINYANENLQYYFNKHVFKLEQEEYIREQIDWTEIAFADNQPVINLISKKPVGILHILDDECNFPQATDHSFLEKCH 447

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  621 EENRKHFRLDTPRKSkvkshrelrdDEGLLIRHYAGSVCYETKHFVEKNDDLLHNSLQILIEQSTIRLLVSLFGS----- 695
Cdd:cd01387   448 YHHALNELYSKPRMP----------LPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSShraqt 517

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  696 -TAYPTKS-------KLKALSVGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGSAILSQLQCAGMTSVLKLM 767
Cdd:cd01387   518 dKAPPRLGkgrfvtmKPRTPTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIR 597

                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  768 QDGFPSRTGFGDLYACYQKKLPPKLSKLDP-RMFCKCLFRALGLD-QHDFQFGLTKVFFR 825
Cdd:cd01387   598 KEGYPVRLPFQVFIDRYRCLVALKLPRPAPgDMCVSLLSRLCTVTpKDMYRLGATKVFLR 657
MYSc_Myo31 cd14892
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ...
 143-825 1.52e-161

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: 498.13  E-value: 1.52e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  143 ATLLNNIRLRYQNGKIYSYVANILISINPYQTIDGFYSLQKIKEYRG--KSLGQKEPHIFAIADKSYREMIRHRK----S 216
Cdd:cd14892     1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKeeATASSPPPHVFSIAERAYRAMKGVGKgqgtP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  217 QSIIVSGESGAGKTESQKAVLRYL------------CENWGSGAGEIQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQ 284
Cdd:cd14892    81 QSIVVSGESGAGKTEASKYIMKYLatasklakgastSKGAANAHESIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  285 IHFADTGNVAGGYVSHYLLETSRICRQAAGERNYHIFYQLIAGSSPELFKFLALGQPNQFNYLkrgfigffthpSSGTTS 364
Cdd:cd14892   161 IHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFL-----------NQGNCV 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  365 KIPKnrlsdpkftqdsmVDDFSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEESLDDSRGGCKVfnGSEQDL 444
Cdd:cd14892   230 EVDG-------------VDDATEFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDVFAQS--ADGVNV 294

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  445 IQAARLLGLETMELKMGLCARimqtTKGGARGTLIRVPLKPHEACSGRDALSKAIYSKLFDWLVSRIN-----------D 513
Cdd:cd14892   295 AKAAGLLGVDAAELMFKLVTQ----TTSTARGSVLEIKLTAREAKNALDALCKYLYGELFDWLISRINachkqqtsgvtG 370

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  514 SIPFEKSTNFVGVLDVAGFEFYAKNSFEQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEFIDNQDCIELFELK 593
Cdd:cd14892   371 GAASPTFSPFIGILDIFGFEIMPTNSFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQDNQDCLDLIQKK 450

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  594 GNGLFDLLDEEA--KFPTSNyKSFTKRAHEEN-RKHFRLDTPRkskvkshrelrdDEGLL--IRHYAGSVCYETKHFVEK 668
Cdd:cd14892   451 PLGLLPLLEEQMllKRKTTD-KQLLTIYHQTHlDKHPHYAKPR------------FECDEfvLRHYAGDVTYDVHGFLAK 517

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  669 NDDLLHNSLqilieqstirllvslfgstayptkskLKALSVGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDG 748
Cdd:cd14892   518 NNDNLHDDL--------------------------RDLLRSSSKFRTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSC 571

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  749 SAILSQLQCAGMTSVLKLMQDGFPSRTGFGDLYACYQ---------KKLPPKLSKLDPRMFC--KCLFRalgLDQHDFQF 817
Cdd:cd14892   572 ELVRDQLIYSGVLEVVRIRREGFPIRRQFEEFYEKFWplarnkagvAASPDACDATTARKKCeeIVARA---LERENFQL 648


                  ....*...
gi 808358096  818 GLTKVFFR 825
Cdd:cd14892   649 GRTKVFLR 656
MYSc_Myo30 cd14891
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ...
 143-825 2.05e-159

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: 491.87  E-value: 2.05e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  143 ATLLNNIRLRY--QNGKIYSYVANILISINPYQTIdgfySLQKIKEYRGKSLGQKEPHIFAIADKSYREMIRHRKS---Q 217
Cdd:cd14891     1 AGILHNLEERSklDNQRPYTFMANVLIAVNPLRRL----PEPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGRmqnQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  218 SIIVSGESGAGKTESQKAVLRYL--------------CENWGSG----AGEIQKRLLETNPILEAFGNAKTLRNNNSSRF 279
Cdd:cd14891    77 SIVISGESGAGKTETSKIILRFLttravggkkasgqdIEQSSKKrklsVTSLDERLMDTNPILESFGNAKTLRNHNSSRF 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  280 GKFVQIHFADTGN-VAGGYVSHYLLETSRICRQAAGERNYHIFYQLIAGSSPELFKFLALGQPNQFNYLKRgfigffthp 358
Cdd:cd14891   157 GKFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNQ--------- 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  359 sSGTTSkipknrlsdpkftqDSMVDDFSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEESlDDSRGGCKVFN 438
Cdd:cd14891   228 -SGCVS--------------DDNIDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEE-DTSEGEAEIAS 291

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  439 GSEQD-LIQAARLLGLETMELKMGLCARIMQTtkggaRGTLIRVPLKPHEACSGRDALSKAIYSKLFDWLVSRINDSIPF 517
Cdd:cd14891   292 ESDKEaLATAAELLGVDEEALEKVITQREIVT-----RGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGH 366

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  518 -EKSTNFVGVLDVAGFE-FYAKNSFEQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEFIDNQDCIELFELKGN 595
Cdd:cd14891   367 dPDPLPYIGVLDIFGFEsFETKNDFEQLLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWPDNRECLDLIASKPN 446

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  596 GLFDLLDEEAKFPTSNYKSFTKRAHEENRKHFRLDTPrkskvkSHRELRddEGLLIRHYAGSVCYETKHFVEKNDDLLHN 675
Cdd:cd14891   447 GILPLLDNEARNPNPSDAKLNETLHKTHKRHPCFPRP------HPKDMR--EMFIVKHYAGTVSYTIGSFIDKNNDIIPE 518

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  676 SLQILIEQStirllvslfgstayptksklkalsvgAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGSAILSQL 755
Cdd:cd14891   519 DFEDLLASS--------------------------AKFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQL 572

                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 808358096  756 QCAGMTSVLKLMQDGFPSRTGFGDLYACYQKKLPPK---LSKLDPRMFCKCLFRALGLDQHDFQFGLTKVFFR 825
Cdd:cd14891   573 RCSGILQTCEVLKVGLPTRVTYAELVDVYKPVLPPSvtrLFAENDRTLTQAILWAFRVPSDAYRLGRTRVFFR 645
MYSc_Myo40 cd14901
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ...
 143-823 3.56e-156

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: 483.91  E-value: 3.56e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  143 ATLLNNIRLRYQNGKIYSYVANILISINPYQTIdGFYSLQKIKEY------RGKSLGQKEPHIFAIADKSYREMIRHRK- 215
Cdd:cd14901     1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRL-PLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRg 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  216 ---SQSIIVSGESGAGKTESQKAVLRYLC-----ENWGSGAGE---IQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQ 284
Cdd:cd14901    80 qkcDQSILVSGESGAGKTETTKIIMNYLAsvssaTTHGQNATErenVRDRVLESNPILEAFGNARTNRNNNSSRFGKFIR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  285 IHFADTGNVAGGYVSHYLLETSRICRQAAGERNYHIFYQLIAGSSPELFKFLALGQPNQFNYLKrgfigffthpSSGTts 364
Cdd:cd14901   160 LGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLN----------SSQC-- 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  365 kipknrlsdpkFTQDSMVDDFSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEeSLDDSRGGCKVFNGSeqDL 444
Cdd:cd14901   228 -----------YDRRDGVDDSVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFV-KKDGEGGTFSMSSLA--NV 293

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  445 IQAARLLGLETMELKMGLCARIMQttkggARGTLIRVPLKPHEACSGRDALSKAIYSKLFDWLVSRINDSIPFEKSTN-- 522
Cdd:cd14901   294 RAACDLLGLDMDVLEKTLCTREIR-----AGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGas 368

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  523 -FVGVLDVAGFEFYAKNSFEQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEFIDNQDCIELFELKGNGLFDLL 601
Cdd:cd14901   369 rFIGIVDIFGFEIFATNSLEQLCINFANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYPNNDACVAMFEARPTGLFSLL 448

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  602 DEEAKFPTSNYKSFTKRAHEENRKHFRLDTPRKSKVKSHrelrddegLLIRHYAGSVCYETKHFVEKNDDLLHNSLQILI 681
Cdd:cd14901   449 DEQCLLPRGNDEKLANKYYDLLAKHASFSVSKLQQGKRQ--------FVIHHYAGAVCYATDGFCDKNKDHVHSEALALL 520

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  682 EQSTIRLLVSlfgstayptksklkalSVGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGSAILSQLQCAGMT 761
Cdd:cd14901   521 RTSSNAFLSS----------------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVL 584

                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 808358096  762 SVLKLMQDGFPSR---TGFGDLYACYQKKLPP---KLSKLDPRMFCKCLFRALGLDQHD-FQFGLTKVF 823
Cdd:cd14901   585 EAVKISRSGYPVRfphDAFVHTYSCLAPDGASdtwKVNELAERLMSQLQHSELNIEHLPpFQVGKTKVF 653
MYSc_Myo3 cd01379
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ...
 152-825 1.05e-155

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: 481.78  E-value: 1.05e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  152 RYQNGKIYSYVANILISINPYQTIdGFYSLQKIKEYRGKSLGQKEPHIFAIADKSYREMIRHRKSQSIIVSGESGAGKTE 231
Cdd:cd01379    10 RYSRDQIYTYIGDILIAVNPFQNL-GIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGESGAGKTE 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  232 SQKAVLRYLCENWGSGAGEIQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFADTGNVAGGYVSHYLLETSRICRQ 311
Cdd:cd01379    89 SANLLVQQLTVLGKANNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEYLLEKSRVVHQ 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  312 AAGERNYHIFYQLIAGsspelfkfLALGQPNQFNYLKrgfigffthpssgtTSKIPKNRLSDPKFTQDSMVDDF--SDFQ 389
Cdd:cd01379   169 AIGERNFHIFYYIYAG--------LAEDKKLAKYKLP--------------ENKPPRYLQNDGLTVQDIVNNSGnrEKFE 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  390 RLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEE--SLDDSRGGCKVFNgsEQDLIQAARLLGLETMELKMGLCARIM 467
Cdd:cd01379   227 EIEQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTEveSNHQTDKSSRISN--PEALNNVAKLLGIEADELQEALTSHSV 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  468 QTtkggaRGTLIRVPLKPHEACSGRDALSKAIYSKLFDWLVSRINDSIPFEKSTNF----VGVLDVAGFEFYAKNSFEQF 543
Cdd:cd01379   305 VT-----RGETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLKPDRSASDeplsIGILDIFGFENFQKNSFEQL 379

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  544 CINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEFIDNQDCIELFELKGNGLFDLLDEEAKFPTSNYKSFTKRAHEEN 623
Cdd:cd01379   380 CINIANEQIQYYFNQHIFAWEQQEYLNEGIDVDLIEYEDNRPLLDMFLQKPMGLLALLDEESRFPKATDQTLVEKFHNNI 459

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  624 RKHFRLdtprkskvkshRELRDDEGLLIRHYAGSVCYETKHFVEKNDDLLHNSLQILIEQSTIRLLvslfgstayptksk 703
Cdd:cd01379   460 KSKYYW-----------RPKSNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLV-------------- 514

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  704 lkALSVGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGSAILSQLQCAGMTSVLKLMQDGFPSRTGFGDL--- 780
Cdd:cd01379   515 --RQTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFlkr 592

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*..
gi 808358096  781 --YACYQKKLPPKLSkldpRMFCKCLFRALGLDqhDFQFGLTKVFFR 825
Cdd:cd01379   593 yyFLAFKWNEEVVAN----RENCRLILERLKLD--NWALGKTKVFLK 633
MYSc_Myo9 cd01385
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ...
 143-825 1.14e-152

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: 475.71  E-value: 1.14e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  143 ATLLNNIRLRYQNGKIYSYVANILISINPYQTIDgFYSLQKIKEYRGKSLGQKEPHIFAIADKSYREMIRHRKSQSIIVS 222
Cdd:cd01385     1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLP-IYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVIS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  223 GESGAGKTESQKAVLRYLC----ENWGSGageIQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFADTGNVAGGYV 298
Cdd:cd01385    80 GESGSGKTESTNFLLHHLTalsqKGYGSG---VEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  299 SHYLLETSRICRQAAGERNYHIFYQLIAGSSPELFKFLALGQPNQFNYLKRgfigffthpssgttskipknrlSDPkFTQ 378
Cdd:cd01385   157 EKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNQ----------------------SDC-YTL 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  379 DSmVDDFSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEESLDDSRGGCKVfnGSEQDLIQAARLLGLETmel 458
Cdd:cd01385   214 EG-EDEKYEFERLKQAMEMVGFLPETQRQIFSVLSAVLHLGNIEYKKKAYHRDESVTV--GNPEVLDIISELLRVKE--- 287

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  459 KMGLCARIMQTTKGGARGTLIRVPLKphEACSGRDALSKAIYSKLFDWLVSRINDSI-----PFEKSTNFVGVLDVAGFE 533
Cdd:cd01385   288 ETLLEALTTKKTVTVGETLILPYKLP--EAIATRDAMAKCLYSALFDWIVLRINHALlnkkdLEEAKGLSIGVLDIFGFE 365

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  534 FYAKNSFEQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEFIDNQDCIELFELKGNGLFDLLDEEAKFPtsNYK 613
Cdd:cd01385   366 DFGNNSFEQFCINYANEHLQYYFNQHIFKLEQEEYKKEGISWHNIEYTDNTGCLQLISKKPTGLLCLLDEESNFP--GAT 443

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  614 SFT-----KRAHEENrKHFrlDTPRKskvkshRELrddeGLLIRHYAGSVCYETKHFVEKNDDLLHNSLQILIEQSTIRL 688
Cdd:cd01385   444 NQTllakfKQQHKDN-KYY--EKPQV------MEP----AFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAF 510

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  689 LVSLFG---------------------------------------------STAYPTKSKLKALSVGAKFKNQLSTLLIK 723
Cdd:cd01385   511 VRELIGidpvavfrwavlrafframaafreagrrraqrtaghsltlhdrttKSLLHLHKKKKPPSVSAQFQTSLSKLMET 590

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  724 LESTGTHFVRCIKPNNQMIPFEFDGSAILSQLQCAGMTSVLKLMQDGFPSRTGFGDLYACYQKKLPPKL--SKLDPRMFc 801
Cdd:cd01385   591 LGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVLLPKGLisSKEDIKDF- 669

                         730       740
                  ....*....|....*....|....
gi 808358096  802 kclFRALGLDQHDFQFGLTKVFFR 825
Cdd:cd01385   670 ---LEKLNLDRDNYQIGKTKVFLK 690
MYSc_Myo42 cd14903
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ...
 143-825 8.23e-152

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: 472.34  E-value: 8.23e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  143 ATLLNNIRLRYQNGKIYSYVANILISINPYQTIDGFYSLQKIKEYRGKSLGQKEPHIFAIADKSYREMIRHRKSQSIIVS 222
Cdd:cd14903     1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPELYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  223 GESGAGKTESQKAVLRYLCENWGSGAGEIQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFADTGNVAGGYVSHYL 302
Cdd:cd14903    81 GESGAGKTETTKILMNHLATIAGGLNDSTIKKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLVGAKCRTYL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  303 LETSRICRQAAGERNYHIFYQLIAGSSPElfKFLALGQPNQFNYlkrgfigffthPSSGTTSKIPKnrlsdpkftqdsmV 382
Cdd:cd14903   161 LEKTRVISHERPERNYHIFYQLLASPDVE--ERLFLDSANECAY-----------TGANKTIKIEG-------------M 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  383 DDFSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFE-ESLDDSRGGCkvfNGSEQDLIQAARLLGLETMELKMG 461
Cdd:cd14903   215 SDRKHFARTKEALSLIGVSEEKQEVLFEVLAGILHLGQLQIQsKPNDDEKSAI---APGDQGAVYATKLLGLSPEALEKA 291

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  462 LCARIMQttkggARGTLIRVPLKPHEACSGRDALSKAIYSKLFDWLVSRINDSIPF-EKSTNFVGVLDVAGFEFYAKNSF 540
Cdd:cd14903   292 LCSRTMR-----AAGDVYTVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNdAKMANHIGVLDIFGFEHFKHNSF 366

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  541 EQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEFIDNQDCIELFELKgNGLFDLLDEEAKFPTSNYKSFTKRAH 620
Cdd:cd14903   367 EQFCINYANEKLQQKFTQDVFKTVQIEYEEEGIRWAHIDFADNQDVLAVIEDR-LGIISLLNDEVMRPKGNEESFVSKLS 445

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  621 EENRKHFRL-DTPRKSKVKshrelrddegLLIRHYAGSVCYETKHFVEKNDDLLHNSLQILIEQSTIRLLVSLFGSTAYP 699
Cdd:cd14903   446 SIHKDEQDViEFPRTSRTQ----------FTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVES 515

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  700 ---TKSKLKALS------------VGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGSAILSQLQCAGMTSVL 764
Cdd:cd14903   516 paaASTSLARGArrrrggalttttVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAI 595

                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 808358096  765 KLMQDGFPSR---TGFGDLYACYQKKLPPKLSKldPRMFCKCLFRALGLDQ-HDFQFGLTKVFFR 825
Cdd:cd14903   596 RISRAAYPNRllhEEFLDKFWLFLPEGRNTDVP--VAERCEALMKKLKLESpEQYQMGLTRIYFQ 658
MYSc_Myo46 cd14907
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ...
 143-784 1.25e-149

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: 467.20  E-value: 1.25e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  143 ATLLNNIRLRYQNGKIYSYVANILISINPYQTIDGFYSLQKIKEY------RGKSLGQKE--PHIFAIADKSYREMIRHR 214
Cdd:cd14907     1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDNLFSEEVMQMYkeqiiqNGEYFDIKKepPHIYAIAALAFKQLFENN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  215 KSQSIIVSGESGAGKTESQKAVLRYL-------------------CENWGSGAGEIQKRLLETNPILEAFGNAKTLRNNN 275
Cdd:cd14907    81 KKQAIVISGESGAGKTENAKYAMKFLtqlsqqeqnseevltltssIRATSKSTKSIEQKILSCNPILEAFGNAKTVRNDN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  276 SSRFGKFVQIHFA-DTGNVAGGYVSHYLLETSRICRQAAGERNYHIFYQLIAGSSPELFKFLAL-GQPNQFN--YLKRGF 351
Cdd:cd14907   161 SSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLkNQLSGDRydYLKKSN 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  352 IgffthpssgttskipknrlsdpkFTQDSMvDDFSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEESLDDSR 431
Cdd:cd14907   241 C-----------------------YEVDTI-NDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTLDDN 296

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  432 GGCKVFNgsEQDLIQAARLLGLETMELKMGLCARIMQTTKGGargtlIRVPLKPHEACSGRDALSKAIYSKLFDWLVSRI 511
Cdd:cd14907   297 SPCCVKN--KETLQIIAKLLGIDEEELKEALTTKIRKVGNQV-----ITSPLSKKECINNRDSLSKELYDRLFNWLVERL 369

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  512 NDSI---------PFEKSTNFVGVLDVAGFEFYAKNSFEQFCINFCNEKLQNFFNQRILREEQELYEKEGLN--VRKIEF 580
Cdd:cd14907   370 NDTImpkdekdqqLFQNKYLSIGLLDIFGFEVFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdyLNQLSY 449

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  581 IDNQDCIELFELKGNGLFDLLDEEAKFPTSNYKSFTKRAHEENRKhfrldtprKSKVKSHRELRDDEgLLIRHYAGSVCY 660
Cdd:cd14907   450 TDNQDVIDLLDKPPIGIFNLLDDSCKLATGTDEKLLNKIKKQHKN--------NSKLIFPNKINKDT-FTIRHTAKEVEY 520

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  661 ETKHFVEKNDDLLHNSLQILIEQSTIRLLVSLF--------GSTAYPTKSKLKALSVGAKFKNQLSTLLIKLESTGTHFV 732
Cdd:cd14907   521 NIEGFREKNKDEISQSIINCIQNSKNRIISSIFsgedgsqqQNQSKQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFI 600

                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|..
gi 808358096  733 RCIKPNNQMIPFEFDGSAILSQLQCAGMTSVLKLMQDGFPSRTGFGDLYACY 784
Cdd:cd14907   601 RCIKPNEEKKADLFIQGYVLNQIRYLGVLESIRVRKQGYPYRKSYEDFYKQY 652
MYSc_Myh10 cd14920
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ...
 143-825 1.15e-144

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: 454.08  E-value: 1.15e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  143 ATLLNNIRLRYQNGKIYSYVANILISINPYQTIDgFYSLQKIKEYRGKSLGQKEPHIFAIADKSYREMIRHRKSQSIIVS 222
Cdd:cd14920     1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  223 GESGAGKTESQKAVLRYLCE--------NWGSGAGEIQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFADTGNVA 294
Cdd:cd14920    80 GESGAGKTENTKKVIQYLAHvasshkgrKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  295 GGYVSHYLLETSRICRQAAGERNYHIFYQLIAGSSPELFKFLALGQPNQFNYLKRGFIgffthPSSGTTskipknrlsdp 374
Cdd:cd14920   160 GANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYI-----PIPGQQ----------- 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  375 kftqdsmvdDFSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEESLDDSRGGCKVfNGSEQDLiqaARLLGLE 454
Cdd:cd14920   224 ---------DKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPE-NTVAQKL---CHLLGMN 290

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  455 TMELKMGLcarIMQTTKGGaRGTLIRVPLKpHEACSGRDALSKAIYSKLFDWLVSRINDSIPFEK--STNFVGVLDVAGF 532
Cdd:cd14920   291 VMEFTRAI---LTPRIKVG-RDYVQKAQTK-EQADFAVEALAKATYERLFRWLVHRINKALDRTKrqGASFIGILDIAGF 365

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  533 EFYAKNSFEQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEF-IDNQDCIELFELKGN--GLFDLLDEEAKFPT 609
Cdd:cd14920   366 EIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPK 445

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  610 SNYKSFTKRAHEENRKHfrldtprkSKVKSHRELRDDEGLLIRHYAGSVCYETKHFVEKNDDLLHNSLQILIEQSTIRLL 689
Cdd:cd14920   446 ATDKTFVEKLVQEQGSH--------SKFQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFV 517

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  690 VSL-------------------FGSTAYPTKSKLkALSVGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGSA 750
Cdd:cd14920   518 AELwkdvdrivgldqvtgmtetAFGSAYKTKKGM-FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHL 596

                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 808358096  751 ILSQLQCAGMTSVLKLMQDGFPSRTGFGDLYACYQKKLPPKLSK--LDPRMFCKCLFRALGLDQHDFQFGLTKVFFR 825
Cdd:cd14920   597 VLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKgfMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
MYSc_Myo43 cd14904
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ...
 143-825 1.67e-144

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: 452.86  E-value: 1.67e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  143 ATLLNNIRLRYQNGKIYSYVANILISINPYQTIDGFYSLQKIKEYRGKSLGQKEPHIFAIADKSYREMIRHRKSQSIIVS 222
Cdd:cd14904     1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDNLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  223 GESGAGKTESQKAVLRYLCENWGSGAGEIQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFADTGNVAGGYVSHYL 302
Cdd:cd14904    81 GESGAGKTETTKIVMNHLASVAGGRKDKTIAKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAKCETYL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  303 LETSRICRQAAGERNYHIFYQLIAGSSPELFKFLALGQPNQFNYLKrgfigffthpssGTTSKipknrlsdpkfTQDSMV 382
Cdd:cd14904   161 LEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLG------------DSLAQ-----------MQIPGL 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  383 DDFSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEESLDDsrgGCKVFNGSEqdLIQAARLLGLETMELKMGL 462
Cdd:cd14904   218 DDAKLFASTQKSLSLIGLDNDAQRTLFKILSGVLHLGEVMFDKSDEN---GSRISNGSQ--LSQVAKMLGLPTTRIEEAL 292

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  463 CARIMQTtkggaRGTLIRVPLKPHEACSGRDALSKAIYSKLFDWLVSRINDSIPFEKSTNF--VGVLDVAGFEFYAKNSF 540
Cdd:cd14904   293 CNRSVVT-----RNESVTVPLAPVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKgqIGVLDIFGFEDFAHNGF 367

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  541 EQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEFIDNQDCIELFELKgNGLFDLLDEEAKFPTSNYKSFTKR-- 618
Cdd:cd14904   368 EQFCINYANEKLQQKFTTDVFKTVEEEYIREGLQWDHIEYQDNQGIVEVIDGK-MGIIALMNDHLRQPRGTEEALVNKir 446

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  619 -AHEENRKHFRLDTPRKSKVKshrelrddegLLIRHYAGSVCYETKHFVEKNDDLLHNSLQILIEQSTIRLLVSLFGSTA 697
Cdd:cd14904   447 tNHQTKKDNESIDFPKVKRTQ----------FIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSE 516

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  698 YPT--------KSKLKALSVGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGSAILSQLQCAGMTSVLKLMQD 769
Cdd:cd14904   517 APSetkegksgKGTKAPKSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRS 596

                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 808358096  770 GFPSRTGFGDLYACYQKKLPPKLSKLDPRMFCKCLFRALGLDQH-DFQFGLTKVFFR 825
Cdd:cd14904   597 GYPSRLTPKELATRYAIMFPPSMHSKDVRRTCSVFMTAIGRKSPlEYQIGKSLIYFK 653
PTZ00014 PTZ00014
myosin-A; Provisional
 137-894 3.49e-138

myosin-A; Provisional


Pssm-ID: 240229 [Multi-domain]  Cd Length: 821  Bit Score: 441.78  E-value: 3.49e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  137 LMHLNEATLLNNIRLRYQNGKIYSYVANILISINPYQTIdGFYSLQKIKEYR-GKSLGQKEPHIFAIADKSYREMIRHRK 215
Cdd:PTZ00014  104 LPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDL-GNTTNDWIRRYRdAKDSDKLPPHVFTTARRALENLHGVKK 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  216 SQSIIVSGESGAGKTESQKAVLRYLcenwGSGAGE-----IQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFADT 290
Cdd:PTZ00014  183 SQTIIVSGESGAGKTEATKQIMRYF----ASSKSGnmdlkIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEE 258

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  291 GNVAGGYVSHYLLETSRICRQAAGERNYHIFYQLIAGSSPELFKFLALGQPNQFNYLkrgfigffthpssgttskipknr 370
Cdd:PTZ00014  259 GGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYI----------------------- 315

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  371 lsDPKFTQDSMVDDFSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEESLDDSRGGCKVF-NGSEQDLIQAAR 449
Cdd:PTZ00014  316 --NPKCLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEGGLTDAAAIsDESLEVFNEACE 393

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  450 LLGLETMELKMGLcarIMQTTKGGarGTLIRVPLKPHEACSGRDALSKAIYSKLFDWLVSRINDSI-PFEKSTNFVGVLD 528
Cdd:PTZ00014  394 LLFLDYESLKKEL---TVKVTYAG--NQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIePPGGFKVFIGMLD 468

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  529 VAGFEFYAKNSFEQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEFIDNQDCIELFELKGNGLFDLLDEEAKFP 608
Cdd:PTZ00014  469 IFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGKSVLSILEDQCLAP 548

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  609 TSNYKSFTKRAHEENRKHFRLDTPRKSKVKShrelrddegLLIRHYAGSVCYETKHFVEKNDDLLHNSLQILIEQSTIRL 688
Cdd:PTZ00014  549 GGTDEKFVSSCNTNLKNNPKYKPAKVDSNKN---------FVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPL 619

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  689 LVSLFgSTAYPTKSKL-KALSVGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGSAILSQLQCAGMTSVLKLM 767
Cdd:PTZ00014  620 VRDLF-EGVEVEKGKLaKGQLIGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLR 698

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  768 QDGFPSRTGFGDLyaCYQKK---LP-PKLSKLDPRMFCKCLFRALGLDQHDFQFGLTKVFfragkfaefdqmMKQDP-ET 842
Cdd:PTZ00014  699 QLGFSYRRTFAEF--LSQFKyldLAvSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVF------------LKKDAaKE 764

                         730       740       750       760       770
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 808358096  843 MTSLI-QKVNEW--LVGArwkqsQYAVWSVIKLKNKIAWRSAQVTRLQSIARGYL 894
Cdd:PTZ00014  765 LTQIQrEKLAAWepLVSV-----LEALILKIKKKRKVRKNIKSLVRIQAHLRRHL 814
MYSc_Myo45 cd14906
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ...
 143-785 4.22e-137

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: 435.56  E-value: 4.22e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  143 ATLLNNIRLRYQNGKIYSYVANILISINPYQTIDGFYSLQKIKEYRG-KSLGQKEPHIFAIADKSYREMIRHRKSQSIIV 221
Cdd:cd14906     1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISSIYSNLILNEYKDiNQNKSPIPHIYAVALRAYQSMVSEKKNQSIII 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  222 SGESGAGKTESQKAVLRYLCENWGSGAGE----------IQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFADT- 290
Cdd:cd14906    81 SGESGSGKTEASKTILQYLINTSSSNQQQnnnnnnnnnsIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSd 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  291 GNVAGGYVSHYLLETSRIC-RQAAGERNYHIFYQLIAGSSPELFKFLAL-GQPNQFNYLKrgfigffthpSSGTTSKIPK 368
Cdd:cd14906   161 GKIDGASIETYLLEKSRIShRPDNINLSYHIFYYLVYGASKDERSKWGLnNDPSKYRYLD----------ARDDVISSFK 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  369 NRLSDPKFTQDSMVDDFSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEESLDDSRGgCKVFNGSEQDLIQAA 448
Cdd:cd14906   231 SQSSNKNSNHNNKTESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKY-AYQKDKVTASLESVS 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  449 RLLGLETMELKMGLCARIMqttKGGARGTLIRVPLKPHEACSGRDALSKAIYSKLFDWLVSRIN------------DSIP 516
Cdd:cd14906   310 KLLGYIESVFKQALLNRNL---KAGGRGSVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINrkfnqntqsndlAGGS 386

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  517 FEKSTNFVGVLDVAGFEFYAKNSFEQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEFIDNQDCIELFELKGNG 596
Cdd:cd14906   387 NKKNNLFIGVLDIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNFIDNKECIELIEKKSDG 466

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  597 LFDLLDEEAKFP----TSNYKSFTKRAHEENRKHFRldTPRKSKvkshrelrddegLLIRHYAGSVCYETKHFVEKNDDL 672
Cdd:cd14906   467 ILSLLDDECIMPkgseQSLLEKYNKQYHNTNQYYQR--TLAKGT------------LGIKHFAGDVTYQTDGWLEKNRDS 532

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  673 LHNSLQILIEQSTIRLLVSLFG----STAYPTKSKLKALSVGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDG 748
Cdd:cd14906   533 LYSDVEDLLLASSNFLKKSLFQqqitSTTNTTKKQTQSNTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNN 612

                         650       660       670
                  ....*....|....*....|....*....|....*..
gi 808358096  749 SAILSQLQCAGMTSVLKLMQDGFPSRTGFGDLYACYQ 785
Cdd:cd14906   613 VHVLSQLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYK 649
MYSc_Myh3 cd14913
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ...
 145-825 7.63e-136

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: 430.63  E-value: 7.63e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  145 LLNNIRLRYQNGKIYSYVANILISINPYQTIDgFYSLQKIKEYRGKSLGQKEPHIFAIADKSYREMIRHRKSQSIIVSGE 224
Cdd:cd14913     3 VLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLP-VYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  225 SGAGKTESQKAVLRYLCENWGSG----------AGEIQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFADTGNVA 294
Cdd:cd14913    82 SGAGKTVNTKRVIQYFATIAATGdlakkkdskmKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  295 GGYVSHYLLETSRICRQAAGERNYHIFYQLIAGSSPELFKFLALG-QPNQFNYLKRGFIGFfthpssgttskipknrlsd 373
Cdd:cd14913   162 SADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITtNPYDYPFISQGEILV------------------- 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  374 pkftqdSMVDDFSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEESLDDSRGGCkvfNGSEQdLIQAARLLGL 453
Cdd:cd14913   223 ------ASIDDAEELLATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEP---DGTEV-ADKTAYLMGL 292

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  454 ETMELKMGLC-ARIMQTTKGGARGTLIRvplKPHEACsgrDALSKAIYSKLFDWLVSRINDSIPFE-KSTNFVGVLDVAG 531
Cdd:cd14913   293 NSSDLLKALCfPRVKVGNEYVTKGQTVD---QVHHAV---NALSKSVYEKLFLWMVTRINQQLDTKlPRQHFIGVLDIAG 366

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  532 FEFYAKNSFEQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEF-IDNQDCIELFElKGNGLFDLLDEEAKFPTS 610
Cdd:cd14913   367 FEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKA 445

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  611 NYKSFTKRAHEEN---RKHFRLDTPRKSKVKSHRELrddeglliRHYAGSVCYETKHFVEKNDDLLHNSLQILIEQSTIR 687
Cdd:cd14913   446 TDTSFKNKLYDQHlgkSNNFQKPKVVKGRAEAHFSL--------IHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNR 517

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  688 LLVSLF----GSTAYPTKSKLKA------LSVGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGSAILSQLQC 757
Cdd:cd14913   518 LLAHLYatfaTADADSGKKKVAKkkgssfQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRC 597

                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808358096  758 AGMTSVLKLMQDGFPSRTGFGDL---YACYQKKLPPKLSKLDPRMFCKCLFRALGLDQHDFQFGLTKVFFR 825
Cdd:cd14913   598 NGVLEGIRICRKGFPNRILYGDFkqrYRVLNASAIPEGQFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
MYSc_Myh15_mammals cd14929
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ...
 143-825 3.75e-135

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: 428.62  E-value: 3.75e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  143 ATLLNNIRLRYQNGKIYSYVANILISINPYQTIDgFYSLQKIKEYRGKSLGQKEPHIFAIADKSYREMIRHRKSQSIIVS 222
Cdd:cd14929     1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLP-VYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  223 GESGAGKTESQKAVLRYLCENWGSGA-----GEIQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFADTGNVAGGY 297
Cdd:cd14929    80 GESGAGKTVNTKHIIQYFATIAAMIEskkklGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSAD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  298 VSHYLLETSRICRQAAGERNYHIFYQLIAGSSPELFKFLALGQPNQFNYLKRGFIGFfthpssgttskipknrlsdpkft 377
Cdd:cd14929   160 IDIYLLEKSRVIFQQPGERNYHIFYQILSGKKELRDLLLVSANPSDFHFCSCGAVAV----------------------- 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  378 qdSMVDDFSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEESLDDSRGGCkvfNGSEqDLIQAARLLGLETME 457
Cdd:cd14929   217 --ESLDDAEELLATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEA---DGTE-NADKAAFLMGINSSE 290

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  458 LKMGLC-ARIMQTTKGGARGTLIRvplkphEACSGRDALSKAIYSKLFDWLVSRINDSIPFEKSTN-FVGVLDVAGFEFY 535
Cdd:cd14929   291 LVKGLIhPRIKVGNEYVTRSQNIE------QVTYAVGALSKSIYERMFKWLVARINRVLDAKLSRQfFIGILDITGFEIL 364

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  536 AKNSFEQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEF-IDNQDCIELFElKGNGLFDLLDEEAKFPTSNYKS 614
Cdd:cd14929   365 DYNSLEQLCINFTNEKLQQFFNQHMFVLEQEEYRKEGIDWVSIDFgLDLQACIDLIE-KPMGIFSILEEECMFPKATDLT 443

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  615 FTKR---AHEENRKHFRLDTPRKSKVKSHRELrddeglliRHYAGSVCYETKHFVEKNDDLLHNSLQILIEQSTIRLLVS 691
Cdd:cd14929   444 FKTKlfdNHFGKSVHFQKPKPDKKKFEAHFEL--------VHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLAS 515

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  692 LF-------GSTAYPTKSKLKALS---VGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGSAILSQLQCAGMT 761
Cdd:cd14929   516 LFenyistdSAIQFGEKKRKKGASfqtVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVL 595

                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 808358096  762 SVLKLMQDGFPSRTGFGDL---YACYQKKLPPKLSKLDPRMFCKCLFRALGLDQHDFQFGLTKVFFR 825
Cdd:cd14929   596 EGIRICREGFPNRLLYADFkqrYCILNPRTFPKSKFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
MYSc_Myo41 cd14902
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ...
 143-796 2.25e-134

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: 428.16  E-value: 2.25e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  143 ATLLNNIRLRYQNGKIYSYVANILISINPYQTIDGFYSLQKIKEYR--------GKSLGQKEPHIFAIADKSYREMIR-H 213
Cdd:cd14902     1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPDLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKpE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  214 RKSQSIIVSGESGAGKTESQKAVLRYLC---------ENWGSGAGEIQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQ 284
Cdd:cd14902    81 RRNQSILVSGESGSGKTESTKFLMQFLTsvgrdqsstEQEGSDAVEIGKRILQTNPILESFGNAQTIRNDNSSRFGKFIK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  285 IHFADTGNVAGGYVSHYLLETSRICRQAAGERNYHIFYQLIAGSSPELFKflALGQPNQFNYLkrgfigffTHPSSGTTS 364
Cdd:cd14902   161 IQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLD--LLGLQKGGKYE--------LLNSYGPSF 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  365 KiPKNRLSDpkftqdsmvDDFSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFeESLDDSRGGCKVFNGSEQDL 444
Cdd:cd14902   231 A-RKRAVAD---------KYAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNF-TAENGQEDATAVTAASRFHL 299

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  445 IQAARLLGLETMELKMGLCARIMQTTkggarGTLIRVPLKPHEACSGRDALSKAIYSKLFDWLVSRINDSIPFEKSTNF- 523
Cdd:cd14902   300 AKCAELMGVDVDKLETLLSSREIKAG-----VEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINYFDSAVSi 374

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  524 ---------VGVLDVAGFEFYAKNSFEQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEFIDNQDCIELFELKG 594
Cdd:cd14902   375 sdedeelatIGILDIFGFESLNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYPSNAACLALFDDKS 454

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  595 NGLFDLLDEEAKFPT-SNYKSFTK--RAHeenrkhfrldtprkskvkshreLRDDEgLLIRHYAGSVCYETKHFVEKNDD 671
Cdd:cd14902   455 NGLFSLLDQECLMPKgSNQALSTKfyRYH----------------------GGLGQ-FVVHHFAGRVCYNVEQFVEKNTD 511

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  672 LLHNSLQILIEQSTIRLLVSLF------------GSTAYPTKSKLKALSVGAKFKNQLSTLLIKLESTGTHFVRCIKPNN 739
Cdd:cd14902   512 ALPADASDILSSSSNEVVVAIGadenrdspgadnGAAGRRRYSMLRAPSVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNE 591

                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 808358096  740 QMIPFEFDGSAILSQLQCAGMTSVLKLMQDGFPSRTGFGDLYACYqKKLPPKLSKLD 796
Cdd:cd14902   592 VKKPGIFDRERMVEQMRSVGVLEAVRIARHGYSVRLAHASFIELF-SGFKCFLSTRD 647
MYSc_Myo47 cd14908
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ...
 143-825 2.77e-134

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: 427.02  E-value: 2.77e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  143 ATLLNNIRLRYQNGKIYSYVANILISINPYQTIDgFYSLQKIKEYRGKSL--------GQK-EPHIFAIADKSYREMIRH 213
Cdd:cd14908     1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLP-LYGKEILESYRQEGLlrsqgiesPQAlGPHVFAIADRSYRQMMSE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  214 -RKSQSIIVSGESGAGKTESQKAVLRYLC-----------ENWGSGAGEIQKRLLETNPILEAFGNAKTLRNNNSSRFGK 281
Cdd:cd14908    80 iRASQSILISGESGAGKTESTKIVMLYLTtlgngeegapnEGEELGKLSIMDRVLQSNPILEAFGNARTLRNDNSSRFGK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  282 FVQIHFADTGNVAGGYVSHYLLETSRICRQAAGERNYHIFYQLIAGSSPE------LFKFLALGQ--PNQFNYLKRGfig 353
Cdd:cd14908   160 FIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEehekyeFHDGITGGLqlPNEFHYTGQG--- 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  354 ffthpssgttskipknrlSDPKFTQdsmVDDFSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEESLDDsrGG 433
Cdd:cd14908   237 ------------------GAPDLRE---FTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEED--GA 293

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  434 CKVFNGSEQD-LIQAARLLGLETMELKMGLCARIMQTtkggaRGTLIRVPLKPHEACSGRDALSKAIYSKLFDWLVSRIN 512
Cdd:cd14908   294 AEIAEEGNEKcLARVAKLLGVDVDKLLRALTSKIIVV-----RGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVN 368

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  513 DSIPFEKSTNF---VGVLDVAGFEFYAKNSFEQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEFIDNQDCIEL 589
Cdd:cd14908   369 SSINWENDKDIrssVGVLDIFGFECFAHNSFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFPDNQDCLDT 448

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  590 FELKGNGLFDLLDEEAKFPTSNY-KSFTKRAHEENRKHFRLDTPRKSKVKSHRELRDDEGLLIRHYAGSVCYETKH-FVE 667
Cdd:cd14908   449 IQAKKKGILTMLDDECRLGIRGSdANYASRLYETYLPEKNQTHSENTRFEATSIQKTKLIFAVRHFAGQVQYTVETtFCE 528

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  668 KNDDLLHNSLQILIEQSTirllvslfgstayptksklkalsvgaKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFD 747
Cdd:cd14908   529 KNKDEIPLTADSLFESGQ--------------------------QFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVT 582

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  748 GSAILSQLQCAGMTSVLKLMQDGFPSRTGFGDLYACY--------QKKLPPKLSKLDP-----RMFCKCLFRA------- 807
Cdd:cd14908   583 RKRVTEQLRYGGVLEAVRVARSGYPVRLPHKDFFKRYrmllplipEVVLSWSMERLDPqklcvKKMCKDLVKGvlspamv 662

                         730       740
                  ....*....|....*....|
gi 808358096  808 --LGLDQHDFQFGLTKVFFR 825
Cdd:cd14908   663 smKNIPEDTMQLGKSKVFMR 682
MYSc_Myo14 cd14876
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ...
 143-823 7.73e-134

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: 424.40  E-value: 7.73e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  143 ATLLNNIRLRYQNGKIYSYVANILISINPYQTIdGFYSLQKIKEYRG-KSLGQKEPHIFAIADKSYREMIRHRKSQSIIV 221
Cdd:cd14876     1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDL-GNATDEWIRKYRDaPDLTKLPPHVFYTARRALENLHGVNKSQTIIV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  222 SGESGAGKTESQKAVLRYLCENwGSGA--GEIQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFADTGNVAGGYVS 299
Cdd:cd14876    80 SGESGAGKTEATKQIMRYFASA-KSGNmdLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIRYGSVV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  300 HYLLETSRICRQAAGERNYHIFYQLIAGSSPELFKFLALGQPNQFNYLkrgfigffthpssgttskipknrlsDPKFTQD 379
Cdd:cd14876   159 AFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFL-------------------------NPKCLDV 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  380 SMVDDFSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEES----LDDSrggCKVFNGSEQDLIQAARLLGLET 455
Cdd:cd14876   214 PGIDDVADFEEVLESLKSMGLTEEQIDTVFSIVSGVLLLGNVKITGKteqgVDDA---AAISNESLEVFKEACSLLFLDP 290

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  456 MELKMGLCARImqtTKGGarGTLIRVPLKPHEACSGRDALSKAIYSKLFDWLVSRINDSI-PFEKSTNFVGVLDVAGFEF 534
Cdd:cd14876   291 EALKRELTVKV---TKAG--GQEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIePPGGFKNFMGMLDIFGFEV 365

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  535 YAKNSFEQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEFIDNQDCIELFELKGNGLFDLLDEEAKFPTSNYKS 614
Cdd:cd14876   366 FKNNSLEQLFINITNEMLQKNFIDIVFERESKLYKDEGIPTAELEYTSNAEVIDVLCGKGKSVLSILEDQCLAPGGSDEK 445

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  615 FT---KRAHEENRKhfrldtPRKSKVKSHRElrddegLLIRHYAGSVCYETKHFVEKNDDLLHNSLQILIEQSTIRLLVS 691
Cdd:cd14876   446 FVsacVSKLKSNGK------FKPAKVDSNIN------FIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKA 513

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  692 LFGSTAYpTKSKL-KALSVGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGSAILSQLQCAGMTSVLKLMQDG 770
Cdd:cd14876   514 LFEGVVV-EKGKIaKGSLIGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLG 592

                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 808358096  771 FPSRTGFGDLyaCYQKK-LPPKLS---KLDPRMFCKCLFRALGLDQHDFQFGLTKVF 823
Cdd:cd14876   593 YSYRRPFEEF--LYQFKfLDLGIAndkSLDPKVAALKLLESSGLSEDEYAIGKTMVF 647
MYSc_Myh2_insects_mollusks cd14911
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ...
 143-825 6.44e-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: 6.44e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  143 ATLLNNIRLRYQNGKIYSYVANILISINPYQTIDgFYSLQKIKEYRGKSLGQKEPHIFAIADKSYREMIRHRKSQSIIVS 222
Cdd:cd14911     1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLP-IYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  223 GESGAGKTESQKAVLRYLC-----ENWGSGA------------GEIQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQI 285
Cdd:cd14911    80 GESGAGKTENTKKVIQFLAyvaasKPKGSGAvphpavnpavliGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  286 HFADTGNVAGGYVSHYLLETSRICRQAAGERNYHIFYQLIAGSSPELFKFLALGQPNQFNYLKRGfigffTHPSSGttsk 365
Cdd:cd14911   160 NFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNG-----SLPVPG---- 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  366 ipknrlsdpkftqdsmVDDFSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEE-------SLDDSRGGCKVfn 438
Cdd:cd14911   231 ----------------VDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQernndqaTLPDNTVAQKI-- 292

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  439 gseqdliqaARLLGLETMEL-KMGLCARImqttKGGaRGTLIRVPLKpHEACSGRDALSKAIYSKLFDWLVSRINDSIPF 517
Cdd:cd14911   293 ---------AHLLGLSVTDMtRAFLTPRI----KVG-RDFVTKAQTK-EQVEFAVEAIAKACYERMFKWLVNRINRSLDR 357

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  518 EK--STNFVGVLDVAGFEFYAKNSFEQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEF-IDNQDCIELFElKG 594
Cdd:cd14911   358 TKrqGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLID-KP 436

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  595 NGLFDLLDEEAKFPTSNYKSFTKR---AHEENRKHFRLDtprkskvkshreLRDDEGLLIRHYAGSVCYETKHFVEKNDD 671
Cdd:cd14911   437 GGIMALLDEECWFPKATDKTFVDKlvsAHSMHPKFMKTD------------FRGVADFAIVHYAGRVDYSAAKWLMKNMD 504

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  672 LLHNSLQILIEQSTIRLLVSLF-------------GSTAYPTKSKlKAL--SVGAKFKNQLSTLLIKLESTGTHFVRCIK 736
Cdd:cd14911   505 PLNENIVSLLQGSQDPFVVNIWkdaeivgmaqqalTDTQFGARTR-KGMfrTVSHLYKEQLAKLMDTLRNTNPNFVRCII 583

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  737 PNNQMIPFEFDGSAILSQLQCAGMTSVLKLMQDGFPSRTGFGDLYACYQKKLPPKLSK--LDPRMFCKCLFRALGLDQHD 814
Cdd:cd14911   584 PNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIPKgfMDGKKACEKMIQALELDSNL 663

                         730
                  ....*....|.
gi 808358096  815 FQFGLTKVFFR 825
Cdd:cd14911   664 YRVGQSKIFFR 674
MYSc_Myh16 cd14934
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ...
 143-825 1.61e-132

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: 421.36  E-value: 1.61e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  143 ATLLNNIRLRYQNGKIYSYVANILISINPYQTIDgFYSLQKIKEYRGKSLGQKEPHIFAIADKSYREMIRHRKSQSIIVS 222
Cdd:cd14934     1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLP-IYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLIT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  223 GESGAGKTESQKAVLRYLCeNWGS-------GAGEIQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFADTGNVAG 295
Cdd:cd14934    80 GESGAGKTENTKKVIQYFA-NIGGtgkqssdGKGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  296 GYVSHYLLETSRICRQAAGERNYHIFYQLIAGSSPELFK-FLALGQPNQFNYLKRGFIgffthpssgttskipknrlsdp 374
Cdd:cd14934   159 ADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIEsLLLVPNPKEYHWVSQGVT---------------------- 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  375 kfTQDSMvDDFSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEESLDDSRGGCKVFNGSEqdliQAARLLGLE 454
Cdd:cd14934   217 --VVDNM-DDGEELQITDVAFDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVAD----KVAHLMGLN 289

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  455 TMELKMGLC-ARIMQTTKGGARGtlirvplKPHEACSGR-DALSKAIYSKLFDWLVSRINDSIPFEKSTN-FVGVLDVAG 531
Cdd:cd14934   290 SGELQKGITrPRVKVGNEFVQKG-------QNMEQCNNSiGALGKAVYDKMFKWLVVRINKTLDTKMQRQfFIGVLDIAG 362

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  532 FEFYAKNSFEQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEF-IDNQDCIELFElKGNGLFDLLDEEAKFPTS 610
Cdd:cd14934   363 FEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKREGIEWVFIDFgLDLQACIDLLE-KPMGIFSILEEQCVFPKA 441

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  611 NYKSFtKRAHEENR--KHFRLDTPRKSKVK---SHRELrddeglliRHYAGSVCYETKHFVEKNDDLLHNSLQILIEQST 685
Cdd:cd14934   442 TDATF-KAALYDNHlgKSSNFLKPKGGKGKgpeAHFEL--------VHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSS 512

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  686 IRLLVSLFGSTAYPTKSKLKA-----LSVGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGSAILSQLQCAGM 760
Cdd:cd14934   513 LGLLALLFKEEEAPAGSKKQKrgssfMTVSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGV 592

                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 808358096  761 TSVLKLMQDGFPSRTGFGDLYACYQKKLPPKLSK--LDPRMFCKCLFRALGLDQHDFQFGLTKVFFR 825
Cdd:cd14934   593 LEGIRICRKGFPNRLQYPEFKQRYQVLNPNVIPQgfVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
MYSc_Myo28 cd14889
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ...
 145-825 2.05e-132

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: 421.24  E-value: 2.05e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  145 LLNNIRLRYQNGKIYSYVANILISINPYQTIDgFYSLQKIKEYRGKSLGQKEPHIFAIADKSYREMI----RHRKSQSII 220
Cdd:cd14889     3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLH-IYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  221 VSGESGAGKTESQKAVLRYLCEnWGSGAGEIQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFADtGNVAGGYVSH 300
Cdd:cd14889    82 ISGESGAGKTESTKLLLRQIME-LCRGNSQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRFRN-GHVKGAKINE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  301 YLLETSRICRQAAGERNYHIFYQLIAGSSPELFKFLALGQPNQFNYLKRGFigffthpssgttskipknrlsdpkfTQDS 380
Cdd:cd14889   160 YLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLLDPGKYRYLNNGA-------------------------GCKR 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  381 MVDDF-SDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEesLDDSrGGCKVFNGSEQDLIQAARLLGLETMELK 459
Cdd:cd14889   215 EVQYWkKKYDEVCNAMDMVGFTEQEEVDMFTILAGILSLGNITFE--MDDD-EALKVENDSNGWLKAAAGQFGVSEEDLL 291

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  460 MGLCARIMQTtkggaRGTLIRVPLKPHEACSGRDALSKAIYSKLFDWLVSRINDSI-PFEKST---NFVGVLDVAGFEFY 535
Cdd:cd14889   292 KTLTCTVTFT-----RGEQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLaPKDDSSvelREIGILDIFGFENF 366

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  536 AKNSFEQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEFIDNQDCIELFELKGNGLFDLLDEEAKFPTSNYKSF 615
Cdd:cd14889   367 AVNRFEQACINLANEQLQYFFNHHIFLMEQKEYKKEGIDWKEITYKDNKPILDLFLNKPIGILSLLDEQSHFPQATDESF 446

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  616 TKRAHeenrKHFRlDTPRKSKVKSHRELrddegLLIRHYAGSVCYETKHFVEKNDDLLHNSLQILIEQSTIRLLVSLFGS 695
Cdd:cd14889   447 VDKLN----IHFK-GNSYYGKSRSKSPK-----FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTA 516

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  696 ------TAYPTKSKLKA----------LSVGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGSAILSQLQCAG 759
Cdd:cd14889   517 trsrtgTLMPRAKLPQAgsdnfnstrkQSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNG 596

                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 808358096  760 MTSVLKLMQDGFPSRTGFGDLYACYQKKL-PPKLSKldPRMFCKCLFRALGLDqhDFQFGLTKVFFR 825
Cdd:cd14889   597 LLETIRIRREGFSWRPSFAEFAERYKILLcEPALPG--TKQSCLRILKATKLV--GWKCGKTRLFFK 659
MYSc_Myh7b cd14927
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ...
 143-825 8.16e-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: 420.13  E-value: 8.16e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  143 ATLLNNIRLRYQNGKIYSYVANILISINPYQTIDgFYSLQKIKEYRGKSLGQKEPHIFAIADKSYREMIRHRKSQSIIVS 222
Cdd:cd14927     1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLIT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  223 GESGAGKTESQKAVLRY------LCENWGSGA--------GEIQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFA 288
Cdd:cd14927    80 GESGAGKTVNTKRVIQYfaivaaLGDGPGKKAqflatktgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  289 DTGNVAGGYVSHYLLETSRICRQAAGERNYHIFYQLIAGSSPELFKFLaLGQPNQFNYlkrgfigFFThpSSGTTskipk 368
Cdd:cd14927   160 PTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDML-LVSMNPYDY-------HFC--SQGVT----- 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  369 nrlsdpkfTQDSMvDDFSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEESLDDSRGGCkvfNGSEQdLIQAA 448
Cdd:cd14927   225 --------TVDNM-DDGEELMATDHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEA---DGTES-ADKAA 291

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  449 RLLGLETMELKMGLC-ARIMQTTKGGARGTLIRvplkphEACSGRDALSKAIYSKLFDWLVSRINDSIPFEKSTN-FVGV 526
Cdd:cd14927   292 YLMGVSSADLLKGLLhPRVKVGNEYVTKGQSVE------QVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQfFIGV 365

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  527 LDVAGFEFYAKNSFEQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEF-IDNQDCIELFElKGNGLFDLLDEEA 605
Cdd:cd14927   366 LDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWVFIDFgLDLQACIDLIE-KPLGILSILEEEC 444

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  606 KFPTSNYKSFTKRAHEE------NRKHFRLDtpRKSKVKSHRELrddeglliRHYAGSVCYETKHFVEKNDDLLHNSLQI 679
Cdd:cd14927   445 MFPKASDASFKAKLYDNhlgkspNFQKPRPD--KKRKYEAHFEV--------VHYAGVVPYNIVGWLDKNKDPLNETVVA 514

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  680 LIEQSTIRLLVSLF-----GSTAYPTKS-----KLKALS---VGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEF 746
Cdd:cd14927   515 IFQKSQNKLLATLYenyvgSDSTEDPKSgvkekRKKAASfqtVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVM 594

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  747 DGSAILSQLQCAGMTSVLKLMQDGFPSRTGFGDLYACYQKKLP---PKLSKLDPRMFCKCLFRALGLDQHDFQFGLTKVF 823
Cdd:cd14927   595 DPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPsaiPDDKFVDSRKATEKLLGSLDIDHTQYQFGHTKVF 674


                  ..
gi 808358096  824 FR 825
Cdd:cd14927   675 FK 676
MYSc_Myo35 cd14896
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ...
 143-825 3.83e-127

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: 406.47  E-value: 3.83e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  143 ATLLNNIRLRYQNGKIYSYVANILISINPYQTIDgFYSLQKIKEYRGKSLGQKEPHIFAIADKSYREMIRHRKSQSIIVS 222
Cdd:cd14896     1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLP-LFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  223 GESGAGKTESQKAVLRYLCENWGSGAGEIQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFADtGNVAGGYVSHYL 302
Cdd:cd14896    80 GHSGSGKTEAAKKIVQFLSSLYQDQTEDRLRQPEDVLPILESFGHAKTILNANASRFGQVLRLHLQH-GVIVGASVSHYL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  303 LETSRICRQAAGERNYHIFYQLIAGSSPELFKFLALGQPNQFNYLKRGfigffthpssGTTSKIPKnrlsdpkftqdsmv 382
Cdd:cd14896   159 LETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQG----------GACRLQGK-------------- 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  383 DDFSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEESLDDSRGGCKVFngSEQDLIQAARLLGLETMELKMGL 462
Cdd:cd14896   215 EDAQDFEGLLKALQGLGLCAEELTAIWAVLAAILQLGNICFSSSERESQEVAAVS--SWAEIHTAARLLQVPPERLEGAV 292

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  463 CARIMQTTKGgargtLIRVPLKPHEACSGRDALSKAIYSKLFDWLVSRINDSI---PFEKSTNFVGVLDVAGFEFYAKNS 539
Cdd:cd14896   293 THRVTETPYG-----RVSRPLPVEGAIDARDALAKTLYSRLFTWLLKRINAWLappGEAESDATIGVVDAYGFEALRVNG 367

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  540 FEQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEFIDNQDCIELFELKGNGLFDLLDEEAKFPTSNYKSFTKRA 619
Cdd:cd14896   368 LEQLCINLASERLQLFSSQTLLAQEEEECQRELLPWVPIPQPPRESCLDLLVDQPHSLLSILDDQTWLSQATDHTFLQKC 447

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  620 HEENRKHfrldtPRKSKVKSHRELrddegLLIRHYAGSVCYETKHFVEKNDDLLHNSLQILIEQSTIRLLVSLFGSTAYP 699
Cdd:cd14896   448 HYHHGDH-----PSYAKPQLPLPV-----FTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQ 517

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  700 TKSKLKALSVGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGSAILSQLQCAGMTSVLKLMQDGFPSRTGFGD 779
Cdd:cd14896   518 YGLGQGKPTLASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQA 597

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*..
gi 808358096  780 LYACYQKKLPPKLSKLDPRMFCKC-LFRALGLDQHDFQFGLTKVFFR 825
Cdd:cd14896   598 FLARFGALGSERQEALSDRERCGAiLSQVLGAESPLYHLGATKVLLK 644
MYSc_Myh18 cd14932
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ...
 143-825 8.08e-127

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: 406.72  E-value: 8.08e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  143 ATLLNNIRLRYQNGKIYSYVANILISINPYQTIDgFYSLQKIKEYRGKSLGQKEPHIFAIADKSYREMIRHRKSQSIIVS 222
Cdd:cd14932     1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLP-IYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  223 GESGAGKTESQKAVLRYLC---------ENWGSGA---GEIQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFADT 290
Cdd:cd14932    80 GESGAGKTENTKKVIQYLAyvassfktkKDQSSIAlshGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVN 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  291 GNVAGGYVSHYLLETSRICRQAAGERNYHIFYQLIAGSSPELFKFLALGQPNQFNYLKRGFIgffthpssgttsKIPKnr 370
Cdd:cd14932   160 GYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNV------------TIPG-- 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  371 LSDPKFTQDSMvddfsdfqrleYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEESLDDSRGGCKVFNGSEQdliqAARL 450
Cdd:cd14932   226 QQDKELFAETM-----------EAFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQK----VCHL 290

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  451 LGLETMELKMGLCARIMQTTKggargTLIRVPLKPHEACSGRDALSKAIYSKLFDWLVSRINDSIPFEK--STNFVGVLD 528
Cdd:cd14932   291 LGMNVTDFTRAILSPRIKVGR-----DYVQKAQTQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKrqGASFIGILD 365

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  529 VAGFEFYAKNSFEQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEF-IDNQDCIELFELKGN--GLFDLLDEEA 605
Cdd:cd14932   366 IAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIELIEKPNGppGILALLDEEC 445

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  606 KFPTSNYKSFTKRAHEENRKHFRLDTPRKskvkshreLRDDEGLLIRHYAGSVCYETKHFVEKNDDLLHNSLQILIEQST 685
Cdd:cd14932   446 WFPKATDKSFVEKVVQEQGNNPKFQKPKK--------LKDDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQST 517

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  686 IRLLVSLF----------------GSTAYPTKSKLKAL-SVGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDG 748
Cdd:cd14932   518 DKFVSELWkdvdrivgldkvagmgESLHGAFKTRKGMFrTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAH 597

                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 808358096  749 SAILSQLQCAGMTSVLKLMQDGFPSRTGFGDLYACYQKKLPPKLSK--LDPRMFCKCLFRALGLDQHDFQFGLTKVFFR 825
Cdd:cd14932   598 HLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKgfMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
MYSc_Myh11 cd14921
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ...
 143-825 1.42e-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: 405.94  E-value: 1.42e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  143 ATLLNNIRLRYQNGKIYSYVANILISINPYQTIDgFYSLQKIKEYRGKSLGQKEPHIFAIADKSYREMIRHRKSQSIIVS 222
Cdd:cd14921     1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLP-IYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  223 GESGAGKTESQKAVLRYLC--------ENWGSGAGEIQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFADTGNVA 294
Cdd:cd14921    80 GESGAGKTENTKKVIQYLAvvasshkgKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  295 GGYVSHYLLETSRICRQAAGERNYHIFYQLIAGSSPELFKFLALGQPNQFNYLKRGFIgffthpssgttsKIPKNrlsdp 374
Cdd:cd14921   160 GANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFV------------PIPAA----- 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  375 kftqdsmvDDFSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEESLDDSRGGCKVFNGSEqdliQAARLLGLE 454
Cdd:cd14921   223 --------QDDEMFQETLEAMSIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQ----KVCHLMGIN 290

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  455 TMELkmglcARIMQTTKGGARGTLIRVPLKPHEACSGRDALSKAIYSKLFDWLVSRINDSIPFEK--STNFVGVLDVAGF 532
Cdd:cd14921   291 VTDF-----TRSILTPRIKVGRDVVQKAQTKEQADFAIEALAKATYERLFRWILTRVNKALDKTHrqGASFLGILDIAGF 365

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  533 EFYAKNSFEQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEF-IDNQDCIELFELKGN--GLFDLLDEEAKFPT 609
Cdd:cd14921   366 EIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIELIERPNNppGVLALLDEECWFPK 445

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  610 SNYKSFTKRAHEENRKHFRLDTPrkskvkshRELRDDEGLLIRHYAGSVCYETKHFVEKNDDLLHNSLQILIEQSTIRLL 689
Cdd:cd14921   446 ATDKSFVEKLCTEQGNHPKFQKP--------KQLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFV 517

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  690 VSLFG---------------STAYPTKSKLKA---LSVGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGSAI 751
Cdd:cd14921   518 ADLWKdvdrivgldqmakmtESSLPSASKTKKgmfRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLV 597

                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 808358096  752 LSQLQCAGMTSVLKLMQDGFPSRTGFGDLYACYQKKLPPKLSK--LDPRMFCKCLFRALGLDQHDFQFGLTKVFFR 825
Cdd:cd14921   598 LEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPKgfMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
MYSc_Myh1_insects_crustaceans cd14909
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ...
 143-825 3.23e-126

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: 404.61  E-value: 3.23e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  143 ATLLNNIRLRYQNGKIYSYVANILISINPYQTIDgFYSLQKIKEYRGKSLGQKEPHIFAIADKSYREMIRHRKSQSIIVS 222
Cdd:cd14909     1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYP-VYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLIT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  223 GESGAGKTESQKAVLRYLC--------ENWGSGAGEIQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFADTGNVA 294
Cdd:cd14909    80 GESGAGKTENTKKVIAYFAtvgaskktDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  295 GGYVSHYLLETSRICRQAAGERNYHIFYQLIAGSSPELfKFLALGQPNQFNYlkrgfigffTHPSSGTTSkIPKnrlsdp 374
Cdd:cd14909   160 GADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGV-KEMCLLSDNIYDY---------YIVSQGKVT-VPN------ 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  375 kftqdsmVDDFSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEESLDDSRggckvfngSEQDLIQA----ARL 450
Cdd:cd14909   223 -------VDDGEEFSLTDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQ--------AEQDGEEEggrvSKL 287

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  451 LGLETMELKMGLCA-RIMQTTKGGARGTlirvplKPHEACSGRDALSKAIYSKLFDWLVSRINDSIPF-EKSTNFVGVLD 528
Cdd:cd14909   288 FGCDTAELYKNLLKpRIKVGNEFVTQGR------NVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTqQKRQHFIGVLD 361

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  529 VAGFEFYAKNSFEQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEF-IDNQDCIELFElKGNGLFDLLDEEAKF 607
Cdd:cd14909   362 IAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQEEYKREGIDWAFIDFgMDLLACIDLIE-KPMGILSILEEESMF 440

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  608 PTSNYKSFTKR---AHEENRKHFRLDTPRKSKVKSHRelrddegLLIRHYAGSVCYETKHFVEKNDDLLHNSLQILIEQS 684
Cdd:cd14909   441 PKATDQTFSEKltnTHLGKSAPFQKPKPPKPGQQAAH-------FAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKS 513

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  685 TIRLLVSLFGStaYPTKSKLKALSVGAK-------------FKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGSAI 751
Cdd:cd14909   514 QNKLLIEIFAD--HAGQSGGGEQAKGGRgkkgggfatvssaYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLV 591

                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 808358096  752 LSQLQCAGMTSVLKLMQDGFPSRTGFGDLYACYQKKLPPKLSK-LDPRMFCKCLFRALGLDQHDFQFGLTKVFFR 825
Cdd:cd14909   592 MHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGIQGeEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
MYSc_Myo39 cd14900
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ...
 144-774 5.87e-125

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: 400.07  E-value: 5.87e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  144 TLLNNIRLRYQNGKIYSYVANILISINPYQTIDGFYSLQKIKEY-----------RGKSLGQKEPHIFAIADKSYREMIR 212
Cdd:cd14900     2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPGLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMML 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  213 HRKS----QSIIVSGESGAGKTESQKAVLRYLCE----------NWGSGAGEIQKRLLETNPILEAFGNAKTLRNNNSSR 278
Cdd:cd14900    82 GLNGvmsdQSILVSGESGSGKTESTKFLMEYLAQagdnnlaasvSMGKSTSGIAAKVLQTNILLESFGNARTLRNDNSSR 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  279 FGKFVQIHFADTGNVAGGYVSHYLLETSRICRQAAGERNYHIFYQLIAGSSPELFKflalgqpnqfnylkrgfigffthp 358
Cdd:cd14900   162 FGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARK------------------------ 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  359 ssgttSKIpknrlsdpkftqdsmvddfsdFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEESLDDSRGGCKVFN 438
Cdd:cd14900   218 -----RDM---------------------YRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSD 271

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  439 ---GSEQDLIQAARLLGLETMELKMGLCARimqTTKGGARGTLIRvpLKPHEACSGRDALSKAIYSKLFDWLVSRIN--- 512
Cdd:cd14900   272 lapSSIWSRDAAATLLSVDATKLEKALSVR---RIRAGTDFVSMK--LSAAQANNARDALAKALYGRLFDWLVGKMNafl 346

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  513 ---DSIPFEKSTNFVGVLDVAGFEFYAKNSFEQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEFIDNQDCIEL 589
Cdd:cd14900   347 kmdDSSKSHGGLHFIGILDIFGFEVFPKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFCDNQDCVNL 426

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  590 FELKGNGLFDLLDEEAKFPTSNYKSFTKRAHEENRKHFRLDTPRKSKVKshrelrddeGLL-IRHYAGSVCYETKHFVEK 668
Cdd:cd14900   427 ISQRPTGILSLIDEECVMPKGSDTTLASKLYRACGSHPRFSASRIQRAR---------GLFtIVHYAGHVEYSTDGFLEK 497

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  669 NDDLLHnslqilieQSTIRLLVSlfgstayptksklkalsvGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDG 748
Cdd:cd14900   498 NKDVLH--------QEAVDLFVY------------------GLQFKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYER 551

                         650       660
                  ....*....|....*....|....*.
gi 808358096  749 SAILSQLQCAGMTSVLKLMQDGFPSR 774
Cdd:cd14900   552 ERVLNQLRCNGVMEAVRVARAGFPIR 577
MYSc_Myh9 cd14919
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ...
 143-825 1.16e-124

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: 400.62  E-value: 1.16e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  143 ATLLNNIRLRYQNGKIYSYVANILISINPYQTIDgFYSLQKIKEYRGKSLGQKEPHIFAIADKSYREMIRHRKSQSIIVS 222
Cdd:cd14919     1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  223 GESGAGKTESQKAVLRYLCENWGS-----GAGEIQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFADTGNVAGGY 297
Cdd:cd14919    80 GESGAGKTENTKKVIQYLAHVASShkskkDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  298 VSHYLLETSRICRQAAGERNYHIFYQLIAGSSPELFKFLALGQPNQFNYLKRGFIgffthpssgttsKIPKNRLSDPkft 377
Cdd:cd14919   160 IETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHV------------TIPGQQDKDM--- 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  378 qdsmvddfsdFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEESLDDSRGGCKVFNGSEqdliQAARLLGLETME 457
Cdd:cd14919   225 ----------FQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQ----KVSHLLGINVTD 290

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  458 LKMGLCARIMQTTKggargTLIRVPLKPHEACSGRDALSKAIYSKLFDWLVSRINDSIPFEK--STNFVGVLDVAGFEFY 535
Cdd:cd14919   291 FTRGILTPRIKVGR-----DYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKrqGASFIGILDIAGFEIF 365

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  536 AKNSFEQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEF-IDNQDCIELFELKGN--GLFDLLDEEAKFPTSNY 612
Cdd:cd14919   366 DLNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIEKPAGppGILALLDEECWFPKATD 445

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  613 KSFTKRAHEENRKHFRLDTPrkskvkshRELRDDEGLLIRHYAGSVCYETKHFVEKNDDLLHNSLQILIEQSTIRLLVSL 692
Cdd:cd14919   446 KSFVEKVVQEQGTHPKFQKP--------KQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSEL 517

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  693 F---------------GSTAYPTKSKLKA---LSVGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGSAILSQ 754
Cdd:cd14919   518 WkdvdriigldqvagmSETALPGAFKTRKgmfRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQ 597

                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 808358096  755 LQCAGMTSVLKLMQDGFPSRTGFGDLYACYQKKLPPKLSK--LDPRMFCKCLFRALGLDQHDFQFGLTKVFFR 825
Cdd:cd14919   598 LRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKgfMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
MYSc_Myh7 cd14917
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ...
 145-825 1.70e-124

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: 400.25  E-value: 1.70e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  145 LLNNIRLRYQNGKIYSYVANILISINPYQTIDgFYSLQKIKEYRGKSLGQKEPHIFAIADKSYREMIRHRKSQSIIVSGE 224
Cdd:cd14917     3 VLYNLKERYASWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  225 SGAGKTESQKAVLRYLC----------ENWGSGAGEIQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFADTGNVA 294
Cdd:cd14917    82 SGAGKTVNTKRVIQYFAviaaigdrskKDQTPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  295 GGYVSHYLLETSRICRQAAGERNYHIFYQLIAGSSPELFKFLALGQpNQFNYlkrGFIgffthpSSGTTSKipknrlsdp 374
Cdd:cd14917   162 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITN-NPYDY---AFI------SQGETTV--------- 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  375 kftqdSMVDDFSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEESLDDSRGGCkvfNGSEQdLIQAARLLGLE 454
Cdd:cd14917   223 -----ASIDDAEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEP---DGTEE-ADKSAYLMGLN 293

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  455 TMELKMGLC-ARIMQTTKGGARGTLIRvplkphEACSGRDALSKAIYSKLFDWLVSRINDSIPFEKSTN-FVGVLDVAGF 532
Cdd:cd14917   294 SADLLKGLChPRVKVGNEYVTKGQNVQ------QVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQyFIGVLDIAGF 367

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  533 EFYAKNSFEQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEF-IDNQDCIELFElKGNGLFDLLDEEAKFPTSN 611
Cdd:cd14917   368 EIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKAT 446

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  612 YKSFTKRAHEENR-KHFRLDTPR--KSKVKSHRELrddeglliRHYAGSVCYETKHFVEKNDDLLHNSLQILIEQSTIRL 688
Cdd:cd14917   447 DMTFKAKLFDNHLgKSNNFQKPRniKGKPEAHFSL--------IHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKL 518

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  689 LVSLF----GSTAYPTKSKLKA------LSVGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGSAILSQLQCA 758
Cdd:cd14917   519 LSNLFanyaGADAPIEKGKGKAkkgssfQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCN 598

                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  759 GMTSVLKLMQDGFPSRTGFGDLYACYQKKLP---PKLSKLDPRMFCKCLFRALGLDQHDFQFGLTKVFFR 825
Cdd:cd14917   599 GVLEGIRICRKGFPNRILYGDFRQRYRILNPaaiPEGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
MYSc_Myh14_mammals cd14930
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ...
 143-825 1.03e-122

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: 395.62  E-value: 1.03e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  143 ATLLNNIRLRYQNGKIYSYVANILISINPYQTIDgFYSLQKIKEYRGKSLGQKEPHIFAIADKSYREMIRHRKSQSIIVS 222
Cdd:cd14930     1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  223 GESGAGKTESQKAVLRYLCENWGSGAG--------EIQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFADTGNVA 294
Cdd:cd14930    80 GESGAGKTENTKKVIQYLAHVASSPKGrkepgvpgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  295 GGYVSHYLLETSRICRQAAGERNYHIFYQLIAGSSPELFKFLALGQPNQFNYLKRGfigffthPSSgttskipknrlsdp 374
Cdd:cd14930   160 GANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNG-------PSS-------------- 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  375 kftqdSMVDDFSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEESLDDSRGGCKVfNGSEQDLiqaARLLGLE 454
Cdd:cd14930   219 -----SPGQERELFQETLESLRVLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPD-NTAAQKL---CRLLGLG 289

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  455 TMELkmglcARIMQTTKGGARGTLIRVPLKPHEACSGRDALSKAIYSKLFDWLVSRIN---DSIPfEKSTNFVGVLDVAG 531
Cdd:cd14930   290 VTDF-----SRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNralDRSP-RQGASFLGILDIAG 363

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  532 FEFYAKNSFEQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEF-IDNQDCIELFELKGN--GLFDLLDEEAKFP 608
Cdd:cd14930   364 FEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPANppGLLALLDEECWFP 443

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  609 TSNYKSFTKRAHEENRKHFRLDTPRKskvkshreLRDDEGLLIRHYAGSVCYETKHFVEKNDDLLHNSLQILIEQSTIRL 688
Cdd:cd14930   444 KATDKSFVEKVAQEQGGHPKFQRPRH--------LRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRL 515

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  689 LVSLFGST------------------AYPTKSKLKalSVGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGSA 750
Cdd:cd14930   516 TAEIWKDVegivgleqvsslgdgppgGRPRRGMFR--TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRL 593

                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 808358096  751 ILSQLQCAGMTSVLKLMQDGFPSRTGFGDLYACYQKKLPPKLSK--LDPRMFCKCLFRALGLDQHDFQFGLTKVFFR 825
Cdd:cd14930   594 VLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKgfMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
MYSc_Myh6 cd14916
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ...
 145-825 3.04e-122

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: 394.43  E-value: 3.04e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  145 LLNNIRLRYQNGKIYSYVANILISINPYQTIDgFYSLQKIKEYRGKSLGQKEPHIFAIADKSYREMIRHRKSQSIIVSGE 224
Cdd:cd14916     3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  225 SGAGKTESQKAVLRYLC-----------ENWGSGAGEIQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFADTGNV 293
Cdd:cd14916    82 SGAGKTVNTKRVIQYFAsiaaigdrskkENPNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  294 AGGYVSHYLLETSRICRQAAGERNYHIFYQLIAGSSPELFKFLAL-GQPNQFNYLKRGFIGFfthpssgttskipknrls 372
Cdd:cd14916   162 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVtNNPYDYAFVSQGEVSV------------------ 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  373 dpkftqdSMVDDFSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEESLDDSRGGCkvfNGSEqDLIQAARLLG 452
Cdd:cd14916   224 -------ASIDDSEELLATDSAFDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEP---DGTE-DADKSAYLMG 292

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  453 LETMELKMGLC-ARIMQTTKGGARGTLIRvplkphEACSGRDALSKAIYSKLFDWLVSRINDSIPFEKSTN-FVGVLDVA 530
Cdd:cd14916   293 LNSADLLKGLChPRVKVGNEYVTKGQSVQ------QVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQyFIGVLDIA 366

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  531 GFEFYAKNSFEQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEF-IDNQDCIELFElKGNGLFDLLDEEAKFPT 609
Cdd:cd14916   367 GFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPK 445

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  610 SNYKSFTKRAHEENR-KHFRLDTPRKSKVKSHRELRddegllIRHYAGSVCYETKHFVEKNDDLLHNSLQILIEQSTIRL 688
Cdd:cd14916   446 ASDMTFKAKLYDNHLgKSNNFQKPRNVKGKQEAHFS------LVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKL 519

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  689 LVSLF--------GSTAYPTKSKLKALS---VGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGSAILSQLQC 757
Cdd:cd14916   520 MATLFstyasadtGDSGKGKGGKKKGSSfqtVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRC 599

                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808358096  758 AGMTSVLKLMQDGFPSRTGFGDLYACYQKKLP---PKLSKLDPRMFCKCLFRALGLDQHDFQFGLTKVFFR 825
Cdd:cd14916   600 NGVLEGIRICRKGFPNRILYGDFRQRYRILNPaaiPEGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
MYSc_Myh1_mammals cd14910
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ...
 145-825 2.51e-121

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: 391.79  E-value: 2.51e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  145 LLNNIRLRYQNGKIYSYVANILISINPYQTIDgFYSLQKIKEYRGKSLGQKEPHIFAIADKSYREMIRHRKSQSIIVSGE 224
Cdd:cd14910     3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  225 SGAGKTESQKAVLRYLC----------ENWGSGA--GEIQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFADTGN 292
Cdd:cd14910    82 SGAGKTVNTKRVIQYFAtiavtgekkkEEATSGKmqGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  293 VAGGYVSHYLLETSRICRQAAGERNYHIFYQLIAGSSPELFKFLAL-GQPNQFNYLKRGFIgffTHPSsgttskipknrl 371
Cdd:cd14910   162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLItTNPYDYAFVSQGEI---TVPS------------ 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  372 sdpkftqdsmVDDFSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEESLDDSRG---GCKVFNgseqdliQAA 448
Cdd:cd14910   227 ----------IDDQEELMATDSAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAepdGTEVAD-------KAA 289

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  449 RLLGLETMELKMGLC-ARIMQTTKGGARGTLIRvplkphEACSGRDALSKAIYSKLFDWLVSRINDSIPFEKSTN-FVGV 526
Cdd:cd14910   290 YLQNLNSADLLKALCyPRVKVGNEYVTKGQTVQ------QVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQyFIGV 363

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  527 LDVAGFEFYAKNSFEQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEF-IDNQDCIELFElKGNGLFDLLDEEA 605
Cdd:cd14910   364 LDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELIE-KPMGIFSILEEEC 442

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  606 KFPTSNYKSFTKRAHEEN---RKHFRLDTPRKSKVKSHRELrddeglliRHYAGSVCYETKHFVEKNDDLLHNSLQILIE 682
Cdd:cd14910   443 MFPKATDTSFKNKLYEQHlgkSNNFQKPKPAKGKVEAHFSL--------IHYAGTVDYNIAGWLDKNKDPLNETVVGLYQ 514

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  683 QSTIRLLVSLF-GSTAYPTKS-------KLKALS---VGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGSAI 751
Cdd:cd14910   515 KSSMKTLALLFsGAAAAEAEEgggkkggKKKGSSfqtVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELV 594

                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 808358096  752 LSQLQCAGMTSVLKLMQDGFPSRTGFGDL---YACYQKKLPPKLSKLDPRMFCKCLFRALGLDQHDFQFGLTKVFFR 825
Cdd:cd14910   595 LHQLRCNGVLEGIRICRKGFPSRILYADFkqrYKVLNASAIPEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
MYSc_Myh19 cd15896
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ...
 143-825 1.72e-120

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: 389.81  E-value: 1.72e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  143 ATLLNNIRLRYQNGKIYSYVANILISINPYQTIDgFYSLQKIKEYRGKSLGQKEPHIFAIADKSYREMIRHRKSQSIIVS 222
Cdd:cd15896     1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  223 GESGAGKTESQKAVLRYLC------------ENWGSGAGEIQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFADT 290
Cdd:cd15896    80 GESGAGKTENTKKVIQYLAhvasshktkkdqNSLALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVN 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  291 GNVAGGYVSHYLLETSRICRQAAGERNYHIFYQLIAGSSPELFKFLALGQPNQFNYLKRGFIgffthpssgttsKIPKNR 370
Cdd:cd15896   160 GYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNV------------TIPGQQ 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  371 lsdpkftqdsmvdDFSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEESLDDSRGGCKVFNGSEqdliQAARL 450
Cdd:cd15896   228 -------------DKDLFTETMEAFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQ----KVCHL 290

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  451 LGLETMELKMGLCARIMQTTKggargTLIRVPLKPHEACSGRDALSKAIYSKLFDWLVSRINDSIPFEK--STNFVGVLD 528
Cdd:cd15896   291 MGMNVTDFTRAILSPRIKVGR-----DYVQKAQTQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKrqGASFIGILD 365

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  529 VAGFEFYAKNSFEQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEF-IDNQDCIELFELKGN--GLFDLLDEEA 605
Cdd:cd15896   366 IAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIEKPASppGILALLDEEC 445

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  606 KFPTSNYKSFTKRAHEENRKHFRLDTPRKskvkshreLRDDEGLLIRHYAGSVCYETKHFVEKNDDLLHNSLQILIEQST 685
Cdd:cd15896   446 WFPKATDKSFVEKVLQEQGTHPKFFKPKK--------LKDEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQST 517

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  686 IRLLVSLF-------------GSTAYPTKSKLKA---LSVGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGS 749
Cdd:cd15896   518 DKFVSELWkdvdrivgldkvsGMSEMPGAFKTRKgmfRTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPH 597

                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 808358096  750 AILSQLQCAGMTSVLKLMQDGFPSRTGFGDLYACYQKKLPPKLSK--LDPRMFCKCLFRALGLDQHDFQFGLTKVFFR 825
Cdd:cd15896   598 LVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKgfMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
MYSc_Myh4 cd14915
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ...
 145-825 1.87e-120

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: 389.47  E-value: 1.87e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  145 LLNNIRLRYQNGKIYSYVANILISINPYQTIDgFYSLQKIKEYRGKSLGQKEPHIFAIADKSYREMIRHRKSQSIIVSGE 224
Cdd:cd14915     3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  225 SGAGKTESQKAVLRYLC----------ENWGSGA--GEIQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFADTGN 292
Cdd:cd14915    82 SGAGKTVNTKRVIQYFAtiavtgekkkEEAASGKmqGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  293 VAGGYVSHYLLETSRICRQAAGERNYHIFYQLIAGSSPELFKFLAL-GQPNQFNYLKRGFIgffTHPSsgttskipknrl 371
Cdd:cd14915   162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLItTNPYDFAFVSQGEI---TVPS------------ 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  372 sdpkftqdsmVDDFSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEESLDDSRG---GCKVFNgseqdliQAA 448
Cdd:cd14915   227 ----------IDDQEELMATDSAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAepdGTEVAD-------KAA 289

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  449 RLLGLETMELKMGLC-ARIMQTTKGGARGTLIRvplkphEACSGRDALSKAIYSKLFDWLVSRINDSIPFEKSTN-FVGV 526
Cdd:cd14915   290 YLTSLNSADLLKALCyPRVKVGNEYVTKGQTVQ------QVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQyFIGV 363

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  527 LDVAGFEFYAKNSFEQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEF-IDNQDCIELFElKGNGLFDLLDEEA 605
Cdd:cd14915   364 LDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELIE-KPMGIFSILEEEC 442

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  606 KFPTSNYKSFTKRAHEEN---RKHFRLDTPRKSKVKSHRELrddeglliRHYAGSVCYETKHFVEKNDDLLHNSLQILIE 682
Cdd:cd14915   443 MFPKATDTSFKNKLYEQHlgkSNNFQKPKPAKGKAEAHFSL--------VHYAGTVDYNIAGWLDKNKDPLNETVVGLYQ 514

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  683 QSTIRLLVSLF-----------GSTAYPTKSKLKALSVGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGSAI 751
Cdd:cd14915   515 KSGMKTLAFLFsggqtaeaeggGGKKGGKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELV 594

                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 808358096  752 LSQLQCAGMTSVLKLMQDGFPSRTGFGDL---YACYQKKLPPKLSKLDPRMFCKCLFRALGLDQHDFQFGLTKVFFR 825
Cdd:cd14915   595 LHQLRCNGVLEGIRICRKGFPSRILYADFkqrYKVLNASAIPEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
MYSc_Myh8 cd14918
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ...
 145-825 3.30e-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: 388.71  E-value: 3.30e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  145 LLNNIRLRYQNGKIYSYVANILISINPYQTIDgFYSLQKIKEYRGKSLGQKEPHIFAIADKSYREMIRHRKSQSIIVSGE 224
Cdd:cd14918     3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  225 SGAGKTESQKAVLRYLC----------ENWGSGAGEIQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFADTGNVA 294
Cdd:cd14918    82 SGAGKTVNTKRVIQYFAtiavtgekkkEESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  295 GGYVSHYLLETSRICRQAAGERNYHIFYQLIAGSSPELFKFLAL-GQPNQFNYLKRGFIgffTHPSsgttskipknrlsd 373
Cdd:cd14918   162 SADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLItTNPYDYAFVSQGEI---TVPS-------------- 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  374 pkftqdsmVDDFSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEESLDDSRG---GCKVFNgseqdliQAARL 450
Cdd:cd14918   225 --------IDDQEELMATDSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAepdGTEVAD-------KAAYL 289

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  451 LGLETMELKMGLC-ARIMQTTKGGARGTLIRvplkphEACSGRDALSKAIYSKLFDWLVSRINDSIPFEKSTN-FVGVLD 528
Cdd:cd14918   290 QSLNSADLLKALCyPRVKVGNEYVTKGQTVQ------QVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQyFIGVLD 363

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  529 VAGFEFYAKNSFEQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEF-IDNQDCIELFElKGNGLFDLLDEEAKF 607
Cdd:cd14918   364 IAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPLGIFSILEEECMF 442

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  608 PTSNYKSFTKRAHEENR-KHFRLDTPR--KSKVKSHRELrddeglliRHYAGSVCYETKHFVEKNDDLLHNSLQILIEQS 684
Cdd:cd14918   443 PKATDTSFKNKLYDQHLgKSANFQKPKvvKGKAEAHFSL--------IHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKS 514

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  685 TIRLLVSLFGSTAYP---------TKSKLKAL-SVGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGSAILSQ 754
Cdd:cd14918   515 AMKTLASLFSTYASAeadsgakkgAKKKGSSFqTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQ 594

                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 808358096  755 LQCAGMTSVLKLMQDGFPSRTGFGDL---YACYQKKLPPKLSKLDPRMFCKCLFRALGLDQHDFQFGLTKVFFR 825
Cdd:cd14918   595 LRCNGVLEGIRICRKGFPSRILYGDFkqrYKVLNASAIPEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
MYSc_Myo34 cd14895
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ...
 152-825 4.67e-120

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: 389.31  E-value: 4.67e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  152 RYQNGKIYSYVANILISINPYQTIDGFYSLQKIKEYRGKSLgQKEPHIFAIADKSYREMIRH-------RKSQSIIVSGE 224
Cdd:cd14895    10 RYGVDQVYCRSGAVLIAVNPFKHIPGLYDLHKYREEMPGWT-ALPPHVFSIAEGAYRSLRRRlhepgasKKNQTILVSGE 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  225 SGAGKTESQKAVLRYLCENWGSGAGEIQKR---------LLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFA-----DT 290
Cdd:cd14895    89 SGAGKTETTKFIMNYLAESSKHTTATSSSKrrraisgseLLSANPILESFGNARTLRNDNSSRFGKFVRMFFEgheldTS 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  291 GNVAGGYVSHYLLETSRICRQAAGERNYHIFYQLIAGSSPELFKFLALG--QPNQFNYLKRGfiGFFTHpssgttskipk 368
Cdd:cd14895   169 LRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLEllSAQEFQYISGG--QCYQR----------- 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  369 nrlsdpkftQDSMVDDfSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEF--------EESLDDSRGGCKVFNGS 440
Cdd:cd14895   236 ---------NDGVRDD-KQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFvassedegEEDNGAASAPCRLASAS 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  441 ------EQDLIQAARLLGLETMELKMGLCARimqttKGGARGTLIRVPLKPHEACSGRDALSKAIYSKLFDWLVSRINDS 514
Cdd:cd14895   306 pssltvQQHLDIVSKLFAVDQDELVSALTTR-----KISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSA 380

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  515 IP------------FEKSTNFVGVLDVAGFEFYAKNSFEQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEFID 582
Cdd:cd14895   381 SPqrqfalnpnkaaNKDTTPCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYED 460

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  583 NQDCIELFELKGNGLFDLLDEEAKFPTSNYKSFTKRAHEENRKHFRLDTPRKSKVkshrelrdDEGLLIRHYAGSVCYET 662
Cdd:cd14895   461 NSVCLEMLEQRPSGIFSLLDEECVVPKGSDAGFARKLYQRLQEHSNFSASRTDQA--------DVAFQIHHYAGAVRYQA 532

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  663 KHFVEKNDDLLHNSLQILIEQST---IRLLVSLFG-------STAYPT----KSKLKALSVGAKFKNQLSTLLIKLESTG 728
Cdd:cd14895   533 EGFCEKNKDQPNAELFSVLGKTSdahLRELFEFFKasesaelSLGQPKlrrrSSVLSSVGIGSQFKQQLASLLDVVQQTQ 612

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  729 THFVRCIKPNNQMIPFEFDGSAILSQLQCAGMTSVLKLMQDGFPSRTGFGDLYACYQKKL-PPKLSKLDprmfCKCLFRA 807
Cdd:cd14895   613 THYIRCIKPNDESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVaAKNASDAT----ASALIET 688

                         730
                  ....*....|....*...
gi 808358096  808 LGLDQhdFQFGLTKVFFR 825
Cdd:cd14895   689 LKVDH--AELGKTRVFLR 704
MYSc_Myo19 cd14880
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ...
 143-823 1.15e-119

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: 386.90  E-value: 1.15e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  143 ATLLNNIRLRYQNGKIYSYVANILISINPYQTIDGFYSLQKIKEYRGKSLGQK-EPHIFAIADKSYREMIRHRK--SQSI 219
Cdd:cd14880     1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPQLYSPELMREYHAAPQPQKlKPHIFTVGEQTYRNVKSLIEpvNQSI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  220 IVSGESGAGKTESQKAVLRYL---------CENwGSGAGEIQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFADT 290
Cdd:cd14880    81 VVSGESGAGKTWTSRCLMKFYavvaasptsWES-HKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  291 GNVAGGYVSHYLLETSRICRQAAGERNYHIFYQLIAGSSPELFKFLALGQPNQFNYLKRgfigffthpssgttskiPKNR 370
Cdd:cd14880   160 QQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPN-----------------PERN 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  371 LSDPKF--TQDSMvddfsdfqrleyaLKLtGLSEQEIHFIWTTIAAILHLGNVEFEESLDDSRGgCKVFNGSEQDLIQAA 448
Cdd:cd14880   223 LEEDCFevTREAM-------------LHL-GIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQP-CQPMDDTKESVRTSA 287

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  449 RLLGLETMELKMGLCARimqTTKGGARGTLIRVPLKPHEACSGRDALSKAIYSKLFDWLVSRINDSIPFEKS--TNFVGV 526
Cdd:cd14880   288 LLLKLPEDHLLETLQIR---TIRAGKQQQVFKKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDswTTFIGL 364

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  527 LDVAGFEFYAKNSFEQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEFIDNQDCIELFELKGNGLFDLLDEEAK 606
Cdd:cd14880   365 LDVYGFESFPENSLEQLCINYANEKLQQHFVAHYLRAQQEEYAVEGLEWSFINYQDNQTCLDLIEGSPISICSLINEECR 444

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  607 FptsnyksftKRAHEENRKHFRLDTP-RKSKVKSHRELRDDEGLLIRHYAGSVCYETKHFVEKNDDLLHNSLQILIEQST 685
Cdd:cd14880   445 L---------NRPSSAAQLQTRIESAlAGNPCLGHNKLSREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQ 515

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  686 IRLLVSLF------GSTAYP-TKSKLKALSVGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGSAILSQLQCA 758
Cdd:cd14880   516 DPLLQKLFpanpeeKTQEEPsGQSRAPVLTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEAC 595

                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 808358096  759 GMTSVLKLMQDGFPSRTGFGDLYACYQkklppKLSKLDPRMfCKCLFRAL--GLDQHDFQFGLTKVF 823
Cdd:cd14880   596 GLVETIHISAAGFPIRVSHQNFVERYK-----LLRRLRPHT-SSGPHSPYpaKGLSEPVHCGRTKVF 656
MYSc_Myh13 cd14923
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ...
 145-825 1.99e-119

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: 386.73  E-value: 1.99e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  145 LLNNIRLRYQNGKIYSYVANILISINPYQTIDgFYSLQKIKEYRGKSLGQKEPHIFAIADKSYREMIRHRKSQSIIVSGE 224
Cdd:cd14923     3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  225 SGAGKTESQKAVLRYLC-----------ENWGSGAGEIQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFADTGNV 293
Cdd:cd14923    82 SGAGKTVNTKRVIQYFAtiavtgdkkkeQQPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  294 AGGYVSHYLLETSRICRQAAGERNYHIFYQLIAGSSPELFKFLALG-QPNQFNYLKRGFIGFfthpssgttskipknrls 372
Cdd:cd14923   162 ASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLIStNPFDFPFVSQGEVTV------------------ 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  373 dpkftqdSMVDDFSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEESLDDSRG---GCKVFNgseqdliQAAR 449
Cdd:cd14923   224 -------ASIDDSEELLATDNAIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAepdGTEVAD-------KAGY 289

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  450 LLGLETMELKMGLC-ARIMQTTKGGARGTLIRvplkphEACSGRDALSKAIYSKLFDWLVSRINDSIPFEK-STNFVGVL 527
Cdd:cd14923   290 LMGLNSAEMLKGLCcPRVKVGNEYVTKGQNVQ------QVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQpRQYFIGVL 363

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  528 DVAGFEFYAKNSFEQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEF-IDNQDCIELFElKGNGLFDLLDEEAK 606
Cdd:cd14923   364 DIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELIE-KPMGIFSILEEECM 442

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  607 FPTSNYKSFTKRAHEEN---RKHFRLDTPRKSKVKSHRELrddeglliRHYAGSVCYETKHFVEKNDDLLHNSLQILIEQ 683
Cdd:cd14923   443 FPKATDTSFKNKLYDQHlgkSNNFQKPKPAKGKAEAHFSL--------VHYAGTVDYNIAGWLDKNKDPLNETVVGLYQK 514

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  684 STIRLLVSLF------------GSTAYPTKSKLKALSVGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGSAI 751
Cdd:cd14923   515 SSLKLLSFLFsnyagaeagdsgGSKKGGKKKGSSFQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLV 594

                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 808358096  752 LSQLQCAGMTSVLKLMQDGFPSRTGFGDL---YACYQKKLPPKLSKLDPRMFCKCLFRALGLDQHDFQFGLTKVFFR 825
Cdd:cd14923   595 MHQLRCNGVLEGIRICRKGFPSRILYADFkqrYRILNASAIPEGQFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
MYSc_Myh2_mammals cd14912
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ...
 145-825 3.14e-117

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: 381.00  E-value: 3.14e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  145 LLNNIRLRYQNGKIYSYVANILISINPYQTIDgFYSLQKIKEYRGKSLGQKEPHIFAIADKSYREMIRHRKSQSIIVSGE 224
Cdd:cd14912     3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  225 SGAGKTESQKAVLRYLC----------ENWGSGA--GEIQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFADTGN 292
Cdd:cd14912    82 SGAGKTVNTKRVIQYFAtiavtgekkkEEITSGKmqGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  293 VAGGYVSHYLLETSRICRQAAGERNYHIFYQLIAGSSPELFKFLAL-GQPNQFNYLKRGFIGFfthpssgttskipknrl 371
Cdd:cd14912   162 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLItTNPYDYPFVSQGEISV----------------- 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  372 sdpkftqdSMVDDFSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEESLDDSRG---GCKVFNgseqdliQAA 448
Cdd:cd14912   225 --------ASIDDQEELMATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAepdGTEVAD-------KAA 289

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  449 RLLGLETMELKMGLC-ARIMQTTKGGARGTLIrvplkpHEACSGRDALSKAIYSKLFDWLVSRINDSIPFEKSTN-FVGV 526
Cdd:cd14912   290 YLQSLNSADLLKALCyPRVKVGNEYVTKGQTV------EQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQyFIGV 363

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  527 LDVAGFEFYAKNSFEQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEF-IDNQDCIELFElKGNGLFDLLDEEA 605
Cdd:cd14912   364 LDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEEC 442

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  606 KFPTSNYKSFTKRAHEENR-KHFRLDTPR--KSKVKSHrelrddegLLIRHYAGSVCYETKHFVEKNDDLLHNSLQILIE 682
Cdd:cd14912   443 MFPKATDTSFKNKLYEQHLgKSANFQKPKvvKGKAEAH--------FSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQ 514

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  683 QSTIRLLVSLF-------------GSTAYPTKSKLKALSVGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGS 749
Cdd:cd14912   515 KSAMKTLAYLFsgaqtaegasaggGAKKGGKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHE 594

                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 808358096  750 AILSQLQCAGMTSVLKLMQDGFPSRTGFGDL---YACYQKKLPPKLSKLDPRMFCKCLFRALGLDQHDFQFGLTKVFFR 825
Cdd:cd14912   595 LVLHQLRCNGVLEGIRICRKGFPSRILYADFkqrYKVLNASAIPEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
MYSc_Myo13 cd14875
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ...
 143-774 3.52e-115

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: 374.92  E-value: 3.52e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  143 ATLLNNIRLRYQNGKI-YSYVANILISINPYQTIdGFYSLQKIKEYRgkSLGQKE---PHIFAIADKSYREM-IRHRKSQ 217
Cdd:cd14875     1 ATLLHCIKERFEKLHQqYSLMGEMVLSVNPFRLM-PFNSEEERKKYL--ALPDPRllpPHIWQVAHKAFNAIfVQGLGNQ 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  218 SIIVSGESGAGKTESQKAVLRYLCE---------NWGSGAGEIQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHF- 287
Cdd:cd14875    78 SVVISGESGSGKTENAKMLIAYLGQlsymhssntSQRSIADKIDENLKWSNPVMESFGNARTVRNDNSSRFGKYIKLYFd 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  288 ADTGNVAGGYVSHYLLETSRICRQAAGERNYHIFYQLIAGSSPELFKFLA-LGQPNQFNYLKRGfiGFFTHpssgttski 366
Cdd:cd14875   158 PTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELGgLKTAQDYKCLNGG--NTFVR--------- 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  367 pknRLSDPKftqdsMVDDFSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEESLDDsrggcKVFNGSEQDLIQ 446
Cdd:cd14875   227 ---RGVDGK-----TLDDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQND-----KAQIADETPFLT 293

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  447 AARLLGLETMELKMGLCARimqttkggARGTLIRVPLKPHEACSGRDALSKAIYSKLFDWLVSRINDSIPFEKSTN---F 523
Cdd:cd14875   294 ACRLLQLDPAKLRECFLVK--------SKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITPQGDCSgckY 365

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  524 VGVLDVAGFEFYAKNSFEQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEFIDNQDCIELFELKGNGLFDLLDE 603
Cdd:cd14875   366 IGLLDIFGFENFTRNSFEQLCINYANESLQNHYNKYTFINDEEECRREGIQIPKIEFPDNSECVNMFDQKRTGIFSMLDE 445

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  604 EAKFPTSNYKSFTKRAHEENRKHFRLDTPRKSKVKSHrelrddegLLIRHYAGSVCYETKHFVEKNDDLLHNSLQILIEQ 683
Cdd:cd14875   446 ECNFKGGTTERFTTNLWDQWANKSPYFVLPKSTIPNQ--------FGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSN 517

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  684 STIRLLVSLFGSTAYPTKSKlkaLSVGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGSAILSQLQCAGMTSV 763
Cdd:cd14875   518 STDEFIRTLLSTEKGLARRK---QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQT 594

                         650
                  ....*....|.
gi 808358096  764 LKLMQDGFPSR 774
Cdd:cd14875   595 IALKRQGYPVR 605
MYSc_Myo25 cd14886
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ...
 143-825 8.63e-113

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: 368.06  E-value: 8.63e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  143 ATLLNNIRLRYQNGKIYSYVANILISINPYQTIDGFYSLQKIKEYRG--KSLG---QKEPHIFAIADKSYREMIRHRKSQ 217
Cdd:cd14886     1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRNLYGTEVIGRYRQadTSRGfpsDLPPHSYAVAQSALNGLISDGISQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  218 SIIVSGESGAGKTESQKAVLRYLCENWGSGAGEIQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFADTGNVAGGY 297
Cdd:cd14886    81 SCIVSGESGAGKTETAKQLMNFFAYGHSTSSTDVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGLKGGK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  298 VSHYLLETSRICRQAAGERNYHIFYQLIAGSSPELFKFLALGQPNQFNYLKRGfigffthpssgttskipknrlsdpKFT 377
Cdd:cd14886   161 ITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNAS------------------------KCY 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  378 QDSMVDDFSDFQRLEYALKLTgLSEQEIHFIWTTIAAILHLGNVEFEESLDD-SRGGCKVFNGSeqDLIQAARLLGLETm 456
Cdd:cd14886   217 DAPGIDDQKEFAPVRSQLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDMgVINAAKISNDE--DFGKMCELLGIES- 292

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  457 elkmGLCARIMQTTKGGARGTLIRVPLKPHEACSGRDALSKAIYSKLFDWLVSRINDSIPFEK-STNFVGVLDVAGFEFY 535
Cdd:cd14886   293 ----SKAAQAIITKVVVINNETIISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDAdARPWIGILDIYGFEFF 368

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  536 AKNSFEQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEFIDNQDCIELFELKGNGLFDLLDEEAKFPTSNYKSF 615
Cdd:cd14886   369 ERNTYEQLLINYANERLQQYFINQVFKSEIQEYEIEGIDHSMITFTDNSNVLAVFDKPNLSIFSFLEEQCLIQTGSSEKF 448

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  616 TKRAheenrkhfrldtprKSKVKSHRELRDDEGLL---IRHYAGSVCYETKHFVEKNDDLLHNSLQILIEQSTIRLLVSL 692
Cdd:cd14886   449 TSSC--------------KSKIKNNSFIPGKGSQCnftIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKA 514

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  693 FGSTAYPTkSKLKALSVGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGSAILSQLQCAGMTSVLKLMQDGFP 772
Cdd:cd14886   515 FSDIPNED-GNMKGKFLGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFA 593

                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 808358096  773 SRTGF------GDLYACYQKKLPPKLSklDPRMFCKCLFRALGLDQHDFQFGLTKVFFR 825
Cdd:cd14886   594 YNDTFeeffhrNKILISHNSSSQNAGE--DLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
MYSc_Myo17 cd14879
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ...
 140-824 2.75e-111

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: 363.79  E-value: 2.75e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  140 LNEATLLNNIRLRYQNGKIYSYV-ANILISINPYQTI----DGfySLQKIKE-YRGKSLGQKE---PHIFAIADKSYREM 210
Cdd:cd14879     1 PSDDAITSHLASRFRSDLPYTRLgSSALVAVNPYKYLssnsDA--SLGEYGSeYYDTTSGSKEplpPHAYDLAARAYLRM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  211 IRHRKSQSIIVSGESGAGKTESQKAVLRYLCE--NWGSGAGEIQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFA 288
Cdd:cd14879    79 RRRSEDQAVVFLGETGSGKSESRRLLLRQLLRlsSHSKKGTKLSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQFN 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  289 DTGNVAGGYVSHYLLETSRICRQAAGERNYHIFYQLIAGSSPELFKFLALGQPNQFNYLKRGfigfFTHPSSGTTSkipk 368
Cdd:cd14879   159 ERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLASY----GCHPLPLGPG---- 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  369 nrlsdpkftqdsmVDDFSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEESLDDSRGGCKVFNGSEqdLIQAA 448
Cdd:cd14879   231 -------------SDDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFTYDHEGGEESAVVKNTDV--LDIVA 295

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  449 RLLGLETMELKMGLcarimqttkgGARGTLIR-----VPLKPHEACSGRDALSKAIYSKLFDWLVSRINDSI--PFEKST 521
Cdd:cd14879   296 AFLGVSPEDLETSL----------TYKTKLVRkelctVFLDPEGAAAQRDELARTLYSLLFAWVVETINQKLcaPEDDFA 365

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  522 NFVGVLDVAGFEFYAK---NSFEQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEFIDNQDCIELFELKGNGLF 598
Cdd:cd14879   366 TFISLLDFPGFQNRSStggNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSYFDNSDCVRLLRGKPGGLL 445

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  599 DLLDEEAkfptsnyKSFTKRA----HEENRKHFRLDTPRKSKVKSHRelRDDEGL-LIRHYAGSVCYETKHFVEKNDDLL 673
Cdd:cd14879   446 GILDDQT-------RRMPKKTdeqmLEALRKRFGNHSSFIAVGNFAT--RSGSASfTVNHYAGEVTYSVEGFLERNGDVL 516

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  674 hnslqilieqSTirLLVSLFGSTayptksklkalsvgAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGSAILS 753
Cdd:cd14879   517 ----------SP--DFVNLLRGA--------------TQLNAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKA 570

                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808358096  754 QLQCAGMTSVLKLMQDGFPSRTGFGDLYACYQKKLPPKlsklDPRMFCKCLFRALGLDQHDFQFGLTKVFF 824
Cdd:cd14879   571 QIRSLGLPELAARLRVEYVVSLEHAEFCERYKSTLRGS----AAERIRQCARANGWWEGRDYVLGNTKVFL 637
MYSc_Myo26 cd14887
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ...
 143-825 1.69e-108

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: 358.58  E-value: 1.69e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  143 ATLLNNIRLRY--------QNGKIYSYVANILISINPYQTIDgFYSLQKIKEYRGKSLGQKEPHIFAIADKSYREMIRHR 214
Cdd:cd14887     1 PNLLENLYQRYnkayinkeNRNCIYTYTGTLLIAVNPYRFFN-LYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  215 KSQSIIVSGESGAGKTESQKAVLRYLC----ENWGSGAGEIQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFADT 290
Cdd:cd14887    80 RSQSILISGESGAGKTETSKHVLTYLAavsdRRHGADSQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  291 GNVAGGYVSHYLLETSRICRQAAGERNYHIFYQLI-AGSSPELFKFLALgqpNQFNYLkrgfigffthpssgttskipkn 369
Cdd:cd14887   160 GKLTRASVATYLLANERVVRIPSDEFSFHIFYALCnAAVAAATQKSSAG---EGDPES---------------------- 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  370 rlsdpkftqdsmvddfSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEESLDDSRG----------------- 432
Cdd:cd14887   215 ----------------TDLRRITAAMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSkkrkltsvsvgceetaa 278

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  433 -------------GCKVFNGSEQDLIQAARLLGLETM-----ELKMGLCARIMQTTkggargtliRVPLKPHEACSGRDA 494
Cdd:cd14887   279 drshssevkclssGLKVTEASRKHLKTVARLLGLPPGvegeeMLRLALVSRSVRET---------RSFFDLDGAAAARDA 349

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  495 LSKAIYSKLFDWLVSRINDS---------------IPFEKSTNFVGVLDVAGFEFY---AKNSFEQFCINFCNEKLQNFF 556
Cdd:cd14887   350 ACKNLYSRAFDAVVARINAGlqrsakpsesdsdedTPSTTGTQTIGILDLFGFEDLrnhSKNRLEQLCINYANERLHCFL 429

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  557 NQRILREEQELYEKEGLNVRKIEFIDNQDCIELFELK----------GNGLFDLLDEEAKFPT--SNYKSFTKR-----A 619
Cdd:cd14887   430 LEQLILNEHMLYTQEGVFQNQDCSAFPFSFPLASTLTsspsstspfsPTPSFRSSSAFATSPSlpSSLSSLSSSlssspP 509

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  620 HEENRKHFRLDTPRKSK--------VKSHREL-RDDEGLLIRHYAGSVCYETKHFVEKNDDLLHNSLQILIEQST--IRL 688
Cdd:cd14887   510 VWEGRDNSDLFYEKLNKniinsakyKNITPALsRENLEFTVSHFACDVTYDARDFCRANREATSDELERLFLACStyTRL 589

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  689 LVSLFGSTAYPTKSKLKALSvgAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGSAILSQLQCAGMTSVLKLMQ 768
Cdd:cd14887   590 VGSKKNSGVRAISSRRSTLS--AQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMA 667

                         730       740       750       760       770
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 808358096  769 DGFPSRTGFGDLYACYQKKLPPKLSK-LDPRMFCKCLFRALGLDQHDFQFGLTKVFFR 825
Cdd:cd14887   668 DGFPCRLPYVELWRRYETKLPMALREaLTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
MYSc_Myo38 cd14899
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ...
 143-788 4.63e-108

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: 357.48  E-value: 4.63e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  143 ATLLNNIRLRYQNGKIYSYVANILISINPYQTIDGFYSLQKIKEY----------RGKSLGQKEPHIFAIADKSYREMIR 212
Cdd:cd14899     1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPQLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  213 HRKSQSIIVSGESGAGKTESQKAVLRYLCENWGSGA-----------------GEIQKRLLETNPILEAFGNAKTLRNNN 275
Cdd:cd14899    81 NGRSQSILISGESGAGKTEATKIIMTYFAVHCGTGNnnltnsesisppaspsrTTIEEQVLQSNPILEAFGNARTVRNDN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  276 SSRFGKFVQIHFADTG-NVAGGYVSHYLLETSRICRQAAGERNYHIFYQLIAGS----SPELFKFLAL-GQPNQFNYLKR 349
Cdd:cd14899   161 SSRFGKFIELRFRDERrRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSADnncvSKEQKQVLALsGGPQSFRLLNQ 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  350 gfigffthpssgttSKIPKNRlsdpkftqdSMVDDFSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEES--- 426
Cdd:cd14899   241 --------------SLCSKRR---------DGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQIphk 297

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  427 ------LDDSRGGCKVfNGSEQDLIQAARLLGLETMELKMGLCARIMQttkggARGTLIRVPLKPHEACSGRDALSKAIY 500
Cdd:cd14899   298 gddtvfADEARVMSST-TGAFDHFTKAAELLGVSTEALDHALTKRWLH-----ASNETLVVGVDVAHARNTRNALTMECY 371

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  501 SKLFDWLVSRIND------SIPF----------EKSTNFVGVLDVAGFEFYAKNSFEQFCINFCNEKLQNFFNQRILREE 564
Cdd:cd14899   372 RLLFEWLVARVNNklqrqaSAPWgadesdvddeEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEE 451

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  565 QELYEKEGLNVRKIEFIDNQDCIELFELKGNGLFDLLDEEAKFPTSNYKSFTKRAHEENRK-----HFRldtprkskvkS 639
Cdd:cd14899   452 QRLYRDEGIRWSFVDFPNNRACLELFEHRPIGIFSLTDQECVFPQGTDRALVAKYYLEFEKknshpHFR----------S 521

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  640 HRELRDDEGLLIRHYAGSVCYETKHFVEKNDDLLHNSLQILIEQSTIRLLVSL------------------FGSTAYPTK 701
Cdd:cd14899   522 APLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFCESAAQLLAGSSNPLIQALaagsndedangdseldgfGGRTRRRAK 601

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  702 SKLKALSVGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGSAILSQLQCAGMTSVLKLMQDGFPSRTGFGDLY 781
Cdd:cd14899   602 SAIAAVSVGTQFKIQLNELLSTVRATTPRYVRCIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFL 681


                  ....*..
gi 808358096  782 ACYQKKL 788
Cdd:cd14899   682 GRYRRVL 688
MYSc_Myo24A cd14937
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ...
 143-755 1.59e-94

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: 317.73  E-value: 1.59e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  143 ATLLNNIRLRYQNGKIYSYVANILISINPYQTIDgfyslQKIKEYRGKSLGQKEPHIFAIADKSYREMIRHRKSQSIIVS 222
Cdd:cd14937     1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVID-----VDINEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIIS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  223 GESGAGKTESQKAVLRYlcenWGSGA---GEIQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFADTGNVAGGYVS 299
Cdd:cd14937    76 GESGSGKTEASKLVIKY----YLSGVkedNEISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSIE 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  300 HYLLETSRICRQAAGERNYHIFYQLIAGSSPELFKFLALGQPNQFNYLkrgfigffthpsSGTTSKIPKnrlsdpkftqd 379
Cdd:cd14937   152 IFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYI------------VNKNVVIPE----------- 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  380 smVDDFSDFQRLEYALKLTGLSEQEIHfIWTTIAAILHLGNVEFEESLDDSRGGCKVFNGSEQDLI-QAARLLGLETMEL 458
Cdd:cd14937   209 --IDDAKDFGNLMISFDKMNMHDMKDD-LFLTLSGLLLLGNVEYQEIEKGGKTNCSELDKNNLELVnEISNLLGINYENL 285

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  459 KMglCARIMQTTKGGARgtlIRVPLKPHEACSGRDALSKAIYSKLFDWLVSRINDSIPFEKS-TNFVGVLDVAGFEFYAK 537
Cdd:cd14937   286 KD--CLVFTEKTIANQK---IEIPLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNKElNNYIGILDIFGFEIFSK 360

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  538 NSFEQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEFIDNQDCIELfeLKGN-GLFDLLDEEAKFPTSNYKSFT 616
Cdd:cd14937   361 NSLEQLLINIANEEIHSIYLYIVYEKETELYKAEDILIESVKYTTNESIIDL--LRGKtSIISILEDSCLGPVKNDESIV 438

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  617 KRAHEENRKHFRLDTPRKSKVKShrelrddegLLIRHYAGSVCYETKHFVEKNDDLLHNSLQILIEQSTIRLLVSLFGST 696
Cdd:cd14937   439 SVYTNKFSKHEKYASTKKDINKN---------FVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDV 509

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 808358096  697 AYPTKSKLKALsVGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGSAILSQL 755
Cdd:cd14937   510 EVSESLGRKNL-ITFKYLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQL 567
MYSc_Myo23 cd14884
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ...
 143-794 4.32e-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: 312.23  E-value: 4.32e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  143 ATLLNNIRLRYQNGKIYSYVANILISINPYQTIDGFYSLQKIKEYRGKSLGQK-------EPHIFAIADKSYREMIRHRK 215
Cdd:cd14884     1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKELYDQDVMNVYLHKKSNSAasaapfpKAHIYDIANMAYKNMRGKLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  216 SQSIIVSGESGAGKTESQKAVLRYLCENWG-SGAGEIQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFADTGNVA 294
Cdd:cd14884    81 RQTIVVSGHSGSGKTENCKFLFKYFHYIQTdSQMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFEEVENTQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  295 GGYVSH---------YLLETSRICRQAAGERNYHIFYQLIAGSSPELF---------KFLALGQPNQFNYlKRGfigfft 356
Cdd:cd14884   161 KNMFNGcfrnikikiLLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLarrnlvrncGVYGLLNPDESHQ-KRS------ 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  357 hpSSGTTSKIPKNRlsdpKFTQDSMVDDFSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNvefeeslDDSRGGCKV 436
Cdd:cd14884   234 --VKGTLRLGSDSL----DPSEEEKAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGN-------RAYKAAAEC 300

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  437 FNGSEQDLIQAARLLGLETmelkmglcarimqttkggaRGTLIRVPLKPHEACSGRDALSKAIYSKLFDWLVSRINDSIP 516
Cdd:cd14884   301 LQIEEEDLENVIKYKNIRV-------------------SHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVL 361

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  517 FEKST-------------NFVGVLDVAGFEFYAKNSFEQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEFIDN 583
Cdd:cd14884   362 KCKEKdesdnediysineAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAPSY 441

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  584 QDCIELFElkgnGLFDLLDEEAKFPTSNYK-----------SFTKRAHEENRKHFRLDTPRKSKVKSHRELRDDEGLLIR 652
Cdd:cd14884   442 SDTLIFIA----KIFRRLDDITKLKNQGQKktddhffryllNNERQQQLEGKVSYGFVLNHDADGTAKKQNIKKNIFFIR 517

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  653 HYAGSVCYETKHFVEKNDDLLHNSLQILIEQSTIRLLvslfgSTAYPTKSKLKALSVGAKFKNQLSTLLIKLESTGTHFV 732
Cdd:cd14884   518 HYAGLVTYRINNWIDKNSDKIETSIETLISCSSNRFL-----REANNGGNKGNFLSVSKKYIKELDNLFTQLQSTDMYYI 592

                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808358096  733 RCIKPNNQMIPFEFDGSAILSQLQCAGMTSVLKLMQDGFPSRTGFGDLYACYQKKLPPKLSK 794
Cdd:cd14884   593 RCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKETAAALKEQIAKELEK 654
MYSc_Myo37 cd14898
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ...
 144-772 3.32e-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: 301.05  E-value: 3.32e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  144 TLLNNIRLRYQNGKIYSYVANILISINPYQTIDGFYSlqkiKEYRGKSLGQKEPHIFAIADKSYREMIRHrKSQSIIVSG 223
Cdd:cd14898     2 ATLEILEKRYASGKIYTKSGLVFLALNPYETIYGAGA----MKAYLKNYSHVEPHVYDVAEASVQDLLVH-GNQTIVISG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  224 ESGAGKTESQKAVLRYLCENwGSGAGEIQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFadTGNVAGGYVSHYLL 303
Cdd:cd14898    77 ESGSGKTENAKLVIKYLVER-TASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKF--DGKITGAKFETYLL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  304 ETSRICRQAAGERNYHIFYQLIAGSspelfkflalgqpnQFNyLKRGFIGFFTHPSSgttskipknrlsdpkftQDSMVD 383
Cdd:cd14898   154 EKSRVTHHEKGERNFHIFYQFCASK--------------RLN-IKNDFIDTSSTAGN-----------------KESIVQ 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  384 DFSDFQRLEYALKLTGLSeqEIHFIWTTIAAILHLGNVEFeeslddSRGGCKVFNGSEQdLIQAARLLGLETMELKMGLC 463
Cdd:cd14898   202 LSEKYKMTCSAMKSLGIA--NFKSIEDCLLGILYLGSIQF------VNDGILKLQRNES-FTEFCKLHNIQEEDFEESLV 272

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  464 ARIMQTtkggaRGTLIRVPLKPHEACSGRDALSKAIYSKLFDWLVSRINDSIPfEKSTNFVGVLDVAGFEFYAKNSFEQF 543
Cdd:cd14898   273 KFSIQV-----KGETIEVFNTLKQARTIRNSMARLLYSNVFNYITASINNCLE-GSGERSISVLDIFGFEIFESNGLDQL 346

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  544 CINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEFIDNQDCIELFElKGNGLFDLLDEEAKFPTSNYKSFTKRAHEEN 623
Cdd:cd14898   347 CINWTNEKIQNDFIKKMFRAKQGMYKEEGIEWPDVEFFDNNQCIRDFE-KPCGLMDLISEESFNAWGNVKNLLVKIKKYL 425

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  624 RKhfRLDTPRKSKVKshrelrddegllIRHYAGSVCYETKHFVEKNDdllhnslqiliEQSTIRLLVSLFGSTAYPTKSK 703
Cdd:cd14898   426 NG--FINTKARDKIK------------VSHYAGDVEYDLRDFLDKNR-----------EKGQLLIFKNLLINDEGSKEDL 480

                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 808358096  704 LKAlsvgakFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGSAILSQLQCAGMTSVLKLMQDGFP 772
Cdd:cd14898   481 VKY------FKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFP 543
MYSc_Myo16 cd14878
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ...
 143-825 2.62e-87

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: 297.88  E-value: 2.62e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  143 ATLLNNIRLRYQNGKIYSYVANILISINPYQTIDgFYSLQKIKEYR---GKSLGQKEPHIFAIADKSYREMIRHRKSQSI 219
Cdd:cd14878     1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  220 IVSGESGAGKTESQKAVLRYLCENWGSGAGEIQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFAD-TGNVAGGYV 298
Cdd:cd14878    80 ILSGERGSGKTEASKQIMKHLTCRASSSRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFCErKKHLTGARI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  299 SHYLLETSRICRQAAGERNYHIFYQLIAGSSPELFKFLALGQPNQFNYLKRGFigffthPSSGTTSKIPKNRlsdpkftq 378
Cdd:cd14878   160 YTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTM------REDVSTAERSLNR-------- 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  379 dsmvddfSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFeESLDDSRggcKVFNGSEQDLIQAARLLGLETMEL 458
Cdd:cd14878   226 -------EKLAVLKQALNVVGFSSLEVENLFVILSAILHLGDIRF-TALTEAD---SAFVSDLQLLEQVAGMLQVSTDEL 294

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  459 KMGLCARImQTTKGgargtliRVPLKPHE---ACSGRDALSKAIYSKLFDWLVSRIN-----DSIPFEKSTNFVGVLDVA 530
Cdd:cd14878   295 ASALTTDI-QYFKG-------DMIIRRHTiqiAEFYRDLLAKSLYSRLFSFLVNTVNcclqsQDEQKSMQTLDIGILDIF 366

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  531 GFEFYAKNSFEQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEFIDNQDCI-ELFELKGNGLFDLLDEEAKFPT 609
Cdd:cd14878   367 GFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLQEQTECVQEGVTMETAYSPGNQTGVlDFFFQKPSGFLSLLDEESQMIW 446

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  610 SNYKSFTKRAHEEnrkhfrLDTPRKSKVKShrELRDDEG----------LLIRHYAGSVCYETKHFVEKNDDLLHNSLQI 679
Cdd:cd14878   447 SVEPNLPKKLQSL------LESSNTNAVYS--PMKDGNGnvalkdqgtaFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLF 518

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  680 LIEQSTIRLLVSLFGStayptksklKALSVGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGSAILSQLQCAG 759
Cdd:cd14878   519 VMKTSENVVINHLFQS---------KLVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIG 589

                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 808358096  760 MTSVLKLMQDGFPSRTGFGDLYACYQ---KKLPPKLSKLDPRMFCKCLFRALGLdqHDFQFGLTKVFFR 825
Cdd:cd14878   590 VLEMVKIFRYGYPVRLSFSDFLSRYKplaDTLLGEKKKQSAEERCRLVLQQCKL--QGWQMGVRKVFLK 656
MYSc_Myo18 cd01386
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ...
 143-825 9.93e-84

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: 288.82  E-value: 9.93e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  143 ATLLNNIRLRYQNGKIYSYVANILISINPyQTIDGFYSLQKIKEYRGKSLGQKEPHIFAIADKSYREMIRHRKSQSIIVS 222
Cdd:cd01386     1 SSVLHTLRQRYGANLIHTYAGPSLIVINP-RHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  223 GESGAGKTESQKAVLRYLCENWGSGAGEIQKRLLE-TNPILEAFGNAKTLRNNNSSRFGKFVQIHFADTGNVAGGYVSHY 301
Cdd:cd01386    80 GRSGSGKTTNCRHILEYLVTAAGSVGGVLSVEKLNaALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASIQTL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  302 LLETSRICRQAAGERNYHIFYQLIAGSSPELFKFLALGQPNQFNylkrgfiGFFTHPSSGTTSKipknrlsdpkftQDSM 381
Cdd:cd01386   160 LLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAESN-------SFGIVPLQKPEDK------------QKAA 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  382 VddfsDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVefeeslddsrGGCKVFNGSEQDLI------QAARLLGLET 455
Cdd:cd01386   221 A----AFSKLQAAMKTLGISEEEQRAIWSILAAIYHLGAA----------GATKAASAGRKQFArpewaqRAAYLLGCTL 286

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  456 MEL-----KMGLCARIMQTTKGGARGTLIRVPL-KPHEacSGRDAL---SKAIYSKLFDWLVSRINDSI-PFEKSTNFVG 525
Cdd:cd01386   287 EELssaifKHHLSGGPQQSTTSSGQESPARSSSgGPKL--TGVEALegfAAGLYSELFAAVVSLINRSLsSSHHSTSSIT 364

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  526 VLDVAGFEFYAKN------SFEQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVrkiEFIDNQDC------------- 586
Cdd:cd01386   365 IVDTPGFQNPAHSgsqrgaTFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEV---DFDLPELSpgalvalidqapq 441

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  587 -----IELFELKGNGLFDLLDEEAKFPTSNYKSFTKR--AHEENRKHFRLDTPRKSKVKSHrelrddeGLLIRHYAGS-- 657
Cdd:cd01386   442 qalvrSDLRDEDRRGLLWLLDEEALYPGSSDDTFLERlfSHYGDKEGGKGHSLLRRSEGPL-------QFVLGHLLGTnp 514

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  658 VCYETKHFVEKnddllhnSLQILIEQSTIRLLVSLFGSTAYPTKsklKALSVGAKFknQLSTLLIKLESTGTHFVRCIKP 737
Cdd:cd01386   515 VEYDVSGWLKA-------AKENPSAQNATQLLQESQKETAAVKR---KSPCLQIKF--QVDALIDTLRRTGLHFVHCLLP 582

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  738 N------------NQMIPFEFDGSAILSQLQCAGMTSVLKLMQDGFPSRTGFGDLYACYQ-------KKLPPKLSKLDPR 798
Cdd:cd01386   583 QhnagkderstssPAAGDELLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQvlappltKKLGLNSEVADER 662

                         730       740
                  ....*....|....*....|....*..
gi 808358096  799 MFCKCLFRALGLDQHDFQFGLTKVFFR 825
Cdd:cd01386   663 KAVEELLEELDLEKSSYRIGLSQVFFR 689
MYSc_Myo20 cd14881
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ...
 152-777 1.28e-80

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: 278.54  E-value: 1.28e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  152 RYQNGKIYSYVANILISINPYQtidgfyslqkikeYRGKSLGQKEPHIFAIA---DKSYREMIRHRK----SQSIIVSGE 224
Cdd:cd14881    10 RFYAKEFFTNVGPILLSVNPYR-------------DVGNPLTLTSTRSSPLApqlLKVVQEAVRQQSetgyPQAIILSGT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  225 SGAGKTESQKAVLRYLCENWGSGA-GEIQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFADtGNVAGGYVSHYLL 303
Cdd:cd14881    77 SGSGKTYASMLLLRQLFDVAGGGPeTDAFKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQVTD-GALYRTKIHCYFL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  304 ETSRICRQAAGERNYHIFYQLIAGSSPELFKFLALG--QPNQFNYLKRGfigffthpssgttskipknrlsdpKFTQDSM 381
Cdd:cd14881   156 DQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDgySPANLRYLSHG------------------------DTRQNEA 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  382 vDDFSDFQRLEYALKLTGlseqeIHF--IWTTIAAILHLGNVEFEEslddsRGGCKVFNGSEQDLIQAARLLGLETMELK 459
Cdd:cd14881   212 -EDAARFQAWKACLGILG-----IPFldVVRVLAAVLLLGNVQFID-----GGGLEVDVKGETELKSVAALLGVSGAALF 280

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  460 MGLCARimqtTKGgARGTLIRVPLKPHEACSGRDALSKAIYSKLFDWLVSRIND------SIPFEKSTNFVGVLDVAGFE 533
Cdd:cd14881   281 RGLTTR----THN-ARGQLVKSVCDANMSNMTRDALAKALYCRTVATIVRRANSlkrlgsTLGTHATDGFIGILDMFGFE 355

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  534 FYAKNSFEQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVR-KIEFIDNQDCIELFELKGNGLFDLLDEEAKfPTSNY 612
Cdd:cd14881   356 DPKPSQLEHLCINLCAETMQHFYNTHIFKSSIESCRDEGIQCEvEVDYVDNVPCIDLISSLRTGLLSMLDVECS-PRGTA 434

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  613 KSFTKRAHEENRKHFRLDTPRKSkvkshrelrDDEGLLIRHYAGSVCYETKHFVEKNDDLLHNSlqilieqstirlLVSL 692
Cdd:cd14881   435 ESYVAKIKVQHRQNPRLFEAKPQ---------DDRMFGIRHFAGRVVYDASDFLDTNRDVVPDD------------LVAV 493

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  693 FgstaYPTKSKLKALSVGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGSAILSQLQCAGMTSVLKLMQDGFP 772
Cdd:cd14881   494 F----YKQNCNFGFATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYP 569


                  ....*
gi 808358096  773 SRTGF 777
Cdd:cd14881   570 HRMRF 574
MYSc_Myo21 cd14882
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ...
 144-785 4.74e-76

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: 265.45  E-value: 4.74e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  144 TLLNNIRLRYQNGKIYSYVANILISINPYQTIDgFYSLQKIKEYRGKSLGQKEPHIFAIADKSYREMIRHRKSQSIIVSG 223
Cdd:cd14882     2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQ-EYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  224 ESGAGKTESQKAVLRYLCeNWGSGAGEIQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFADTGNVAGGYVSHYLL 303
Cdd:cd14882    81 ESYSGKTTNARLLIKHLC-YLGDGNRGATGRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFWMYQL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  304 ETSRICRQAAGERNYHIFYQLIAG-SSPELFKFLALGQPNQFNYLKrgfigffthpssgTTSKIPKNRLsdpKFTQDSMV 382
Cdd:cd14882   160 EKLRVSTTDGNQSNFHIFYYFYDFiEAQNRLKEYNLKAGRNYRYLR-------------IPPEVPPSKL---KYRRDDPE 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  383 DDFSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEES-----LDDSRGGCKVfngseqdliqaARLLGLETME 457
Cdd:cd14882   224 GNVERYKEFEEILKDLDFNEEQLETVRKVLAAILNLGEIRFRQNggyaeLENTEIASRV-----------AELLRLDEKK 292

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  458 LKMGLCARIMQTtkggaRGTLIRVPLKPHEACSGRDALSKAIYSKLFDWLVSRINDSIPFEKS----TNFVGVLDVAGFE 533
Cdd:cd14882   293 FMWALTNYCLIK-----GGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSFPRAvfgdKYSISIHDMFGFE 367

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  534 FYAKNSFEQFCINFCNEKLQNFFNQRILREEQELYEKEGLNVRKIEFIDNQDCIELFELKGNGLFDLLDEEAK-FPTSNY 612
Cdd:cd14882   368 CFHRNRLEQLMVNTLNEQMQYHYNQRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPDGLFYIIDDASRsCQDQNY 447

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  613 ksFTKRAHEENRKHFRldtprksKVKSHRelrddegLLIRHYAGSVCYETKHFVEKNDDLL------------HNSLQIL 680
Cdd:cd14882   448 --IMDRIKEKHSQFVK-------KHSAHE-------FSVAHYTGRIIYDAREFADKNRDFVppemietmrsslDESVKLM 511

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  681 IEQSTIRLLVSLFGSTAYPTKSKLKALSVGAKfknqlstllikleSTGTHFVRCIKPNNQMIPFEFDGSAILSQLQCAGM 760
Cdd:cd14882   512 FTNSQVRNMRTLAATFRATSLELLKMLSIGAN-------------SGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAV 578

                         650       660
                  ....*....|....*....|....*
gi 808358096  761 TSVLKLMQDGFPSRTGFGDLYACYQ 785
Cdd:cd14882   579 LDTAKARQKGFSYRIPFQEFLRRYQ 603
MYSc_Myo12 cd14874
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ...
 143-825 3.56e-71

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: 250.94  E-value: 3.56e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  143 ATLLNNIRLRYQNGKIYSYVANILISINPYQTIDGFyslqkikeyrgKSLGQKEPHIFAIADKSYREMIRHR-KSQSIIV 221
Cdd:cd14874     1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQ-----------DQLVIKKCHISGVAENALDRIKSMSsNAESIVF 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  222 SGESGAGKTESQKAVLRYLCENWGSGAGEIQKRLLETnpILEAFGNAKTLRNNNSSRFGKFVQIHFADtgNVAGGYVSHY 301
Cdd:cd14874    70 GGESGSGKSYNAFQVFKYLTSQPKSKVTTKHSSAIES--VFKSFGCAKTLKNDEATRFGCSIDLLYKR--NVLTGLNLKY 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  302 L--LETSRICRQAAGERNYHIFYQLIAGSSPELFKFLALGQPNQFNYLKRGfigffthpssgttskipknrlsdpkFTQD 379
Cdd:cd14874   146 TvpLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQG-------------------------NSTE 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  380 SMVDDFSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEESLDDSRGGCKVFNGSEQDLIQAARLLGLETMELK 459
Cdd:cd14874   201 NIQSDVNHFKHLEDALHVLGFSDDHCISIYKIISTILHIGNIYFRTKRNPNVEQDVVEIGNMSEVKWVAFLLEVDFDQLV 280

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  460 MGLCARimqttkggargTLIRVPLKPHEACSGRDALSKAIYSKLFDWLVSRINDSIPFEKSTNFVGVLDVAGFEFYAKNS 539
Cdd:cd14874   281 NFLLPK-----------SEDGTTIDLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGVISILDHYGFEKYNNNG 349

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  540 FEQFCINFCNEKLQNFFNQRILREEQELYEKEGLNV--RKIEFIDNQDCIELFELKGNGLFDLLDEEAKFPTSNYKSFTK 617
Cdd:cd14874   350 VEEFLINSVNERIENLFVKHSFHDQLVDYAKDGISVdyKVPNSIENGKTVELLFKKPYGLLPLLTDECKFPKGSHESYLE 429

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  618 RAheeNRKHfrldTPRKSKVKSHRELRDDEGllIRHYAGSVCYETKHFVEKNDDLLHNSLQILIEQSTIRLLVSLFGSTA 697
Cdd:cd14874   430 HC---NLNH----TDRSSYGKARNKERLEFG--VRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESYS 500

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  698 YPTKSKLkaLSVGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGSAILSQLQCAGMTSVLKLMQDGFP---SR 774
Cdd:cd14874   501 SNTSDMI--VSQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPvkiSK 578

                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|...
gi 808358096  775 TGFGDLYACYqkkLPPKLSKL-DPRMFCKCLFRALGLD-QHDFQFGLTKVFFR 825
Cdd:cd14874   579 TTFARQYRCL---LPGDIAMCqNEKEIIQDILQGQGVKyENDFKIGTEYVFLR 628
MYSc_Myo44 cd14905
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ...
 144-771 8.05e-69

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: 245.39  E-value: 8.05e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  144 TLLNNIRLRYQNGKIYSYVANILISINPYQTIDGFYSLQKIKEYRGKSlgQKEPHIFAIADKSYREMIRHRKSQSIIVSG 223
Cdd:cd14905     2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPFLHSQELVRNYNQRR--GLPPHLFALAAKAISDMQDFRRDQLIFIGG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  224 ESGAGKTESQKAVLRYLCENWGSGAGEIQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFADTGNVAGGYVSHYLL 303
Cdd:cd14905    80 ESGSGKSENTKIIIQYLLTTDLSRSKYLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKLYSYFL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  304 ETSRICRQAAGERNYHIFYQLIAGSSPELFKFLALGQPNQFNYLKRGfigffthpSSGTTSKIPKNRLsdpkftqdsmvd 383
Cdd:cd14905   160 DENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQG--------GSISVESIDDNRV------------ 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  384 dfsdFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVEFEEslddSRGGCKVfngSEQDLIQA-ARLLGLETMELKmgl 462
Cdd:cd14905   220 ----FDRLKMSFVFFDFPSEKIDLIFKTLSFIIILGNVTFFQ----KNGKTEV---KDRTLIESlSHNITFDSTKLE--- 285

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  463 caRIMQTTKGgargtlirVPLkpHEACSGRDALSKAIYSKLFDWLVSRINDSIPFEKSTNFVGVLDVAGFEFYAKNSFEQ 542
Cdd:cd14905   286 --NILISDRS--------MPV--NEAVENRDSLARSLYSALFHWIIDFLNSKLKPTQYSHTLGILDLFGQESSQLNGYEQ 353

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  543 FCINFCNEKLQNFFNQRILREEQELYEKEGLN-VRKIEFIDNQDCIELFElkgnGLFDLLDEEAKFPTSNYKSFTKRAHE 621
Cdd:cd14905   354 FSINFLEERLQQIYLQTVLKQEQREYQTERIPwMTPISFKDNEESVEMME----KIINLLDQESKNINSSDQIFLEKLQN 429

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  622 -ENRKHFRLDTPRKskvkshrelrddegLLIRHYAGSVCYETKHFVEKNDDLLHNSLQILIEQSTIRLLVS--------- 691
Cdd:cd14905   430 fLSRHHLFGKKPNK--------------FGIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYLFSrdgvfnina 495

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  692 -------LFGSTAYPTKSKLKA----LSVGAKFKNQLS-----------------------TLLIKLESTGT-------- 729
Cdd:cd14905   496 tvaelnqMFDAKNTAKKSPLSIvkvlLSCGSNNPNNVNnpnnnsgggggggnsgggsgsggSTYTTYSSTNKainnsncd 575

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|...
gi 808358096  730 -HFVRCIKPNNQMIPFEFDGSAILSQLQCAGMTSVLKLMQDGF 771
Cdd:cd14905   576 fHFIRCIKPNSKKTHLTFDVKSVNEQIKSLCLLETTRIQRFGY 618
MYSc_Myo32 cd14893
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ...
 145-824 8.01e-64

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: 232.17  E-value: 8.01e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  145 LLNNIRLRYQNGKIYSYVANILISINPYQ-----TIDGFYSLQKIKE----YRGKSLGQKEPHIFAIADKSYREMIRHRK 215
Cdd:cd14893     3 ALYTLRARYRMEQVYTWVDRVLVGVNPVTplpiyTPDHMQAYNKSREqtplYEKDTVNDAPPHVFALAQNALRCMQDAGE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  216 SQSIIVSGESGAGKTESQKAVLRYLCEnWGSGAG-------------EIQKRLLETNPILEAFGNAKTLRNNNSSRFGKF 282
Cdd:cd14893    83 DQAVILLGGMGAGKSEAAKLIVQYLCE-IGDETEprpdsegasgvlhPIGQQILHAFTILEAFGNAATRQNRNSSRFAKM 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  283 VQIHFADTGNV-AGGYVSHYLlETSRICRQAAGERNYHIFYQLIAG--SSPELFKFLALGQ-PNQFNYLKRgfigffthp 358
Cdd:cd14893   162 ISVEFSKHGHViGGGFTTHYF-EKSRVIDCRSHERNFHVFYQVLAGvqHDPTLRDSLEMNKcVNEFVMLKQ--------- 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  359 ssgttskipknrlSDPKFTQDSM-VDDFSDFQRLEYALKLTGLSEQEIHFIwttIAAILHLGNVEFeesLDDSRGGCKVf 437
Cdd:cd14893   232 -------------ADPLATNFALdARDYRDLMSSFSALRIRKNQRVEIVRI---VAALLHLGNVDF---VPDPEGGKSV- 291

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  438 NGSEQDLIQ---------------AARLLGLETMELKMGLCARIMQTTKGGARGTLIRVpLKPHEACSGRDALSKAIYSK 502
Cdd:cd14893   292 GGANSTTVSdaqscalkdpaqillAAKLLEVEPVVLDNYFRTRQFFSKDGNKTVSSLKV-VTVHQARKARDTFVRSLYES 370

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  503 LFDWLVSRINDSI-----PFEKS-----TNFVGVLDVAGFEFY--AKNSFEQFCINFCNEKLQNFFNQRILREEQELYEK 570
Cdd:cd14893   371 LFNFLVETLNGILggifdRYEKSnivinSQGVHVLDMVGFENLtpSQNSFDQLCFNYWSEKVHHFYVQNTLAINFSFLED 450

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  571 EG------LNVRKIEFI--DNQDCIELFELKGNGLFDLLDEEAKFPTSNYKSFTKRAHEENRKHFRLDTPRKSKVKSHRE 642
Cdd:cd14893   451 ESqqvenrLTVNSNVDItsEQEKCLQLFEDKPFGIFDLLTENCKVRLPNDEDFVNKLFSGNEAVGGLSRPNMGADTTNEY 530

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  643 LRD--DEGLL--IRHYAGSVCYETKHFVEKN----------------DDLLH---------NSLQILIEQSTIRLLV-SL 692
Cdd:cd14893   531 LAPskDWRLLfiVQHHCGKVTYNGKGLSSKNmlsisstcaaimqsskNAVLHavgaaqmaaASSEKAAKQTEERGSTsSK 610

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  693 FGSTAYPTK-SKLKALSVGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIPFEFDGSAILSQLQcagMTSVLKLMQDG- 770
Cdd:cd14893   611 FRKSASSAReSKNITDSAATDVYNQADALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIR---MNHLVELMQASr 687

                         730       740       750       760       770       780
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  771 --FPSRTGFGDLYACYQkklppklSKLDPRMFCKCLFRALG----LDQHDFQFGLTKVFF 824
Cdd:cd14893   688 siFTVHLTYGHFFRRYK-------NVCGHRGTLESLLRSLSaigvLEEEKFVVGKTKVYL 740
CBD_MYO6-like cd21759
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, ...
 836-987 3.72e-46

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: 162.68  E-value: 3.72e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  836 MKQDPETMTSLIQKVNEWLVGARWKQSQYAVWSVIKLKNKIAWRSAQVTRLQSIARGYLTRQRFSRQIALYRKSVALLKN 915
Cdd:cd21759     1 MKSDPENLKELVKKVKKWLIRSRWRKAQWCALSVIKLKNKILYRREALIKIQKTVRGYLARKKHRPRIKGLRKIRALEKQ 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808358096  916 SKEIEKILFRLNEhSRAKYTSSAHSTIRDLEKLVSHIKltTSANDHFEKAENAYEHYVKRVDSMIADLKKQQ 987
Cdd:cd21759    81 LKEMEEIASQLKK-DKDKWTKQVKELKKEIDALIKKIK--TNDMITRKEIDKLYNALVKKVDKQLAELQKKL 149
MYSc_Myo24B cd14938
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ...
 144-787 6.31e-44

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: 171.56  E-value: 6.31e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  144 TLLNNIRLRYQNGKIYSYVANILISINPYQTIDgFYSLQKIKEYR----GKSLGQKEPHIFAIADKSYREMirhRKSQSI 219
Cdd:cd14938     2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNN-INNEETIEKYKcidcIEDLSLNEYHVVHNALKNLNEL---KRNQSI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  220 IVSGESGAGKTESQKAVLRYLC---------ENWGSGAGEIQKRLLETNP--------------ILEAFGNAKTLRNNNS 276
Cdd:cd14938    78 IISGESGSGKSEIAKNIINFIAyqvkgsrrlPTNLNDQEEDNIHNEENTDyqfnmsemlkhvnvVMEAFGNAKTVKNNNS 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  277 SRFGKFVQIHFaDTGNVAGGYVSHYLLETSRICRQAAGERNYHIFYQLIAGSSPELFKFLALGQPNQFNYLkrgfigfft 356
Cdd:cd14938   158 SRFSKFCTIHI-ENEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSML--------- 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  357 hpssgttskipKNRLSDPKFTQDSmvddfSDFQRLEYALKLTGLSEQEIHFIWTTIAAILHLGNVE-----FEESLDDSR 431
Cdd:cd14938   228 -----------NNEKGFEKFSDYS-----GKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTEivkafRKKSLLMGK 291

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  432 GGCKVFNGSEQDL--IQAARLLGLETMELKMGLCARIMQ----------TTKGGARGTLIrvpLKPHEACSGRDALS--- 496
Cdd:cd14938   292 NQCGQNINYETILseLENSEDIGLDENVKNLLLACKLLSfdietfvkyfTTNYIFNDSIL---IKVHNETKIQKKLEnfi 368

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  497 KAIYSKLFDWLVSRINDSIP----FEKSTNFVGVLDVAGFEFYAKNSFEQFCINFCNEKLQNFFNQRILREEQELYEKEG 572
Cdd:cd14938   369 KTCYEELFNWIIYKINEKCTqlqnININTNYINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDG 448

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  573 LNVR-KIEFIDNQDCIELFELKGNG-LFDLLDE---EAKFPTSNYKSFTKRAHEENRKHfrldtprkskVKSHRELRDDE 647
Cdd:cd14938   449 IFCEyNSENIDNEPLYNLLVGPTEGsLFSLLENvstKTIFDKSNLHSSIIRKFSRNSKY----------IKKDDITGNKK 518

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  648 GLLIRHYAGSVCYETKHFVEKNDDLLHNSLQILIEQSTIRLLVSLFGSTAYPT-------------KSKLKALSVGAKFK 714
Cdd:cd14938   519 TFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSENEYMRQFCMFYNYDNsgniveekrrysiQSALKLFKRRYDTK 598

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  715 NQLSTLLIK---------LESTGTHFVRCIKPN-NQMIPFEFDGSAILSQLQCAGMTSVLKLMQDGFPSRTGFGDLYACY 784
Cdd:cd14938   599 NQMAVSLLRnnlteleklQETTFCHFIVCMKPNeSKRELCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIF 678


                  ...
gi 808358096  785 QKK 787
Cdd:cd14938   679 DIK 681
Myosin-VI_CBD pfam16521
Myosin VI cargo binding domain; Myosin-VI_CBD is a C-terminal family that allows ...
 1180-1276 1.56e-42

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: 150.12  E-value: 1.56e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  1180 QRYFKCEFKENNQKGTcswgssikcEDLDQVSMWFVHFSGQQIQRQLTFTSSRPPQTLIAGRDDAQMCTLALQETLLVGK 1259
Cdd:pfam16521    1 QRYFRIPFVRPSDKKR---------DGGRKKGWWYAHFDGQWIARQMELHPDKPPVLLVAGKDDMQMCELSLEETGLTRK 71

                           90
                   ....*....|....*..
gi 808358096  1260 RGAEISEDEFESHWKLG 1276
Cdd:pfam16521   72 RGAEILEEEFEEEWKKH 88
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
 165-285 9.89e-38

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: 139.40  E-value: 9.89e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  165 ILISINPYQTIDGFYSLQKIKEYRGKSLGQKEPHIFAIADKSYREMIRHRKSQSIIVSGESGAGKTESQKAVLRYLCENW 244
Cdd:cd01363     1 VLVRVNPFKELPIYRDSKIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 808358096  245 GSG---------------AGEIQKRLLETNPILEAFGNAKTLRNNNSSRFGKFVQI 285
Cdd:cd01363    81 FNGinkgetegwvylteiTVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEI 136
MYSc_Myo33 cd14894
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ...
 255-743 9.29e-24

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: 108.68  E-value: 9.29e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  255 LLETNPILEAFGNAKTLRNNNSSRFGKFVQIHFAD-----TGNVAGGYVSHYLLETSRICRQAA------GERNYHIFYQ 323
Cdd:cd14894   249 VLDSNIVLEAFGHATTSMNLNSSRFGKMTTLQVAFglhpwEFQICGCHISPFLLEKSRVTSERGresgdqNELNFHILYA 328

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  324 LIAGSSPelFKFLALGQP----NQFNYLKRGFIGFFTHPSSGTTSKipknrlsdpkftQDSMVDDFSDFQRLEYALKLTG 399
Cdd:cd14894   329 MVAGVNA--FPFMRLLAKelhlDGIDCSALTYLGRSDHKLAGFVSK------------EDTWKKDVERWQQVIDGLDELN 394

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  400 LSEQEIHFIWTTIAAILHLGNVEfeesLDDSRGGCKVFNGSE------QDLIQAARLLGLETMELKMGLCARIMQTTKgg 473
Cdd:cd14894   395 VSPDEQKTIFKVLSAVLWLGNIE----LDYREVSGKLVMSSTgalnapQKVVELLELGSVEKLERMLMTKSVSLQSTS-- 468

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  474 argTLIRVPLKPHEACSGRDALSKAIYSKLFDWLVSRINDSIPFE------------------KSTNFVGVLDVAGFEFY 535
Cdd:cd14894   469 ---ETFEVTLEKGQVNHVRDTLARLLYQLAFNYVVFVMNEATKMSalstdgnkhqmdsnasapEAVSLLKIVDVFGFEDL 545

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  536 AKNSFEQFCINFCNEKLqnffnqrILREEQELYEKEGLNVRKIEFIDNQDCIELFElKGNGLFDLLDE----------EA 605
Cdd:cd14894   546 THNSLDQLCINYLSEKL-------YAREEQVIAVAYSSRPHLTARDSEKDVLFIYE-HPLGVFASLEEltilhqsenmNA 617

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  606 KFPTSNYKSFTKRAHEENRKhfRLDTPRK--SKVKSHRE-LRDDEGLLIRHYAGSVCYETKHFVEKNDDLLHNSLQILIE 682
Cdd:cd14894   618 QQEEKRNKLFVRNIYDRNSS--RLPEPPRvlSNAKRHTPvLLNVLPFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLK 695

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 808358096  683 QST----IRLL--VSLFGSTAYPTKSKLKAL--------SVGAKFKNQLSTLLIKLESTGTHFVRCIKPNNQMIP 743
Cdd:cd14894   696 TSNsshfCRMLneSSQLGWSPNTNRSMLGSAesrlsgtkSFVGQFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQP 770
MyUb_Myo6 cd21958
myosin VI ubiquitin-binding domain (MyUb) found in unconventional myosin-VI and similar ...
 1099-1139 8.04e-18

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: 77.80  E-value: 8.04e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 808358096 1099 GKYDVGGCSFAYLRDTINTSMDINLLKACEEEFRRRLRIYN 1139
Cdd:cd21958     1 KKYDLSKWKYAELRDTINTSCDIELLEACREEFHRRLKVYH 41
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 983-1076 2.24e-08

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 57.55  E-value: 2.24e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   983 LKKQQKSDELAEIERKRRESEEKERLEIEAKKEAERQREIKRKLEEQQQNAQKEHENYLISEIHKAAEEtEKKRQNEEKE 1062
Cdd:TIGR02794   55 IQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEE-AKAKQAAEAK 133

                           90
                   ....*....|....
gi 808358096  1063 KLDKMVSNRLAEAD 1076
Cdd:TIGR02794  134 AKAEAEAERKAKEE 147
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 983-1075 5.11e-08

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 56.74  E-value: 5.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  983 LKKQQKSDELAEIERKRRESEEKERLEIEAKKEAERQREI-KRKLEEQQQNAQKEHENYLISEIHKAAEETEKKRQNEEK 1061
Cdd:PRK09510   67 QQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLeKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAK 146

                          90
                  ....*....|....
gi 808358096 1062 EKLDKMvSNRLAEA 1075
Cdd:PRK09510  147 AKAEAE-AKRAAAA 159
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 963-1066 4.17e-07

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 54.45  E-value: 4.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  963 EKAENAyEHYVKRVDSMIADLKkqQKSDELAEIERKRRESEEKERLEI--EAKKEAERQREIKRKLEEQQQNAQKEHEny 1040
Cdd:PRK00409  534 QKAEEA-EALLKEAEKLKEELE--EKKEKLQEEEDKLLEEAEKEAQQAikEAKKEADEIIKELRQLQKGGYASVKAHE-- 608

                          90       100
                  ....*....|....*....|....*....
gi 808358096 1041 lISEIHKA---AEETEKKRQNEEKEKLDK 1066
Cdd:PRK00409  609 -LIEARKRlnkANEKKEKKKKKQKEKQEE 636
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 963-1075 9.15e-07

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 52.54  E-value: 9.15e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   963 EKAENAYEHYVKRVDSMIADLKKQQKSDELA-EIERKRRESEE-KERLEIEAKK------------EAERQREIKRKLEE 1028
Cdd:TIGR02794   81 EKQRAAEQARQKELEQRAAAEKAAKQAEQAAkQAEEKQKQAEEaKAKQAAEAKAkaeaeaerkakeEAAKQAEEEAKAKA 160

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 808358096  1029 QQQNAQKEHENYLISEIH-KAAEETEKKRQNEE-KEKLDKMVSNRLAEA 1075
Cdd:TIGR02794  161 AAEAKKKAEEAKKKAEAEaKAKAEAEAKAKAEEaKAKAEAAKAKAAAEA 209
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 991-1075 1.05e-06

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 49.65  E-value: 1.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   991 ELAEIERKRRESEEKERLEIEAKKEAE---RQREIKRKLEEQQQNAQKEHEnyliseiHKAAEETEKKRQNEEKEKLDKM 1067
Cdd:pfam05672   28 EREEQERLEKEEEERLRKEELRRRAEEeraRREEEARRLEEERRREEEERQ-------RKAEEEAEEREQREQEEQERLQ 100


                   ....*...
gi 808358096  1068 VSNRLAEA 1075
Cdd:pfam05672  101 KQKEEAEA 108
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 983-1064 2.66e-06

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: 51.49  E-value: 2.66e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   983 LKKQQKSDElaeiERKRRESEEKERLEIEAKKEAER--QREIKRKLEEQQQNAQKEhenylisEIHKAAEetEKKRQNEE 1060
Cdd:pfam15709  391 LRKQRLEEE----RQRQEEEERKQRLQLQAAQERARqqQEEFRRKLQELQRKKQQE-------EAERAEA--EKQRQKEL 457


                   ....
gi 808358096  1061 KEKL 1064
Cdd:pfam15709  458 EMQL 461
PTZ00121 PTZ00121
MAEBL; Provisional
 962-1076 3.66e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.68  E-value: 3.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  962 FEKAENAyeHYVKRVDSMIADLKKqqKSDELAEIERKR-----RESEEKERLEiEAKKEAERQR---EIKRKLEEQQQNA 1033
Cdd:PTZ00121 1257 FEEARMA--HFARRQAAIKAEEAR--KADELKKAEEKKkadeaKKAEEKKKAD-EAKKKAEEAKkadEAKKKAEEAKKKA 1331

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 808358096 1034 QKEHENyliSEIHKAAEETEKKRQNEEKEKLDKmvSNRLAEAD 1076
Cdd:PTZ00121 1332 DAAKKK---AEEAKKAAEAAKAEAEAAADEAEA--AEEKAEAA 1369
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 983-1063 4.60e-06

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: 50.72  E-value: 4.60e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   983 LKKQQKSDELAEIERKRRESEE---------------KERLEIEAKKEAERQREIKRKLEEQQQNAQKEHENYLI----- 1042
Cdd:pfam15709  338 LRAERAEMRRLEVERKRREQEEqrrlqqeqleraekmREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLqlqaa 417

                           90       100
                   ....*....|....*....|....*....
gi 808358096  1043 --------SEIHKAAEETEKKRQNEEKEK 1063
Cdd:pfam15709  418 qerarqqqEEFRRKLQELQRKKQQEEAER 446
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
 926-1077 5.30e-06

Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.


Pssm-ID: 430783 [Multi-domain]  Cd Length: 618  Bit Score: 50.91  E-value: 5.30e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   926 LNEHSRAKYTS---SAHSTIRDLEKLVSHIKLttsanDHFEKAENAYEHYVKRvdsmiadlKKQQKSDELAEIERKRRES 1002
Cdd:pfam09731  277 DNLLSNDDLNSliaHAHREIDQLSKKLAELKK-----REEKHIERALEKQKEE--------LDKLAEELSARLEEVRAAD 343

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 808358096  1003 EEKERLEIEaKKEAERQREIKRKLEEQQQNAQKEHENYLISEIHKAAEETEKKRQNEEKEKLDKMVSNR---LAEADG 1077
Cdd:pfam09731  344 EAQLRLEFE-REREEIRESYEEKLRTELERQAEAHEEHLKDVLVEQEIELQREFLQDIKEKVEEERAGRllkLNELLA 420
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
980-1063 1.33e-05

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 49.10  E-value: 1.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  980 IADLKKQQKSDElAEIERKRR-ESEEKERLEIEAKKEAERQREIKRKLEEQQQNAQKEHENYLISEIHKAAEETEKKRQN 1058
Cdd:COG2268   194 IAEIIRDARIAE-AEAERETEiAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAEAAYEIAE 272


                  ....*
gi 808358096 1059 EEKEK 1063
Cdd:COG2268   273 ANAER 277
PTZ00121 PTZ00121
MAEBL; Provisional
 907-1067 1.58e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.75  E-value: 1.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  907 RKSVALLKNSKEIEKILFRLNEHSRAKYTSSAHSTIRDLEKLVSHIKLTTSANDHFEKAENAYEHyVKRVDSMIADLKKQ 986
Cdd:PTZ00121 1365 KAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEE-KKKADEAKKKAEEA 1443

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  987 QKSDEL---AEIERK----RRESEEKERLEiEAKKEAERQR---EIKRKLEEQQQNA----QKEHENYLISEIHKAAE-- 1050
Cdd:PTZ00121 1444 KKADEAkkkAEEAKKaeeaKKKAEEAKKAD-EAKKKAEEAKkadEAKKKAEEAKKKAdeakKAAEAKKKADEAKKAEEak 1522

                         170
                  ....*....|....*..
gi 808358096 1051 ETEKKRQNEEKEKLDKM 1067
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEA 1539
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 881-1067 2.94e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 2.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  881 AQVTRLQ---SIARGYltrQRFSRQIALYRKSVALLK---NSKEIEKILFRLNEHSRAKytSSAHSTIRDLEKLVSHIKL 954
Cdd:COG1196   200 RQLEPLErqaEKAERY---RELKEELKELEAELLLLKlreLEAELEELEAELEELEAEL--EELEAELAELEAELEELRL 274

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  955 T-TSANDHFEKAENAYEHYVKRVDSMIADLK--KQQKSDELAEIERKRRESEEKERLEIEAKKEAERQREIKRKLEEQQQ 1031
Cdd:COG1196   275 ElEELELELEEAQAEEYELLAELARLEQDIArlEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 808358096 1032 NAQKEHENYL--ISEIHKAAEETEKKRQNEEKEKLDKM 1067
Cdd:COG1196   355 EAEAELAEAEeaLLEAEAELAEAEEELEELAEELLEAL 392
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
963-1157 3.82e-05

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 47.73  E-value: 3.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  963 EKAENAYEHYVKRVDSMIAdlKKQQKSDELAEIERKRRESEEKERleIEAKKEAERqrEIKRKLEEQQQNAQKEHENYLI 1042
Cdd:COG3064    80 AEAEKAAAEAEKKAAAEKA--KAAKEAEAAAAAEKAAAAAEKEKA--EEAKRKAEE--EAKRKAEEERKAAEAEAAAKAE 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096 1043 SEIHKAAEETEKKRQNEEKEKLDKMVSNRLAEADGVALISSKMEIEPSSGSATFRDGKYDVGGCSFAYLRDTINTSMDIN 1122
Cdd:COG3064   154 AEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAA 233

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 808358096 1123 LLKACEEEFRRRLRIYNEWKSRNAPVQDRPPARAA 1157
Cdd:COG3064   234 LAAVEATEEAALGGAEEAADLAAVGVLGAALAAAA 268
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 981-1088 5.92e-05

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 46.76  E-value: 5.92e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   981 ADLKKQQKSDE--LAEIERKRRESEEKERLEiEAKKEAERQR----EIKRK-LEEQQQNAQKEHENYLISE-IHKAAEET 1052
Cdd:TIGR02794   78 EEAEKQRAAEQarQKELEQRAAAEKAAKQAE-QAAKQAEEKQkqaeEAKAKqAAEAKAKAEAEAERKAKEEaAKQAEEEA 156

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 808358096  1053 EKKRQNEEKEKLDKMVSNRLAEADGVALISSKMEIE 1088
Cdd:TIGR02794  157 KAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAE 192
PTZ00121 PTZ00121
MAEBL; Provisional
 953-1067 8.55e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 8.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  953 KLTTSANDHFEKAENAYEHYVKRVDSMIADLKKQQKSDELAEIERKRRESEEKERLE-----IEAKKEAERQR----EIK 1023
Cdd:PTZ00121 1256 KFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEeakkaDEAKKKAEEAKkkadAAK 1335

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 808358096 1024 RKLEEQQQNAQ--KEHENYLISEIHKAAE--ETEKKRQNEEKEKLDKM 1067
Cdd:PTZ00121 1336 KKAEEAKKAAEaaKAEAEAAADEAEAAEEkaEAAEKKKEEAKKKADAA 1383
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
963-1094 9.56e-05

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 46.57  E-value: 9.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  963 EKAENAyehyvKRVDSMIADLKKQQKSDELAEIERKRRESEEKERLEIEAKKEAERQREI----KRKLEEQQQNAQKEhe 1038
Cdd:COG3064    60 AKAEAE-----QRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAaaaeKEKAEEAKRKAEEE-- 132

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 808358096 1039 nyliseihkAAEETEKKRQNEEKEKLDKMVSNRLAEADGVALISSKMEIEPSSGSA 1094
Cdd:COG3064   133 ---------AKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAA 179
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
 974-1066 9.73e-05

Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.


Pssm-ID: 402959 [Multi-domain]  Cd Length: 164  Bit Score: 44.29  E-value: 9.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   974 KRVDSMIADLKKQQKSDelAEIERKRRESEEKERLEIEAKKEAERQREIKRKLEEQQQNAQKEHENYLISEIHKAAEETE 1053
Cdd:pfam11600   16 QRLEKDKERLRRQLKLE--AEKEEKERLKEEAKAEKERAKEEARRKKEEEKELKEKERREKKEKDEKEKAEKLRLKEEKR 93

                           90
                   ....*....|...
gi 808358096  1054 KKRQNEEKEKLDK 1066
Cdd:pfam11600   94 KEKQEALEAKLEE 106
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 975-1075 9.94e-05

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 46.74  E-value: 9.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  975 RVDSMIADLKKQQKS--DELAEIERKRRESEE-KERLEIEAKKEAERQREIKRKLEEQQQ----NAQKEhenylISEIHK 1047
Cdd:PRK00409  517 KLNELIASLEELEREleQKAEEAEALLKEAEKlKEELEEKKEKLQEEEDKLLEEAEKEAQqaikEAKKE-----ADEIIK 591

                          90       100
                  ....*....|....*....|....*...
gi 808358096 1048 AAEETEKKRQNEEKEKLDKMVSNRLAEA 1075
Cdd:PRK00409  592 ELRQLQKGGYASVKAHELIEARKRLNKA 619
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
 964-1064 1.02e-04

Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


Pssm-ID: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 45.74  E-value: 1.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   964 KAENAYEHYVKRVDSMIADLKKQQKSDELAEIERKrresEEKERLEiEAKKEAERQREIKRKLE---EQQQNAQKEHENY 1040
Cdd:pfam02841  173 KAEEVLQEFLQSKEAVEEAILQTDQALTAKEKAIE----AERAKAE-AAEAEQELLREKQKEEEqmmEAQERSYQEHVKQ 247

                           90       100
                   ....*....|....*....|....
gi 808358096  1041 LISEIhkaaeETEKKRQNEEKEKL 1064
Cdd:pfam02841  248 LIEKM-----EAEREQLLAEQERM 266
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 981-1071 1.23e-04

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 45.68  E-value: 1.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   981 ADLKKQQKSDELAEIERKRRESEEKERLEIEAKKEAERQREIKRKLEEQQQNAQKEHENYLI--SEIHKAAEETEKKRQN 1058
Cdd:pfam13868   37 EEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQerEQMDEIVERIQEEDQA 116

                           90
                   ....*....|...
gi 808358096  1059 EEKEKLDKMVSNR 1071
Cdd:pfam13868  117 EAEEKLEKQRQLR 129
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
963-1066 1.27e-04

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 46.19  E-value: 1.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  963 EKAENAYEhyVKRVDSMIADLKKQQKSDEL-AEIERKRRESE-EKERLEIEAKKEAerqREIKRKLEEQQQNAQKEHENY 1040
Cdd:COG3064    33 QKAKEEAE--EERLAELEAKRQAEEEAREAkAEAEQRAAELAaEAAKKLAEAEKAA---AEAEKKAAAEKAKAAKEAEAA 107

                          90       100
                  ....*....|....*....|....*.
gi 808358096 1041 LISEihKAAEETEKKRQNEEKEKLDK 1066
Cdd:COG3064   108 AAAE--KAAAAAEKEKAEEAKRKAEE 131
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
915-1074 1.44e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.21  E-value: 1.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  915 NSKEIEKILFRLNEHSR-----AKYTSSAHSTIRDLEKLVSHIKLTTSANDHFEKAENAYEHYVKRVDSMIADLKKqqks 989
Cdd:PRK03918  198 KEKELEEVLREINEISSelpelREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKK---- 273

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  990 dELAEIERKRRESEEKErleiEAKKEAERQREIKRKLEEQQQNAQKEHENY--LISEIHKAAEETE-KKRQNEEKEKLDK 1066
Cdd:PRK03918  274 -EIEELEEKVKELKELK----EKAEEYIKLSEFYEEYLDELREIEKRLSRLeeEINGIEERIKELEeKEERLEELKKKLK 348


                  ....*...
gi 808358096 1067 MVSNRLAE 1074
Cdd:PRK03918  349 ELEKRLEE 356
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 984-1061 1.50e-04

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 43.49  E-value: 1.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   984 KKQQKSDELAEIERKRRESEEKERLEIEAKKEAE-RQREIKRKLEEQQQNAQKEHENYLISEIH---------------- 1046
Cdd:pfam05672   29 REEQERLEKEEEERLRKEELRRRAEEERARREEEaRRLEEERRREEEERQRKAEEEAEEREQREqeeqerlqkqkeeaea 108

                           90
                   ....*....|....*
gi 808358096  1047 KAAEETEKKRQNEEK 1061
Cdd:pfam05672  109 KAREEAERQRQEREK 123
PTZ00121 PTZ00121
MAEBL; Provisional
 982-1076 1.69e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.29  E-value: 1.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  982 DLKKQQKSDELAEIERKRRESEEKERLEiEAKKEAERqreiKRKLEEQQQnaQKEHENYLISEIHKAAEETEKK----RQ 1057
Cdd:PTZ00121 1651 ELKKAEEENKIKAAEEAKKAEEDKKKAE-EAKKAEED----EKKAAEALK--KEAEEAKKAEELKKKEAEEKKKaeelKK 1723

                          90
                  ....*....|....*....
gi 808358096 1058 NEEKEKLDKMVSNRLAEAD 1076
Cdd:PTZ00121 1724 AEEENKIKAEEAKKEAEED 1742
PTZ00121 PTZ00121
MAEBL; Provisional
 879-1078 1.90e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.90  E-value: 1.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  879 RSAQVTRLQSIARGYLTRQRFSRQIALYRKSVALLKNSKEiEKILFRLNEHSRAKYTSSAHSTIRDLEKLVSHIKLTTSA 958
Cdd:PTZ00121 1570 KKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKA-EEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKK 1648

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  959 NDHFEKAENayEHYVKRVDSMIADLKKQQKSDELAEIERKRRESEEKERLEIEAKKEAErqrEIKRKLEEQQQNAQK--- 1035
Cdd:PTZ00121 1649 AEELKKAEE--ENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAE---ELKKKEAEEKKKAEElkk 1723

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 808358096 1036 -EHENYLISEIHKAAEETEKKR------QNEEKEKLDKMVSNRLAEADGV 1078
Cdd:PTZ00121 1724 aEEENKIKAEEAKKEAEEDKKKaeeakkDEEEKKKIAHLKKEEEKKAEEI 1773
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 984-1076 1.95e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 45.18  E-value: 1.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  984 KKQQKSDELAE---IERKRRESEEKERL-EIEAKKEAERQReikRKLEEQQQNAqkEHENYLISEIHKAAEETEKKRQN- 1058
Cdd:PRK09510   84 KEQQQAEELQQkqaAEQERLKQLEKERLaAQEQKKQAEEAA---KQAALKQKQA--EEAAAKAAAAAKAKAEAEAKRAAa 158

                          90       100
                  ....*....|....*....|....
gi 808358096 1059 ------EEKEKLDKMVSNRLAEAD 1076
Cdd:PRK09510  159 aakkaaAEAKKKAEAEAAKKAAAE 182
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 960-1072 2.14e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 44.15  E-value: 2.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  960 DHFEKAENAYEHYVKRVDSMIADLKKQQKS----DEL----AEIERKRRESEEKERLEIEAKKEAERQREIKRKLEEQQQ 1031
Cdd:COG1579    55 EDLEKEIKRLELEIEEVEARIKKYEEQLGNvrnnKEYealqKEIESLKRRISDLEDEILELMERIEELEEELAELEAELA 134

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 808358096 1032 NAQKEHENyLISEIHKAAEETEKKRQ--NEEKEKLDKMVSNRL 1072
Cdd:COG1579   135 ELEAELEE-KKAELDEELAELEAELEelEAEREELAAKIPPEL 176
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 963-1070 2.86e-04

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 44.99  E-value: 2.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   963 EKAENAYEHYVKRVDSMIADLKKQQKSDELAEIErkrrESEEKERLEIEAKKEAER-QREIKRKLEEQQQNaqKEHENYL 1041
Cdd:pfam05262  234 QKADFAQDNADKQRDEVRQKQQEAKNLPKPADTS----SPKEDKQVAENQKREIEKaQIEIKKNDEEALKA--KDHKAFD 307

                           90       100
                   ....*....|....*....|....*....
gi 808358096  1042 ISEIHKAAEETEKKRQNEEKEKLDKMVSN 1070
Cdd:pfam05262  308 LKQESKASEKEAEDKELEAQKKREPVAED 336
Nop53 pfam07767
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ...
 990-1066 2.92e-04

Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ribosomal biogenesis. They are specifically involved in the processing beyond the 27S stage of 25S rRNA maturation. This family contains sequences that bear similarity to the glioma tumour suppressor candidate region gene 2 protein (p60). This protein has been found to interact with herpes simplex type 1 regulatory proteins.


Pssm-ID: 462259 [Multi-domain]  Cd Length: 353  Bit Score: 44.59  E-value: 2.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   990 DELAEIERKRRESEEKERLEIEA---------------KKEAERQREIKRKLEEQQQNA-----QKEHENYLISEIHKAA 1049
Cdd:pfam07767  202 QKAVEAEKKRLKEEEKLERVLEKiaesaataeareekrKTKAQRNKEKRRKEEEREAKEekalkKKLAQLERLKEIAKEI 281

                           90
                   ....*....|....*..
gi 808358096  1050 EETEKKRQNEEKEKLDK 1066
Cdd:pfam07767  282 AEKEKEREEKAEARKRE 298
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
 684-737 3.15e-04

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: 42.72  E-value: 3.15e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 808358096  684 STIRLLVSLFGSTayptksklkalsvgaKFKNQLSTLLIKLESTGTHFVRCIKP 737
Cdd:cd01363   132 KFIEILLDIAGFE---------------IINESLNTLMNVLRATRPHFVRCISP 170
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 942-1075 3.24e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.05  E-value: 3.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   942 IRDLEKLVSHIKLTtSANDHFEKAENAYEHYVKRVDSMIADLKKQQksdelAEIERKRRESEEKERLEIEAKKEAERQRE 1021
Cdd:TIGR02168  222 LRELELALLVLRLE-ELREELEELQEELKEAEEELEELTAELQELE-----EKLEELRLEVSELEEEIEELQKELYALAN 295

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 808358096  1022 IKRKLEEQQQNAQKEHENYLISEIHKAAEETEKKRQNEEKEKLDKMVSNRLAEA 1075
Cdd:TIGR02168  296 EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL 349
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
 971-1092 3.46e-04

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 45.11  E-value: 3.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  971 HYVKRVD------SMIADLKKQQKSDELAEIERKR---RESEEKERLEIEAKKEAERQREIKRKLEEQQQNaqkehenyl 1041
Cdd:PTZ00266  425 HYGGRVDkdhaerARIEKENAHRKALEMKILEKKRierLEREERERLERERMERIERERLERERLERERLE--------- 495

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 808358096 1042 iseihkaAEETEKKRQNE-EKEKLDKMVSNRLAEADGVALISSKMEIEPSSG 1092
Cdd:PTZ00266  496 -------RDRLERDRLDRlERERVDRLERDRLEKARRNSYFLKGMENGLSAG 540
PTZ00121 PTZ00121
MAEBL; Provisional
 907-1074 3.46e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 3.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  907 RKSVALLKNSKEIEKilfRLNEHSRAKYTSSAHSTIRDLEKLVSHIKLTTSANDHFEKAENAyehyvKRVDSMIADLKKQ 986
Cdd:PTZ00121 1411 KKAAAAKKKADEAKK---KAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEA-----KKADEAKKKAEEA 1482

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  987 QKSDELAEIERKRRESEEKERLEIEAKKEAE--RQREIKRKLEE--------QQQNAQKEHENYLISEIHKAAE--ETEK 1054
Cdd:PTZ00121 1483 KKADEAKKKAEEAKKKADEAKKAAEAKKKADeaKKAEEAKKADEakkaeeakKADEAKKAEEKKKADELKKAEElkKAEE 1562

                         170       180
                  ....*....|....*....|..
gi 808358096 1055 KRQNEEKEKL--DKMVSNRLAE 1074
Cdd:PTZ00121 1563 KKKAEEAKKAeeDKNMALRKAE 1584
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 964-1074 3.77e-04

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 44.11  E-value: 3.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  964 KAENAYEHYVKRVDSMIADLKKQQKSdeLAEIERKRRESEEKERLeieAKKEAERQREIKRKLEEQQQNAQKEHENYlis 1043
Cdd:cd16269   167 KAEEVLQEFLQSKEAEAEAILQADQA--LTEKEKEIEAERAKAEA---AEQERKLLEEQQRELEQKLEDQERSYEEH--- 238

                          90       100       110
                  ....*....|....*....|....*....|.
gi 808358096 1044 eIHKAAEETEKKRQNEEKEKlDKMVSNRLAE 1074
Cdd:cd16269   239 -LRQLKEKMEEERENLLKEQ-ERALESKLKE 267
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
981-1062 4.72e-04

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 44.26  E-value: 4.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  981 ADLKKQQKSDELAEIERKRRESEEKERLEI--EAKKEAERQR----EIKRKLEEQQQNAQKEHENYLI---SEIHKAAEE 1051
Cdd:COG3064     2 QEALEEKAAEAAAQERLEQAEAEKRAAAEAeqKAKEEAEEERlaelEAKRQAEEEAREAKAEAEQRAAelaAEAAKKLAE 81

                          90
                  ....*....|.
gi 808358096 1052 TEKKRQNEEKE 1062
Cdd:COG3064    82 AEKAAAEAEKK 92
PTZ00121 PTZ00121
MAEBL; Provisional
 907-1067 4.81e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 4.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  907 RKSVALLKNSKEIEKILFRLNEHSRAKYTSSAHSTIRDLEKLVSHIKLTTSANDHFEKAENAYEhyvKRVDSMIADLKKQ 986
Cdd:PTZ00121 1457 KKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEE---AKKADEAKKAEEA 1533

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  987 QKSDELAEIERKR-----------RESEEKERLEiEAKKEAERQREIKRKLEEQQQNAQKEHENYL-ISEIHKAAEETEK 1054
Cdd:PTZ00121 1534 KKADEAKKAEEKKkadelkkaeelKKAEEKKKAE-EAKKAEEDKNMALRKAEEAKKAEEARIEEVMkLYEEEKKMKAEEA 1612

                         170
                  ....*....|...
gi 808358096 1055 KRQNEEKEKLDKM 1067
Cdd:PTZ00121 1613 KKAEEAKIKAEEL 1625
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 896-1076 5.20e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 44.58  E-value: 5.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   896 RQRFSRQIALYRKSVALLKNSKEIEKILFRLNEHSRAKYTSSAHSTIRDLEKLVSHIKLTTSAndhFEKAENAYEHYVKR 975
Cdd:pfam02463  232 LKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKE---EEELKSELLKLERR 308

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   976 VDSMIADLKKQQKSDELAEIERKRrESEEKERLEIEaKKEAERQR-----EIKRKLEEQQQNAQKEHENYLISEIHKAAE 1050
Cdd:pfam02463  309 KVDDEEKLKESEKEKKKAEKELKK-EKEEIEELEKE-LKELEIKReaeeeEEEELEKLQEKLEQLEEELLAKKKLESERL 386

                          170       180
                   ....*....|....*....|....*.
gi 808358096  1051 ETEKKRQNEEKEKLDKMVSNRLAEAD 1076
Cdd:pfam02463  387 SSAAKLKEEELELKSEEEKEAQLLLE 412
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 1000-1076 5.35e-04

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: 41.06  E-value: 5.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  1000 RESEEKERLEIE------------AKKEAERQREIKRKLEEQQQNAQKEHEnyLISEIHKAAEET------EKKRQNEEK 1061
Cdd:pfam20492    1 REEAEREKQELEerlkqyeeetkkAQEELEESEETAEELEEERRQAEEEAE--RLEQKRQEAEEEkerleeSAEMEAEEK 78

                           90
                   ....*....|....*
gi 808358096  1062 EKLDKmvsnRLAEAD 1076
Cdd:pfam20492   79 EQLEA----ELAEAQ 89
Casc1_N pfam15927
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ...
 991-1061 5.38e-04

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: 42.73  E-value: 5.38e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808358096   991 ELAEIERKRRESEEKERLEIEAKKEAERQREIKrklEEQQQNAQKEHENYLISEIHKAAEETEKKRQNEEK 1061
Cdd:pfam15927    4 REEEEERLRAEEEEAERLEEERREEEEEERLAA---EQDRRAEELEELKHLLEERKEALEKLRAEAREEAE 71
PTZ00121 PTZ00121
MAEBL; Provisional
 879-1067 5.79e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 5.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  879 RSAQVTRLQSIARGYLTRQRFSRQIALYRKSVALLKNSKEIEKILFRLNEHSRAKYTSSAHSTIRDLEKLVSHIKltTSA 958
Cdd:PTZ00121 1261 RMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAK--KKA 1338

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  959 NDHFEKAENAYEHYVKRVDSMIADlKKQQKSDELAEIERKRRESEEKERLE-----IEAKKEAERQR----EIKRKLEEQ 1029
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAEAAADEAEAA-EEKAEAAEKKKEEAKKKADAAKKKAEekkkaDEAKKKAEEDKkkadELKKAAAAK 1417

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 808358096 1030 QQNAQ---KEHENYLISEIHKAAEETEK----KRQNEEKEKLDKM 1067
Cdd:PTZ00121 1418 KKADEakkKAEEKKKADEAKKKAEEAKKadeaKKKAEEAKKAEEA 1462
DDRGK pfam09756
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ...
 984-1064 6.13e-04

DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and vertebrates. They contain a highly conserved DDRGK motif.


Pssm-ID: 370664 [Multi-domain]  Cd Length: 188  Bit Score: 42.33  E-value: 6.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   984 KKQQKSDELAEIERKR-----RESEEKERLEIEAKKEAERQREIKRKLEEQQQNAQKEHENylISEIHKAAEETEKKRQN 1058
Cdd:pfam09756   17 KRQQREAEEEEREEREkleekREEEYKEREEREEEAEKEKEEEERKQEEEQERKEQEEYEK--LKSQFVVEEEGTDKLSA 94


                   ....*.
gi 808358096  1059 EEKEKL 1064
Cdd:pfam09756   95 EDESQL 100
PTZ00121 PTZ00121
MAEBL; Provisional
 913-1067 6.46e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 6.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  913 LKNSKEIEKILFRLNEHSRAKYTSSAHSTIRDLEKLVSHIKLTTSANDHFEKAENAYEHYVKRVDSmiADLKKQQKSDEL 992
Cdd:PTZ00121 1557 LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA--EELKKAEEEKKK 1634

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  993 AEiERKRRESEEKERLEiEAKKEAE----RQREIKRKLEEQQQNAQK-----EHENYLISEIHKAAEETEK-----KRQN 1058
Cdd:PTZ00121 1635 VE-QLKKKEAEEKKKAE-ELKKAEEenkiKAAEEAKKAEEDKKKAEEakkaeEDEKKAAEALKKEAEEAKKaeelkKKEA 1712


                  ....*....
gi 808358096 1059 EEKEKLDKM 1067
Cdd:PTZ00121 1713 EEKKKAEEL 1721
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 855-1071 6.53e-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: 43.96  E-value: 6.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   855 VGARWKQSQYAVWSVIKLKNKIAWRSAQVTRLQSIARGYLTRQ-RFSRQIALYRKSVAL-LKNSKEIEKILF----RLNE 928
Cdd:pfam17380  284 VSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQaEMDRQAAIYAEQERMaMERERELERIRQeerkRELE 363

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   929 HSRAKYTSSAHSTIRDLEKL-VSHIKLTTSANDHFEKA----------------------------ENAYEHYVKRVDSM 979
Cdd:pfam17380  364 RIRQEEIAMEISRMRELERLqMERQQKNERVRQELEAArkvkileeerqrkiqqqkvemeqiraeqEEARQREVRRLEEE 443

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   980 IA---------DLKKQQKSDEL--AEIERKR------RESEEKERLEIEAKK--------------EAERQREIKRKLEE 1028
Cdd:pfam17380  444 RAremervrleEQERQQQVERLrqQEEERKRkkleleKEKRDRKRAEEQRRKilekeleerkqamiEEERKRKLLEKEME 523

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 808358096  1029 QQQNAQKEHENYLISEIHKAAE-ETEKKRQ--------NEEKEKLDKMVSNR 1071
Cdd:pfam17380  524 ERQKAIYEEERRREAEEERRKQqEMEERRRiqeqmrkaTEERSRLEAMERER 575
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 963-1094 6.65e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 44.19  E-value: 6.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   963 EKAENAYEHYVKRVDSMIADLK---------KQQKSDELAEIERKRRESEEKERLEIEAKKEAERQREIKRKLEEQQQNA 1033
Cdd:pfam02463  204 EQAKKALEYYQLKEKLELEEEYllyldylklNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKL 283

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 808358096  1034 QKEHENYLISEIHKAAEETEKKRQ-----NEEKEKLDKMVSNRLAEADGVALISSKMEIEPSSGSA 1094
Cdd:pfam02463  284 QEEELKLLAKEEEELKSELLKLERrkvddEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEI 349
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 914-1105 7.20e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 43.67  E-value: 7.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  914 KNSKEIEKILFRLNEHSRAKYTSSahSTIRDLEKLVShiklTTSANDHFEKAEnAYEHYVKRVDSMIADLKKQQKS--DE 991
Cdd:COG3883    76 EAEAEIEERREELGERARALYRSG--GSVSYLDVLLG----SESFSDFLDRLS-ALSKIADADADLLEELKADKAEleAK 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  992 LAEIERKRRESEEKERLEIEAKKEAERQREIKRKLEEQQQNAQKEHENYLISEIHKAAEETEKKRQNEEKEKLDKMVSNR 1071
Cdd:COG3883   149 KAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228

                         170       180       190
                  ....*....|....*....|....*....|....
gi 808358096 1072 LAEADGVALISSKMEIEPSSGSATFRDGKYDVGG 1105
Cdd:COG3883   229 AAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSA 262
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 861-1075 8.27e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 8.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  861 QSQYAVWSVIKLKNKIAWRSAQVTRLQS-IARGYLTRQRFSRQIALYRKSVALLKnsKEIEKILFRLNEHSRAKYtssah 939
Cdd:COG1196   219 KEELKELEAELLLLKLRELEAELEELEAeLEELEAELEELEAELAELEAELEELR--LELEELELELEEAQAEEY----- 291

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  940 STIRDLEKLVSHIKLTTSANDHFEKAEnayehyvKRVDSMIADLKKQQKSD--ELAEIERKRRESEEKERLEIEAKKEAE 1017
Cdd:COG1196   292 ELLAELARLEQDIARLEERRRELEERL-------EELEEELAELEEELEELeeELEELEEELEEAEEELEEAEAELAEAE 364

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 808358096 1018 RQREikrKLEEQQQNAQKEHENYLISEIHKAAEETEKKRQNEEKEKLDKMVSNRLAEA 1075
Cdd:COG1196   365 EALL---EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
G_path_suppress pfam15991
G-protein pathway suppressor; This family of proteins inhibits G-protein- and ...
 984-1064 8.83e-04

G-protein pathway suppressor; This family of proteins inhibits G-protein- and mitogen-activated protein kinase-mediated signal transduction.


Pssm-ID: 464961 [Multi-domain]  Cd Length: 272  Bit Score: 42.60  E-value: 8.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   984 KKQQKSDELAEIERKRRESEEKERleiEAKKEAERQREIKRKLEEQQQNAQKE-HEnyLISEIHKAAEETEK-KRQNEEK 1061
Cdd:pfam15991   24 RKKQEQEAKMEEERLRREREEREK---EDRMTLEETKEQILKLEKKLADLKEEkHQ--LFLQLKKVLHEDETrKRQLKEQ 98


                   ...
gi 808358096  1062 EKL 1064
Cdd:pfam15991   99 SEL 101
PRK13453 PRK13453
F0F1 ATP synthase subunit B; Provisional
 982-1085 1.10e-03

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184060  Cd Length: 173  Bit Score: 41.43  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  982 DLKKQQKSDELAEIERKRRESEEKERLEIEAKKE-AERQREIKRKLEEQQQNAQKEHENYliseIHKAAE------ETEK 1054
Cdd:PRK13453   45 DVMDKRERDINRDIDDAEQAKLNAQKLEEENKQKlKETQEEVQKILEDAKVQARQQQEQI----IHEANVrangmiETAQ 120

                          90       100       110
                  ....*....|....*....|....*....|.
gi 808358096 1055 KRQNEEKEKLDKMVSNRLAEADgvALISSKM 1085
Cdd:PRK13453  121 SEINSQKERAIADINNQVSELS--VLIASKV 149
PRK09173 PRK09173
F0F1 ATP synthase subunit B; Validated
 972-1083 1.11e-03

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 169691 [Multi-domain]  Cd Length: 159  Bit Score: 40.88  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  972 YVKrVDSMIA---DLKKQQKSDELAEIERKRRESEEkerleieakKEAERQReiKRKLEEQQQN-----AQKEHEnYLIS 1043
Cdd:PRK09173   20 YLK-VPGMIArslDARADRIKNELAEARRLREEAQQ---------LLAEYQR--KRKEAEKEAAdivaaAEREAE-ALTA 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 808358096 1044 EIHKAAEETEKKRQNEEKEKLDKmvsnrlAEADGVALISS 1083
Cdd:PRK09173   87 EAKRKTEEYVARRNKLAEQKIAQ------AETDAINAVRS 120
PTZ00121 PTZ00121
MAEBL; Provisional
 963-1076 1.12e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  963 EKAENAYEHYVKRVDSMIADLKKQQKSDELaeierKRRESEEKERLEIEAKKEAERQ---REIKRKLEEQQQNAQ----- 1034
Cdd:PTZ00121 1678 EEAKKAEEDEKKAAEALKKEAEEAKKAEEL-----KKKEAEEKKKAEELKKAEEENKikaEEAKKEAEEDKKKAEeakkd 1752

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 808358096 1035 ---KEHENYLISEIHKAAEETEKKRQNEEKEKLDKMVSNRLAEAD 1076
Cdd:PTZ00121 1753 eeeKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD 1797
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 981-1063 1.25e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 42.60  E-value: 1.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   981 ADLKKQQKSDELAEIER---------KRRESEEKERLEIEAKKEAERQReiKRKLEEQQQNAQKEHENYLISEIHKAAEE 1051
Cdd:pfam13868  140 AEWKELEKEEEREEDERileylkekaEREEEREAEREEIEEEKEREIAR--LRAQQEKAQDEKAERDELRAKLYQEEQER 217

                           90
                   ....*....|..
gi 808358096  1052 TEKKRQNEEKEK 1063
Cdd:pfam13868  218 KERQKEREEAEK 229
PRK02292 PRK02292
V-type ATP synthase subunit E; Provisional
 986-1084 1.40e-03

V-type ATP synthase subunit E; Provisional


Pssm-ID: 235026 [Multi-domain]  Cd Length: 188  Bit Score: 41.14  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  986 QQKSDE-LAEIERKRRESEEKERLEIEAKKEAERQREIKR-KLEEQQQ--NAQKEhenyLISEIHKAAEETEKKRQNEEK 1061
Cdd:PRK02292   26 DEEAEEiIAEAEADAEEILEDREAEAEREIEQLREQELSSaKLEAKRErlNARKE----VLEDVRNQVEDEIASLDGDKR 101

                          90       100
                  ....*....|....*....|...
gi 808358096 1062 EKLDKMVSNRlAEADGVALISSK 1084
Cdd:PRK02292  102 EELTKSLLDA-ADADGVRVYSRK 123
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 987-1064 1.44e-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: 42.63  E-value: 1.44e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 808358096   987 QKSDELAEIERKRRESEEKERLEIEAKKeaeRQREIKRKLEEQQQNAQKEHENYLISEIHKAAEETEKKRQNEEKEKL 1064
Cdd:pfam15709  327 KREQEKASRDRLRAERAEMRRLEVERKR---REQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQ 401
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 974-1098 1.45e-03

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 42.68  E-value: 1.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   974 KRVDSMIADLKKQQKSDELAE--IERKRRESEEKERLE--------IEAKKEAER-QREIKRKLEEQQQNAQKEHENYLI 1042
Cdd:pfam05262  220 EELDKKQIDADKAQQKADFAQdnADKQRDEVRQKQQEAknlpkpadTSSPKEDKQvAENQKREIEKAQIEIKKNDEEALK 299

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 808358096  1043 SEIHKaAEETEKKRQNEEKEKLDKMV---SNRLAEADGVALISSKMEIEPSSGSATFRD 1098
Cdd:pfam05262  300 AKDHK-AFDLKQESKASEKEAEDKELeaqKKREPVAEDLQKTKPQVEAQPTSLNEDAID 357
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
980-1081 1.51e-03

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 42.55  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  980 IADLKKQQKSDEL------AEIERKRRESEEK-ERLEIEAKK-----EAERQREIKRKLEEQQQNAQ--------KEHEN 1039
Cdd:COG2268   225 EAELEQEREIETAriaeaeAELAKKKAEERREaETARAEAEAayeiaEANAEREVQRQLEIAEREREielqekeaEREEA 304

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 808358096 1040 YLISEIHKAAE-ETEKKRQNEEKEkLDKMVSNRLAEADGVALI 1081
Cdd:COG2268   305 ELEADVRKPAEaEKQAAEAEAEAE-AEAIRAKGLAEAEGKRAL 346
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 917-1075 1.67e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.74  E-value: 1.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   917 KEIEKILF--RLNEH--SRAKYTSSAHSTIRDLEKLVSHIKLTTSA----NDHFEKAENAYEHYVKRVDSM---IADLK- 984
Cdd:TIGR02168  223 RELELALLvlRLEELreELEELQEELKEAEEELEELTAELQELEEKleelRLEVSELEEEIEELQKELYALaneISRLEq 302

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   985 -KQQKSDELAEIERKRRESEEkERLEIEAKKEaeRQREIKRKLEEQQQNAQKEHENYLISEIHKAAEETEKKRQNEEKEK 1063
Cdd:TIGR02168  303 qKQILRERLANLERQLEELEA-QLEELESKLD--ELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEE 379

                          170
                   ....*....|..
gi 808358096  1064 LDKMVSNRLAEA 1075
Cdd:TIGR02168  380 QLETLRSKVAQL 391
PTZ00121 PTZ00121
MAEBL; Provisional
 907-1067 1.98e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 1.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  907 RKSVALLKNSKEIEKILFRLNEHSRAKYTSSahstirDLEKLVSHIKLTTSANDHFEKAENAYEHYVKRVDSMIADlKKQ 986
Cdd:PTZ00121 1391 KKADEAKKKAEEDKKKADELKKAAAAKKKAD------EAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAE-EAK 1463

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  987 QKSDELAEIERKRRESEEKERLEiEAKKEAE---RQREIKRKLEEQQQNA---QKEHENYLISEIHKAAE--ETEKKRQN 1058
Cdd:PTZ00121 1464 KKAEEAKKADEAKKKAEEAKKAD-EAKKKAEeakKKADEAKKAAEAKKKAdeaKKAEEAKKADEAKKAEEakKADEAKKA 1542


                  ....*....
gi 808358096 1059 EEKEKLDKM 1067
Cdd:PTZ00121 1543 EEKKKADEL 1551
fliH PRK06669
flagellar assembly protein H; Validated
 981-1063 2.04e-03

flagellar assembly protein H; Validated


Pssm-ID: 235850 [Multi-domain]  Cd Length: 281  Bit Score: 41.54  E-value: 2.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  981 ADLKKQQKSDELAEIERKRRESEEKERLEIEAKKEAERQREIKRKLEEQQQNAQKEHEN---YLISEIHKAAEETEKKRQ 1057
Cdd:PRK06669   79 AKEELLKKTDEASSIIEKLQMQIEREQEEWEEELERLIEEAKAEGYEEGYEKGREEGLEevrELIEQLNKIIEKLIKKRE 158


                  ....*...
gi 808358096 1058 N--EEKEK 1063
Cdd:PRK06669  159 EilESSEE 166
PTZ00121 PTZ00121
MAEBL; Provisional
 955-1075 2.14e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 2.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  955 TTSANDHFEKAENAYEHYVKRVDSMIADLKKQQKSDELAEIERKR-----------RESEEKERLEIEAKKEAERQREIK 1023
Cdd:PTZ00121 1090 DEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARkaedarkaeeaRKAEDAKRVEIARKAEDARKAEEA 1169

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 808358096 1024 RKLEEQQ--QNAQKEHENYLISEIHKAAE----ETEKKRQNEEK-EKLDKMVSNRLAEA 1075
Cdd:PTZ00121 1170 RKAEDAKkaEAARKAEEVRKAEELRKAEDarkaEAARKAEEERKaEEARKAEDAKKAEA 1228
PTZ00121 PTZ00121
MAEBL; Provisional
 905-1074 2.51e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 2.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  905 LYRKSVALLKNSKEIEKilfRLNEHSRAKYTSSAHSTIRDLEKLVSHIKLTTSANDHFEKAENAyehyvKRVDSMIADLK 984
Cdd:PTZ00121 1396 AKKKAEEDKKKADELKK---AAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA-----KKAEEAKKKAE 1467

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  985 KQQKSDELAEIERKRRESEEKERLEIEAKKEAERQR---EIKRKLEE--QQQNAQKEHENYLISEIHKA-----AEETEK 1054
Cdd:PTZ00121 1468 EAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKkaaEAKKKADEakKAEEAKKADEAKKAEEAKKAdeakkAEEKKK 1547

                         170       180
                  ....*....|....*....|
gi 808358096 1055 KRQNEEKEKLDKMVSNRLAE 1074
Cdd:PTZ00121 1548 ADELKKAEELKKAEEKKKAE 1567
Pinin_SDK_memA pfam04696
pinin/SDK/memA/ protein conserved region; Members of this family have very varied ...
 984-1070 2.81e-03

pinin/SDK/memA/ protein conserved region; Members of this family have very varied localizations within the eukaryotic cell. pinin is known to localize at the desmosomes and is implicated in anchoring intermediate filaments to the desmosomal plaque. SDK2/3 is a dynamically localized nuclear protein thought to be involved in modulation of alternative pre-mRNA splicing. memA is a tumour marker preferentially expressed in human melanoma cell lines. A common feature of the members of this family is that they may all participate in regulating protein-protein interactions.


Pssm-ID: 461396 [Multi-domain]  Cd Length: 130  Bit Score: 39.20  E-value: 2.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   984 KKQQKSDELAEIERKRRESEEkeRLEIEAKKEAERQREIKRKLEEQQQNAQKEHENylisEIHKAAEETEKKRQNEEKEK 1063
Cdd:pfam04696   20 KFKKEESKQKEKEERRAEIEK--RLEEKAKQEKEELEERKREEREELFEERRAEQI----ELRALEEKLELKELMETWHE 93


                   ....*..
gi 808358096  1064 LDKMVSN 1070
Cdd:pfam04696   94 NLKALAN 100
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 895-1062 2.96e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.08  E-value: 2.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   895 TRQRFSRQIALYRKSVALLKNSKEIEKILFRLNEHSRAKYTssahstiRDLEKLVSHIKLTTSANDHFEKAENAYEhyvK 974
Cdd:pfam01576  511 AKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQ-------RELEALTQQLEEKAAAYDKLEKTKNRLQ---Q 580

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   975 RVDSMIADL-----------KKQQKSDE-LAEI---------ERKR--RESEEKERLEIEAKKEAERQREIKRKLEEQQQ 1031
Cdd:pfam01576  581 ELDDLLVDLdhqrqlvsnleKKQKKFDQmLAEEkaisaryaeERDRaeAEAREKETRALSLARALEEALEAKEELERTNK 660

                          170       180       190
                   ....*....|....*....|....*....|...
gi 808358096  1032 NAQKEHENYLIS--EIHKAAEETEKKRQNEEKE 1062
Cdd:pfam01576  661 QLRAEMEDLVSSkdDVGKNVHELERSKRALEQQ 693
PTZ00121 PTZ00121
MAEBL; Provisional
 964-1067 3.10e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 3.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  964 KAENAYEHYVKRVDSMIADLKKQQKSDELAEIERKRRESEEKERLEIEAKKEAERQREIKRKLEE-------QQQNAQKE 1036
Cdd:PTZ00121 1195 KAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEarmahfaRRQAAIKA 1274

                          90       100       110
                  ....*....|....*....|....*....|...
gi 808358096 1037 HENYLISEIHKAAE--ETEKKRQNEEKEKLDKM 1067
Cdd:PTZ00121 1275 EEARKADELKKAEEkkKADEAKKAEEKKKADEA 1307
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 868-1075 3.20e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.97  E-value: 3.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   868 SVIKLKNKIAWRSAQVTRLQsIARGYLTRQRFSRQIALYRKSVALLKNSKEIEKilfrlNEHSRAKYTSSAHSTIRDLEK 947
Cdd:TIGR02168  734 DLARLEAEVEQLEERIAQLS-KELTELEAEIEELEERLEEAEEELAEAEAEIEE-----LEAQIEQLKEELKALREALDE 807

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   948 LVSHIKLTtsaNDHFEKAENAYEHYVKRVDSMIADLK--KQQKSDELAEIERKRRESEEKERLEIEAKKEAERQREIKRK 1025
Cdd:TIGR02168  808 LRAELTLL---NEEAANLRERLESLERRIAATERRLEdlEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS 884

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 808358096  1026 LEEQQQNAQKEHENyLISEIHKAaeETEKKRQNEEKEKLDKMVS---NRLAEA 1075
Cdd:TIGR02168  885 LEEALALLRSELEE-LSEELREL--ESKRSELRRELEELREKLAqleLRLEGL 934
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
984-1076 3.42e-03

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 41.56  E-value: 3.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  984 KKQQKSDElAEIERKRRESEEKERLEIEAKKEAERQREIKRKLEEQQQnaqkehenyliseihKAAEETEKKRQNEEKEK 1063
Cdd:COG3064     4 ALEEKAAE-AAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAK---------------RQAEEEAREAKAEAEQR 67

                          90
                  ....*....|....*.
gi 808358096 1064 LDKMVS---NRLAEAD 1076
Cdd:COG3064    68 AAELAAeaaKKLAEAE 83
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
912-1079 3.64e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 3.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  912 LLKNSKEIEKILFRLNEHSRAKYTSSahsTIRDLEKLVSHIKLttsandhfEKAENAYEHYVKrVDSMIADLKKQQKS-- 989
Cdd:PRK03918  478 LRKELRELEKVLKKESELIKLKELAE---QLKELEEKLKKYNL--------EELEKKAEEYEK-LKEKLIKLKGEIKSlk 545

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  990 ---DELAEIERKRRESEEKERlEIEAKKeAERQREIKRK-------LEEQQQNAQKEHENYLISEIHKAAEETEKKRQNE 1059
Cdd:PRK03918  546 kelEKLEELKKKLAELEKKLD-ELEEEL-AELLKELEELgfesveeLEERLKELEPFYNEYLELKDAEKELEREEKELKK 623

                         170       180
                  ....*....|....*....|
gi 808358096 1060 EKEKLDKMVSNrLAEADGVA 1079
Cdd:PRK03918  624 LEEELDKAFEE-LAETEKRL 642
HOATZ-like pfam17664
Cilia- and flagella-associated protein HOATZ-like; This entry represents cilia- and ...
 988-1057 3.74e-03

Cilia- and flagella-associated protein HOATZ-like; This entry represents cilia- and flagella-associated protein, HOATZ, and related proteins, found in metazoa. In mice HOATZ is encoded by the gene designated 4833427G06Rik (C11orf88). Mouse Hoatz mRNA is specifically expressed in tissues with motile cilia and flagella. Hoatz knockout mice developed hydrocephalus and male infertility, and the ependymal cilia frequently showed disorganized axonemes.


Pssm-ID: 465445  Cd Length: 168  Bit Score: 39.71  E-value: 3.74e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   988 KSDELAEIERKRRESEEKERLEIEAKKEAERQREIKRKLEEQqqnAQKEhenyLISEIHKAAEETEKKRQ 1057
Cdd:pfam17664   89 KNTDILAEALKIQESEEKEKYLQKAKKRDEILQLLRKQREER---ILKE----LISLPYKPKGKVHKAKK 151
AhaH TIGR02926
ATP synthase archaeal, H subunit; he A1/A0 ATP synthase is homologous to the V-type (V1/V0, ...
 983-1065 3.96e-03

ATP synthase archaeal, H subunit; he A1/A0 ATP synthase is homologous to the V-type (V1/V0, vacuolar) ATPase, but functions in the ATP synthetic direction as does the F1/F0 ATPase of bacteria. The hydrophilic A1 "stalk" complex (AhaABCDEFG) is the site of ATP generation and is coupled to the membrane-embedded proton translocating A0 complex. It is unclear precisely where AhaH fits into these complexes.


Pssm-ID: 131972 [Multi-domain]  Cd Length: 85  Bit Score: 37.52  E-value: 3.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   983 LKKQQKSDELAEiERKRRESEEKERLEIEAKKEAerqREIkrkLEEQQQNAQKEHENYLISEIHKAAEETEKKRQNEEKE 1062
Cdd:TIGR02926    1 LEEIKKAEEDAE-ELIEEAEEERKQRIAEAREEA---REL---LEEAEEEASKLGEEIIKEAEEEIEKEAEKIREEGEKE 73


                   ...
gi 808358096  1063 KLD 1065
Cdd:TIGR02926   74 IEA 76
Stathmin pfam00836
Stathmin family; The Stathmin family of proteins play an important role in the regulation of ...
 986-1071 4.41e-03

Stathmin family; The Stathmin family of proteins play an important role in the regulation of the microtubule cytoskeleton. They regulate microtubule dynamics by promoting depolymerization of microtubules and/or preventing polymerization of tubulin heterodimers.


Pssm-ID: 459956 [Multi-domain]  Cd Length: 136  Bit Score: 38.87  E-value: 4.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   986 QQKSDELAEIERK------RRESEEKERLEIEAKKEaERQREIKRKLEEQQQNAQKEHENYL------ISEIHKAAEETE 1053
Cdd:pfam00836   38 KKKDSSLEEIQKKleaaeeRRKSLEAQKLKQLAEKR-EKEEEALQKADEENNNFSKMAEEKLkqkmeaYKENREAQIAAL 116

                           90
                   ....*....|....*...
gi 808358096  1054 KKRQNEEKEKLDKMVSNR 1071
Cdd:pfam00836  117 KEKLKEKEKHVEEVRKNK 134
PTZ00121 PTZ00121
MAEBL; Provisional
 963-1076 4.84e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 4.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  963 EKAENAYEHYVKRVDSMIADLKKQQKSDELAEIERKR-----RESEEKERLE----IEAKKEAE--------RQREIKRK 1025
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKkadeaKKAEEAKKADeakkAEEKKKADelkkaeelKKAEEKKK 1565

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 808358096 1026 LEEQQQNAQKEHENYLISEIHKAAEETEKKRQNEEKEKLDKMVSNRLAEAD 1076
Cdd:PTZ00121 1566 AEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAE 1616
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
942-1062 4.85e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 4.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  942 IRDLEKLVSHIKLTTSANDHFEKAENAYEHYVK---RVDSMIADLKKQQKS--DELAEIERKRRESEEKERLEIEAKKEA 1016
Cdd:PRK03918  275 IEELEEKVKELKELKEKAEEYIKLSEFYEEYLDelrEIEKRLSRLEEEINGieERIKELEEKEERLEELKKKLKELEKRL 354

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 808358096 1017 ERQREIKRKLEE------QQQNAQKEHENYLISEIHKAAEETEKKRQNEEKE 1062
Cdd:PRK03918  355 EELEERHELYEEakakkeELERLKKRLTGLTPEKLEKELEELEKAKEEIEEE 406
PRK08404 PRK08404
V-type ATP synthase subunit H; Validated
 990-1063 5.01e-03

V-type ATP synthase subunit H; Validated


Pssm-ID: 169428 [Multi-domain]  Cd Length: 103  Bit Score: 37.85  E-value: 5.01e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 808358096  990 DELAEIERKRRESEEK-ERLEIEAKKEAERQREIKRKLEEQQQNAQKEHENYLISEIHKAAEEtEKKRQNEEKEK 1063
Cdd:PRK08404    3 DVIKEIVKAEKEAEERiEKAKEEAKKIIRKAKEEAKKIEEEIIKKAEEEAQKLIEKKKKEGEE-EAKKILEEGEK 76
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
 984-1067 6.93e-03

Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.


Pssm-ID: 402959 [Multi-domain]  Cd Length: 164  Bit Score: 38.90  E-value: 6.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   984 KKQQKSDELAEIERKRRESEEKERLEIEAKKEAERQREIKRKLEEQQQNAQKEHENYLISEIHKAAEETEKKRQNE--EK 1061
Cdd:pfam11600    1 RRSQKSVQSQEEKEKQRLEKDKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEARRKKEEEKELKEKERREKKEkdEK 80


                   ....*.
gi 808358096  1062 EKLDKM 1067
Cdd:pfam11600   81 EKAEKL 86
PRK12705 PRK12705
hypothetical protein; Provisional
 846-1052 7.17e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 40.46  E-value: 7.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  846 LIQKVNEWLVGARWKQSQYAVWSVIKLKNKIAWRSAQVTRLQSIARGYLTRQRfSRQIALYRKSVALLKNSkeiEKILFR 925
Cdd:PRK12705   13 LIGLLLGVLVVLLKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRER-NQQRQEARREREELQRE---EERLVQ 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  926 LNEhsrakytssahstirDLEKLVSHIKLTTSANDHFEKAENAYEHYVkrvdsmiaDLKKQQKSDELAEIERKRRESEEK 1005
Cdd:PRK12705   89 KEE---------------QLDARAEKLDNLENQLEEREKALSARELEL--------EELEKQLDNELYRVAGLTPEQARK 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 808358096 1006 E---RLEIEAKKEAerQREIKRKLEEQQQNAQKEHENYLISEIHKAAEET 1052
Cdd:PRK12705  146 LllkLLDAELEEEK--AQRVKKIEEEADLEAERKAQNILAQAMQRIASET 193
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 963-1076 7.51e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 40.29  E-value: 7.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096   963 EKAENAYEHYVKRVDSMIADLKKQQKSDELAEIERKRRESEEKERLeIEAKKEAERqreIKRKLEEQQQNAQKEHENYLI 1042
Cdd:pfam13868  221 QKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERM-LRKQAEDEE---IEQEEAEKRRMKRLEHRRELE 296

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 808358096  1043 SEI--HKAAEETEKKRQNEEKEKLDKMVSNRLAEAD 1076
Cdd:pfam13868  297 KQIeeREEQRAAEREEELEEGERLREEEAERRERIE 332
UDM1_RNF168_RNF169-like cd22249
UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, ...
 992-1035 7.61e-03

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: 36.09  E-value: 7.61e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 808358096  992 LAEIERKRRESEEKERLEIEAKKEAERQREIKRKLEEQQQNAQK 1035
Cdd:cd22249    18 LEEERRKEREEEEKASEELIRKLQEEEERQRKREREEQLKQDEE 61
PTZ00121 PTZ00121
MAEBL; Provisional
 963-1067 7.77e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 7.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  963 EKAENAYEHYVKRVDSMIADLKKQQKSDELAEIERKRRESEEKE---RLEIEAKKEAERQREIKRKLEEQQ-----QNAQ 1034
Cdd:PTZ00121 1534 KKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNmalRKAEEAKKAEEARIEEVMKLYEEEkkmkaEEAK 1613

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 808358096 1035 KEHENYLISEIHKAAEETEK------KRQNEEKEKLDKM 1067
Cdd:PTZ00121 1614 KAEEAKIKAEELKKAEEEKKkveqlkKKEAEEKKKAEEL 1652
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
 944-1081 8.10e-03

Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442073 [Multi-domain]  Cd Length: 171  Bit Score: 38.66  E-value: 8.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  944 DLEKLVSHIKLTTSANDHFEKAENAYEhyvKRVDSMIADLKKQQKsdelaEIERKRRESEEKERleieakkeAERQREIK 1023
Cdd:COG2825    30 DVQRILQESPEGKAAQKKLEKEFKKRQ---AELQKLEKELQALQE-----KLQKEAATLSEEER--------QKKERELQ 93

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096 1024 RKLEEQQQNAQkehenyliseihKAAEETEKKRQNEEKEKLDKM--VSNRLAEADGVALI 1081
Cdd:COG2825    94 KKQQELQRKQQ------------EAQQDLQKRQQELLQPILEKIqkAIKEVAKEEGYDLV 141
Nup88 pfam10168
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ...
 961-1035 9.22e-03

Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.


Pssm-ID: 462975 [Multi-domain]  Cd Length: 713  Bit Score: 40.41  E-value: 9.22e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 808358096   961 HFEKAENAYEHYVKRVDsMIADLKKQQksdeLAEIERKRresEEKERLEIEAKKEAERQREIKRKLEEQQQNAQK 1035
Cdd:pfam10168  548 YLKKHDLAREEIQKRVK-LLKLQKEQQ----LQELQSLE---EERKSLSERAEKLAEKYEEIKDKQEKLMRRCKK 614
PRK00106 PRK00106
ribonuclease Y;
867-1075 9.80e-03

ribonuclease Y;


Pssm-ID: 178867 [Multi-domain]  Cd Length: 535  Bit Score: 40.24  E-value: 9.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  867 WSVIKLKNKIAWRSAQVTRLQSIARGYLTRQRFSRQIALYRKSVAllKNSKEIEK-ILFRLNEHSRaKYTSSAH----ST 941
Cdd:PRK00106   19 YVLISIKMKSAKEAAELTLLNAEQEAVNLRGKAERDAEHIKKTAK--RESKALKKeLLLEAKEEAR-KYREEIEqefkSE 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808358096  942 IRDLEKLVShiKLTTSANDHFEKAENAYEhyvkrvDSMIADLKKQQKSDELAEIERKrreseEKERLEIEAKKEAERQRE 1021
Cdd:PRK00106   96 RQELKQIES--RLTERATSLDRKDENLSS------KEKTLESKEQSLTDKSKHIDER-----EEQVEKLEEQKKAELERV 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 808358096 1022 IKRKLEEQQQNAQKEHENYLISEIHKAAEETEKkrqnEEKEKLDKMVSNRLAEA 1075
Cdd:PRK00106  163 AALSQAEAREIILAETENKLTHEIATRIREAER----EVKDRSDKMAKDLLAQA 212
 
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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