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Conserved domains on  [gi|1063705616|ref|NP_001324212|]
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myosin XI D [Arabidopsis thaliana]

Protein Classification

kinesin family protein; myosin/kinesin family protein( domain architecture ID 13678080)

kinesin family protein is a microtubule-dependent molecular motor that plays an important role in intracellular transport and in cell division and has an ATPase-containing motor domain; similar to N-type kinesins that are (+) end-directed motors and have an N-terminal motor domain| myosin/kinesin family protein; contains an ATPase-containing motor domain found in myosins and kinesins, which provides the driving force in myosin and kinesin mediated processes; may have a coiled-coil segment C-terminal to the motor domain

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MYSc_Myo11 cd01384
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ...
 74-718 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: 1382.39  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   74 PGVLLNLKARYNANEIYTYTGNILIAVNPFKRLPHLYGNEIMEQYKGTDFGELSPHPFAVADSAYRKMINEGVSQAILVS 153
Cdd:cd01384      1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPHLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  154 GESGAGKTESTKMLMQYLAYMGGKAESEGRSVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFNHMGRISGAAIR 233
Cdd:cd01384     81 GESGAGKTETTKMLMQYLAYMGGRAVTEGRSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAAIR 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  234 TYLLERSRVCQVSDPERNYHCFYMLCA-APEQETERYQLGKPSTFHYLNQSNCHALDAIDDSKEYLATRKAMDVVGISPE 312
Cdd:cd01384    161 TYLLERSRVVQVSDPERNYHCFYQLCAgAPPEDREKYKLKDPKQFHYLNQSKCFELDGVDDAEEYRATRRAMDVVGISEE 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  313 EQDAIFRVVAAILHLGNIEFAKSEESDGAEPKDDKSRFHLKVAAKLFMCDEKALENSLCNRVMVTRGESITKPLDPGSAA 392
Cdd:cd01384    241 EQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKSEFHLKAAAELLMCDEKALEDALCKRVIVTPDGIITKPLDPDAAT 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  393 LSRDALAKIVYSKLFDWLVTKINNSIGQDSSSKYIIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKMEQEEY 472
Cdd:cd01384    321 LSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQHVFKMEQEEY 400

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  473 TKEEIDWSYIEFIDNQDVLDLIEKKPGGIIALLDEACMFPRSTHDTLAEKLYQTFGSHKRFTKPKLARTDFTICHYAGDV 552
Cdd:cd01384    401 TKEEIDWSYIEFVDNQDVLDLIEKKPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHKRFSKPKLSRTDFTIDHYAGDV 480

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  553 TYQTELFLDKNKDYVVGEHQSLMNSSDCSFVSSLFPKSREESSKSSKF-SSIGSQFKQQLQSLLETLNTTEPHYIRCVKP 631
Cdd:cd01384    481 TYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPREGTSSSSKfSSIGSRFKQQLQELMETLNTTEPHYIRCIKP 560

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  632 NNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILAPEATERSFDEVDACKKLLARVDLKGFQIG 711
Cdd:cd01384    561 NNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPEVLKGSDDEKAACKKILEKAGLKGYQIG 640


                   ....*..
gi 1063705616  712 KTKVFLR 718
Cdd:cd01384    641 KTKVFLR 647
MyosinXI_CBD cd15475
cargo binding domain of myosin XI; Class XI myosins are a plant specific group, homologous to ...
 1274-1715 8.36e-179

cargo binding domain of myosin XI; Class XI myosins are a plant specific group, homologous to class V myosins. C-terminal domain of Arabidopsis myosin XI has been shown to be homologous to the cargo-binding domain of yeast myosin V myo2p, which targets myosin to vacuole- and mitochondria, as well as secretory vesicle.


:

Pssm-ID: 271259  Cd Length: 326  Bit Score: 540.62  E-value: 8.36e-179
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1274 QQPHEFVDVLLKCVSKNVGFSHGKPVAAFTIYKCLIHWKLFEAEKTSVFDRIVPIFGSAIENPEDDSNLAYWLTNTSTLL 1353
Cdd:cd15475      1 ERQQENVDALIKCVSENLGFSEGKPVAAFTIYKCLLHWKSFEAEKTSVFDRIIQTIGSAIEDQDNNDHLAYWLSNTSTLL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1354 FLLQRSLkshsttgaspkkppqptsffgrmtqgfrspssaslsgdvvqqvdaryPALLFKQQLTAYIETIYGIFQENVKR 1433
Cdd:cd15475     81 FLLQRSL-----------------------------------------------PALLFKQQLTAYVEKIYGIIRDNLKK 113

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1434 KLAPVLSSCIQGLKDSShefsaetlsaesseqnspekpseenppeklsednssgklsedylaakpsednspakpseensq 1513
Cdd:cd15475    114 ELSPLLSLCIQAPRTSR--------------------------------------------------------------- 130

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1514 aklsevnpqAKPSAENSLAKPSEENSPTETWQDVIGLLNQLLGTLKKNYVPLFLAQKIFCQTFQDINVQLFNSLL-QREC 1592
Cdd:cd15475    131 ---------GSSSKSSSSANSLGQQSPSSHWQSIIKSLNSLLSTLKENHVPPFLVQKIFTQVFSFINVQLFNSLLlRREC 201

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1593 CTFIMGKKVNVWLNELESWCSQATEDFVGSSWDELKNTRQALVLLVTEQKSTITYDDLTTNLCPALSTQQLYRICTLCKI 1672
Cdd:cd15475    202 CSFSNGEYVKAGLAELELWCSQATEEYAGSSWDELKHIRQAVGFLVIHQKSRKSYDEITNDLCPVLSVQQLYRICTMYWD 281

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 1063705616 1673 DDHEDQNVSPDVISNLKLLVTDEDED--SRSFLLDNNSSIPFAAD 1715
Cdd:cd15475    282 DKYGTQSVSPEVISSMRVLMTEDSNNavSNSFLLDDDSSIPFSVE 326
Mplasa_alph_rch super family cl37461
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 885-1180 2.24e-11

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


The actual alignment was detected with superfamily member TIGR04523:

Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 68.89  E-value: 2.24e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  885 LQDAKTKLEKEVEELTS-CLELEKQMRMELEQVKT---------QEVEDLRSALNDMKLQLGETQVTKSEeilkLQSALQ 954
Cdd:TIGR04523  340 LNEQISQLKKELTNSESeNSEKQRELEEKQNEIEKlkkenqsykQEIKNLESQINDLESKIQNQEKLNQQ----KDEQIK 415

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  955 DMQLEFEELAKELEmtnDLAAENEQLKDLVSSLQRKIDESDSKYEETSKLSEErVKQEVPVIDqgviIKLEAENQKLKAL 1034
Cdd:TIGR04523  416 KLQQEKELLEKEIE---RLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES-LETQLKVLS----RSINKIKQNLEQK 487

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1035 VSTLEKK---IDSLDRKHDVTSSNISDqLKESASSDYEMLSNLAAENERLKALVSSLENE-NYENDGNDSPNeqkegpqm 1110
Cdd:TIGR04523  488 QKELKSKekeLKKLNEEKKELEEKVKD-LTKKISSLKEKIEKLESEKKEKESKISDLEDElNKDDFELKKEN-------- 558

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063705616 1111 LKEEILAEDFSIDD--EMTNKLAAENKDLYDLVDLLERKIDETEKKYEEASKLCEERLKQVVDTEKKYEEAS 1180
Cdd:TIGR04523  559 LEKEIDEKNKEIEElkQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLS 630
Myosin_N pfam02736
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ...
 7-50 5.93e-07

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


:

Pssm-ID: 460670  Cd Length: 45  Bit Score: 47.43  E-value: 5.93e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1063705616    7 TVGSQVWVEDPDEAWLDGEVVEANGQEIKVNCQT-KTVVAKVNAV 50
Cdd:pfam02736    1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVETEDgKTVTVKKDDV 45
 
Name Accession Description Interval E-value
MYSc_Myo11 cd01384
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ...
 74-718 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: 1382.39  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   74 PGVLLNLKARYNANEIYTYTGNILIAVNPFKRLPHLYGNEIMEQYKGTDFGELSPHPFAVADSAYRKMINEGVSQAILVS 153
Cdd:cd01384      1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPHLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  154 GESGAGKTESTKMLMQYLAYMGGKAESEGRSVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFNHMGRISGAAIR 233
Cdd:cd01384     81 GESGAGKTETTKMLMQYLAYMGGRAVTEGRSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAAIR 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  234 TYLLERSRVCQVSDPERNYHCFYMLCA-APEQETERYQLGKPSTFHYLNQSNCHALDAIDDSKEYLATRKAMDVVGISPE 312
Cdd:cd01384    161 TYLLERSRVVQVSDPERNYHCFYQLCAgAPPEDREKYKLKDPKQFHYLNQSKCFELDGVDDAEEYRATRRAMDVVGISEE 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  313 EQDAIFRVVAAILHLGNIEFAKSEESDGAEPKDDKSRFHLKVAAKLFMCDEKALENSLCNRVMVTRGESITKPLDPGSAA 392
Cdd:cd01384    241 EQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKSEFHLKAAAELLMCDEKALEDALCKRVIVTPDGIITKPLDPDAAT 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  393 LSRDALAKIVYSKLFDWLVTKINNSIGQDSSSKYIIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKMEQEEY 472
Cdd:cd01384    321 LSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQHVFKMEQEEY 400

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  473 TKEEIDWSYIEFIDNQDVLDLIEKKPGGIIALLDEACMFPRSTHDTLAEKLYQTFGSHKRFTKPKLARTDFTICHYAGDV 552
Cdd:cd01384    401 TKEEIDWSYIEFVDNQDVLDLIEKKPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHKRFSKPKLSRTDFTIDHYAGDV 480

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  553 TYQTELFLDKNKDYVVGEHQSLMNSSDCSFVSSLFPKSREESSKSSKF-SSIGSQFKQQLQSLLETLNTTEPHYIRCVKP 631
Cdd:cd01384    481 TYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPREGTSSSSKfSSIGSRFKQQLQELMETLNTTEPHYIRCIKP 560

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  632 NNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILAPEATERSFDEVDACKKLLARVDLKGFQIG 711
Cdd:cd01384    561 NNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPEVLKGSDDEKAACKKILEKAGLKGYQIG 640


                   ....*..
gi 1063705616  712 KTKVFLR 718
Cdd:cd01384    641 KTKVFLR 647
MYSc smart00242
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...
 58-726 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: 1027.87  E-value: 0e+00
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616    58 PELGVDDMTKLAYLHEPGVLLNLKARYNANEIYTYTGNILIAVNPFKRLPhLYGNEIMEQYKGTDFGELSPHPFAVADSA 137
Cdd:smart00242    4 KFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLP-IYTDEVIKKYRGKSRGELPPHVFAIADNA 82

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   138 YRKMINEGVSQAILVSGESGAGKTESTKMLMQYLAYMGGKAEsEGRSVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFV 217
Cdd:smart00242   83 YRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNT-EVGSVEDQILESNPILEAFGNAKTLRNNNSSRFGKFI 161

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   218 EIQFNHMGRISGAAIRTYLLERSRVCQVSDPERNYHCFYMLCA-APEQETERYQLGKPSTFHYLNQSNCHALDAIDDSKE 296
Cdd:smart00242  162 EIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAgASEELKKELGLKSPEDYRYLNQGGCLTVDGIDDAEE 241

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   297 YLATRKAMDVVGISPEEQDAIFRVVAAILHLGNIEFAKSEESDGAEPKDDKSrfHLKVAAKLFMCDEKALENSLCNRVMV 376
Cdd:smart00242  242 FKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKE--ELSNAAELLGVDPEELEKALTKRKIK 319

                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   377 TRGESITKPLDPGSAALSRDALAKIVYSKLFDWLVTKINNSIGQDSSSKYIIGVLDIYGFESFKTNSFEQFCINLTNEKL 456
Cdd:smart00242  320 TGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSFEQLCINYANEKL 399

                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   457 QQHFNQHVFKMEQEEYTKEEIDWSYIEFIDNQDVLDLIEKKPGGIIALLDEACMFPRSTHDTLAEKLYQTFGSHKRFTKP 536
Cdd:smart00242  400 QQFFNQHVFKLEQEEYEREGIDWTFIDFFDNQDCIDLIEKKPPGILSLLDEECRFPKGTDQTFLEKLNQHHKKHPHFSKP 479

                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   537 -KLARTDFTICHYAGDVTYQTELFLDKNKDYVVGEHQSLMNSSDCSFVSSLFPKSREESSKSSKFSSIGSQFKQQLQSLL 615
Cdd:smart00242  480 kKKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVSNAGSKKRFQTVGSQFKEQLNELM 559

                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   616 ETLNTTEPHYIRCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILAPEATER-SFDEVD 694
Cdd:smart00242  560 DTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFDEFLQRYRVLLPDTWPPwGGDAKK 639

                           650       660       670
                    ....*....|....*....|....*....|....
gi 1063705616   695 ACKKLLARVDLK--GFQIGKTKVFLRAGQMAELD 726
Cdd:smart00242  640 ACEALLQSLGLDedEYQLGKTKVFLRPGQLAELE 673
COG5022 COG5022
Myosin heavy chain [General function prediction only];
1-1238 0e+00

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 884.42  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616    1 MASVKVTVGSQVWVEDPDEAWLDGEVVEANGQEIKVNCQTKTVVAKVNAVHPKDPEF------PELGVDDMTKLAYLHEP 74
Cdd:COG5022      1 MSTTNAEVGSGCWIPDEEKGWIWAEIIKEAFNKGKVTEEGKKEDGESVSVKKKVLGNdriklpKFDGVDDLTELSYLNEP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   75 GVLLNLKARYNANEIYTYTGNILIAVNPFKRLPhLYGNEIMEQYKGTDFGELSPHPFAVADSAYRKMINEGVSQAILVSG 154
Cdd:COG5022     81 AVLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLG-IYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISG 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  155 ESGAGKTESTKMLMQYLAYMGGKAESEGRSVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFNHMGRISGAAIRT 234
Cdd:COG5022    160 ESGAGKTENAKRIMQYLASVTSSSTVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIET 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  235 YLLERSRVCQVSDPERNYHCFYMLCA-APEQETERYQLGKPSTFHYLNQSNCHALDAIDDSKEYLATRKAMDVVGISPEE 313
Cdd:COG5022    240 YLLEKSRVVHQNKNERNYHIFYQLLAgDPEELKKLLLLQNPKDYIYLSQGGCDKIDGIDDAKEFKITLDALKTIGIDEEE 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  314 QDAIFRVVAAILHLGNIEFaKSEESDGAEPKDDKsrfHLKVAAKLFMCDEKALENSLCNRVMVTRGESITKPLDPGSAAL 393
Cdd:COG5022    320 QDQIFKILAAILHIGNIEF-KEDRNGAAIFSDNS---VLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALA 395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  394 SRDALAKIVYSKLFDWLVTKINNSIGQDSSSKYIIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKMEQEEYT 473
Cdd:COG5022    396 IRDSLAKALYSNLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYV 475

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  474 KEEIDWSYIEFIDNQDVLDLIEKK-PGGIIALLDEACMFPRSTHDTLAEKLYQTF--GSHKRFTKPKLARTDFTICHYAG 550
Cdd:COG5022    476 KEGIEWSFIDYFDNQPCIDLIEKKnPLGILSLLDEECVMPHATDESFTSKLAQRLnkNSNPKFKKSRFRDNKFVVKHYAG 555

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  551 DVTYQTELFLDKNKDYVVGEHQSLMNSSDCSFVSSLFPkSREESSKSSKFSSIGSQFKQQLQSLLETLNTTEPHYIRCVK 630
Cdd:COG5022    556 DVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFD-DEENIESKGRFPTLGSRFKESLNSLMSTLNSTQPHYIRCIK 634

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  631 PNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILAPEAT-----ERSFDEVDACKKLL--ARV 703
Cdd:COG5022    635 PNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKSwtgeyTWKEDTKNAVKSILeeLVI 714

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  704 DLKGFQIGKTKVFLRAGQMAELDAHRAEVLGHSARIIQRKVITYLSRKKYLLLQSASTEIQAFCRGHIARVQFKATRREA 783
Cdd:COG5022    715 DSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLRRLVDYELKWR 794

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  784 ASVRIQKQARTYICQTAFKKLCASAISIQSGLRAMAARVEFQYR-TKRKAAIIIQSQIRRCLCRRRYLRTKKAAITTQCG 862
Cdd:COG5022    795 LFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIKREKKLRETEEVeFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSA 874

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  863 WRVKVAHRELRKLKMAAKETGALQDAKTKLEKEVEELTSclELEKQMRMELEqVKTQEVEDLRSALNDMKLQLGET-QVT 941
Cdd:COG5022    875 QRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKK--SLSSDLIENLE-FKTELIARLKKLLNNIDLEEGPSiEYV 951

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  942 KSEEILKLQ---SALQDMQLEFEELAKELEMT-NDLAAENEQLKDLVSSLQRKIDESDSKYEETSKLSEERVKqevpvid 1017
Cdd:COG5022    952 KLPELNKLHeveSKLKETSEEYEDLLKKSTILvREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVE------- 1024

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1018 qgvIIKLEAENQKLKALVSTL--EKKIDSLDRKHDvtssnisdqLKESA-SSDYEMLSNLAAENERLKALVSSLENENYE 1094
Cdd:COG5022   1025 ---VAELQSASKIISSESTELsiLKPLQKLKGLLL---------LENNQlQARYKALKLRRENSLLDDKQLYQLESTENL 1092

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1095 NDGNDSPNEQKEGPQMLKEEilAEDFSIDDEMTNklaaeNKDLYDLVDLLERKIDETEKKYEEASKLCEER--LKQVVDT 1172
Cdd:COG5022   1093 LKTINVKDLEVTNRNLVKPA--NVLQFIVAQMIK-----LNLLQEISKFLSQLVNTLEPVFQKLSVLQLELdgLFWEANL 1165

                         1210      1220      1230      1240      1250      1260      1270
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1173 EKK--YEEASRLCEERLKQVVDTETKLIELKTSMQRLEEKVSDMEAEDK--ILRQQALRNSASRKMSPQV 1238
Cdd:COG5022   1166 EALpsPPPFAALSEKRLYQSALYDEKSKLSSSEVNDLKNELIALFSKIFsgWPRGDKLKKLISEGWVPTE 1235
Myosin_head pfam00063
Myosin head (motor domain);
62-718 0e+00

Myosin head (motor domain);


Pssm-ID: 395017 [Multi-domain]  Cd Length: 674  Bit Score: 878.92  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   62 VDDMTKLAYLHEPGVLLNLKARYNANEIYTYTGNILIAVNPFKRLPhLYGNEIMEQYKGTDFGELSPHPFAVADSAYRKM 141
Cdd:pfam00063    1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLP-IYSEDMIKAYRGKRRGELPPHIFAIADEAYRSM 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  142 INEGVSQAILVSGESGAGKTESTKMLMQYLAYMGGKAES-EGRSVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQ 220
Cdd:pfam00063   80 LQDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAgNVGRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQ 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  221 FNHMGRISGAAIRTYLLERSRVCQVSDPERNYHCFYMLCA-APEQETERYQLGKPSTFHYLNQSNCHALDAIDDSKEYLA 299
Cdd:pfam00063  160 FDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAgASAQLKKELRLTNPKDYHYLSQSGCYTIDGIDDSEEFKI 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  300 TRKAMDVVGISPEEQDAIFRVVAAILHLGNIEFAKSEESDGAEPKDDKSrfhLKVAAKLFMCDEKALENSLCNRVMVTRG 379
Cdd:pfam00063  240 TDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTEN---LQKAASLLGIDSTELEKALCKRRIKTGR 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  380 ESITKPLDPGSAALSRDALAKIVYSKLFDWLVTKINNSIGQDSSSK-YIIGVLDIYGFESFKTNSFEQFCINLTNEKLQQ 458
Cdd:pfam00063  317 ETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKaSFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQ 396

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  459 HFNQHVFKMEQEEYTKEEIDWSYIEFIDNQDVLDLIEKKPGGIIALLDEACMFPRSTHDTLAEKLYQTFGSHKRFTKPKL 538
Cdd:pfam00063  397 FFNHHMFKLEQEEYVREGIEWTFIDFGDNQPCIDLIEKKPLGILSLLDEECLFPKATDQTFLDKLYSTFSKHPHFQKPRL 476

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  539 -ARTDFTICHYAGDVTYQTELFLDKNKDYVVGEHQSLMNSSDCSFVSSLFPKSREESSKSSKFSS--------------I 603
Cdd:pfam00063  477 qGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGkstpkrtkkkrfitV 556

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  604 GSQFKQQLQSLLETLNTTEPHYIRCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILAP 683
Cdd:pfam00063  557 GSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRYRILAP 636

                          650       660       670
                   ....*....|....*....|....*....|....*...
gi 1063705616  684 EATERSF-DEVDACKKLLARVDL--KGFQIGKTKVFLR 718
Cdd:pfam00063  637 KTWPKWKgDAKKGCEAILQSLNLdkEEYQFGKTKIFFR 674
MyosinXI_CBD cd15475
cargo binding domain of myosin XI; Class XI myosins are a plant specific group, homologous to ...
 1274-1715 8.36e-179

cargo binding domain of myosin XI; Class XI myosins are a plant specific group, homologous to class V myosins. C-terminal domain of Arabidopsis myosin XI has been shown to be homologous to the cargo-binding domain of yeast myosin V myo2p, which targets myosin to vacuole- and mitochondria, as well as secretory vesicle.


Pssm-ID: 271259  Cd Length: 326  Bit Score: 540.62  E-value: 8.36e-179
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1274 QQPHEFVDVLLKCVSKNVGFSHGKPVAAFTIYKCLIHWKLFEAEKTSVFDRIVPIFGSAIENPEDDSNLAYWLTNTSTLL 1353
Cdd:cd15475      1 ERQQENVDALIKCVSENLGFSEGKPVAAFTIYKCLLHWKSFEAEKTSVFDRIIQTIGSAIEDQDNNDHLAYWLSNTSTLL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1354 FLLQRSLkshsttgaspkkppqptsffgrmtqgfrspssaslsgdvvqqvdaryPALLFKQQLTAYIETIYGIFQENVKR 1433
Cdd:cd15475     81 FLLQRSL-----------------------------------------------PALLFKQQLTAYVEKIYGIIRDNLKK 113

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1434 KLAPVLSSCIQGLKDSShefsaetlsaesseqnspekpseenppeklsednssgklsedylaakpsednspakpseensq 1513
Cdd:cd15475    114 ELSPLLSLCIQAPRTSR--------------------------------------------------------------- 130

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1514 aklsevnpqAKPSAENSLAKPSEENSPTETWQDVIGLLNQLLGTLKKNYVPLFLAQKIFCQTFQDINVQLFNSLL-QREC 1592
Cdd:cd15475    131 ---------GSSSKSSSSANSLGQQSPSSHWQSIIKSLNSLLSTLKENHVPPFLVQKIFTQVFSFINVQLFNSLLlRREC 201

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1593 CTFIMGKKVNVWLNELESWCSQATEDFVGSSWDELKNTRQALVLLVTEQKSTITYDDLTTNLCPALSTQQLYRICTLCKI 1672
Cdd:cd15475    202 CSFSNGEYVKAGLAELELWCSQATEEYAGSSWDELKHIRQAVGFLVIHQKSRKSYDEITNDLCPVLSVQQLYRICTMYWD 281

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 1063705616 1673 DDHEDQNVSPDVISNLKLLVTDEDED--SRSFLLDNNSSIPFAAD 1715
Cdd:cd15475    282 DKYGTQSVSPEVISSMRVLMTEDSNNavSNSFLLDDDSSIPFSVE 326
PTZ00014 PTZ00014
myosin-A; Provisional
 48-718 6.66e-161

myosin-A; Provisional


Pssm-ID: 240229 [Multi-domain]  Cd Length: 821  Bit Score: 511.88  E-value: 6.66e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   48 NAVHPKDPE-FPELGVddmtkLAYLHEPGVLLNLKARYNANEIYTYTGNILIAVNPFKRLpHLYGNEIMEQYKGT-DFGE 125
Cdd:PTZ00014    88 NANSQIDPMtYGDIGL-----LPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDL-GNTTNDWIRRYRDAkDSDK 161

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  126 LSPHPFAVADSAYRKMINEGVSQAILVSGESGAGKTESTKMLMQYLAYmgGKAESEGRSVEQQVLESNPVLEAFGNAKTV 205
Cdd:PTZ00014   162 LPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFAS--SKSGNMDLKIQNAIMAANPVLEAFGNAKTI 239

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  206 RNNNSSRFGKFVEIQFNHMGRISGAAIRTYLLERSRVCQVSDPERNYHCFYMLC-AAPEQETERYQLGKPSTFHYLNqSN 284
Cdd:PTZ00014   240 RNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLkGANDEMKEKYKLKSLEEYKYIN-PK 318

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  285 CHALDAIDDSKEYLATRKAMDVVGISPEEQDAIFRVVAAILHLGNIEFAKSEE---SDGAEpKDDKSRFHLKVAAKLFMC 361
Cdd:PTZ00014   319 CLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEgglTDAAA-ISDESLEVFNEACELLFL 397

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  362 DEKALENSLCNRVMVTRGESITKPLDPGSAALSRDALAKIVYSKLFDWLVTKINNSIGQDSSSKYIIGVLDIYGFESFKT 441
Cdd:PTZ00014   398 DYESLKKELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKVFIGMLDIFGFEVFKN 477

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  442 NSFEQFCINLTNEKLQQHFNQHVFKMEQEEYTKEEIDWSYIEFIDNQDVLDLIEKKPGGIIALLDEACMFPRSTHDTLAE 521
Cdd:PTZ00014   478 NSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGKSVLSILEDQCLAPGGTDEKFVS 557

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  522 KLYQTFGSHKRFTKPKLA-RTDFTICHYAGDVTYQTELFLDKNKDYVVGEHQSLMNSSDCSFVSSLFPKSREESSKSSKF 600
Cdd:PTZ00014   558 SCNTNLKNNPKYKPAKVDsNKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGVEVEKGKLAKG 637

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  601 SSIGSQFKQQLQSLLETLNTTEPHYIRCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRI 680
Cdd:PTZ00014   638 QLIGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKY 717

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|.
gi 1063705616  681 LAPEATERS-FDEVDACKKLLARVDL--KGFQIGKTKVFLR 718
Cdd:PTZ00014   718 LDLAVSNDSsLDPKEKAEKLLERSGLpkDSYAIGKTMVFLK 758
DIL pfam01843
DIL domain; The DIL domain has no known function.
 1570-1674 8.78e-24

DIL domain; The DIL domain has no known function.


Pssm-ID: 460359 [Multi-domain]  Cd Length: 103  Bit Score: 97.28  E-value: 8.78e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1570 KIFCQTFQDINVQLFNSLLQR-ECCTFIMGKKVNVWLNELESWCSQAteDFVGSSWDELKNTRQALVLLVTeQKSTITYD 1648
Cdd:pfam01843    1 QLFSQLFYFINAELFNRLLLRkKYCSWSKGMQIRYNLSRLEEWARSN--GLESEARDHLAPLIQAAQLLQL-RKSTLEDL 77

                           90       100
                   ....*....|....*....|....*.
gi 1063705616 1649 DLTTNLCPALSTQQLYRICTLCKIDD 1674
Cdd:pfam01843   78 DSILQVCPALNPLQLHRLLTLYQPDD 103
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 885-1180 2.24e-11

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 68.89  E-value: 2.24e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  885 LQDAKTKLEKEVEELTS-CLELEKQMRMELEQVKT---------QEVEDLRSALNDMKLQLGETQVTKSEeilkLQSALQ 954
Cdd:TIGR04523  340 LNEQISQLKKELTNSESeNSEKQRELEEKQNEIEKlkkenqsykQEIKNLESQINDLESKIQNQEKLNQQ----KDEQIK 415

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  955 DMQLEFEELAKELEmtnDLAAENEQLKDLVSSLQRKIDESDSKYEETSKLSEErVKQEVPVIDqgviIKLEAENQKLKAL 1034
Cdd:TIGR04523  416 KLQQEKELLEKEIE---RLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES-LETQLKVLS----RSINKIKQNLEQK 487

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1035 VSTLEKK---IDSLDRKHDVTSSNISDqLKESASSDYEMLSNLAAENERLKALVSSLENE-NYENDGNDSPNeqkegpqm 1110
Cdd:TIGR04523  488 QKELKSKekeLKKLNEEKKELEEKVKD-LTKKISSLKEKIEKLESEKKEKESKISDLEDElNKDDFELKKEN-------- 558

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063705616 1111 LKEEILAEDFSIDD--EMTNKLAAENKDLYDLVDLLERKIDETEKKYEEASKLCEERLKQVVDTEKKYEEAS 1180
Cdd:TIGR04523  559 LEKEIDEKNKEIEElkQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLS 630
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
864-1227 2.83e-11

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 68.55  E-value: 2.83e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  864 RVKVAHRELRKLKM---------AAKETGALQDAKTKLEKEVEELTsclelekQMRMELEQvktqEVEDLRSALNDMKLQ 934
Cdd:PRK03918   366 EAKAKKEELERLKKrltgltpekLEKELEELEKAKEEIEEEISKIT-------ARIGELKK----EIKELKKAIEELKKA 434

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  935 LGETQVTK----------------------SEEILKLQSALQDMQLEFEELAKELEMTNDLAAEN---EQLKDLVSSLQR 989
Cdd:PRK03918   435 KGKCPVCGrelteehrkelleeytaelkriEKELKEIEEKERKLRKELRELEKVLKKESELIKLKelaEQLKELEEKLKK 514

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  990 -KIDESDSKYEETSKLSEERVKQEvpvidqGVIIKLEAENQKLKALVS---TLEKKIDSLDRKhdvtSSNISDQLKESAS 1065
Cdd:PRK03918   515 yNLEELEKKAEEYEKLKEKLIKLK------GEIKSLKKELEKLEELKKklaELEKKLDELEEE----LAELLKELEELGF 584

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1066 SDYEMLsnlaaeNERLKALvsslenENYENDGNDSPNEQKEGPQMLKE-EILAEDFSIDDEMTNKLAAENKDLYDLVDLL 1144
Cdd:PRK03918   585 ESVEEL------EERLKEL------EPFYNEYLELKDAEKELEREEKElKKLEEELDKAFEELAETEKRLEELRKELEEL 652

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1145 ERKIDETE-----KKYEEASKLCEERLKQVVDTEKKYEEASRLCEERLKQVVDTETKLIELKT------SMQRLEEKVSD 1213
Cdd:PRK03918   653 EKKYSEEEyeelrEEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKlekaleRVEELREKVKK 732

                          410
                   ....*....|....
gi 1063705616 1214 MEAEdkiLRQQALR 1227
Cdd:PRK03918   733 YKAL---LKERALS 743
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 885-1228 6.52e-10

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 63.72  E-value: 6.52e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  885 LQDAKTKLEKEVEELTSCLELEKQMRMELEQVKtQEVEDLRSALNDMKLQLGETqvtkseeILKLQSALQDMQLEFEELA 964
Cdd:pfam06160   95 LDDIEEDIKQILEELDELLESEEKNREEVEELK-DKYRELRKTLLANRFSYGPA-------IDELEKQLAEIEEEFSQFE 166

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  965 KELEMTNDLAAEN--EQLKDLVSSLQRKIDESDSKYEETSKLSEERVKQevpvIDQGvIIKLEAENQKLKALvsTLEKKI 1042
Cdd:pfam06160  167 ELTESGDYLEAREvlEKLEEETDALEELMEDIPPLYEELKTELPDQLEE----LKEG-YREMEEEGYALEHL--NVDKEI 239

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1043 DSLDRKHDVTSSNISDQLKESASSDYEMLsnlaaeNERLKALVSSLENE----NY--ENDGN--DSPNEQKEGPQMLKEE 1114
Cdd:pfam06160  240 QQLEEQLEENLALLENLELDEAEEALEEI------EERIDQLYDLLEKEvdakKYveKNLPEieDYLEHAEEQNKELKEE 313

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1115 I--LAEDFSIDDEMTNKlaaenkdlydlVDLLERKIDETEKKYEEASKLCEErlKQVVDTE--KKYEEasrlCEERLKQV 1190
Cdd:pfam06160  314 LerVQQSYTLNENELER-----------VRGLEKQLEELEKRYDEIVERLEE--KEVAYSElqEELEE----ILEQLEEI 376

                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 1063705616 1191 vdtETKLIELKTSMQRLEEkvSDMEAEDKILR-QQALRN 1228
Cdd:pfam06160  377 ---EEEQEEFKESLQSLRK--DELEAREKLDEfKLELRE 410
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
864-1233 3.51e-08

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 58.24  E-value: 3.51e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  864 RVKVAHRELRKLKMAAKETGALQDAKTKLEKEVEELTSCLELEKQMRMELEQVK-----TQEVEDLRSALNDMKLQLgET 938
Cdd:COG4717     72 ELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLqllplYQELEALEAELAELPERL-EE 150

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  939 QVTKSEEILKLQSALQDMQLEFEELAKELEMT-------------------NDLAAENEQLKDLVSSLQRKIDESDSKYE 999
Cdd:COG4717    151 LEERLEELRELEEELEELEAELAELQEELEELleqlslateeelqdlaeelEELQQRLAELEEELEEAQEELEELEEELE 230

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1000 ETSKLSE-----ERVKQE-----------------------------VPVIDQGVIIKLEAENQKLKALVSTLEKKIDSL 1045
Cdd:COG4717    231 QLENELEaaaleERLKEArlllliaaallallglggsllsliltiagVLFLVLGLLALLFLLLAREKASLGKEAEELQAL 310

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1046 DRKHDVTSSNISDQLKE---SASSDYEMLSNLAAENERLKALVSSLENENYENDGNDSPNEQKEgpqmLKEEILAEDfsi 1122
Cdd:COG4717    311 PALEELEEEELEELLAAlglPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAA----LLAEAGVED--- 383

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1123 DDEMTNKLAA--ENKDLYDLVDLLERKIDETEKKYEE-ASKLCEERLKQvvdTEKKYEEASRLCEERLKQVvdtETKLIE 1199
Cdd:COG4717    384 EEELRAALEQaeEYQELKEELEELEEQLEELLGELEElLEALDEEELEE---ELEELEEELEELEEELEEL---REELAE 457

                          410       420       430
                   ....*....|....*....|....*....|....
gi 1063705616 1200 LKTSMQRLEEKVSDMEAEDKILRQQALRNSASRK 1233
Cdd:COG4717    458 LEAELEQLEEDGELAELLQELEELKAELRELAEE 491
Myosin_N pfam02736
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ...
 7-50 5.93e-07

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


Pssm-ID: 460670  Cd Length: 45  Bit Score: 47.43  E-value: 5.93e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1063705616    7 TVGSQVWVEDPDEAWLDGEVVEANGQEIKVNCQT-KTVVAKVNAV 50
Cdd:pfam02736    1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVETEDgKTVTVKKDDV 45
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
 867-1227 2.82e-04

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 45.77  E-value: 2.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  867 VAHRELRKLKMAAKETGALQDAKTKLEKEVEE-LTSCLElekQMRMELEQVKTQEVEDLRSALNDMKLQ-LGETQVTKSE 944
Cdd:NF033838    34 VVHAEEVRGGNNPTVTSSGNESQKEHAKEVEShLEKILS---EIQKSLDKRKHTQNVALNKKLSDIKTEyLYELNVLKEK 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  945 EILKLQSALQ-DMQLEFEELAKELEMTNDLAAENEqlKDLVSSLQRKIDESDSKYEETSKLSEERVKQEVPVIDQGVIiK 1023
Cdd:NF033838   111 SEAELTSKTKkELDAAFEQFKKDTLEPGKKVAEAT--KKVEEAEKKAKDQKEEDRRNYPTNTYKTLELEIAESDVEVK-K 187

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1024 LEAENQKLKALVSTLEKKIDSLDRKhdvtssnisdqlKESASSDYEMLSNLAAENERLK--ALVSSLENENYENDGNDSP 1101
Cdd:NF033838   188 AELELVKEEAKEPRDEEKIKQAKAK------------VESKKAEATRLEKIKTDREKAEeeAKRRADAKLKEAVEKNVAT 255

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1102 NEQKEGPQMLKEEILAE----DFSIDDEMTNKLAAENKDLYDLVDLLERKIDETEKKYEEASKLC-----EERLKQVVDT 1172
Cdd:NF033838   256 SEQDKPKRRAKRGVLGEpatpDKKENDAKSSDSSVGEETLPSPSLKPEKKVAEAEKKVEEAKKKAkdqkeEDRRNYPTNT 335

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1063705616 1173 EKKYEeaSRLCEERLKqVVDTETKLIELKTSMQRLEEKVSDMEAEDKILRQQALR 1227
Cdd:NF033838   336 YKTLE--LEIAESDVK-VKEAELELVKEEAKEPRNEEKIKQAKAKVESKKAEATR 387
 
Name Accession Description Interval E-value
MYSc_Myo11 cd01384
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ...
 74-718 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: 1382.39  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   74 PGVLLNLKARYNANEIYTYTGNILIAVNPFKRLPHLYGNEIMEQYKGTDFGELSPHPFAVADSAYRKMINEGVSQAILVS 153
Cdd:cd01384      1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPHLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  154 GESGAGKTESTKMLMQYLAYMGGKAESEGRSVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFNHMGRISGAAIR 233
Cdd:cd01384     81 GESGAGKTETTKMLMQYLAYMGGRAVTEGRSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAAIR 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  234 TYLLERSRVCQVSDPERNYHCFYMLCA-APEQETERYQLGKPSTFHYLNQSNCHALDAIDDSKEYLATRKAMDVVGISPE 312
Cdd:cd01384    161 TYLLERSRVVQVSDPERNYHCFYQLCAgAPPEDREKYKLKDPKQFHYLNQSKCFELDGVDDAEEYRATRRAMDVVGISEE 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  313 EQDAIFRVVAAILHLGNIEFAKSEESDGAEPKDDKSRFHLKVAAKLFMCDEKALENSLCNRVMVTRGESITKPLDPGSAA 392
Cdd:cd01384    241 EQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKSEFHLKAAAELLMCDEKALEDALCKRVIVTPDGIITKPLDPDAAT 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  393 LSRDALAKIVYSKLFDWLVTKINNSIGQDSSSKYIIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKMEQEEY 472
Cdd:cd01384    321 LSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQHVFKMEQEEY 400

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  473 TKEEIDWSYIEFIDNQDVLDLIEKKPGGIIALLDEACMFPRSTHDTLAEKLYQTFGSHKRFTKPKLARTDFTICHYAGDV 552
Cdd:cd01384    401 TKEEIDWSYIEFVDNQDVLDLIEKKPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHKRFSKPKLSRTDFTIDHYAGDV 480

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  553 TYQTELFLDKNKDYVVGEHQSLMNSSDCSFVSSLFPKSREESSKSSKF-SSIGSQFKQQLQSLLETLNTTEPHYIRCVKP 631
Cdd:cd01384    481 TYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPREGTSSSSKfSSIGSRFKQQLQELMETLNTTEPHYIRCIKP 560

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  632 NNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILAPEATERSFDEVDACKKLLARVDLKGFQIG 711
Cdd:cd01384    561 NNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPEVLKGSDDEKAACKKILEKAGLKGYQIG 640


                   ....*..
gi 1063705616  712 KTKVFLR 718
Cdd:cd01384    641 KTKVFLR 647
MYSc smart00242
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...
 58-726 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: 1027.87  E-value: 0e+00
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616    58 PELGVDDMTKLAYLHEPGVLLNLKARYNANEIYTYTGNILIAVNPFKRLPhLYGNEIMEQYKGTDFGELSPHPFAVADSA 137
Cdd:smart00242    4 KFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLP-IYTDEVIKKYRGKSRGELPPHVFAIADNA 82

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   138 YRKMINEGVSQAILVSGESGAGKTESTKMLMQYLAYMGGKAEsEGRSVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFV 217
Cdd:smart00242   83 YRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNT-EVGSVEDQILESNPILEAFGNAKTLRNNNSSRFGKFI 161

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   218 EIQFNHMGRISGAAIRTYLLERSRVCQVSDPERNYHCFYMLCA-APEQETERYQLGKPSTFHYLNQSNCHALDAIDDSKE 296
Cdd:smart00242  162 EIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAgASEELKKELGLKSPEDYRYLNQGGCLTVDGIDDAEE 241

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   297 YLATRKAMDVVGISPEEQDAIFRVVAAILHLGNIEFAKSEESDGAEPKDDKSrfHLKVAAKLFMCDEKALENSLCNRVMV 376
Cdd:smart00242  242 FKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKE--ELSNAAELLGVDPEELEKALTKRKIK 319

                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   377 TRGESITKPLDPGSAALSRDALAKIVYSKLFDWLVTKINNSIGQDSSSKYIIGVLDIYGFESFKTNSFEQFCINLTNEKL 456
Cdd:smart00242  320 TGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSFEQLCINYANEKL 399

                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   457 QQHFNQHVFKMEQEEYTKEEIDWSYIEFIDNQDVLDLIEKKPGGIIALLDEACMFPRSTHDTLAEKLYQTFGSHKRFTKP 536
Cdd:smart00242  400 QQFFNQHVFKLEQEEYEREGIDWTFIDFFDNQDCIDLIEKKPPGILSLLDEECRFPKGTDQTFLEKLNQHHKKHPHFSKP 479

                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   537 -KLARTDFTICHYAGDVTYQTELFLDKNKDYVVGEHQSLMNSSDCSFVSSLFPKSREESSKSSKFSSIGSQFKQQLQSLL 615
Cdd:smart00242  480 kKKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVSNAGSKKRFQTVGSQFKEQLNELM 559

                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   616 ETLNTTEPHYIRCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILAPEATER-SFDEVD 694
Cdd:smart00242  560 DTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFDEFLQRYRVLLPDTWPPwGGDAKK 639

                           650       660       670
                    ....*....|....*....|....*....|....
gi 1063705616   695 ACKKLLARVDLK--GFQIGKTKVFLRAGQMAELD 726
Cdd:smart00242  640 ACEALLQSLGLDedEYQLGKTKVFLRPGQLAELE 673
MYSc cd00124
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ...
 74-718 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: 932.77  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   74 PGVLLNLKARYNANEIYTYTGNILIAVNPFKRLPhLYGNEIMEQYKGTDFG-ELSPHPFAVADSAYRKMINEGVSQAILV 152
Cdd:cd00124      1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLP-LYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  153 SGESGAGKTESTKMLMQYLAYMGGKAESEGR----SVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFNHMGRIS 228
Cdd:cd00124     80 SGESGAGKTETTKLVLKYLAALSGSGSSKSSssasSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLV 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  229 GAAIRTYLLERSRVCQVSDPERNYHCFYMLCA-----APEQETERYQLGKPSTFHYLNQSNCHALDAIDDSKEYLATRKA 303
Cdd:cd00124    160 GASIETYLLEKSRVVSQAPGERNFHIFYQLLAglsdgAREELKLELLLSYYYLNDYLNSSGCDRIDGVDDAEEFQELLDA 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  304 MDVVGISPEEQDAIFRVVAAILHLGNIEFAKSEEsDGAEPKDDKSRFHLKVAAKLFMCDEKALENSLCNRVMVTRGESIT 383
Cdd:cd00124    240 LDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEE-DEDSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETIT 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  384 KPLDPGSAALSRDALAKIVYSKLFDWLVTKINNSIGQDSS--SKYIIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFN 461
Cdd:cd00124    319 KPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAaeSTSFIGILDIFGFENFEVNSFEQLCINYANEKLQQFFN 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  462 QHVFKMEQEEYTKEEIDWSYIEFIDNQDVLDLIEKKPGGIIALLDEACMFPRSTHDTLAEKLYQTFGSHKRF-TKPKLAR 540
Cdd:cd00124    399 QHVFKLEQEEYEEEGIDWSFIDFPDNQDCLDLIEGKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFfSKKRKAK 478

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  541 TDFTICHYAGDVTYQTELFLDKNKDYVVGEHQSLMNSsdcsfvsslfpksreessksskfssiGSQFKQQLQSLLETLNT 620
Cdd:cd00124    479 LEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRS--------------------------GSQFRSQLDALMDTLNS 532

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  621 TEPHYIRCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILAPEATERSF---DEVDACK 697
Cdd:cd00124    533 TQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAPGATEKASdskKAAVLAL 612

                          650       660
                   ....*....|....*....|.
gi 1063705616  698 KLLARVDLKGFQIGKTKVFLR 718
Cdd:cd00124    613 LLLLKLDSSGYQLGKTKVFLR 633
COG5022 COG5022
Myosin heavy chain [General function prediction only];
1-1238 0e+00

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 884.42  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616    1 MASVKVTVGSQVWVEDPDEAWLDGEVVEANGQEIKVNCQTKTVVAKVNAVHPKDPEF------PELGVDDMTKLAYLHEP 74
Cdd:COG5022      1 MSTTNAEVGSGCWIPDEEKGWIWAEIIKEAFNKGKVTEEGKKEDGESVSVKKKVLGNdriklpKFDGVDDLTELSYLNEP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   75 GVLLNLKARYNANEIYTYTGNILIAVNPFKRLPhLYGNEIMEQYKGTDFGELSPHPFAVADSAYRKMINEGVSQAILVSG 154
Cdd:COG5022     81 AVLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLG-IYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISG 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  155 ESGAGKTESTKMLMQYLAYMGGKAESEGRSVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFNHMGRISGAAIRT 234
Cdd:COG5022    160 ESGAGKTENAKRIMQYLASVTSSSTVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIET 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  235 YLLERSRVCQVSDPERNYHCFYMLCA-APEQETERYQLGKPSTFHYLNQSNCHALDAIDDSKEYLATRKAMDVVGISPEE 313
Cdd:COG5022    240 YLLEKSRVVHQNKNERNYHIFYQLLAgDPEELKKLLLLQNPKDYIYLSQGGCDKIDGIDDAKEFKITLDALKTIGIDEEE 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  314 QDAIFRVVAAILHLGNIEFaKSEESDGAEPKDDKsrfHLKVAAKLFMCDEKALENSLCNRVMVTRGESITKPLDPGSAAL 393
Cdd:COG5022    320 QDQIFKILAAILHIGNIEF-KEDRNGAAIFSDNS---VLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALA 395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  394 SRDALAKIVYSKLFDWLVTKINNSIGQDSSSKYIIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKMEQEEYT 473
Cdd:COG5022    396 IRDSLAKALYSNLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYV 475

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  474 KEEIDWSYIEFIDNQDVLDLIEKK-PGGIIALLDEACMFPRSTHDTLAEKLYQTF--GSHKRFTKPKLARTDFTICHYAG 550
Cdd:COG5022    476 KEGIEWSFIDYFDNQPCIDLIEKKnPLGILSLLDEECVMPHATDESFTSKLAQRLnkNSNPKFKKSRFRDNKFVVKHYAG 555

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  551 DVTYQTELFLDKNKDYVVGEHQSLMNSSDCSFVSSLFPkSREESSKSSKFSSIGSQFKQQLQSLLETLNTTEPHYIRCVK 630
Cdd:COG5022    556 DVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFD-DEENIESKGRFPTLGSRFKESLNSLMSTLNSTQPHYIRCIK 634

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  631 PNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILAPEAT-----ERSFDEVDACKKLL--ARV 703
Cdd:COG5022    635 PNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKSwtgeyTWKEDTKNAVKSILeeLVI 714

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  704 DLKGFQIGKTKVFLRAGQMAELDAHRAEVLGHSARIIQRKVITYLSRKKYLLLQSASTEIQAFCRGHIARVQFKATRREA 783
Cdd:COG5022    715 DSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLRRLVDYELKWR 794

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  784 ASVRIQKQARTYICQTAFKKLCASAISIQSGLRAMAARVEFQYR-TKRKAAIIIQSQIRRCLCRRRYLRTKKAAITTQCG 862
Cdd:COG5022    795 LFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIKREKKLRETEEVeFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSA 874

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  863 WRVKVAHRELRKLKMAAKETGALQDAKTKLEKEVEELTSclELEKQMRMELEqVKTQEVEDLRSALNDMKLQLGET-QVT 941
Cdd:COG5022    875 QRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKK--SLSSDLIENLE-FKTELIARLKKLLNNIDLEEGPSiEYV 951

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  942 KSEEILKLQ---SALQDMQLEFEELAKELEMT-NDLAAENEQLKDLVSSLQRKIDESDSKYEETSKLSEERVKqevpvid 1017
Cdd:COG5022    952 KLPELNKLHeveSKLKETSEEYEDLLKKSTILvREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVE------- 1024

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1018 qgvIIKLEAENQKLKALVSTL--EKKIDSLDRKHDvtssnisdqLKESA-SSDYEMLSNLAAENERLKALVSSLENENYE 1094
Cdd:COG5022   1025 ---VAELQSASKIISSESTELsiLKPLQKLKGLLL---------LENNQlQARYKALKLRRENSLLDDKQLYQLESTENL 1092

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1095 NDGNDSPNEQKEGPQMLKEEilAEDFSIDDEMTNklaaeNKDLYDLVDLLERKIDETEKKYEEASKLCEER--LKQVVDT 1172
Cdd:COG5022   1093 LKTINVKDLEVTNRNLVKPA--NVLQFIVAQMIK-----LNLLQEISKFLSQLVNTLEPVFQKLSVLQLELdgLFWEANL 1165

                         1210      1220      1230      1240      1250      1260      1270
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1173 EKK--YEEASRLCEERLKQVVDTETKLIELKTSMQRLEEKVSDMEAEDK--ILRQQALRNSASRKMSPQV 1238
Cdd:COG5022   1166 EALpsPPPFAALSEKRLYQSALYDEKSKLSSSEVNDLKNELIALFSKIFsgWPRGDKLKKLISEGWVPTE 1235
Myosin_head pfam00063
Myosin head (motor domain);
62-718 0e+00

Myosin head (motor domain);


Pssm-ID: 395017 [Multi-domain]  Cd Length: 674  Bit Score: 878.92  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   62 VDDMTKLAYLHEPGVLLNLKARYNANEIYTYTGNILIAVNPFKRLPhLYGNEIMEQYKGTDFGELSPHPFAVADSAYRKM 141
Cdd:pfam00063    1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLP-IYSEDMIKAYRGKRRGELPPHIFAIADEAYRSM 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  142 INEGVSQAILVSGESGAGKTESTKMLMQYLAYMGGKAES-EGRSVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQ 220
Cdd:pfam00063   80 LQDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAgNVGRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQ 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  221 FNHMGRISGAAIRTYLLERSRVCQVSDPERNYHCFYMLCA-APEQETERYQLGKPSTFHYLNQSNCHALDAIDDSKEYLA 299
Cdd:pfam00063  160 FDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAgASAQLKKELRLTNPKDYHYLSQSGCYTIDGIDDSEEFKI 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  300 TRKAMDVVGISPEEQDAIFRVVAAILHLGNIEFAKSEESDGAEPKDDKSrfhLKVAAKLFMCDEKALENSLCNRVMVTRG 379
Cdd:pfam00063  240 TDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTEN---LQKAASLLGIDSTELEKALCKRRIKTGR 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  380 ESITKPLDPGSAALSRDALAKIVYSKLFDWLVTKINNSIGQDSSSK-YIIGVLDIYGFESFKTNSFEQFCINLTNEKLQQ 458
Cdd:pfam00063  317 ETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKaSFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQ 396

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  459 HFNQHVFKMEQEEYTKEEIDWSYIEFIDNQDVLDLIEKKPGGIIALLDEACMFPRSTHDTLAEKLYQTFGSHKRFTKPKL 538
Cdd:pfam00063  397 FFNHHMFKLEQEEYVREGIEWTFIDFGDNQPCIDLIEKKPLGILSLLDEECLFPKATDQTFLDKLYSTFSKHPHFQKPRL 476

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  539 -ARTDFTICHYAGDVTYQTELFLDKNKDYVVGEHQSLMNSSDCSFVSSLFPKSREESSKSSKFSS--------------I 603
Cdd:pfam00063  477 qGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGkstpkrtkkkrfitV 556

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  604 GSQFKQQLQSLLETLNTTEPHYIRCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILAP 683
Cdd:pfam00063  557 GSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRYRILAP 636

                          650       660       670
                   ....*....|....*....|....*....|....*...
gi 1063705616  684 EATERSF-DEVDACKKLLARVDL--KGFQIGKTKVFLR 718
Cdd:pfam00063  637 KTWPKWKgDAKKGCEAILQSLNLdkEEYQFGKTKIFFR 674
MYSc_Myo5 cd01380
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ...
 74-718 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: 836.81  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   74 PGVLLNLKARY-NANEIYTYTGNILIAVNPFKRLPhLYGNEIMEQYKGTDFGELSPHPFAVADSAYRKMINEGVSQAILV 152
Cdd:cd01380      1 PAVLHNLKVRFcQRNAIYTYCGIVLVAINPYEDLP-IYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  153 SGESGAGKTESTKMLMQYLAYMGGKAESEgRSVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFNHMGRISGAAI 232
Cdd:cd01380     80 SGESGAGKTVSAKYAMRYFATVGGSSSGE-TQVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANM 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  233 RTYLLERSRVCQVSDPERNYHCFYMLCAA-PEQETERYQLGKPSTFHYLNQSNCHALDAIDDSKEYLATRKAMDVVGISP 311
Cdd:cd01380    159 RTYLLEKSRVVFQAEEERNYHIFYQLCAAaSLPELKELHLGSAEDFFYTNQGGSPVIDGVDDAAEFEETRKALTLLGISE 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  312 EEQDAIFRVVAAILHLGNIEFAKSEESDGAEPKDDKsrfHLKVAAKLFMCDEKALENSLCNRVMVTRGESITKPLDPGSA 391
Cdd:cd01380    239 EEQMEIFRILAAILHLGNVEIKATRNDSASISPDDE---HLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQA 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  392 ALSRDALAKIVYSKLFDWLVTKINNSIGQDSSSKY--IIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKMEQ 469
Cdd:cd01380    316 IVARDALAKHIYAQLFDWIVDRINKALASPVKEKQhsFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQ 395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  470 EEYTKEEIDWSYIEFIDNQDVLDLIEKKPgGIIALLDEACMFPRSTHDTLAEKLYQTFGSHKR--FTKPKLARTDFTICH 547
Cdd:cd01380    396 EEYVKEEIEWSFIDFYDNQPCIDLIEGKL-GILDLLDEECRLPKGSDENWAQKLYNQHLKKPNkhFKKPRFSNTAFIVKH 474

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  548 YAGDVTYQTELFLDKNKDYVVGEHQSLMNSSDcsfvsslfpksreessksSKFSSIGSQFKQQLQSLLETLNTTEPHYIR 627
Cdd:cd01380    475 FADDVEYQVEGFLEKNRDTVSEEHLNVLKASK------------------NRKKTVGSQFRDSLILLMETLNSTTPHYVR 536

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  628 CVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILAPEATERSFDEVDACKKLLAR--VDL 705
Cdd:cd01380    537 CIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSKEWLRDDKKKTCENILENliLDP 616

                          650
                   ....*....|...
gi 1063705616  706 KGFQIGKTKVFLR 718
Cdd:cd01380    617 DKYQFGKTKIFFR 629
MYSc_Myo22 cd14883
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ...
 75-718 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: 773.03  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   75 GVLLNLKARYNANEIYTYTGNILIAVNPFKRLPhLYGNEIMEQYKGTDFGELSPHPFAVADSAYRKMINEGVSQAILVSG 154
Cdd:cd14883      2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELP-IYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  155 ESGAGKTESTKMLMQYLAYMGGKAESegrsVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFNHMGRISGAAIRT 234
Cdd:cd14883     81 ESGAGKTETTKLILQYLCAVTNNHSW----VEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGAIIQD 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  235 YLLERSRVCQVSDPERNYHCFYMLCAAPEQETER---YQLGKPSTFHYLNQSNCHALDAIDDSKEYLATRKAMDVVGISP 311
Cdd:cd14883    157 YLLEQSRITFQAPGERNYHVFYQLLAGAKHSKELkekLKLGEPEDYHYLNQSGCIRIDNINDKKDFDHLRLAMNVLGIPE 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  312 EEQDAIFRVVAAILHLGNIEFAKSEESDGAEPKDDKSRfhLKVAAKLFMCDEKALENSLCNRVMVTRGESITKPLDPGSA 391
Cdd:cd14883    237 EMQEGIFSVLSAILHLGNLTFEDIDGETGALTVEDKEI--LKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQEA 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  392 ALSRDALAKIVYSKLFDWLVTKINNSIGQDSSSKYIIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKMEQEE 471
Cdd:cd14883    315 RDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKLEQEE 394

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  472 YTKEEIDWSYIEFIDNQDVLDLIEKKPGGIIALLDEACMFPRSTHDTLAEKLYQTFGSHKRFTKP--KLARTDFTICHYA 549
Cdd:cd14883    395 YEKEGINWSHIVFTDNQECLDLIEKPPLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEKPdrRRWKTEFGVKHYA 474

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  550 GDVTYQTELFLDKNKDYVVGEHQSLMNSSDCSFVSSLFPKSREESSKSSKFSS---------------IGSQFKQQLQSL 614
Cdd:cd14883    475 GEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTYPDLLALTGLSISLggdttsrgtskgkptVGDTFKHQLQSL 554

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  615 LETLNTTEPHYIRCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILAPEATERSFD-EV 693
Cdd:cd14883    555 VDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPRARSADHKeTC 634

                          650       660
                   ....*....|....*....|....*..
gi 1063705616  694 DACKKLLARVDLKG--FQIGKTKVFLR 718
Cdd:cd14883    635 GAVRALMGLGGLPEdeWQVGKTKVFLR 661
MYSc_Myo8 cd01383
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ...
 74-718 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: 772.26  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   74 PGVLLNLKARYNANEIYTYTGNILIAVNPFKRLPhLYGNEIMEQYKgtDFGELSPHPFAVADSAYRKMINEGVSQAILVS 153
Cdd:cd01383      1 PSVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVP-LYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIIS 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  154 GESGAGKTESTKMLMQYLAYMGGkaesEGRSVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFNHMGRISGAAIR 233
Cdd:cd01383     78 GESGAGKTETAKIAMQYLAALGG----GSSGIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQ 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  234 TYLLERSRVCQVSDPERNYHCFYMLCA-APEQETERYQLGKPSTFHYLNQSNCHALDAIDDSKEYLATRKAMDVVGISPE 312
Cdd:cd01383    154 TYLLEKSRVVQLANGERSYHIFYQLCAgASPALREKLNLKSASEYKYLNQSNCLTIDGVDDAKKFHELKEALDTVGISKE 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  313 EQDAIFRVVAAILHLGNIEFAKSEESDGAEPKDDKSrfhLKVAAKLFMCDEKALENSLCNRVMVTRGESITKPLDPGSAA 392
Cdd:cd01383    234 DQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEA---VSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAI 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  393 LSRDALAKIVYSKLFDWLVTKINNSIGQDSSSKYI-IGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKMEQEE 471
Cdd:cd01383    311 DARDALAKAIYASLFDWLVEQINKSLEVGKRRTGRsISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEE 390

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  472 YTKEEIDWSYIEFIDNQDVLDLIEKKPGGIIALLDEACMFPRSTHDTLAEKLYQTFGSHKRFTKPKlaRTDFTICHYAGD 551
Cdd:cd01383    391 YELDGIDWTKVDFEDNQECLDLIEKKPLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCFKGER--GGAFTIRHYAGE 468

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  552 VTYQTELFLDKNKDYVVGEHQSLMNSSDCSFV---SSLFPKSREESSKSSKFSSIGSQ-------FKQQLQSLLETLNTT 621
Cdd:cd01383    469 VTYDTSGFLEKNRDLLHSDLIQLLSSCSCQLPqlfASKMLDASRKALPLTKASGSDSQkqsvatkFKGQLFKLMQRLENT 548

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  622 EPHYIRCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILAPEATERSFDEVDACKKLLA 701
Cdd:cd01383    549 TPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDVSASQDPLSTSVAILQ 628

                          650
                   ....*....|....*....
gi 1063705616  702 RVDLKG--FQIGKTKVFLR 718
Cdd:cd01383    629 QFNILPemYQVGYTKLFFR 647
MYSc_class_II cd01377
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ...
 74-718 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: 768.55  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   74 PGVLLNLKARYNANEIYTYTGNILIAVNPFKRLPhLYGNEIMEQYKGTDFGELSPHPFAVADSAYRKMINEGVSQAILVS 153
Cdd:cd01377      1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLP-IYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILIT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  154 GESGAGKTESTKMLMQYLAYMGGKAESEGR------SVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFNHMGRI 227
Cdd:cd01377     80 GESGAGKTENTKKVIQYLASVAASSKKKKEsgkkkgTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKI 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  228 SGAAIRTYLLERSRVCQVSDPERNYHCFYMLCA-APEQETERYQLGKPSTFHYLNQSNCHALDAIDDSKEYLATRKAMDV 306
Cdd:cd01377    160 AGADIETYLLEKSRVVRQAKGERNYHIFYQLLSgADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAFDI 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  307 VGISPEEQDAIFRVVAAILHLGNIEFAKSEESDGAEPKDDKSrfhLKVAAKLFMCDEKALENSLCN-RVMVTRgESITKP 385
Cdd:cd01377    240 LGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEE---ADKAAHLLGVNSSDLLKALLKpRIKVGR-EWVTKG 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  386 LDPGSAALSRDALAKIVYSKLFDWLVTKINNSIGQDSSSKYIIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVF 465
Cdd:cd01377    316 QNKEQVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMF 395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  466 KMEQEEYTKEEIDWSYIEF-IDNQDVLDLIEKKPGGIIALLDEACMFPRSTHDTLAEKLYQTFGSHKRFT---KPKLART 541
Cdd:cd01377    396 VLEQEEYKKEGIEWTFIDFgLDLQPTIDLIEKPNMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFkkpKPKKSEA 475

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  542 DFTICHYAGDVTYQTELFLDKNKDyVVGEH-QSLMNSSDCSFVSSLFPKSREESSKSSKFSSIGSQF-------KQQLQS 613
Cdd:cd01377    476 HFILKHYAGDVEYNIDGWLEKNKD-PLNENvVALLKKSSDPLVASLFKDYEESGGGGGKKKKKGGSFrtvsqlhKEQLNK 554

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  614 LLETLNTTEPHYIRCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILAPEATERSF-DE 692
Cdd:cd01377    555 LMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIPKGFdDG 634

                          650       660
                   ....*....|....*....|....*...
gi 1063705616  693 VDACKKLLARVDLK--GFQIGKTKVFLR 718
Cdd:cd01377    635 KAACEKILKALQLDpeLYRIGNTKVFFK 662
MYSc_Myo1 cd01378
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ...
 79-718 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: 755.92  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   79 NLKARYNANEIYTYTGNILIAVNPFKRLPhLYGNEIMEQYKGTDFGELSPHPFAVADSAYRKMINEGVSQAILVSGESGA 158
Cdd:cd01378      6 NLKKRFENDEIYTYIGHVLISVNPFKDLG-IYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGESGA 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  159 GKTESTKMLMQYLAYMGGKAESEGRSVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFNHMGRISGAAIRTYLLE 238
Cdd:cd01378     85 GKTEASKRIMQYIAAVSGGSESEVERVKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGHITNYLLE 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  239 RSRVCQVSDPERNYHCFYMLCA-APEQETERYQLGKPSTFHYLNQSNCHALDAIDDSKEYLATRKAMDVVGISPEEQDAI 317
Cdd:cd01378    165 KSRVVGQIKGERNFHIFYQLLKgASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVIGFTEEEQDSI 244

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  318 FRVVAAILHLGNIEFaKSEESDGAEPKDDKsrfHLKVAAKLFMCDEKALENSLCNRVMVTRGE---SITKPLDPGSAALS 394
Cdd:cd01378    245 FRILAAILHLGNIQF-AEDEEGNAAISDTS---VLDFVAYLLGVDPDQLEKALTHRTIETGGGgrsVYEVPLNVEQAAYA 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  395 RDALAKIVYSKLFDWLVTKINNSI-GQDSSSKYIIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKMEQEEYT 473
Cdd:cd01378    321 RDALAKAIYSRLFDWIVERINKSLaAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELTLKAEQEEYV 400

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  474 KEEIDWSYIEFIDNQDVLDLIEKKPGGIIALLDEACMFP-RSTHDTLAEKLYQTFGSHKRFTKPK----LARTDFTICHY 548
Cdd:cd01378    401 REGIEWTPIKYFNNKIICDLIEEKPPGIFAILDDACLTAgDATDQTFLQKLNQLFSNHPHFECPSghfeLRRGEFRIKHY 480

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  549 AGDVTYQTELFLDKNKDYVVGEHQSLMNSSDCSFVSSLFPKSREESSKSSKFSSiGSQFKQQLQSLLETLNTTEPHYIRC 628
Cdd:cd01378    481 AGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVDLDSKKRPPTA-GTKFKNSANALVETLMKKQPSYIRC 559

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  629 VKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILAPeATERSFDEV--DACKKLLARVDLK 706
Cdd:cd01378    560 IKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSP-KTWPAWDGTwqGGVESILKDLNIP 638

                          650
                   ....*....|....
gi 1063705616  707 G--FQIGKTKVFLR 718
Cdd:cd01378    639 PeeYQMGKTKIFIR 652
MYSc_Myo7 cd01381
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ...
 75-718 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: 735.60  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   75 GVLLNLKARYNANEIYTYTGNILIAVNPFKRLPhLYGNEIMEQYKGTDFGELSPHPFAVADSAYRKMINEGVSQAILVSG 154
Cdd:cd01381      2 GILRNLLIRYREKLIYTYTGSILVAVNPYQILP-IYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  155 ESGAGKTESTKMLMQYLAYMGGKAesegRSVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFNHMGRISGAAIRT 234
Cdd:cd01381     81 ESGAGKTESTKLILQYLAAISGQH----SWIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKIEQ 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  235 YLLERSRVCQVSDPERNYHCFY-MLCAAPEQETERYQLGKPSTFHYLNQSNCHALDAIDDSKEYLATRKAMDVVGISPEE 313
Cdd:cd01381    157 YLLEKSRIVSQAPDERNYHIFYcMLAGLSAEEKKKLELGDASDYYYLTQGNCLTCEGRDDAAEFADIRSAMKVLMFTDEE 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  314 QDAIFRVVAAILHLGNIEFaKSEESDGAEPKDDKSRFHLKVAAKLFMCDEKALENSLCNRVMVTRGESITKPLDPGSAAL 393
Cdd:cd01381    237 IWDIFKLLAAILHLGNIKF-EATVVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAEQALD 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  394 SRDALAKIVYSKLFDWLVTKINNSIGQ---DSSSKYIIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKMEQE 470
Cdd:cd01381    316 VRDAFVKGIYGRLFIWIVNKINSAIYKprgTDSSRTSIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFKLEQE 395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  471 EYTKEEIDWSYIEFIDNQDVLDLIEKKPGGIIALLDEACMFPRSTHDTLAEKLYQTFGSHKRFTKPK-LARTDFTICHYA 549
Cdd:cd01381    396 EYDKEGINWQHIEFVDNQDVLDLIALKPMNIMSLIDEESKFPKGTDQTMLEKLHSTHGNNKNYLKPKsDLNTSFGINHFA 475

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  550 GDVTYQTELFLDKNKDYVVGEHQSLMNSSDCSFVSSLFPKSREESSKSSKFSS-IGSQFKQQLQSLLETLNTTEPHYIRC 628
Cdd:cd01381    476 GVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDISMGSETRKKSPtLSSQFRKSLDQLMKTLSACQPFFVRC 555

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  629 VKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILAP--EATERSFDEVDACKK----LLAR 702
Cdd:cd01381    556 IKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVPgiPPAHKTDCRAATRKIccavLGGD 635

                          650
                   ....*....|....*.
gi 1063705616  703 VDlkgFQIGKTKVFLR 718
Cdd:cd01381    636 AD---YQLGKTKIFLK 648
MYSc_Myo6 cd01382
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ...
 77-718 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: 694.38  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   77 LLNLKARYNANEIYTYTGNILIAVNPFKRLPHLYGNEIMEQYKGTDFGELSPHPFAVADSAYRKMINEGVSQAILVSGES 156
Cdd:cd01382      4 LNNIRVRYSKDKIYTYVANILIAVNPYFDIPKLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVSGES 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  157 GAGKTESTKMLMQYLAYMGGkaeSEGRSVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFNHMGRISGAAIRTYL 236
Cdd:cd01382     84 GAGKTESTKYILRYLTESWG---SGAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYL 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  237 LERSRVCQVSDPERNYHCFYMLCA-APEQEteRYQLGKPSTfhylnqsnchaldaIDDSKEYLATRKAMDVVGISPEEQD 315
Cdd:cd01382    161 LEKSRICVQSKEERNYHIFYRLCAgAPEDL--REKLLKDPL--------------LDDVGDFIRMDKAMKKIGLSDEEKL 224

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  316 AIFRVVAAILHLGNIEF-AKSEESDGAEPKDDKSRFHLKVAAKLFMCDEKALENSLCNRVMVT-----RGESITKPLDPG 389
Cdd:cd01382    225 DIFRVVAAVLHLGNIEFeENGSDSGGGCNVKPKSEQSLEYAAELLGLDQDELRVSLTTRVMQTtrggaKGTVIKVPLKVE 304

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  390 SAALSRDALAKIVYSKLFDWLVTKINNSIGQDSSSKYIiGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKMEQ 469
Cdd:cd01382    305 EANNARDALAKAIYSKLFDHIVNRINQCIPFETSSYFI-GVLDIAGFEYFEVNSFEQFCINYCNEKLQQFFNERILKEEQ 383

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  470 EEYTKEEIDWSYIEFIDNQDVLDLIEKKPGGIIALLDEACMFPRSTHDTLAEKLYQTFGSHKRFTKP---KLA-----RT 541
Cdd:cd01382    384 ELYEKEGLGVKEVEYVDNQDCIDLIEAKLVGILDLLDEESKLPKPSDQHFTSAVHQKHKNHFRLSIPrksKLKihrnlRD 463

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  542 D--FTICHYAGDVTYQTELFLDKNKDYVVGEHQSLMNSSDCSFVSSLFPKSREESSKSSKFS------SIGSQFKQQLQS 613
Cdd:cd01382    464 DegFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNNNKDSKQKAgklsfiSVGNKFKTQLNL 543

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  614 LLETLNTTEPHYIRCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILAPEATERsFDEV 693
Cdd:cd01382    544 LMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSFHDLYNMYKKYLPPKLAR-LDPR 622

                          650       660
                   ....*....|....*....|....*..
gi 1063705616  694 DACKKLLARVDL--KGFQIGKTKVFLR 718
Cdd:cd01382    623 LFCKALFKALGLneNDFKFGLTKVFFR 649
MYSc_Myo4 cd14872
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ...
 74-718 0e+00

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


Pssm-ID: 276839  Cd Length: 644  Bit Score: 669.95  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   74 PGVLLNLKARYNANEIYTYTGNILIAVNPFKRLPhLYGNEIMEQYKGTDFGELSPHPFAVADSAYRKMINEGVSQAILVS 153
Cdd:cd14872      1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLP-LYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILIS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  154 GESGAGKTESTKMLMQYLAYMGGKAESegrsVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFNHMGRISGAAIR 233
Cdd:cd14872     80 GESGAGKTEATKQCLSFFAEVAGSTNG----VEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGASTE 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  234 TYLLERSRVCQVSDPERNYHCFYMLCAAPEQETeRYQLGKPSTFHYLNQSNCHALDAIDDSKEYLATRKAMDVVGISPEE 313
Cdd:cd14872    156 NYLLEKSRVVYQIKGERNFHIFYQLLASPDPAS-RGGWGSSAAYGYLSLSGCIEVEGVDDVADFEEVVLAMEQLGFDDAD 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  314 QDAIFRVVAAILHLGNIEFAKSEESDGAEPKDDKSRFHLKVAAKLFMCDEKALENSLCNRVMVTRGESITK-PLDPGSAA 392
Cdd:cd14872    235 INNVMSLIAAILKLGNIEFASGGGKSLVSGSTVANRDVLKEVATLLGVDAATLEEALTSRLMEIKGCDPTRiPLTPAQAT 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  393 LSRDALAKIVYSKLFDWLVTKINNSIGQDSSSK-YIIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKMEQEE 471
Cdd:cd14872    315 DACDALAKAAYSRLFDWLVKKINESMRPQKGAKtTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTFKLEEAL 394

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  472 YTKEEIDWSYIEFIDNQDVLDLIEKKPGGIIALLDEACMFPRSTHDTLAEKLYQTFGSHKRF--TKPKLARTDFTICHYA 549
Cdd:cd14872    395 YQSEGVKFEHIDFIDNQPVLDLIEKKQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKSTFvyAEVRTSRTEFIVKHYA 474

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  550 GDVTYQTELFLDKNKDYVVGEHQSLMNSSDCSFVSSLFPksREESSKSSKFSSIGSQFKQQLQSLLETLNTTEPHYIRCV 629
Cdd:cd14872    475 GDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFP--PSEGDQKTSKVTLGGQFRKQLSALMTALNATEPHYIRCV 552

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  630 KPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRIL-APEATERSFDEVDACKKLLARV--DLK 706
Cdd:cd14872    553 KPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFLvKTIAKRVGPDDRQRCDLLLKSLkqDFS 632

                          650
                   ....*....|..
gi 1063705616  707 GFQIGKTKVFLR 718
Cdd:cd14872    633 KVQVGKTRVLYR 644
MYSc_Myo27 cd14888
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ...
 74-718 0e+00

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: 662.93  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   74 PGVLLNLKARYNANEIYTYTGNILIAVNPFKRLPHLYGNEIMEQYKgTDFGELSPHPFAVADSAYRKMINEGVSQAILVS 153
Cdd:cd14888      1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPGLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  154 GESGAGKTESTKMLMQYLAYMGGKAESEGRSVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFNHM--------- 224
Cdd:cd14888     80 GESGAGKTESTKYVMKFLACAGSEDIKKRSLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSKLkskrmsgdr 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  225 GRISGAAIRTYLLERSRVCQVSDPERNYHCFYMLCAA----------PEQETERYQLG---KP-----------STFHYL 280
Cdd:cd14888    160 GRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAareakntglsYEENDEKLAKGadaKPisidmssfephLKFRYL 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  281 NQSNCHALDAIDDSKEYLATRKAMDVVGISPEEQDAIFRVVAAILHLGNIEFAKSEESDGAEPKDDKSRFHLKVAAKLFM 360
Cdd:cd14888    240 TKSSCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGAVVSASCTDDLEKVASLLG 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  361 CDEKALENSLCNRVMVTRGESITKPLDPGSAALSRDALAKIVYSKLFDWLVTKINNSIGQDSSSKYII-GVLDIYGFESF 439
Cdd:cd14888    320 VDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNSLLFcGVLDIFGFECF 399

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  440 KTNSFEQFCINLTNEKLQQHFNQHVFKMEQEEYTKEEIDWSYIEFIDNQDVLDLIEKKPGGIIALLDEACMFPRSTHDTL 519
Cdd:cd14888    400 QLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFPDNQDCVDLLQEKPLGIFCMLDEECFVPGGKDQGL 479

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  520 AEKLYQTFGSHKRFTKPKLARTDFTICHYAGDVTYQTELFLDKNKDYVVGEHQSLMNSSDCSFVSSLFPK----SREESS 595
Cdd:cd14888    480 CNKLCQKHKGHKRFDVVKTDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNLFSAylrrGTDGNT 559

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  596 KSSKFSSIGSQFKQQLQSLLETLNTTEPHYIRCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFL 675
Cdd:cd14888    560 KKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGVLQAVQVSRAGYPVRLSHAEFY 639

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|...
gi 1063705616  676 TRFRILAPEATERSFdevdackkllarvdlKGFQIGKTKVFLR 718
Cdd:cd14888    640 NDYRILLNGEGKKQL---------------SIWAVGKTLCFFK 667
MYSc_Myo40 cd14901
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ...
 74-717 0e+00

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: 659.94  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   74 PGVLLNLKARYNANEIYTYTGNILIAVNPFKRLPhLYGNEIMEQY------KGTDFGELSPHPFAVADSAYRKMI----N 143
Cdd:cd14901      1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLP-LYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLfasrG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  144 EGVSQAILVSGESGAGKTESTKMLMQYLAYMG-----GKAESEGRSVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVE 218
Cdd:cd14901     80 QKCDQSILVSGESGAGKTETTKIIMNYLASVSsatthGQNATERENVRDRVLESNPILEAFGNARTNRNNNSSRFGKFIR 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  219 IQFNHMGRISGAAIRTYLLERSRVCQVSDPERNYHCFYMLC-AAPEQETERYQLGKPSTFHYLNQSNCH-ALDAIDDSKE 296
Cdd:cd14901    160 LGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLrGASSDELHALGLTHVEEYKYLNSSQCYdRRDGVDDSVQ 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  297 YLATRKAMDVVGISPEEQDAIFRVVAAILHLGNIEFAKSEESDGAEpkDDKSRFHLKVAAKLFMCDEKALENSLCNRVMV 376
Cdd:cd14901    240 YAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGGTF--SMSSLANVRAACDLLGLDMDVLEKTLCTREIR 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  377 TRGESITKPLDPGSAALSRDALAKIVYSKLFDWLVTKINNSIGQDSSS--KYIIGVLDIYGFESFKTNSFEQFCINLTNE 454
Cdd:cd14901    318 AGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTgaSRFIGIVDIFGFEIFATNSLEQLCINFANE 397

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  455 KLQQHFNQHVFKMEQEEYTKEEIDWSYIEFIDNQDVLDLIEKKPGGIIALLDEACMFPRSTHDTLAEKLYQTFGSHKRFT 534
Cdd:cd14901    398 KLQQLFGKFVFEMEQDEYVAEAIPWTFVEYPNNDACVAMFEARPTGLFSLLDEQCLLPRGNDEKLANKYYDLLAKHASFS 477

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  535 KPKL--ARTDFTICHYAGDVTYQTELFLDKNKDYVVGEHQSLMNSSDCSFVSSlfpksreessksskfsSIGSQFKQQLQ 612
Cdd:cd14901    478 VSKLqqGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS----------------TVVAKFKVQLS 541

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  613 SLLETLNTTEPHYIRCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILAPEA------- 685
Cdd:cd14901    542 SLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHTYSCLAPDGasdtwkv 621

                          650       660       670
                   ....*....|....*....|....*....|...
gi 1063705616  686 -TERSFDEVDACKKLLARVDLKGFQIGKTKVFL 717
Cdd:cd14901    622 nELAERLMSQLQHSELNIEHLPPFQVGKTKVFL 654
MYSc_Myo29 cd14890
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ...
 76-718 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: 653.38  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   76 VLLNLKARYNANEIYTYTGNILIAVNPFKRLPHLYGNEIMEQYKGTDFGELSPHPFAVADSAYRKMINEGVS----QAIL 151
Cdd:cd14890      3 LLHTLRLRYERDEIYTYVGPILISINPYKSIPDLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQSGVLdpsnQSII 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  152 VSGESGAGKTESTKMLMQYLAYM----------GGKAESEGR-----SVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKF 216
Cdd:cd14890     83 ISGESGAGKTEATKIIMQYLARItsgfaqgasgEGEAASEAIeqtlgSLEDRVLSSNPLLESFGNAKTLRNDNSSRFGKF 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  217 VEIQFNHMGRISGAAIRTYLLERSRVCQVSDPERNYHCFYMLCA-APEQETERYQLGKPSTFHYLnQSNCHALDAIDDSK 295
Cdd:cd14890    163 IEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAgADEALRERLKLQTPVEYFYL-RGECSSIPSCDDAK 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  296 EYLATRKAMDVVGISPEEQDAIFRVVAAILHLGNIEFAKSEESDGaePKDDKSRFHLKVAAKLFMCDEKALENSLCNRVM 375
Cdd:cd14890    242 AFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTV--LEDATTLQSLKLAAELLGVNEDALEKALLTRQL 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  376 VTRGESITKPLDPGSAALSRDALAKIVYSKLFDWLVTKINNSIGQDSSSKYIIGVLDIYGFESFKTNSFEQFCINLTNEK 455
Cdd:cd14890    320 FVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYANEK 399

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  456 LQQHFNQHVFKMEQEEYTKEEIDWSYIEFIDNQDVLDLIEKKPGGIIAL---LDEACMFPRSTHDT-LAEKLYQTFG--- 528
Cdd:cd14890    400 LQRHFNQHMFEVEQVEYSNEGIDWQYITFNDNQACLELIEGKVNGKPGIfitLDDCWRFKGEEANKkFVSQLHASFGrks 479

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  529 ----------SHKRFTKPKL-ARTDFTICHYAGDVTYQTELFLDKNKDYVVGEHQSLMNSSDCSF--VSslfpksreess 595
Cdd:cd14890    480 gsggtrrgssQHPHFVHPKFdADKQFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSRRSIreVS----------- 548

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  596 ksskfssIGSQFKQQLQSLLETLNTTEPHYIRCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFL 675
Cdd:cd14890    549 -------VGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQIRQQGFALREEHDSFF 621

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|...
gi 1063705616  676 TRFRILAPEAtERSFDEVDACKKLLArVDLKGFQIGKTKVFLR 718
Cdd:cd14890    622 YDFQVLLPTA-ENIEQLVAVLSKMLG-LGKADWQIGSSKIFLK 662
MYSc_Myo31 cd14892
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ...
 77-718 0e+00

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: 631.02  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   77 LLN-LKARYNANEIYTYTGNILIAVNPFKRLPHLYG-NEIMEQYKGTDFGELS-PHPFAVADSAYRKM----INEGVSQA 149
Cdd:cd14892      3 LLDvLRRRYERDAIYTFTADILISINPYKSIPLLYDvPGFDSQRKEEATASSPpPHVFSIAERAYRAMkgvgKGQGTPQS 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  150 ILVSGESGAGKTESTKMLMQYLA---------YMGGKAESEGRSVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQ 220
Cdd:cd14892     83 IVVSGESGAGKTEASKYIMKYLAtasklakgaSTSKGAANAHESIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQIH 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  221 FNHMGRISGAAIRTYLLERSRVCQVSDPERNYHCFYMLCAA-PEQETERYQLGKPSTFHYLNQSNCHALDAIDDSKEYLA 299
Cdd:cd14892    163 YNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGlDANENAALELTPAESFLFLNQGNCVEVDGVDDATEFKQ 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  300 TRKAMDVVGISPEEQDAIFRVVAAILHLGNIEFAKSEESDGAEPKDDKSRfHLKVAAKLFMCDEKALENSLCNRVMVT-R 378
Cdd:cd14892    243 LRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDVFAQSADGV-NVAKAAGLLGVDAAELMFKLVTQTTSTaR 321

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  379 GESITKPLDPGSAALSRDALAKIVYSKLFDWLVTKINNSIGQDSSSKYI----------IGVLDIYGFESFKTNSFEQFC 448
Cdd:cd14892    322 GSVLEIKLTAREAKNALDALCKYLYGELFDWLISRINACHKQQTSGVTGgaasptfspfIGILDIFGFEIMPTNSFEQLC 401

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  449 INLTNEKLQQHFNQHVFKMEQEEYTKEEIDWSYIEFIDNQDVLDLIEKKPGGIIALLDEACMFPRSTHD-TLAEKLYQT- 526
Cdd:cd14892    402 INFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQDNQDCLDLIQKKPLGLLPLLEEQMLLKRKTTDkQLLTIYHQTh 481

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  527 FGSHKRFTKPKLARTDFTICHYAGDVTYQTELFLDKNKDYVVGEHQSLMNSSdcsfvsslfpksreessksskfssigSQ 606
Cdd:cd14892    482 LDKHPHYAKPRFECDEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSS--------------------------SK 535

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  607 FKQQLQSLLETLNTTEPHYIRCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILA---- 682
Cdd:cd14892    536 FRTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREGFPIRRQFEEFYEKFWPLArnka 615

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|.
gi 1063705616  683 ----PEATERSFDEVDACKKLLAR-VDLKGFQIGKTKVFLR 718
Cdd:cd14892    616 gvaaSPDACDATTARKKCEEIVARaLERENFQLGRTKVFLR 656
MYSc_Myo9 cd01385
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ...
 77-718 0e+00

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: 627.48  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   77 LLNLKARYNANEIYTYTGNILIAVNPFKRLPhLYGNEIMEQYKGTDFGELSPHPFAVADSAYRKMINEGVSQAILVSGES 156
Cdd:cd01385      4 LENLRARFKHGKIYTYVGSILIAVNPFKFLP-IYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISGES 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  157 GAGKTESTKMLMQYLAYMGGKAEseGRSVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFNHMGRISGAAIRTYL 236
Cdd:cd01385     83 GSGKTESTNFLLHHLTALSQKGY--GSGVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVEKYL 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  237 LERSRVCQVSDPERNYHCFYMLCA-APEQETERYQLGKPSTFHYLNQSNCHALDAIDDSKEYLATRKAMDVVGISPEEQD 315
Cdd:cd01385    161 LEKSRIVSQEKNERNYHVFYYLLAgASEEERKELHLKQPEDYHYLNQSDCYTLEGEDEKYEFERLKQAMEMVGFLPETQR 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  316 AIFRVVAAILHLGNIEFAK----SEESDGAEPKDDksrfhLKVAAKLFMCDEKALENSLCNRVMVTRGESITKPLDPGSA 391
Cdd:cd01385    241 QIFSVLSAVLHLGNIEYKKkayhRDESVTVGNPEV-----LDIISELLRVKEETLLEALTTKKTVTVGETLILPYKLPEA 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  392 ALSRDALAKIVYSKLFDWLVTKIN----NSIGQDSSSKYIIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKM 467
Cdd:cd01385    316 IATRDAMAKCLYSALFDWIVLRINhallNKKDLEEAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIFKL 395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  468 EQEEYTKEEIDWSYIEFIDNQDVLDLIEKKPGGIIALLDEACMFPRSTHDTLAEKLYQTFGSHKRFTKPKLARTDFTICH 547
Cdd:cd01385    396 EQEEYKKEGISWHNIEYTDNTGCLQLISKKPTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNKYYEKPQVMEPAFIIAH 475

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  548 YAGDVTYQTELFLDKNKDYVVGEHQSLMNSSDCSFVSSLF---------------------------------------- 587
Cdd:cd01385    476 YAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVRELIgidpvavfrwavlrafframaafreagrrraqrtaghslt 555

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  588 -----PKSREESSKSSKFSSIGSQFKQQLQSLLETLNTTEPHYIRCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISC 662
Cdd:cd01385    556 lhdrtTKSLLHLHKKKKPPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTGMLETVRIRR 635

                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1063705616  663 AGYPTRKPFNEFLTRFRILAPEATERSFDEVdacKKLLAR--VDLKGFQIGKTKVFLR 718
Cdd:cd01385    636 SGYSVRYTFQEFITQFQVLLPKGLISSKEDI---KDFLEKlnLDRDNYQIGKTKVFLK 690
MYSc_Myo42 cd14903
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ...
 74-718 0e+00

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: 622.18  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   74 PGVLLNLKARYNANEIYTYTGNILIAVNPFKRLPHLYGNEIMEQYKGTDFGELSPHPFAVADSAYRKMINEGVSQAILVS 153
Cdd:cd14903      1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPELYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  154 GESGAGKTESTKMLMQYLAYMGGKAESegrSVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFNHMGRISGAAIR 233
Cdd:cd14903     81 GESGAGKTETTKILMNHLATIAGGLND---STIKKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLVGAKCR 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  234 TYLLERSRVCQVSDPERNYHCFYMLCAAPEQEtERYQLGKPSTFHYLNQSNCHALDAIDDSKEYLATRKAMDVVGISPEE 313
Cdd:cd14903    158 TYLLEKTRVISHERPERNYHIFYQLLASPDVE-ERLFLDSANECAYTGANKTIKIEGMSDRKHFARTKEALSLIGVSEEK 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  314 QDAIFRVVAAILHLGNIEF-AKS--EESDGAEPKDDksrfHLKVAAKLFMCDEKALENSLCNRVMVTRGESITKPLDPGS 390
Cdd:cd14903    237 QEVLFEVLAGILHLGQLQIqSKPndDEKSAIAPGDQ----GAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKKDQ 312

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  391 AALSRDALAKIVYSKLFDWLVTKINNSIGQDSSSKYIIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKMEQE 470
Cdd:cd14903    313 AEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFKTVQI 392

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  471 EYTKEEIDWSYIEFIDNQDVLDLIEKKPgGIIALLDEACMFPRSTHDTLAEKLYqtfGSHKRFTK----PKLARTDFTIC 546
Cdd:cd14903    393 EYEEEGIRWAHIDFADNQDVLAVIEDRL-GIISLLNDEVMRPKGNEESFVSKLS---SIHKDEQDviefPRTSRTQFTIK 468

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  547 HYAGDVTYQTELFLDKNKDYVVGEHQSLMNSSDCSFVSSLFPKSREESSKSSKFSS---------------IGSQFKQQL 611
Cdd:cd14903    469 HYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAASTSLArgarrrrggalttttVGTQFKDSL 548

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  612 QSLLETLNTTEPHYIRCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILAPEATERSFD 691
Cdd:cd14903    549 NELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFLPEGRNTDVP 628

                          650       660       670
                   ....*....|....*....|....*....|
gi 1063705616  692 EVDACKKLLARVDLKG---FQIGKTKVFLR 718
Cdd:cd14903    629 VAERCEALMKKLKLESpeqYQMGLTRIYFQ 658
MYSc_Myo10 cd14873
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ...
 76-718 0e+00

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: 615.65  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   76 VLLNLKARYNANEIYTYTGNILIAVNPFKRLPHLYGNEIMEQYKGTDFGELSPHPFAVADSAYRKMINEGVSQAILVSGE 155
Cdd:cd14873      3 IMYNLFQRYKRNQIYTYIGSILASVNPYQPIAGLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILISGE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  156 SGAGKTESTKMLMQYLAYM-----GGKAESEGRSVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFNHMGRISGA 230
Cdd:cd14873     83 SGAGKTESTKLILKFLSVIsqqslELSLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQGG 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  231 AIRTYLLERSRVCQVSDPERNYHCFYMLCA-APEQETERYQLGKPSTFHYLNQSNCHALDAIDDSKEYLATRKAMDVVGI 309
Cdd:cd14873    163 RIVDYLLEKNRVVRQNPGERNYHIFYALLAgLEHEEREEFYLSTPENYHYLNQSGCVEDKTISDQESFREVITAMEVMQF 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  310 SPEEQDAIFRVVAAILHLGNIEFAKseeSDGAEPKDDKSrfhLKVAAKLFMCDEKALENSLCNRVMVTRGESITKPLDPG 389
Cdd:cd14873    243 SKEEVREVSRLLAGILHLGNIEFIT---AGGAQVSFKTA---LGRSAELLGLDPTQLTDALTQRSMFLRGEEILTPLNVQ 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  390 SAALSRDALAKIVYSKLFDWLVTKINNSI-GQDSSSKyiIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKME 468
Cdd:cd14873    317 QAVDSRDSLAMALYARCFEWVIKKINSRIkGKEDFKS--IGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLE 394

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  469 QEEYTKEEIDWSYIEFIDNQDVLDLIEKKPgGIIALLDEACMFPRSTHDTLAEKLYQTFGSHKRFTKPKLARTDFTICHY 548
Cdd:cd14873    395 QLEYSREGLVWEDIDWIDNGECLDLIEKKL-GLLALINEESHFPQATDSTLLEKLHSQHANNHFYVKPRVAVNNFGVKHY 473

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  549 AGDVTYQTELFLDKNKDYVVGEHQSLMNSSDCSFVSSLFPKSREESSKSSKFS-------SIGSQFKQQLQSLLETLNTT 621
Cdd:cd14873    474 AGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSRNNQDTLKCgskhrrpTVSSQFKDSLHSLMATLSSS 553

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  622 EPHYIRCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILAPEATErSFDEVDACKKLLA 701
Cdd:cd14873    554 NPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNLAL-PEDVRGKCTSLLQ 632

                          650
                   ....*....|....*....
gi 1063705616  702 RVDL--KGFQIGKTKVFLR 718
Cdd:cd14873    633 LYDAsnSEWQLGKTKVFLR 651
MYSc_Myo15 cd01387
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ...
 76-718 0e+00

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: 614.84  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   76 VLLNLKARYNANEIYTYTGNILIAVNPFKRLpHLYGNEIMEQYKGTDFGELSPHPFAVADSAYRKMINEGVSQAILVSGE 155
Cdd:cd01387      3 VLWNLKTRYERNLIYTYIGSILVSVNPYKMF-DIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISGE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  156 SGAGKTESTKMLMQYLAYMggkAESEGRSVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFNHmGRISGAAIRTY 235
Cdd:cd01387     82 SGSGKTEATKLIMQYLAAV---NQRRNNLVTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFFEG-GVIVGAITSQY 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  236 LLERSRVCQVSDPERNYHCFY-MLCAAPEQETERYQLGKPSTFHYLNQSNCHALDAIDDSKEYLATRKAMDVVGISPEEQ 314
Cdd:cd01387    158 LLEKSRIVTQAKNERNYHVFYeLLAGLPAQLRQKYGLQEAEKYFYLNQGGNCEIAGKSDADDFRRLLAAMQVLGFSSEEQ 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  315 DAIFRVVAAILHLGNIEFAKSEESDGAEPKDDKSRFHLKVAAKLFMCDEKALENSLCNRVMVTRGESITKPLDPGSAALS 394
Cdd:cd01387    238 DSIFRILASVLHLGNVYFHKRQLRHGQEGVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRERIFTPLTIDQALDA 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  395 RDALAKIVYSKLFDWLVTKINNSIGQDSSSKYIIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKMEQEEYTK 474
Cdd:cd01387    318 RDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVFKLEQEEYIR 397

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  475 EEIDWSYIEFIDNQDVLDLIEKKPGGIIALLDEACMFPRSTHDTLAEKLYQTFGSHKRFTKPKLARTDFTICHYAGDVTY 554
Cdd:cd01387    398 EQIDWTEIAFADNQPVINLISKKPVGILHILDDECNFPQATDHSFLEKCHYHHALNELYSKPRMPLPEFTIKHYAGQVWY 477

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  555 QTELFLDKNKDYVVGEHQSLMNSSDCSFVSSLFPKSREESSKSSKFSSIGS-------------QFKQQLQSLLETLNTT 621
Cdd:cd01387    478 QVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHRAQTDKAPPRLGKGRfvtmkprtptvaaRFQDSLLQLLEKMERC 557

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  622 EPHYIRCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILAPEATERS--FDEVDACKKL 699
Cdd:cd01387    558 NPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVALKLPRPapGDMCVSLLSR 637

                          650       660
                   ....*....|....*....|
gi 1063705616  700 LARVDLKG-FQIGKTKVFLR 718
Cdd:cd01387    638 LCTVTPKDmYRLGATKVFLR 657
MYSc_Myo3 cd01379
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ...
 80-718 0e+00

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: 611.59  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   80 LKARYNANEIYTYTGNILIAVNPFKRLPhLYGNEIMEQYKGTDFGELSPHPFAVADSAYRKMINEGVSQAILVSGESGAG 159
Cdd:cd01379      7 LQKRYSRDQIYTYIGDILIAVNPFQNLG-IYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGESGAG 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  160 KTESTKMLMQYLAYMGgKAESegRSVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFNHMGRISGAAIRTYLLER 239
Cdd:cd01379     86 KTESANLLVQQLTVLG-KANN--RTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEYLLEK 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  240 SRVCQVSDPERNYHCFYMLCA--APEQETERYQLGKPSTFHYLNQSNCHALDAIDDS---KEYLATRKAMDVVGISPEEQ 314
Cdd:cd01379    163 SRVVHQAIGERNFHIFYYIYAglAEDKKLAKYKLPENKPPRYLQNDGLTVQDIVNNSgnrEKFEEIEQCFKVIGFTKEEV 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  315 DAIFRVVAAILHLGNIEFakseESDGAEPKDDKSRF-----HLKVAAKLFMCDEKALENSLCNRVMVTRGESITKPLDPG 389
Cdd:cd01379    243 DSVYSILAAILHIGDIEF----TEVESNHQTDKSSRisnpeALNNVAKLLGIEADELQEALTSHSVVTRGETIIRNNTVE 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  390 SAALSRDALAKIVYSKLFDWLVTKINNSIGQDSSS---KYIIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFK 466
Cdd:cd01379    319 EATDARDAMAKALYGRLFSWIVNRINSLLKPDRSAsdePLSIGILDIFGFENFQKNSFEQLCINIANEQIQYYFNQHIFA 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  467 MEQEEYTKEEIDWSYIEFIDNQDVLDLIEKKPGGIIALLDEACMFPRSTHDTLAEKLYQTFgSHKRFTKPKLARTDFTIC 546
Cdd:cd01379    399 WEQQEYLNEGIDVDLIEYEDNRPLLDMFLQKPMGLLALLDEESRFPKATDQTLVEKFHNNI-KSKYYWRPKSNALSFGIH 477

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  547 HYAGDVTYQTELFLDKNKDYVVGEHQSLMNSSDCSFVsslfpksreessksskFSSIGSQFKQQLQSLLETLNTTEPHYI 626
Cdd:cd01379    478 HYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLV----------------RQTVATYFRYSLMDLLSKMVVGQPHFV 541

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  627 RCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILAPEATERSFDEVDACKKLLARVDLK 706
Cdd:cd01379    542 RCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYYFLAFKWNEEVVANRENCRLILERLKLD 621

                          650
                   ....*....|..
gi 1063705616  707 GFQIGKTKVFLR 718
Cdd:cd01379    622 NWALGKTKVFLK 633
MYSc_Myo36 cd14897
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ...
 76-718 0e+00

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: 600.91  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   76 VLLNLKARYNANEIYTYTGNILIAVNPFKRLPhLYGNEIMEQYKG-TDFGELSPHPFAVADSAYRKMINEGVSQAILVSG 154
Cdd:cd14897      3 IVQTLKSRYNKDKFYTYIGDILVAVNPCKPLP-IFDKKHHEEYSNlSVRSQRPPHLFWIADQAYRRLLETGRNQCILVSG 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  155 ESGAGKTESTKMLMQYLAYMggkAESEGRSVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFNHMGRISGAAIRT 234
Cdd:cd14897     82 ESGAGKTESTKYMIKHLMKL---SPSDDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAKIDD 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  235 YLLERSRVCQVSDPERNYHCFYMLCA-APEQETERYQLGKPSTFHYLNQSNCHAlDAIDDSKEYLATR-------KAMDV 306
Cdd:cd14897    159 YLLEKSRVVHRGNGEKNFHIFYALFAgMSRDRLLYYFLEDPDCHRILRDDNRNR-PVFNDSEELEYYRqmfhdltNIMKL 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  307 VGISPEEQDAIFRVVAAILHLGNIEFAKSEESDGAEPKDDksrFHLKVAAKLFMCDEKALENSLCNRVMVTRGESITKPL 386
Cdd:cd14897    238 IGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADE---YPLHAVAKLLGIDEVELTEALISNVNTIRGERIQSWK 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  387 DPGSAALSRDALAKIVYSKLFDWLVTKINNSI--GQDSSSKY---IIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFN 461
Cdd:cd14897    315 SLRQANDSRDALAKDLYSRLFGWIVGQINRNLwpDKDFQIMTrgpSIGILDMSGFENFKINSFDQLCINLSNERLQQYFN 394

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  462 QHVFKMEQEEYTKEEIDWSYIEFIDNQDVLDLIEKKPGGIIALLDEACMFPRSTHDTLAEKLYQTFGSHKRFTKPKLART 541
Cdd:cd14897    395 DYVFPRERSEYEIEGIEWRDIEYHDNDDVLELFFKKPLGILPLLDEESTFPQSTDSSLVQKLNKYCGESPRYVASPGNRV 474

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  542 DFTICHYAGDVTYQTELFLDKNKDYVVGEHQSLMNSSDCSFVSSLFPksreessksskfssigSQFKQQLQSLLETLNTT 621
Cdd:cd14897    475 AFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFT----------------SYFKRSLSDLMTKLNSA 538

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  622 EPHYIRCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILAPEATERSFDEVDACKKLLA 701
Cdd:cd14897    539 DPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRYKEICDFSNKVRSDDLGKCQKILK 618

                          650
                   ....*....|....*..
gi 1063705616  702 RVDLKGFQIGKTKVFLR 718
Cdd:cd14897    619 TAGIKGYQFGKTKVFLK 635
MYSc_Myo47 cd14908
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ...
 74-718 0e+00

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: 583.79  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   74 PGVLLNLKARYNANEIYTYTGNILIAVNPFKRLPhLYGNEIMEQY--------KGTDFGE-LSPHPFAVADSAYRKMINE 144
Cdd:cd14908      1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLP-LYGKEILESYrqegllrsQGIESPQaLGPHVFAIADRSYRQMMSE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  145 G-VSQAILVSGESGAGKTESTKMLMQYLAYMGG--------KAESEGRSVEQQVLESNPVLEAFGNAKTVRNNNSSRFGK 215
Cdd:cd14908     80 IrASQSILISGESGAGKTESTKIVMLYLTTLGNgeegapneGEELGKLSIMDRVLQSNPILEAFGNARTLRNDNSSRFGK 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  216 FVEIQFNHMGRISGAAIRTYLLERSRVCQVSDPERNYHCFYMLC-AAPEQETERYQLGK--------PSTFHYLNQSNCH 286
Cdd:cd14908    160 FIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLrGGDEEEHEKYEFHDgitgglqlPNEFHYTGQGGAP 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  287 ALDAIDDSKEYLATRKAMDVVGISPEEQDAIFRVVAAILHLGNIEFAKSEESDGAEPKDDKSRFHLKVAAKLFMCDEKAL 366
Cdd:cd14908    240 DLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEEGNEKCLARVAKLLGVDVDKL 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  367 ENSLCNRVMVTRGESITKPLDPGSAALSRDALAKIVYSKLFDWLVTKINNSIG--QDSSSKYIIGVLDIYGFESFKTNSF 444
Cdd:cd14908    320 LRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINweNDKDIRSSVGVLDIFGFECFAHNSF 399

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  445 EQFCINLTNEKLQQHFNQHVFKMEQEEYTKEEIDWSYIEFIDNQDVLDLIEKKPGGIIALLDEACMFP-RSTHDTLAEKL 523
Cdd:cd14908    400 EQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFPDNQDCLDTIQAKKKGILTMLDDECRLGiRGSDANYASRL 479

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  524 Y--------QTFGSHKRFTKPKLARTD--FTICHYAGDVTYQTEL-FLDKNKDYVVGEHQSLMNSsdcsfvsslfpksre 592
Cdd:cd14908    480 YetylpeknQTHSENTRFEATSIQKTKliFAVRHFAGQVQYTVETtFCEKNKDEIPLTADSLFES--------------- 544

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  593 essksskfssiGSQFKQQLQSLLETLNTTEPHYIRCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFN 672
Cdd:cd14908    545 -----------GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAVRVARSGYPVRLPHK 613

                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063705616  673 EFLTRFRILAPEATE----RSFDEVD---ACKKLLARVDLKG----------------FQIGKTKVFLR 718
Cdd:cd14908    614 DFFKRYRMLLPLIPEvvlsWSMERLDpqkLCVKKMCKDLVKGvlspamvsmknipedtMQLGKSKVFMR 682
MYSc_Myo43 cd14904
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ...
 74-718 0e+00

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: 571.12  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   74 PGVLLNLKARYNANEIYTYTGNILIAVNPFKRLPHLYGNEIMEQYKGTDFGELSPHPFAVADSAYRKMINEGVSQAILVS 153
Cdd:cd14904      1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDNLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  154 GESGAGKTESTKMLMQYLAYMGGkaeseGR--SVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFNHMGRISGAA 231
Cdd:cd14904     81 GESGAGKTETTKIVMNHLASVAG-----GRkdKTIAKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAK 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  232 IRTYLLERSRVCQVSDPERNYHCFY-MLCAAPEQETERYQLGKPSTFHYLNQSNCH-ALDAIDDSKEYLATRKAMDVVGI 309
Cdd:cd14904    156 CETYLLEKSRVVSIAEGERNYHIFYqLLAGLSSEERKEFGLDPNCQYQYLGDSLAQmQIPGLDDAKLFASTQKSLSLIGL 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  310 SPEEQDAIFRVVAAILHLGNIEFAKSEESDGAEPKDDKsrfhLKVAAKLFMCDEKALENSLCNRVMVTRGESITKPLDPG 389
Cdd:cd14904    236 DNDAQRTLFKILSGVLHLGEVMFDKSDENGSRISNGSQ----LSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLAPV 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  390 SAALSRDALAKIVYSKLFDWLVTKINNSIGQDSSSKYI-IGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKME 468
Cdd:cd14904    312 EAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKGqIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKTV 391

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  469 QEEYTKEEIDWSYIEFIDNQDVLDLIEKKPgGIIALLDEACMFPRSTHDTLAEKL---YQTFGSHKRFTKPKLARTDFTI 545
Cdd:cd14904    392 EEEYIREGLQWDHIEYQDNQGIVEVIDGKM-GIIALMNDHLRQPRGTEEALVNKIrtnHQTKKDNESIDFPKVKRTQFII 470

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  546 CHYAGDVTYQTELFLDKNKDYVVGEHQSLMNSSDCSFVSSLFPKSREESSKSSKFS--------SIGSQFKQQLQSLLET 617
Cdd:cd14904    471 NHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSEAPSETKEGKSgkgtkapkSLGSQFKTSLSQLMDN 550

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  618 LNTTEPHYIRCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILAPEATERSfDEVDACK 697
Cdd:cd14904    551 IKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFPPSMHSK-DVRRTCS 629

                          650       660
                   ....*....|....*....|....
gi 1063705616  698 KLLARVDLKG---FQIGKTKVFLR 718
Cdd:cd14904    630 VFMTAIGRKSpleYQIGKSLIYFK 653
MYSc_Myo30 cd14891
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ...
 74-718 0e+00

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


Pssm-ID: 276856  Cd Length: 645  Bit Score: 568.52  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   74 PGVLLNLKARYNANEI--YTYTGNILIAVNPFKRLPhlygNEIMEQYKGTDFGELSPHPFAVADSAYRKMI-NEGV--SQ 148
Cdd:cd14891      1 AGILHNLEERSKLDNQrpYTFMANVLIAVNPLRRLP----EPDKSDYINTPLDPCPPHPYAIAEMAYQQMClGSGRmqNQ 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  149 AILVSGESGAGKTESTKMLMQYLAY--MGGKAESE-------------GRSVEQQVLESNPVLEAFGNAKTVRNNNSSRF 213
Cdd:cd14891     77 SIVISGESGAGKTETSKIILRFLTTraVGGKKASGqdieqsskkrklsVTSLDERLMDTNPILESFGNAKTLRNHNSSRF 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  214 GKFVEIQF-NHMGRISGAAIRTYLLERSRVCQVSDPERNYHCFYMLCAAPEQE-TERYQLGKPSTFHYLNQSNCHALDAI 291
Cdd:cd14891    157 GKFMKLQFtKDKFKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAElLKELLLLSPEDFIYLNQSGCVSDDNI 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  292 DDSKEYLATRKAMDVVGISPEEQDAIFRVVAAILHLGNIEFAKSEESDG-AEPKDDKSRFHLKVAAKLFMCDEKALENSL 370
Cdd:cd14891    237 DDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEGeAEIASESDKEALATAAELLGVDEEALEKVI 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  371 CNRVMVTRGESITKPLDPGSAALSRDALAKIVYSKLFDWLVTKINNSIGQDSSSKYIIGVLDIYGFESFKT-NSFEQFCI 449
Cdd:cd14891    317 TQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFETkNDFEQLLI 396

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  450 NLTNEKLQQHFNQHVFKMEQEEYTKEEIDWSYIEFIDNQDVLDLIEKKPGGIIALLDEACMFPRSTHDTLAEKLYQTFGS 529
Cdd:cd14891    397 NYANEALQATFNQQVFIAEQELYKSEGIDVGVITWPDNRECLDLIASKPNGILPLLDNEARNPNPSDAKLNETLHKTHKR 476

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  530 HKRF--TKPKLARTDFTICHYAGDVTYQTELFLDKNKDYVVGEHQSLMNSSdcsfvsslfpksreessksskfssigSQF 607
Cdd:cd14891    477 HPCFprPHPKDMREMFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASS--------------------------AKF 530

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  608 KQQLQSLLETLNTTEPHYIRCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILAPEATE 687
Cdd:cd14891    531 SDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRVTYAELVDVYKPVLPPSVT 610

                          650       660       670
                   ....*....|....*....|....*....|....*..
gi 1063705616  688 RSFDEVDacKKLLA------RVDLKGFQIGKTKVFLR 718
Cdd:cd14891    611 RLFAEND--RTLTQailwafRVPSDAYRLGRTRVFFR 645
MYSc_Myo46 cd14907
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ...
 76-718 0e+00

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: 561.19  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   76 VLLNLKARYNANEIYTYTGNILIAVNPFKRLPHLYGNEIMEQYK--------GTDFGELSPHPFAVADSAYRKMINEGVS 147
Cdd:cd14907      3 LLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDNLFSEEVMQMYKeqiiqngeYFDIKKEPPHIYAIAALAFKQLFENNKK 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  148 QAILVSGESGAGKTESTKMLMQYLAYMGGKAESEGR----------------SVEQQVLESNPVLEAFGNAKTVRNNNSS 211
Cdd:cd14907     83 QAIVISGESGAGKTENAKYAMKFLTQLSQQEQNSEEvltltssiratskstkSIEQKILSCNPILEAFGNAKTVRNDNSS 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  212 RFGKFVEIQFNH-MGRISGAAIRTYLLERSRVCQVSDPERNYHCFY-MLCAAPEQETERYQLGKPST---FHYLNQSNCH 286
Cdd:cd14907    163 RFGKYVSILVDKkKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYhLLYGADQQLLQQLGLKNQLSgdrYDYLKKSNCY 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  287 ALDAIDDSKEYLATRKAMDVVGISPEEQDAIFRVVAAILHLGNIEFAKSEESDGaEPKDDKSRFHLKVAAKLFMCDEKAL 366
Cdd:cd14907    243 EVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTLDDN-SPCCVKNKETLQIIAKLLGIDEEEL 321

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  367 ENSLCNRVMVTRGESITKPLDPGSAALSRDALAKIVYSKLFDWLVTKINNSIGQDSSSKY--------IIGVLDIYGFES 438
Cdd:cd14907    322 KEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTIMPKDEKDQqlfqnkylSIGLLDIFGFEV 401

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  439 FKTNSFEQFCINLTNEKLQQHFNQHVFKMEQEEYTKE--EIDWSYIEFIDNQDVLDLIEKKPGGIIALLDEACMFPRSTH 516
Cdd:cd14907    402 FQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEglEDYLNQLSYTDNQDVIDLLDKPPIGIFNLLDDSCKLATGTD 481

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  517 DTLAEKLYQTFGSHKRFTKP-KLARTDFTICHYAGDVTYQTELFLDKNKDYVVGEHQSLMNSSDCSFVSSLFPKSREESS 595
Cdd:cd14907    482 EKLLNKIKKQHKNNSKLIFPnKINKDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFSGEDGSQQ 561

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  596 KSSKFSS--------IGSQFKQQLQSLLETLNTTEPHYIRCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPT 667
Cdd:cd14907    562 QNQSKQKksqkkdkfLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLESIRVRKQGYPY 641

                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1063705616  668 RKPFNEFLTRFRILApeatersfdevdacKKLLarvdlkgfqIGKTKVFLR 718
Cdd:cd14907    642 RKSYEDFYKQYSLLK--------------KNVL---------FGKTKIFMK 669
MyosinXI_CBD cd15475
cargo binding domain of myosin XI; Class XI myosins are a plant specific group, homologous to ...
 1274-1715 8.36e-179

cargo binding domain of myosin XI; Class XI myosins are a plant specific group, homologous to class V myosins. C-terminal domain of Arabidopsis myosin XI has been shown to be homologous to the cargo-binding domain of yeast myosin V myo2p, which targets myosin to vacuole- and mitochondria, as well as secretory vesicle.


Pssm-ID: 271259  Cd Length: 326  Bit Score: 540.62  E-value: 8.36e-179
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1274 QQPHEFVDVLLKCVSKNVGFSHGKPVAAFTIYKCLIHWKLFEAEKTSVFDRIVPIFGSAIENPEDDSNLAYWLTNTSTLL 1353
Cdd:cd15475      1 ERQQENVDALIKCVSENLGFSEGKPVAAFTIYKCLLHWKSFEAEKTSVFDRIIQTIGSAIEDQDNNDHLAYWLSNTSTLL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1354 FLLQRSLkshsttgaspkkppqptsffgrmtqgfrspssaslsgdvvqqvdaryPALLFKQQLTAYIETIYGIFQENVKR 1433
Cdd:cd15475     81 FLLQRSL-----------------------------------------------PALLFKQQLTAYVEKIYGIIRDNLKK 113

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1434 KLAPVLSSCIQGLKDSShefsaetlsaesseqnspekpseenppeklsednssgklsedylaakpsednspakpseensq 1513
Cdd:cd15475    114 ELSPLLSLCIQAPRTSR--------------------------------------------------------------- 130

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1514 aklsevnpqAKPSAENSLAKPSEENSPTETWQDVIGLLNQLLGTLKKNYVPLFLAQKIFCQTFQDINVQLFNSLL-QREC 1592
Cdd:cd15475    131 ---------GSSSKSSSSANSLGQQSPSSHWQSIIKSLNSLLSTLKENHVPPFLVQKIFTQVFSFINVQLFNSLLlRREC 201

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1593 CTFIMGKKVNVWLNELESWCSQATEDFVGSSWDELKNTRQALVLLVTEQKSTITYDDLTTNLCPALSTQQLYRICTLCKI 1672
Cdd:cd15475    202 CSFSNGEYVKAGLAELELWCSQATEEYAGSSWDELKHIRQAVGFLVIHQKSRKSYDEITNDLCPVLSVQQLYRICTMYWD 281

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 1063705616 1673 DDHEDQNVSPDVISNLKLLVTDEDED--SRSFLLDNNSSIPFAAD 1715
Cdd:cd15475    282 DKYGTQSVSPEVISSMRVLMTEDSNNavSNSFLLDDDSSIPFSVE 326
MYSc_Myo39 cd14900
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ...
 76-707 1.14e-176

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: 547.21  E-value: 1.14e-176
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   76 VLLNLKARYNANEIYTYTGNILIAVNPFKRLPHLYGNEIMEQY-------------KGTDfgELSPHPFAVADSAYRKMI 142
Cdd:cd14900      3 ILSALETRFYAQKIYTNTGAILLAVNPFQKLPGLYSSDTMAKYllsfearssstrnKGSD--PMPPHIYQVAGEAYKAMM 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  143 NEGVS----QAILVSGESGAGKTESTKMLMQYLAYMGG-------KAESEGRSVEQQVLESNPVLEAFGNAKTVRNNNSS 211
Cdd:cd14900     81 LGLNGvmsdQSILVSGESGSGKTESTKFLMEYLAQAGDnnlaasvSMGKSTSGIAAKVLQTNILLESFGNARTLRNDNSS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  212 RFGKFVEIQFNHMGRISGAAIRTYLLERSRVCQVSDPERNYHCFY-MLCAAPEQETERyqlgkpstfhylnqsnchalda 290
Cdd:cd14900    161 RFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYeMAIGASEAARKR---------------------- 218

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  291 iddsKEYLATRKAMDVVGISPEEQDAIFRVVAAILHLGNIEFAKSEESD-GAEPKDD---KSRFHLKVAAKLFMCDEKAL 366
Cdd:cd14900    219 ----DMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDrLGQLKSDlapSSIWSRDAAATLLSVDATKL 294

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  367 ENSLCNRVMVTRGESITKPLDPGSAALSRDALAKIVYSKLFDWLVTKINNSIGQDSSSK-----YIIGVLDIYGFESFKT 441
Cdd:cd14900    295 EKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLKMDDSSKshgglHFIGILDIFGFEVFPK 374

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  442 NSFEQFCINLTNEKLQQHFNQHVFKMEQEEYTKEEIDWSYIEFIDNQDVLDLIEKKPGGIIALLDEACMFPRSTHDTLAE 521
Cdd:cd14900    375 NSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFCDNQDCVNLISQRPTGILSLIDEECVMPKGSDTTLAS 454

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  522 KLYQTFGSHKRFTKPKL--ARTDFTICHYAGDVTYQTELFLDKNKDYVvgeHQSLMNssdcsfvssLFpksreesskssk 599
Cdd:cd14900    455 KLYRACGSHPRFSASRIqrARGLFTIVHYAGHVEYSTDGFLEKNKDVL---HQEAVD---------LF------------ 510

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  600 fsSIGSQFKQQLQSLLETLNTTEPHYIRCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFR 679
Cdd:cd14900    511 --VYGLQFKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVARAGFPIRLLHDEFVARYF 588

                          650       660
                   ....*....|....*....|....*...
gi 1063705616  680 ILAPEATERSfdevdACKKLLARVDLKG 707
Cdd:cd14900    589 SLARAKNRLL-----AKKQGTSLPDTDS 611
MYSc_Myh2_insects_mollusks cd14911
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ...
 76-718 1.18e-172

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: 538.03  E-value: 1.18e-172
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   76 VLLNLKARYNANEIYTYTGNILIAVNPFKRLPhLYGNEIMEQYKGTDFGELSPHPFAVADSAYRKMINEGVSQAILVSGE 155
Cdd:cd14911      3 VLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLP-IYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  156 SGAGKTESTKMLMQYLAYMGG-KAESEGRS-------------VEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQF 221
Cdd:cd14911     82 SGAGKTENTKKVIQFLAYVAAsKPKGSGAVphpavnpavligeLEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  222 NHMGRISGAAIRTYLLERSRVCQVSDPERNYHCFYMLC--AAPEQETErYQLGKPSTFHYLNQSNcHALDAIDDSKEYLA 299
Cdd:cd14911    162 DASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLagATPEQREK-FILDDVKSYAFLSNGS-LPVPGVDDYAEFQA 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  300 TRKAMDVVGISPEEQDAIFRVVAAILHLGNIEFAKSEESDGAEPKDDKsrFHLKVAAKLFMCDEKALENSLCNRVMVTRg 379
Cdd:cd14911    240 TVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNT--VAQKIAHLLGLSVTDMTRAFLTPRIKVGR- 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  380 ESITKPLDPGSAALSRDALAKIVYSKLFDWLVTKINNSIGQDS-SSKYIIGVLDIYGFESFKTNSFEQFCINLTNEKLQQ 458
Cdd:cd14911    317 DFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKrQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQ 396

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  459 HFNQHVFKMEQEEYTKEEIDWSYIEF-IDNQDVLDLIEkKPGGIIALLDEACMFPRSTHDTLAEKLYQTFGSHKRFTKPK 537
Cdd:cd14911    397 LFNHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLID-KPGGIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMKTD 475

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  538 L-ARTDFTICHYAGDVTYQTELFLDKNKDYVVGEHQSLMNSSDCSFVSSLFPKSREESSKSSKFS--------------S 602
Cdd:cd14911    476 FrGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIVGMAQQALTdtqfgartrkgmfrT 555

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  603 IGSQFKQQLQSLLETLNTTEPHYIRCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILA 682
Cdd:cd14911    556 VSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLT 635

                          650       660       670
                   ....*....|....*....|....*....|....*....
gi 1063705616  683 PEATERSF-DEVDACKKLLARVDLKG--FQIGKTKVFLR 718
Cdd:cd14911    636 PNVIPKGFmDGKKACEKMIQALELDSnlYRVGQSKIFFR 674
MYSc_Myo28 cd14889
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ...
 76-718 4.35e-170

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: 530.63  E-value: 4.35e-170
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   76 VLLN-LKARYNANEIYTYTGNILIAVNPFKRLpHLYGNEIMEQYKGTDFGELSPHPFAVADSAYRKMINEGVS----QAI 150
Cdd:cd14889      2 VLLEvLKVRFMQSNIYTYVGDILVAINPFKYL-HIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLGRLARgpknQCI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  151 LVSGESGAGKTESTKMLMQYLAYMGgKAESEgrsVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFNHmGRISGA 230
Cdd:cd14889     81 VISGESGAGKTESTKLLLRQIMELC-RGNSQ---LEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRFRN-GHVKGA 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  231 AIRTYLLERSRVCQVSDPERNYHCFY-MLCAAPEQETERYQLGKPSTFHYLNqsncHALDAIDD----SKEYLATRKAMD 305
Cdd:cd14889    156 KINEYLLEKSRVVHQDGGEENFHIFYyMFAGISAEDRENYGLLDPGKYRYLN----NGAGCKREvqywKKKYDEVCNAMD 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  306 VVGISPEEQDAIFRVVAAILHLGNIEFAKSEesDGAEPKDDKSRFHLKVAAKLFMCDEKALENSLCNRVMVTRGESITKP 385
Cdd:cd14889    232 MVGFTEQEEVDMFTILAGILSLGNITFEMDD--DEALKVENDSNGWLKAAAGQFGVSEEDLLKTLTCTVTFTRGEQIQRH 309

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  386 LDPGSAALSRDALAKIVYSKLFDWLVTKINNSIG-QDSSSKYI--IGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQ 462
Cdd:cd14889    310 HTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLApKDDSSVELreIGILDIFGFENFAVNRFEQACINLANEQLQYFFNH 389

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  463 HVFKMEQEEYTKEEIDWSYIEFIDNQDVLDLIEKKPGGIIALLDEACMFPRSTHDTLAEKLYQTFGSHKRFTKPKLARTD 542
Cdd:cd14889    390 HIFLMEQKEYKKEGIDWKEITYKDNKPILDLFLNKPIGILSLLDEQSHFPQATDESFVDKLNIHFKGNSYYGKSRSKSPK 469

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  543 FTICHYAGDVTYQTELFLDKNKDYVVGEHQSLMNSSDCSFVSSLF----------------PKSREESSKSSKFSSIGSQ 606
Cdd:cd14889    470 FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFtatrsrtgtlmpraklPQAGSDNFNSTRKQSVGAQ 549

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  607 FKQQLQSLLETLNTTEPHYIRCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILAPEAt 686
Cdd:cd14889    550 FKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAERYKILLCEP- 628

                          650       660       670
                   ....*....|....*....|....*....|..
gi 1063705616  687 ERSFDEvDACKKLLARVDLKGFQIGKTKVFLR 718
Cdd:cd14889    629 ALPGTK-QSCLRILKATKLVGWKCGKTRLFFK 659
MYSc_Myh10 cd14920
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ...
 76-718 1.71e-167

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: 524.19  E-value: 1.71e-167
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   76 VLLNLKARYNANEIYTYTGNILIAVNPFKRLPhLYGNEIMEQYKGTDFGELSPHPFAVADSAYRKMINEGVSQAILVSGE 155
Cdd:cd14920      3 VLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  156 SGAGKTESTKMLMQYLAYM-----GGKAESEGRSVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFNHMGRISGA 230
Cdd:cd14920     82 SGAGKTENTKKVIQYLAHVasshkGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  231 AIRTYLLERSRVCQVSDPERNYHCFY-MLCAAPEQETERYQLGKPSTFHYLNQSNChALDAIDDSKEYLATRKAMDVVGI 309
Cdd:cd14920    162 NIETYLLEKSRAVRQAKDERTFHIFYqLLSGAGEHLKSDLLLEGFNNYRFLSNGYI-PIPGQQDKDNFQETMEAMHIMGF 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  310 SPEEQDAIFRVVAAILHLGNIEFAKSEESDGAEPKDDksrfhlKVAAKL-FMCDEKALENS---LCNRVMVTRgESITKP 385
Cdd:cd14920    241 SHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPEN------TVAQKLcHLLGMNVMEFTraiLTPRIKVGR-DYVQKA 313

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  386 LDPGSAALSRDALAKIVYSKLFDWLVTKINNSIGQ-DSSSKYIIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHV 464
Cdd:cd14920    314 QTKEQADFAVEALAKATYERLFRWLVHRINKALDRtKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 393

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  465 FKMEQEEYTKEEIDWSYIEF-IDNQDVLDLIEK--KPGGIIALLDEACMFPRSTHDTLAEKLYQTFGSHKRFTKPKLAR- 540
Cdd:cd14920    394 FILEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKd 473

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  541 -TDFTICHYAGDVTYQTELFLDKNKDYVVGEHQSLMNSSDCSFVSSLFPKSREESSKSSKFS------------------ 601
Cdd:cd14920    474 kADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGmtetafgsayktkkgmfr 553

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  602 SIGSQFKQQLQSLLETLNTTEPHYIRCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRIL 681
Cdd:cd14920    554 TVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 633

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|
gi 1063705616  682 APEATERSF-DEVDACKKLLARVDLKG--FQIGKTKVFLR 718
Cdd:cd14920    634 TPNAIPKGFmDGKQACERMIRALELDPnlYRIGQSKIFFR 673
MYSc_Myh3 cd14913
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ...
 74-718 4.87e-164

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: 514.99  E-value: 4.87e-164
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   74 PGVLLNLKARYNANEIYTYTGNILIAVNPFKRLPhLYGNEIMEQYKGTDFGELSPHPFAVADSAYRKMINEGVSQAILVS 153
Cdd:cd14913      1 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLP-VYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  154 GESGAGKTESTKMLMQYLAYMGG------KAESEGR-SVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFNHMGR 226
Cdd:cd14913     80 GESGAGKTVNTKRVIQYFATIAAtgdlakKKDSKMKgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  227 ISGAAIRTYLLERSRVCQVSDPERNYHCFYMLCAAPEQETERYQL--GKPSTFHYLNQSNChALDAIDDSKEYLATRKAM 304
Cdd:cd14913    160 LASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLitTNPYDYPFISQGEI-LVASIDDAEELLATDSAI 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  305 DVVGISPEEQDAIFRVVAAILHLGNIEFAKSEESDGAEPkdDKSRFHLKVAAkLFMCDEKALENSLCNRVMVTRGESITK 384
Cdd:cd14913    239 DILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEP--DGTEVADKTAY-LMGLNSSDLLKALCFPRVKVGNEYVTK 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  385 PLDPGSAALSRDALAKIVYSKLFDWLVTKINNSIGQDSSSKYIIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHV 464
Cdd:cd14913    316 GQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHM 395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  465 FKMEQEEYTKEEIDWSYIEF-IDNQDVLDLIEkKPGGIIALLDEACMFPRSTHDTLAEKLY-QTFGSHKRFTKPKLAR-- 540
Cdd:cd14913    396 FVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKVVKgr 474

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  541 --TDFTICHYAGDVTYQTELFLDKNKD----YVVGEHQS----LMNSSDCSFVSSLFPKSREESSKS--SKFSSIGSQFK 608
Cdd:cd14913    475 aeAHFSLIHYAGTVDYSVSGWLEKNKDplneTVVGLYQKssnrLLAHLYATFATADADSGKKKVAKKkgSSFQTVSALFR 554

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  609 QQLQSLLETLNTTEPHYIRCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILAPEAT-E 687
Cdd:cd14913    555 ENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIpE 634

                          650       660       670
                   ....*....|....*....|....*....|....
gi 1063705616  688 RSF-DEVDACKKLLARVDL--KGFQIGKTKVFLR 718
Cdd:cd14913    635 GQFiDSKKACEKLLASIDIdhTQYKFGHTKVFFK 668
MYSc_Myo14 cd14876
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ...
 74-718 9.89e-163

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: 510.69  E-value: 9.89e-163
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   74 PGVLLNLKARYNANEIYTYTGNILIAVNPFKRLphlyGN---EIMEQYKGT-DFGELSPHPFAVADSAYRKMINEGVSQA 149
Cdd:cd14876      1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDL----GNatdEWIRKYRDApDLTKLPPHVFYTARRALENLHGVNKSQT 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  150 ILVSGESGAGKTESTKMLMQYLAYmGGKAESEGRsVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFNHMGRISG 229
Cdd:cd14876     77 IIVSGESGAGKTEATKQIMRYFAS-AKSGNMDLR-IQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIRY 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  230 AAIRTYLLERSRVCQVSDPERNYHCFYMLC-AAPEQETERYQLGKPSTFHYLNqSNCHALDAIDDSKEYLATRKAMDVVG 308
Cdd:cd14876    155 GSVVAFLLEKSRIVTQDDNERSYHIFYQLLkGADSEMKSKYHLLGLKEYKFLN-PKCLDVPGIDDVADFEEVLESLKSMG 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  309 ISPEEQDAIFRVVAAILHLGNIEFAKSEES--DGAEPKDDKSRFHLKVAAKLFMCDEKALENSLCNRVMVTRGESITKPL 386
Cdd:cd14876    234 LTEEQIDTVFSIVSGVLLLGNVKITGKTEQgvDDAAAISNESLEVFKEACSLLFLDPEALKRELTVKVTKAGGQEIEGRW 313

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  387 DPGSAALSRDALAKIVYSKLFDWLVTKINNSIGQDSSSKYIIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFK 466
Cdd:cd14876    314 TKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFIDIVFE 393

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  467 MEQEEYTKEEIDWSYIEFIDNQDVLDLIEKKPGGIIALLDEACMFPRSTHDTLAEKLYQTFGSHKRFTKPKLA-RTDFTI 545
Cdd:cd14876    394 RESKLYKDEGIPTAELEYTSNAEVIDVLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSKLKSNGKFKPAKVDsNINFIV 473

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  546 CHYAGDVTYQTELFLDKNKDYVVGEHQSLMNSSDCSFVSSLFPKSREESSKSSKFSSIGSQFKQQLQSLLETLNTTEPHY 625
Cdd:cd14876    474 VHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVVVEKGKIAKGSLIGSQFLKQLESLMGLINSTEPHF 553

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  626 IRCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILAPEATE-RSFDEVDACKKLLARVD 704
Cdd:cd14876    554 IRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFLDLGIANdKSLDPKVAALKLLESSG 633

                          650
                   ....*....|....*.
gi 1063705616  705 LK--GFQIGKTKVFLR 718
Cdd:cd14876    634 LSedEYAIGKTMVFLK 649
MYSc_Myo35 cd14896
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ...
 74-718 5.33e-162

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: 508.55  E-value: 5.33e-162
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   74 PGVLLNLKARYNANEIYTYTGNILIAVNPFKRLPhLYGNEIMEQYKGTDFGELSPHPFAVADSAYRKMINEGVSQAILVS 153
Cdd:cd14896      1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLP-LFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  154 GESGAGKTESTKMLMQYLAYMGgkaESEGRSVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFNHmGRISGAAIR 233
Cdd:cd14896     80 GHSGSGKTEAAKKIVQFLSSLY---QDQTEDRLRQPEDVLPILESFGHAKTILNANASRFGQVLRLHLQH-GVIVGASVS 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  234 TYLLERSRVCQVSDPERNYHCFY-MLCAAPEQETERYQLGKPSTFHYLNQSNCHALDAIDDSKEYLATRKAMDVVGISPE 312
Cdd:cd14896    156 HYLLETSRVVFQAQAERSFHVFYeLLAGLDPEEREQLSLQGPETYYYLNQGGACRLQGKEDAQDFEGLLKALQGLGLCAE 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  313 EQDAIFRVVAAILHLGNIEFAkSEESDGAEPKDDKSRFHLKVAAKLFMCDEKALENSLCNRVMVTRGESITKPLDPGSAA 392
Cdd:cd14896    236 ELTAIWAVLAAILQLGNICFS-SSERESQEVAAVSSWAEIHTAARLLQVPPERLEGAVTHRVTETPYGRVSRPLPVEGAI 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  393 LSRDALAKIVYSKLFDWLVTKINNSIG--QDSSSKYIIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKMEQE 470
Cdd:cd14896    315 DARDALAKTLYSRLFTWLLKRINAWLAppGEAESDATIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLLAQEEE 394

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  471 EYTKEEIDWSYIEFIDNQDVLDLIEKKPGGIIALLDEACMFPRSTHDTLAEKLYQTFGSHKRFTKPKLARTDFTICHYAG 550
Cdd:cd14896    395 ECQRELLPWVPIPQPPRESCLDLLVDQPHSLLSILDDQTWLSQATDHTFLQKCHYHHGDHPSYAKPQLPLPVFTVRHYAG 474

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  551 DVTYQTELFLDKNKDYVVGEHQSLMNSSDCSFVSSLFPKSREESSKSSKFSSIGSQFKQQLQSLLETLNTTEPHYIRCVK 630
Cdd:cd14896    475 TVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQYGLGQGKPTLASRFQQSLGDLTARLGRSHVYFIHCLN 554

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  631 PNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILAPEATERSFDEvDACKKLLARV-----DL 705
Cdd:cd14896    555 PNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALGSERQEALSDR-ERCGAILSQVlgaesPL 633

                          650
                   ....*....|...
gi 1063705616  706 kgFQIGKTKVFLR 718
Cdd:cd14896    634 --YHLGATKVLLK 644
MYSc_Myh7b cd14927
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ...
 76-718 3.66e-161

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: 507.57  E-value: 3.66e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   76 VLLNLKARYNANEIYTYTGNILIAVNPFKRLPhLYGNEIMEQYKGTDFGELSPHPFAVADSAYRKMINEGVSQAILVSGE 155
Cdd:cd14927      3 VLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITGE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  156 SGAGKTESTKMLMQYLAYM-----------GGKAESEGRSVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFNHM 224
Cdd:cd14927     82 SGAGKTVNTKRVIQYFAIVaalgdgpgkkaQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  225 GRISGAAIRTYLLERSRVCQVSDPERNYHCFYMLCAAPEQETERYQL--GKPSTFHYLNQSNChALDAIDDSKEYLATRK 302
Cdd:cd14927    162 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLvsMNPYDYHFCSQGVT-TVDNMDDGEELMATDH 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  303 AMDVVGISPEEQDAIFRVVAAILHLGNIEFAKSE-----ESDGAEPKDdksrfhlKVAAKLFMCDEKALENSLCNRVMVT 377
Cdd:cd14927    241 AMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQreeqaEADGTESAD-------KAAYLMGVSSADLLKGLLHPRVKVG 313

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  378 rGESITKPLDPGSAALSRDALAKIVYSKLFDWLVTKINNSIGQDSSSKYIIGVLDIYGFESFKTNSFEQFCINLTNEKLQ 457
Cdd:cd14927    314 -NEYVTKGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQ 392

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  458 QHFNQHVFKMEQEEYTKEEIDWSYIEF-IDNQDVLDLIEkKPGGIIALLDEACMFPRSTHDTLAEKLYQT-FGSHKRFTK 535
Cdd:cd14927    393 QFFNHHMFILEQEEYKREGIEWVFIDFgLDLQACIDLIE-KPLGILSILEEECMFPKASDASFKAKLYDNhLGKSPNFQK 471

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  536 PKLAR-----TDFTICHYAGDVTYQTELFLDKNKDYVVGEHQSLMNSSDCSFVSSLFPKSREESSKSSKFSSIG------ 604
Cdd:cd14927    472 PRPDKkrkyeAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENYVGSDSTEDPKSGVKekrkka 551

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  605 ------SQF-KQQLQSLLETLNTTEPHYIRCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTR 677
Cdd:cd14927    552 asfqtvSQLhKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQR 631

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*
gi 1063705616  678 FRILAPEAT-ERSF-DEVDACKKLLARVDL--KGFQIGKTKVFLR 718
Cdd:cd14927    632 YRILNPSAIpDDKFvDSRKATEKLLGSLDIdhTQYQFGHTKVFFK 676
MYSc_Myh15_mammals cd14929
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ...
 74-718 4.81e-161

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: 506.44  E-value: 4.81e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   74 PGVLLNLKARYNANEIYTYTGNILIAVNPFKRLPhLYGNEIMEQYKGTDFGELSPHPFAVADSAYRKMINEGVSQAILVS 153
Cdd:cd14929      1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLP-VYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  154 GESGAGKTESTKMLMQYLAYMGGKAESEGR--SVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFNHMGRISGAA 231
Cdd:cd14929     80 GESGAGKTVNTKHIIQYFATIAAMIESKKKlgALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSAD 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  232 IRTYLLERSRVCQVSDPERNYHCFYMLCAApEQETERYQL--GKPSTFHYLNQSNChALDAIDDSKEYLATRKAMDVVGI 309
Cdd:cd14929    160 IDIYLLEKSRVIFQQPGERNYHIFYQILSG-KKELRDLLLvsANPSDFHFCSCGAV-AVESLDDAEELLATEQAMDILGF 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  310 SPEEQDAIFRVVAAILHLGNIEFAKSE-----ESDGAEPKDDksrfhlkvAAKLFMCDEKALENSLCNRVMVTRGESITK 384
Cdd:cd14929    238 LPDEKYGCYKLTGAIMHFGNMKFKQKPreeqlEADGTENADK--------AAFLMGINSSELVKGLIHPRIKVGNEYVTR 309

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  385 PLDPGSAALSRDALAKIVYSKLFDWLVTKINNSIGQDSSSKYIIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHV 464
Cdd:cd14929    310 SQNIEQVTYAVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHM 389

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  465 FKMEQEEYTKEEIDWSYIEF-IDNQDVLDLIEkKPGGIIALLDEACMFPRSTHDTLAEKLYQT-FGSHKRFTKPKLAR-- 540
Cdd:cd14929    390 FVLEQEEYRKEGIDWVSIDFgLDLQACIDLIE-KPMGIFSILEEECMFPKATDLTFKTKLFDNhFGKSVHFQKPKPDKkk 468

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  541 --TDFTICHYAGDVTYQTELFLDKNKDYVVGEHQSLMNSSDCSFVSSLF----------PKSREESSKSSKFSSIGSQFK 608
Cdd:cd14929    469 feAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFenyistdsaiQFGEKKRKKGASFQTVASLHK 548

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  609 QQLQSLLETLNTTEPHYIRCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILAPEATER 688
Cdd:cd14929    549 ENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTFPK 628

                          650       660       670
                   ....*....|....*....|....*....|....
gi 1063705616  689 S--FDEVDACKKLLA--RVDLKGFQIGKTKVFLR 718
Cdd:cd14929    629 SkfVSSRKAAEELLGslEIDHTQYRFGITKVFFK 662
PTZ00014 PTZ00014
myosin-A; Provisional
 48-718 6.66e-161

myosin-A; Provisional


Pssm-ID: 240229 [Multi-domain]  Cd Length: 821  Bit Score: 511.88  E-value: 6.66e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   48 NAVHPKDPE-FPELGVddmtkLAYLHEPGVLLNLKARYNANEIYTYTGNILIAVNPFKRLpHLYGNEIMEQYKGT-DFGE 125
Cdd:PTZ00014    88 NANSQIDPMtYGDIGL-----LPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDL-GNTTNDWIRRYRDAkDSDK 161

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  126 LSPHPFAVADSAYRKMINEGVSQAILVSGESGAGKTESTKMLMQYLAYmgGKAESEGRSVEQQVLESNPVLEAFGNAKTV 205
Cdd:PTZ00014   162 LPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFAS--SKSGNMDLKIQNAIMAANPVLEAFGNAKTI 239

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  206 RNNNSSRFGKFVEIQFNHMGRISGAAIRTYLLERSRVCQVSDPERNYHCFYMLC-AAPEQETERYQLGKPSTFHYLNqSN 284
Cdd:PTZ00014   240 RNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLkGANDEMKEKYKLKSLEEYKYIN-PK 318

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  285 CHALDAIDDSKEYLATRKAMDVVGISPEEQDAIFRVVAAILHLGNIEFAKSEE---SDGAEpKDDKSRFHLKVAAKLFMC 361
Cdd:PTZ00014   319 CLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEgglTDAAA-ISDESLEVFNEACELLFL 397

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  362 DEKALENSLCNRVMVTRGESITKPLDPGSAALSRDALAKIVYSKLFDWLVTKINNSIGQDSSSKYIIGVLDIYGFESFKT 441
Cdd:PTZ00014   398 DYESLKKELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKVFIGMLDIFGFEVFKN 477

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  442 NSFEQFCINLTNEKLQQHFNQHVFKMEQEEYTKEEIDWSYIEFIDNQDVLDLIEKKPGGIIALLDEACMFPRSTHDTLAE 521
Cdd:PTZ00014   478 NSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGKSVLSILEDQCLAPGGTDEKFVS 557

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  522 KLYQTFGSHKRFTKPKLA-RTDFTICHYAGDVTYQTELFLDKNKDYVVGEHQSLMNSSDCSFVSSLFPKSREESSKSSKF 600
Cdd:PTZ00014   558 SCNTNLKNNPKYKPAKVDsNKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGVEVEKGKLAKG 637

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  601 SSIGSQFKQQLQSLLETLNTTEPHYIRCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRI 680
Cdd:PTZ00014   638 QLIGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKY 717

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|.
gi 1063705616  681 LAPEATERS-FDEVDACKKLLARVDL--KGFQIGKTKVFLR 718
Cdd:PTZ00014   718 LDLAVSNDSsLDPKEKAEKLLERSGLpkDSYAIGKTMVFLK 758
MYSc_Myo34 cd14895
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ...
 74-718 4.86e-160

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: 505.26  E-value: 4.86e-160
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   74 PGVLLNLKARYNANEIYTYTGNILIAVNPFKRLPHLYGneiMEQYKGTDFG--ELSPHPFAVADSAYRKM-------INE 144
Cdd:cd14895      1 PAFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIPGLYD---LHKYREEMPGwtALPPHVFSIAEGAYRSLrrrlhepGAS 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  145 GVSQAILVSGESGAGKTESTKMLMQYLA------YMGGKAESEGRSVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVE 218
Cdd:cd14895     78 KKNQTILVSGESGAGKTETTKFIMNYLAesskhtTATSSSKRRRAISGSELLSANPILESFGNARTLRNDNSSRFGKFVR 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  219 IQF-----NHMGRISGAAIRTYLLERSRVCQVSDPERNYHCFYMLCAAPEQETER---YQLGKPSTFHYLNQSNCHAL-D 289
Cdd:cd14895    158 MFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLelqLELLSAQEFQYISGGQCYQRnD 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  290 AIDDSKEYLATRKAMDVVGISPEEQDAIFRVVAAILHLGNIEFAKSEESDG---------------AEPKDDKSRFHLKV 354
Cdd:cd14895    238 GVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEGeedngaasapcrlasASPSSLTVQQHLDI 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  355 AAKLFMCDEKALENSLCNRVMVTRGESITKPLDPGSAALSRDALAKIVYSKLFDWLVTKINNSIGQ-----------DSS 423
Cdd:cd14895    318 VSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQrqfalnpnkaaNKD 397

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  424 SKYIIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKMEQEEYTKEEIDWSYIEFIDNQDVLDLIEKKPGGIIA 503
Cdd:cd14895    398 TTPCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDNSVCLEMLEQRPSGIFS 477

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  504 LLDEACMFPRSTHDTLAEKLYQTFGSHKRFTKPKLARTD--FTICHYAGDVTYQTELFLDKNKDYVVGEHQSLMNSSDCS 581
Cdd:cd14895    478 LLDEECVVPKGSDAGFARKLYQRLQEHSNFSASRTDQADvaFQIHHYAGAVRYQAEGFCEKNKDQPNAELFSVLGKTSDA 557

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  582 FVSSLFPKSREESSKSSKFSS--------------IGSQFKQQLQSLLETLNTTEPHYIRCVKPNNVLKPEIFENVNVLH 647
Cdd:cd14895    558 HLRELFEFFKASESAELSLGQpklrrrssvlssvgIGSQFKQQLASLLDVVQQTQTHYIRCIKPNDESASDQFDMAKVSS 637

                          650       660       670       680       690       700       710
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063705616  648 QLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILAPEATERSFDEVDACKKLlaRVDlkGFQIGKTKVFLR 718
Cdd:cd14895    638 QLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKNASDATASALIETL--KVD--HAELGKTRVFLR 704
MYSc_Myo41 cd14902
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ...
 74-718 1.17e-159

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: 504.81  E-value: 1.17e-159
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   74 PGVLLNLKARYNANEIYTYTGNILIAVNPFKRLPHLYGNEIMEQYKGTDFG--------ELSPHPFAVADSAYRKMI-NE 144
Cdd:cd14902      1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPDLYSESQLNAYKASMTStspvsqlsELPPHVFAIGGKAFGGLLkPE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  145 GVSQAILVSGESGAGKTESTKMLMQYLAYMG---GKAESEGRS---VEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVE 218
Cdd:cd14902     81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGrdqSSTEQEGSDaveIGKRILQTNPILESFGNAQTIRNDNSSRFGKFIK 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  219 IQFNHMGRISGAAIRTYLLERSRVCQVSDPERNYHCFYMLCAAPEQETERYqLGKPSTFHY--LNQSNC----HALDAID 292
Cdd:cd14902    161 IQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDL-LGLQKGGKYelLNSYGPsfarKRAVADK 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  293 DSKEYLATRKAMDVVGISPEEQDAIFRVVAAILHLGNIEFAKSEESDGAEPKDDKSRFHLKVAAKLFMCDEKALENSLCN 372
Cdd:cd14902    240 YAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAVTAASRFHLAKCAELMGVDVDKLETLLSS 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  373 RVMVTRGESITKPLDPGSAALSRDALAKIVYSKLFDWLVTKINNSIGQDSSSKYI---------IGVLDIYGFESFKTNS 443
Cdd:cd14902    320 REIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINYFDSAVSIsdedeelatIGILDIFGFESLNRNG 399

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  444 FEQFCINLTNEKLQQHFNQHVFKMEQEEYTKEEIDWSYIEFIDNQDVLDLIEKKPGGIIALLDEACMFPRSTHDTLAEKL 523
Cdd:cd14902    400 FEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYPSNAACLALFDDKSNGLFSLLDQECLMPKGSNQALSTKF 479

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  524 YQTFGShkrftkpklaRTDFTICHYAGDVTYQTELFLDKNKDYVVGEHQSLMNSSDCSFVSSLFPKSREESSKSSK---- 599
Cdd:cd14902    480 YRYHGG----------LGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGADENRDSPGADNgaag 549

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  600 --------FSSIGSQFKQQLQSLLETLNTTEPHYIRCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPF 671
Cdd:cd14902    550 rrrysmlrAPSVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRIARHGYSVRLAH 629

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  672 NEFLTRFRILAPEATER-------------SFDEVDACKKLLAR---------------------------VDLKGFQIG 711
Cdd:cd14902    630 ASFIELFSGFKCFLSTRdraakmnnhdlaqALVTVLMDRVLLEDgvereeknpgaltavtgdgsgtafendCRRKDVQVG 709


                   ....*..
gi 1063705616  712 KTKVFLR 718
Cdd:cd14902    710 RTLVFCK 716
MYSc_Myh1_insects_crustaceans cd14909
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ...
 74-718 1.82e-158

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: 499.75  E-value: 1.82e-158
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   74 PGVLLNLKARYNANEIYTYTGNILIAVNPFKRLPhLYGNEIMEQYKGTDFGELSPHPFAVADSAYRKMINEGVSQAILVS 153
Cdd:cd14909      1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYP-VYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLIT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  154 GESGAGKTESTKMLMQYLAYMGG--KAESEGR---SVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFNHMGRIS 228
Cdd:cd14909     80 GESGAGKTENTKKVIAYFATVGAskKTDEAAKskgSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLA 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  229 GAAIRTYLLERSRVCQVSDPERNYHCFYMLCAAPEQETERYQLGKPSTFHYLNQSNCH-ALDAIDDSKEYLATRKAMDVV 307
Cdd:cd14909    160 GADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLSDNIYDYYIVSQGKvTVPNVDDGEEFSLTDQAFDIL 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  308 GISPEEQDAIFRVVAAILHLGNIEFAKSEESDGAEP--KDDKSRfhlkvAAKLFMCDEKALENSLCNRVMVTRGESITKP 385
Cdd:cd14909    240 GFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQdgEEEGGR-----VSKLFGCDTAELYKNLLKPRIKVGNEFVTQG 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  386 LDPGSAALSRDALAKIVYSKLFDWLVTKINNSIGQDSSSKYIIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVF 465
Cdd:cd14909    315 RNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMF 394

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  466 KMEQEEYTKEEIDWSYIEF-IDNQDVLDLIEkKPGGIIALLDEACMFPRSTHDTLAEKLYQT-FGSHKRFTKPKLAR--- 540
Cdd:cd14909    395 VLEQEEYKREGIDWAFIDFgMDLLACIDLIE-KPMGILSILEEESMFPKATDQTFSEKLTNThLGKSAPFQKPKPPKpgq 473

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  541 --TDFTICHYAGDVTYQTELFLDKNKDYVVGEHQSLMNSSDCSFVSSLFPKSREESSKSSKF-----------SSIGSQF 607
Cdd:cd14909    474 qaAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGEQAkggrgkkgggfATVSSAY 553

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  608 KQQLQSLLETLNTTEPHYIRCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILAPEATE 687
Cdd:cd14909    554 KEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGIQ 633

                          650       660       670
                   ....*....|....*....|....*....|...
gi 1063705616  688 RSFDEVDACKKLLARVDL--KGFQIGKTKVFLR 718
Cdd:cd14909    634 GEEDPKKAAEIILESIALdpDQYRLGHTKVFFR 666
MYSc_Myo19 cd14880
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ...
 76-717 4.21e-158

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: 498.61  E-value: 4.21e-158
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   76 VLLNLKARYNANEIYTYTGNILIAVNPFKRLPHLYGNEIMEQYKGTDFGE-LSPHPFAVADSAYR--KMINEGVSQAILV 152
Cdd:cd14880      3 VLRCLQARYTADTFYTNAGCTLVALNPFKPVPQLYSPELMREYHAAPQPQkLKPHIFTVGEQTYRnvKSLIEPVNQSIVV 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  153 SGESGAGKTESTKMLMQYLAYMGG-----KAESEGRSVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFNHMGRI 227
Cdd:cd14880     83 SGESGAGKTWTSRCLMKFYAVVAAsptswESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQQM 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  228 SGAAIRTYLLERSRV-CQVSDpERNYHCFYMLC-AAPEQETERYQLGKPSTFHYLNQSNcHALDaiDDSKEylATRKAMD 305
Cdd:cd14880    163 TGAAVQTYLLEKTRVaCQAPS-ERNFHIFYQICkGASADERLQWHLPEGAAFSWLPNPE-RNLE--EDCFE--VTREAML 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  306 VVGISPEEQDAIFRVVAAILHLGNIEFAKSE-ESDGAEPKDDKSRFhLKVAAKLFMCDEKALENSLCNRVmVTRGES--- 381
Cdd:cd14880    237 HLGIDTPTQNNIFKVLAGLLHLGNIQFADSEdEAQPCQPMDDTKES-VRTSALLLKLPEDHLLETLQIRT-IRAGKQqqv 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  382 ITKPLDPGSAALSRDALAKIVYSKLFDWLVTKINNSIGQDSSS-KYIIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHF 460
Cdd:cd14880    315 FKKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSwTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQHF 394

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  461 NQHVFKMEQEEYTKEEIDWSYIEFIDNQDVLDLIEKKPGGIIALLDEACMFPR-STHDTLAEKLYQTFGSHKRFTKPKLA 539
Cdd:cd14880    395 VAHYLRAQQEEYAVEGLEWSFINYQDNQTCLDLIEGSPISICSLINEECRLNRpSSAAQLQTRIESALAGNPCLGHNKLS 474

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  540 RT-DFTICHYAGDVTYQTELFLDKNKDYVVGEHQSLMNSSDCSFVSSLFPKSREESSKSSKFSS-------IGSQFKQQL 611
Cdd:cd14880    475 REpSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEKTQEEPSGQsrapvltVVSKFKASL 554

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  612 QSLLETLNTTEPHYIRCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILAPEATERSFD 691
Cdd:cd14880    555 EQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYKLLRRLRPHTSSG 634

                          650       660
                   ....*....|....*....|....*.
gi 1063705616  692 EVDACKkllARVDLKGFQIGKTKVFL 717
Cdd:cd14880    635 PHSPYP---AKGLSEPVHCGRTKVFM 657
MYSc_Myo45 cd14906
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ...
 76-681 1.11e-157

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: 499.51  E-value: 1.11e-157
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   76 VLLNLKARYNANEIYTYTGNILIAVNPFKRLPHLYGNEIMEQYKGTDF-GELSPHPFAVADSAYRKMINEGVSQAILVSG 154
Cdd:cd14906      3 ILNNLGKRYKSDSIYTYIGNVLISINPYKDISSIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIIISG 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  155 ESGAGKTESTKMLMQYLAYMGGKAESEGR-------SVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFNHM-GR 226
Cdd:cd14906     83 ESGSGKTEASKTILQYLINTSSSNQQQNNnnnnnnnSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSdGK 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  227 ISGAAIRTYLLERSRVCQVSDPER-NYHCFY-MLCAAPEQETERYQL-GKPSTFHYLNQS--------------NCHALD 289
Cdd:cd14906    163 IDGASIETYLLEKSRISHRPDNINlSYHIFYyLVYGASKDERSKWGLnNDPSKYRYLDARddvissfksqssnkNSNHNN 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  290 AIDDSKEYLATRKAMDVVGISPEEQDAIFRVVAAILHLGNIEFAKSEESDGAEPKDDKSRFHLKVAAKLFMCDEKALENS 369
Cdd:cd14906    243 KTESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAYQKDKVTASLESVSKLLGYIESVFKQA 322

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  370 LCNRVMVT--RGESITKPLDPGSAALSRDALAKIVYSKLFDWLVTKINNSIGQDSSSK-----------YIIGVLDIYGF 436
Cdd:cd14906    323 LLNRNLKAggRGSVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQNTQSNdlaggsnkknnLFIGVLDIFGF 402

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  437 ESFKTNSFEQFCINLTNEKLQQHFNQHVFKMEQEEYTKEEIDWSYIEFIDNQDVLDLIEKKPGGIIALLDEACMFPRSTH 516
Cdd:cd14906    403 ENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNFIDNKECIELIEKKSDGILSLLDDECIMPKGSE 482

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  517 DTLAEKLYQTFGSHKRFTKPKLARTDFTICHYAGDVTYQTELFLDKNKDYVVGEHQSLMNSSDCSFVSSLFPKSREESSK 596
Cdd:cd14906    483 QSLLEKYNKQYHNTNQYYQRTLAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLFQQQITSTTN 562

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  597 SSKFS----SIGSQFKQQLQSLLETLNTTEPHYIRCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFN 672
Cdd:cd14906    563 TTKKQtqsnTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLNTIKVRKMGYSYRRDFN 642


                   ....*....
gi 1063705616  673 EFLTRFRIL 681
Cdd:cd14906    643 QFFSRYKCI 651
MYSc_Myh16 cd14934
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ...
 76-718 6.90e-156

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: 492.62  E-value: 6.90e-156
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   76 VLLNLKARYNANEIYTYTGNILIAVNPFKRLPhLYGNEIMEQYKGTDFGELSPHPFAVADSAYRKMINEGVSQAILVSGE 155
Cdd:cd14934      3 VLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLP-IYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITGE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  156 SGAGKTESTKMLMQYLAYMG--GKAESEGR-SVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFNHMGRISGAAI 232
Cdd:cd14934     82 SGAGKTENTKKVIQYFANIGgtGKQSSDGKgSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGADI 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  233 RTYLLERSRVCQVSDPERNYHCFYMLCA--APEQETERYQLGKPSTFHYLNQSnCHALDAIDDSKEYLATRKAMDVVGIS 310
Cdd:cd14934    162 ESYLLEKSRVISQQAAERGYHIFYQILSnkKPELIESLLLVPNPKEYHWVSQG-VTVVDNMDDGEELQITDVAFDVLGFS 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  311 PEEQDAIFRVVAAILHLGNIEFAKSEESDGAEPkdDKSRFHLKVAaKLFMCDEKALENSLCNRVMVTRGESITKPLDPGS 390
Cdd:cd14934    241 AEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEV--DTTEVADKVA-HLMGLNSGELQKGITRPRVKVGNEFVQKGQNMEQ 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  391 AALSRDALAKIVYSKLFDWLVTKINNSIGQDSSSKYIIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKMEQE 470
Cdd:cd14934    318 CNNSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQE 397

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  471 EYTKEEIDWSYIEF-IDNQDVLDLIEkKPGGIIALLDEACMFPRSTHDTLAEKLYQT-FGSHKRFTKPKLAR-----TDF 543
Cdd:cd14934    398 EYKREGIEWVFIDFgLDLQACIDLLE-KPMGIFSILEEQCVFPKATDATFKAALYDNhLGKSSNFLKPKGGKgkgpeAHF 476

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  544 TICHYAGDVTYQTELFLDKNKD----YVVGEHQ-SLMNSSDCSFVSSLFPKSREESSKSSKFSSIGSQFKQQLQSLLETL 618
Cdd:cd14934    477 ELVHYAGTVGYNITGWLEKNKDplneTVVGLFQkSSLGLLALLFKEEEAPAGSKKQKRGSSFMTVSNFYREQLNKLMTTL 556

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  619 NTTEPHYIRCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILAPEATERSF-DEVDACK 697
Cdd:cd14934    557 HSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVIPQGFvDNKKASE 636

                          650       660
                   ....*....|....*....|...
gi 1063705616  698 KLLARVDL--KGFQIGKTKVFLR 718
Cdd:cd14934    637 LLLGSIDLdvNEYKIGHTKVFFR 659
MYSc_Myh18 cd14932
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ...
 76-718 9.13e-155

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: 490.31  E-value: 9.13e-155
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   76 VLLNLKARYNANEIYTYTGNILIAVNPFKRLPhLYGNEIMEQYKGTDFGELSPHPFAVADSAYRKMINEGVSQAILVSGE 155
Cdd:cd14932      3 VLHNLKERYYSGLIYTYSGLFCVVINPYKYLP-IYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  156 SGAGKTESTKMLMQYLAYM----------GGKAESEGRsVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFNHMG 225
Cdd:cd14932     82 SGAGKTENTKKVIQYLAYVassfktkkdqSSIALSHGE-LEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  226 RISGAAIRTYLLERSRVCQVSDPERNYHCF-YMLCAAPEQETERYQLGKPSTFHYLNQSNChALDAIDDSKEYLATRKAM 304
Cdd:cd14932    161 YIVGANIETYLLEKSRAIRQAKDERAFHIFyYLLTGAGDKLRSELCLEDYSKYRFLSNGNV-TIPGQQDKELFAETMEAF 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  305 DVVGISPEEQDAIFRVVAAILHLGNIEFAKSEESDGAEPKDDKSRfhLKVAAKLFMCDEKALENSLCNRVMVTRgESITK 384
Cdd:cd14932    240 RIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAA--QKVCHLLGMNVTDFTRAILSPRIKVGR-DYVQK 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  385 PLDPGSAALSRDALAKIVYSKLFDWLVTKINNSIGQDS-SSKYIIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQH 463
Cdd:cd14932    317 AQTQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKrQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHT 396

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  464 VFKMEQEEYTKEEIDWSYIEF-IDNQDVLDLIEKK--PGGIIALLDEACMFPRSTHDTLAEKLYQTFGSHKRFTKPKLAR 540
Cdd:cd14932    397 MFILEQEEYQREGIEWSFIDFgLDLQPCIELIEKPngPPGILALLDEECWFPKATDKSFVEKVVQEQGNNPKFQKPKKLK 476

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  541 --TDFTICHYAGDVTYQTELFLDKNKDYVVGEHQSLMNSSDCSFVSSLF-----------------PKSREESSKSSKFS 601
Cdd:cd14932    477 ddADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWkdvdrivgldkvagmgeSLHGAFKTRKGMFR 556

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  602 SIGSQFKQQLQSLLETLNTTEPHYIRCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRIL 681
Cdd:cd14932    557 TVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 636

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|
gi 1063705616  682 APEATERSF-DEVDACKKLLARVDLKG--FQIGKTKVFLR 718
Cdd:cd14932    637 TPNAIPKGFmDGKQACVLMVKALELDPnlYRIGQSKVFFR 676
MYSc_Myh7 cd14917
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ...
 74-718 8.61e-152

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: 481.91  E-value: 8.61e-152
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   74 PGVLLNLKARYNANEIYTYTGNILIAVNPFKRLPhLYGNEIMEQYKGTDFGELSPHPFAVADSAYRKMINEGVSQAILVS 153
Cdd:cd14917      1 PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  154 GESGAGKTESTKMLMQYLAYMGG------KAESEGR-SVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFNHMGR 226
Cdd:cd14917     80 GESGAGKTVNTKRVIQYFAVIAAigdrskKDQTPGKgTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  227 ISGAAIRTYLLERSRVCQVSDPERNYHCFYMLCAAPEQETERYQL--GKPSTFHYLNQSNChALDAIDDSKEYLATRKAM 304
Cdd:cd14917    160 LASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLitNNPYDYAFISQGET-TVASIDDAEELMATDNAF 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  305 DVVGISPEEQDAIFRVVAAILHLGNIEFAKSEESDGAEP----KDDKSrfhlkvaAKLFMCDEKALENSLCNRVMVTRGE 380
Cdd:cd14917    239 DVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPdgteEADKS-------AYLMGLNSADLLKGLCHPRVKVGNE 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  381 SITKPLDPGSAALSRDALAKIVYSKLFDWLVTKINNSIGQDSSSKYIIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHF 460
Cdd:cd14917    312 YVTKGQNVQQVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFF 391

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  461 NQHVFKMEQEEYTKEEIDWSYIEF-IDNQDVLDLIEkKPGGIIALLDEACMFPRSTHDTLAEKLYQT-FGSHKRFTKPKL 538
Cdd:cd14917    392 NHHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKATDMTFKAKLFDNhLGKSNNFQKPRN 470

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  539 AR----TDFTICHYAGDVTYQTELFLDKNKDYVVGEHQSLMNSSDCSFVSSLFPKSREESSKSSK---FSSIGSQF---- 607
Cdd:cd14917    471 IKgkpeAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANYAGADAPIEKgkgKAKKGSSFqtvs 550

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  608 ---KQQLQSLLETLNTTEPHYIRCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILAPE 684
Cdd:cd14917    551 alhRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPA 630

                          650       660       670
                   ....*....|....*....|....*....|....*...
gi 1063705616  685 AT-ERSF-DEVDACKKLLARVDL--KGFQIGKTKVFLR 718
Cdd:cd14917    631 AIpEGQFiDSRKGAEKLLSSLDIdhNQYKFGHTKVFFK 668
MYSc_Myh6 cd14916
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ...
 74-718 1.11e-149

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: 476.09  E-value: 1.11e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   74 PGVLLNLKARYNANEIYTYTGNILIAVNPFKRLPhLYGNEIMEQYKGTDFGELSPHPFAVADSAYRKMINEGVSQAILVS 153
Cdd:cd14916      1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  154 GESGAGKTESTKMLMQYLAYMGG--------KAESEGRSVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFNHMG 225
Cdd:cd14916     80 GESGAGKTVNTKRVIQYFASIAAigdrskkeNPNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  226 RISGAAIRTYLLERSRVCQVSDPERNYHCFYMLCAAPEQETERYQL--GKPSTFHYLNQSNChALDAIDDSKEYLATRKA 303
Cdd:cd14916    160 KLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLvtNNPYDYAFVSQGEV-SVASIDDSEELLATDSA 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  304 MDVVGISPEEQDAIFRVVAAILHLGNIEFAKSEESDGAEPKD----DKSrfhlkvaAKLFMCDEKALENSLCNRVMVTRG 379
Cdd:cd14916    239 FDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGtedaDKS-------AYLMGLNSADLLKGLCHPRVKVGN 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  380 ESITKPLDPGSAALSRDALAKIVYSKLFDWLVTKINNSIGQDSSSKYIIGVLDIYGFESFKTNSFEQFCINLTNEKLQQH 459
Cdd:cd14916    312 EYVTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQF 391

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  460 FNQHVFKMEQEEYTKEEIDWSYIEF-IDNQDVLDLIEkKPGGIIALLDEACMFPRSTHDTLAEKLYQT-FGSHKRFTKPK 537
Cdd:cd14916    392 FNHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKASDMTFKAKLYDNhLGKSNNFQKPR 470

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  538 LAR----TDFTICHYAGDVTYQTELFLDKNKDYVVGEHQSLMNSSDCSFVSSLFPKSREESS----KSSKFSSIGSQF-- 607
Cdd:cd14916    471 NVKgkqeAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTgdsgKGKGGKKKGSSFqt 550

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  608 -----KQQLQSLLETLNTTEPHYIRCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILA 682
Cdd:cd14916    551 vsalhRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILN 630

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|
gi 1063705616  683 PEATERS--FDEVDACKKLLARVDL--KGFQIGKTKVFLR 718
Cdd:cd14916    631 PAAIPEGqfIDSRKGAEKLLGSLDIdhNQYKFGHTKVFFK 670
MYSc_Myh8 cd14918
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ...
 74-718 1.47e-149

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: 475.76  E-value: 1.47e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   74 PGVLLNLKARYNANEIYTYTGNILIAVNPFKRLPhLYGNEIMEQYKGTDFGELSPHPFAVADSAYRKMINEGVSQAILVS 153
Cdd:cd14918      1 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  154 GESGAGKTESTKMLMQYLAYMG----GKAESEGR---SVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFNHMGR 226
Cdd:cd14918     80 GESGAGKTVNTKRVIQYFATIAvtgeKKKEESGKmqgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  227 ISGAAIRTYLLERSRVCQVSDPERNYHCFYMLCAAPEQETERYQL--GKPSTFHYLNQSNChALDAIDDSKEYLATRKAM 304
Cdd:cd14918    160 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLitTNPYDYAFVSQGEI-TVPSIDDQEELMATDSAI 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  305 DVVGISPEEQDAIFRVVAAILHLGNIEFAKSEESDGAEPkdDKSRFHLKvAAKLFMCDEKALENSLCNRVMVTRGESITK 384
Cdd:cd14918    239 DILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEP--DGTEVADK-AAYLQSLNSADLLKALCYPRVKVGNEYVTK 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  385 PLDPGSAALSRDALAKIVYSKLFDWLVTKINNSIGQDSSSKYIIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHV 464
Cdd:cd14918    316 GQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHM 395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  465 FKMEQEEYTKEEIDWSYIEF-IDNQDVLDLIEkKPGGIIALLDEACMFPRSTHDTLAEKLY-QTFGSHKRFTKPKL---- 538
Cdd:cd14918    396 FVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPLGIFSILEEECMFPKATDTSFKNKLYdQHLGKSANFQKPKVvkgk 474

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  539 ARTDFTICHYAGDVTYQTELFLDKNKDYVVGEHQSLMNSSDCSFVSSLFPKSREESSKSSKF----------SSIGSQFK 608
Cdd:cd14918    475 AEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSGAKkgakkkgssfQTVSALFR 554

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  609 QQLQSLLETLNTTEPHYIRCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILAPEATER 688
Cdd:cd14918    555 ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPE 634

                          650       660       670
                   ....*....|....*....|....*....|....
gi 1063705616  689 S--FDEVDACKKLLARVDL--KGFQIGKTKVFLR 718
Cdd:cd14918    635 GqfIDSKKASEKLLASIDIdhTQYKFGHTKVFFK 668
MYSc_Myh4 cd14915
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ...
 74-718 1.61e-147

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: 470.37  E-value: 1.61e-147
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   74 PGVLLNLKARYNANEIYTYTGNILIAVNPFKRLPhLYGNEIMEQYKGTDFGELSPHPFAVADSAYRKMINEGVSQAILVS 153
Cdd:cd14915      1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  154 GESGAGKTESTKMLMQYLAYM---GGKAESEGRS------VEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFNHM 224
Cdd:cd14915     80 GESGAGKTVNTKRVIQYFATIavtGEKKKEEAASgkmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  225 GRISGAAIRTYLLERSRVCQVSDPERNYHCFYMLCAAPEQETERYQL--GKPSTFHYLNQSNChALDAIDDSKEYLATRK 302
Cdd:cd14915    160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLitTNPYDFAFVSQGEI-TVPSIDDQEELMATDS 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  303 AMDVVGISPEEQDAIFRVVAAILHLGNIEFAKSEESDGAEPkdDKSRFHLKvAAKLFMCDEKALENSLCNRVMVTRGESI 382
Cdd:cd14915    239 AVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEP--DGTEVADK-AAYLTSLNSADLLKALCYPRVKVGNEYV 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  383 TKPLDPGSAALSRDALAKIVYSKLFDWLVTKINNSIGQDSSSKYIIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQ 462
Cdd:cd14915    316 TKGQTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNH 395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  463 HVFKMEQEEYTKEEIDWSYIEF-IDNQDVLDLIEkKPGGIIALLDEACMFPRSTHDTLAEKLY-QTFGSHKRFTKPKLAR 540
Cdd:cd14915    396 HMFVLEQEEYKKEGIEWEFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYeQHLGKSNNFQKPKPAK 474

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  541 ----TDFTICHYAGDVTYQTELFLDKNKDYVVGEHQSLMNSSDCSFVSSLFPKSREE-----------SSKSSKFSSIGS 605
Cdd:cd14915    475 gkaeAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQTAeaeggggkkggKKKGSSFQTVSA 554

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  606 QFKQQLQSLLETLNTTEPHYIRCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILAPEA 685
Cdd:cd14915    555 LFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASA 634

                          650       660       670
                   ....*....|....*....|....*....|....*..
gi 1063705616  686 TERS--FDEVDACKKLLARVDL--KGFQIGKTKVFLR 718
Cdd:cd14915    635 IPEGqfIDSKKASEKLLGSIDIdhTQYKFGHTKVFFK 671
MYSc_Myh9 cd14919
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ...
 76-718 2.58e-147

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: 469.57  E-value: 2.58e-147
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   76 VLLNLKARYNANEIYTYTGNILIAVNPFKRLPhLYGNEIMEQYKGTDFGELSPHPFAVADSAYRKMINEGVSQAILVSGE 155
Cdd:cd14919      3 VLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  156 SGAGKTESTKMLMQYLAYMGG--KAESEGRSVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFNHMGRISGAAIR 233
Cdd:cd14919     82 SGAGKTENTKKVIQYLAHVASshKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIE 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  234 TYLLERSRVCQVSDPERNYHCFYMLCAAPEQETERYQLGKP-STFHYLnqSNCH-ALDAIDDSKEYLATRKAMDVVGISP 311
Cdd:cd14919    162 TYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPyNKYRFL--SNGHvTIPGQQDKDMFQETMEAMRIMGIPE 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  312 EEQDAIFRVVAAILHLGNIEFAKSEESDGAEPKDDKSRfhLKVAAKLFMCDEKALENSLCNRVMVTRgESITKPLDPGSA 391
Cdd:cd14919    240 EEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAA--QKVSHLLGINVTDFTRGILTPRIKVGR-DYVQKAQTKEQA 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  392 ALSRDALAKIVYSKLFDWLVTKINNSIGQDS-SSKYIIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKMEQE 470
Cdd:cd14919    317 DFAIEALAKATYERMFRWLVLRINKALDKTKrQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQE 396

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  471 EYTKEEIDWSYIEF-IDNQDVLDLIEKK--PGGIIALLDEACMFPRSTHDTLAEKLYQTFGSHKRFTKPKLA--RTDFTI 545
Cdd:cd14919    397 EYQREGIEWNFIDFgLDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLkdKADFCI 476

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  546 CHYAGDVTYQTELFLDKNKDYVVGEHQSLMNSSDCSFVSSLFPKSR------------------EESSKSSKFSSIGSQF 607
Cdd:cd14919    477 IHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDriigldqvagmsetalpgAFKTRKGMFRTVGQLY 556

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  608 KQQLQSLLETLNTTEPHYIRCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILAPEATE 687
Cdd:cd14919    557 KEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIP 636

                          650       660       670
                   ....*....|....*....|....*....|....
gi 1063705616  688 RSF-DEVDACKKLLARVDLKG--FQIGKTKVFLR 718
Cdd:cd14919    637 KGFmDGKQACVLMIKALELDSnlYRIGQSKVFFR 670
MYSc_Myh13 cd14923
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ...
 74-718 3.18e-147

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: 469.55  E-value: 3.18e-147
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   74 PGVLLNLKARYNANEIYTYTGNILIAVNPFKRLPhLYGNEIMEQYKGTDFGELSPHPFAVADSAYRKMINEGVSQAILVS 153
Cdd:cd14923      1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILIT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  154 GESGAGKTESTKMLMQYLAYMG--GKAESEGR------SVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFNHMG 225
Cdd:cd14923     80 GESGAGKTVNTKRVIQYFATIAvtGDKKKEQQpgkmqgTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  226 RISGAAIRTYLLERSRVCQVSDPERNYHCFYMLCAAPEQETERYQL--GKPSTFHYLNQSNChALDAIDDSKEYLATRKA 303
Cdd:cd14923    160 KLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLisTNPFDFPFVSQGEV-TVASIDDSEELLATDNA 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  304 MDVVGISPEEQDAIFRVVAAILHLGNIEFAKSEESDGAEPkdDKSRFHLKVAAKLFMCDEKALENSLCNRVMVTrGESIT 383
Cdd:cd14923    239 IDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEP--DGTEVADKAGYLMGLNSAEMLKGLCCPRVKVG-NEYVT 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  384 KPLDPGSAALSRDALAKIVYSKLFDWLVTKINNSIGQDSSSKYIIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQH 463
Cdd:cd14923    316 KGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHH 395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  464 VFKMEQEEYTKEEIDWSYIEF-IDNQDVLDLIEkKPGGIIALLDEACMFPRSTHDTLAEKLY-QTFGSHKRFTKPKLAR- 540
Cdd:cd14923    396 MFVLEQEEYKKEGIEWEFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKPAKg 474

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  541 ---TDFTICHYAGDVTYQTELFLDKNKDYVVGEHQSLMNSSDCSFVSSLFPKSREESSKSSKFSSIGSQ----------- 606
Cdd:cd14923    475 kaeAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAGDSGGSKKGGKkkgssfqtvsa 554

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  607 -FKQQLQSLLETLNTTEPHYIRCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILAPEA 685
Cdd:cd14923    555 vFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASA 634

                          650       660       670
                   ....*....|....*....|....*....|....*..
gi 1063705616  686 TERS--FDEVDACKKLLARVDL--KGFQIGKTKVFLR 718
Cdd:cd14923    635 IPEGqfIDSKNASEKLLNSIDVdrEQYRFGHTKVFFK 671
MYSc_Myh11 cd14921
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ...
 76-718 1.09e-146

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: 467.96  E-value: 1.09e-146
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   76 VLLNLKARYNANEIYTYTGNILIAVNPFKRLPhLYGNEIMEQYKGTDFGELSPHPFAVADSAYRKMINEGVSQAILVSGE 155
Cdd:cd14921      3 VLHNLRERYFSGLIYTYSGLFCVVVNPYKHLP-IYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  156 SGAGKTESTKMLMQYLA-----YMGGKAESEGRSVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFNHMGRISGA 230
Cdd:cd14921     82 SGAGKTENTKKVIQYLAvvassHKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  231 AIRTYLLERSRVCQVSDPERNYHCF-YMLCAAPEQETERYQLGKPSTFHYLnqSNCHA-LDAIDDSKEYLATRKAMDVVG 308
Cdd:cd14921    162 NIETYLLEKSRAIRQARDERTFHIFyYLIAGAKEKMRSDLLLEGFNNYTFL--SNGFVpIPAAQDDEMFQETLEAMSIMG 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  309 ISPEEQDAIFRVVAAILHLGNIEFAKSEESDGAEPKDDKSRfhLKVAAKLFMCDEKALENSLCNRVMVTRgESITKPLDP 388
Cdd:cd14921    240 FSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAA--QKVCHLMGINVTDFTRSILTPRIKVGR-DVVQKAQTK 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  389 GSAALSRDALAKIVYSKLFDWLVTKINNSIGQDS-SSKYIIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKM 467
Cdd:cd14921    317 EQADFAIEALAKATYERLFRWILTRVNKALDKTHrQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFIL 396

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  468 EQEEYTKEEIDWSYIEF-IDNQDVLDLIEK--KPGGIIALLDEACMFPRSTHDTLAEKLYQTFGSHKRFTKPKLA--RTD 542
Cdd:cd14921    397 EQEEYQREGIEWNFIDFgLDLQPCIELIERpnNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKPKQLkdKTE 476

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  543 FTICHYAGDVTYQTELFLDKNKDYVVGEHQSLMNSSDCSFVSSLFPKS------------------REESSKSSKFSSIG 604
Cdd:cd14921    477 FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVdrivgldqmakmtesslpSASKTKKGMFRTVG 556

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  605 SQFKQQLQSLLETLNTTEPHYIRCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILAPE 684
Cdd:cd14921    557 QLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAAN 636

                          650       660       670
                   ....*....|....*....|....*....|....*..
gi 1063705616  685 ATERSF-DEVDACKKLLARVDLKG--FQIGKTKVFLR 718
Cdd:cd14921    637 AIPKGFmDGKQACILMIKALELDPnlYRIGQSKIFFR 673
MYSc_Myh1_mammals cd14910
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ...
 74-718 2.70e-145

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: 464.20  E-value: 2.70e-145
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   74 PGVLLNLKARYNANEIYTYTGNILIAVNPFKRLPhLYGNEIMEQYKGTDFGELSPHPFAVADSAYRKMINEGVSQAILVS 153
Cdd:cd14910      1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  154 GESGAGKTESTKMLMQYLAYM---GGKAESEGRS------VEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFNHM 224
Cdd:cd14910     80 GESGAGKTVNTKRVIQYFATIavtGEKKKEEATSgkmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  225 GRISGAAIRTYLLERSRVCQVSDPERNYHCFYMLCAAPEQETERYQL--GKPSTFHYLNQSNChALDAIDDSKEYLATRK 302
Cdd:cd14910    160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLitTNPYDYAFVSQGEI-TVPSIDDQEELMATDS 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  303 AMDVVGISPEEQDAIFRVVAAILHLGNIEFAKSEESDGAEPkdDKSRFHLKvAAKLFMCDEKALENSLCNRVMVTRGESI 382
Cdd:cd14910    239 AIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEP--DGTEVADK-AAYLQNLNSADLLKALCYPRVKVGNEYV 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  383 TKPLDPGSAALSRDALAKIVYSKLFDWLVTKINNSIGQDSSSKYIIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQ 462
Cdd:cd14910    316 TKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNH 395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  463 HVFKMEQEEYTKEEIDWSYIEF-IDNQDVLDLIEkKPGGIIALLDEACMFPRSTHDTLAEKLY-QTFGSHKRFTKPKLAR 540
Cdd:cd14910    396 HMFVLEQEEYKKEGIEWEFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYeQHLGKSNNFQKPKPAK 474

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  541 ----TDFTICHYAGDVTYQTELFLDKNKDYVVGEHQSLMNSSDCSFVSSLFPKSREESSKS-----------SKFSSIGS 605
Cdd:cd14910    475 gkveAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAAAEAEEgggkkggkkkgSSFQTVSA 554

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  606 QFKQQLQSLLETLNTTEPHYIRCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILAPEA 685
Cdd:cd14910    555 LFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASA 634

                          650       660       670
                   ....*....|....*....|....*....|....*..
gi 1063705616  686 TERS--FDEVDACKKLLARVDL--KGFQIGKTKVFLR 718
Cdd:cd14910    635 IPEGqfIDSKKASEKLLGSIDIdhTQYKFGHTKVFFK 671
MYSc_Myh2_mammals cd14912
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ...
 74-718 1.65e-144

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: 462.28  E-value: 1.65e-144
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   74 PGVLLNLKARYNANEIYTYTGNILIAVNPFKRLPhLYGNEIMEQYKGTDFGELSPHPFAVADSAYRKMINEGVSQAILVS 153
Cdd:cd14912      1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  154 GESGAGKTESTKMLMQYLAYMGGKAESEGRSV---------EQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFNHM 224
Cdd:cd14912     80 GESGAGKTVNTKRVIQYFATIAVTGEKKKEEItsgkmqgtlEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  225 GRISGAAIRTYLLERSRVCQVSDPERNYHCFYMLCAAPEQETERYQL--GKPSTFHYLNQSNChALDAIDDSKEYLATRK 302
Cdd:cd14912    160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLitTNPYDYPFVSQGEI-SVASIDDQEELMATDS 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  303 AMDVVGISPEEQDAIFRVVAAILHLGNIEFAKSEESDGAEPkdDKSRFHLKvAAKLFMCDEKALENSLCNRVMVTRGESI 382
Cdd:cd14912    239 AIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEP--DGTEVADK-AAYLQSLNSADLLKALCYPRVKVGNEYV 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  383 TKPLDPGSAALSRDALAKIVYSKLFDWLVTKINNSIGQDSSSKYIIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQ 462
Cdd:cd14912    316 TKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNH 395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  463 HVFKMEQEEYTKEEIDWSYIEF-IDNQDVLDLIEkKPGGIIALLDEACMFPRSTHDTLAEKLY-QTFGSHKRFTKPKL-- 538
Cdd:cd14912    396 HMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYeQHLGKSANFQKPKVvk 474

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  539 --ARTDFTICHYAGDVTYQTELFLDKNKDYVVGEHQSLMNSSDCSFVSSLFPKSREE-------------SSKSSKFSSI 603
Cdd:cd14912    475 gkAEAHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAegasagggakkggKKKGSSFQTV 554

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  604 GSQFKQQLQSLLETLNTTEPHYIRCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILAP 683
Cdd:cd14912    555 SALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNA 634

                          650       660       670
                   ....*....|....*....|....*....|....*....
gi 1063705616  684 EATERS--FDEVDACKKLLARVDL--KGFQIGKTKVFLR 718
Cdd:cd14912    635 SAIPEGqfIDSKKASEKLLASIDIdhTQYKFGHTKVFFK 673
MYSc_Myh19 cd15896
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ...
 76-718 2.53e-144

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: 461.84  E-value: 2.53e-144
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   76 VLLNLKARYNANEIYTYTGNILIAVNPFKRLPhLYGNEIMEQYKGTDFGELSPHPFAVADSAYRKMINEGVSQAILVSGE 155
Cdd:cd15896      3 VLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  156 SGAGKTESTKMLMQYLAYMGGKAESEGRS---------VEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFNHMGR 226
Cdd:cd15896     82 SGAGKTENTKKVIQYLAHVASSHKTKKDQnslalshgeLEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  227 ISGAAIRTYLLERSRVCQVSDPERNYHCF-YMLCAAPEQETERYQLGKPSTFHYLNQSNChALDAIDDSKEYLATRKAMD 305
Cdd:cd15896    162 IVGANIETYLLEKSRAIRQAKEERTFHIFyYLLTGAGDKLRSELLLENYNNYRFLSNGNV-TIPGQQDKDLFTETMEAFR 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  306 VVGISPEEQDAIFRVVAAILHLGNIEFAKSEESDGAEPKDDKSRfhLKVAAKLFMCDEKALENSLCNRVMVTRgESITKP 385
Cdd:cd15896    241 IMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAA--QKVCHLMGMNVTDFTRAILSPRIKVGR-DYVQKA 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  386 LDPGSAALSRDALAKIVYSKLFDWLVTKINNSIGQDS-SSKYIIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHV 464
Cdd:cd15896    318 QTQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKrQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 397

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  465 FKMEQEEYTKEEIDWSYIEF-IDNQDVLDLIEK--KPGGIIALLDEACMFPRSTHDTLAEKLYQTFGSHKRFTKPKLAR- 540
Cdd:cd15896    398 FILEQEEYQREGIEWSFIDFgLDLQPCIDLIEKpaSPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKKLKd 477

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  541 -TDFTICHYAGDVTYQTELFLDKNKDYVVGEHQSLMNSSDCSFVSSLFPKSREE----------------SSKSSKFSSI 603
Cdd:cd15896    478 eADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIvgldkvsgmsempgafKTRKGMFRTV 557

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  604 GSQFKQQLQSLLETLNTTEPHYIRCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILAP 683
Cdd:cd15896    558 GQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 637

                          650       660       670
                   ....*....|....*....|....*....|....*...
gi 1063705616  684 EATERSF-DEVDACKKLLARVDLKG--FQIGKTKVFLR 718
Cdd:cd15896    638 NAIPKGFmDGKQACVLMIKSLELDPnlYRIGQSKVFFR 675
MYSc_Myh14_mammals cd14930
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ...
 76-718 3.49e-141

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: 453.01  E-value: 3.49e-141
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   76 VLLNLKARYNANEIYTYTGNILIAVNPFKRLPhLYGNEIMEQYKGTDFGELSPHPFAVADSAYRKMINEGVSQAILVSGE 155
Cdd:cd14930      3 VLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  156 SGAGKTESTKMLMQYLAYM-----GGKAESEGRSVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFNHMGRISGA 230
Cdd:cd14930     82 SGAGKTENTKKVIQYLAHVasspkGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVGA 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  231 AIRTYLLERSRVCQVSDPERNYHCFYMLCAAPEQETERYQLGKPSTfHYLNQSNCHALDAIDDSKEYLATRKAMDVVGIS 310
Cdd:cd14930    162 NIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCS-HYRFLTNGPSSSPGQERELFQETLESLRVLGFS 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  311 PEEQDAIFRVVAAILHLGNIEFAKSEESDGAEPKDDKSRFHLKVAAKLFMCD-EKALensLCNRVMVTRgESITKPLDPG 389
Cdd:cd14930    241 HEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDfSRAL---LTPRIKVGR-DYVQKAQTKE 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  390 SAALSRDALAKIVYSKLFDWLVTKINNSIGQD-SSSKYIIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKME 468
Cdd:cd14930    317 QADFALEALAKATYERLFRWLVLRLNRALDRSpRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLE 396

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  469 QEEYTKEEIDWSYIEF-IDNQDVLDLIEK--KPGGIIALLDEACMFPRSTHDTLAEKLYQTFGSHKRFTKPKLAR--TDF 543
Cdd:cd14930    397 QEEYQREGIPWTFLDFgLDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLRdqADF 476

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  544 TICHYAGDVTYQTELFLDKNKDYVVGEHQSLMNSSDCSF----------------VSSLFPKSREESSKSSKFSSIGSQF 607
Cdd:cd14930    477 SVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLtaeiwkdvegivgleqVSSLGDGPPGGRPRRGMFRTVGQLY 556

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  608 KQQLQSLLETLNTTEPHYIRCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILAPEATE 687
Cdd:cd14930    557 KESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIP 636

                          650       660       670
                   ....*....|....*....|....*....|....
gi 1063705616  688 RSF-DEVDACKKLLARVDLKG--FQIGKTKVFLR 718
Cdd:cd14930    637 KGFmDGKQACEKMIQALELDPnlYRVGQSKIFFR 670
MYSc_Myo25 cd14886
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ...
 80-718 3.05e-137

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: 441.25  E-value: 3.05e-137
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   80 LKARYNANEIYTYTGNILIAVNPFKRLPHLYGNEIMEQYKGTD--FG---ELSPHPFAVADSAYRKMINEGVSQAILVSG 154
Cdd:cd14886      7 LRDRFAKDKIYTYAGKLLVALNPFKQIRNLYGTEVIGRYRQADtsRGfpsDLPPHSYAVAQSALNGLISDGISQSCIVSG 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  155 ESGAGKTESTKMLMQYLAYmgGKAESEgRSVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFNHMGRISGAAIRT 234
Cdd:cd14886     87 ESGAGKTETAKQLMNFFAY--GHSTSS-TDVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGLKGGKITS 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  235 YLLERSRVCQVSDPERNYHCFY-MLCAAPEQETERYQLGKPSTFHYLNQSNCHALDAIDDSKEYLATRKAMDVVgISPEE 313
Cdd:cd14886    164 YMLELSRIEFQSTNERNYHIFYqCIKGLSPEEKKSLGFKSLESYNFLNASKCYDAPGIDDQKEFAPVRSQLEKL-FSKNE 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  314 QDAIFRVVAAILHLGNIEFakSEESD----GAEPKDDKSRFhlKVAAKLFMCDEKALENSLCNRVMVTRGESITKPLDPG 389
Cdd:cd14886    243 IDSFYKCISGILLAGNIEF--SEEGDmgviNAAKISNDEDF--GKMCELLGIESSKAAQAIITKVVVINNETIISPVTQA 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  390 SAALSRDALAKIVYSKLFDWLVTKINNSIGQDSSSKYIIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKMEQ 469
Cdd:cd14886    319 QAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFINQVFKSEI 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  470 EEYTKEEIDWSYIEFIDNQDVLDLIEKKPGGIIALLDEACMFPRSThdtlAEKLYQTFGSH---KRFTKPKLARTDFTIC 546
Cdd:cd14886    399 QEYEIEGIDHSMITFTDNSNVLAVFDKPNLSIFSFLEEQCLIQTGS----SEKFTSSCKSKiknNSFIPGKGSQCNFTIV 474

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  547 HYAGDVTYQTELFLDKNKDYVVGEHQSLMNSSDCSFVSSLFpKSREESSKSSKFSSIGSQFKQQLQSLLETLNTTEPHYI 626
Cdd:cd14886    475 HTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAF-SDIPNEDGNMKGKFLGSTFQLSIDQLMKTLSATKSHFI 553

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  627 RCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILAPEATERSF---DEVDACKKLLAR- 702
Cdd:cd14886    554 RCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILISHNSSSQNageDLVEAVKSILENl 633

                          650
                   ....*....|....*..
gi 1063705616  703 -VDLKGFQIGKTKVFLR 718
Cdd:cd14886    634 gIPCSDYRIGKTKVFLR 650
MYSc_Myo38 cd14899
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ...
 76-679 4.88e-136

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: 440.69  E-value: 4.88e-136
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   76 VLLNLKARYNANEIYTYTGNILIAVNPFKRLPHLYGNEIMEQYK---GTDFGE-------LSPHPFAVADSAYRKMINEG 145
Cdd:cd14899      3 ILNALRLRYERHAIYTHIGDILISINPFQDLPQLYGDEILRGYAydhNSQFGDrvtstdpREPHLFAVARAAYIDIVQNG 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  146 VSQAILVSGESGAGKTESTKMLMQYLAYMGGKAESEGR--------------SVEQQVLESNPVLEAFGNAKTVRNNNSS 211
Cdd:cd14899     83 RSQSILISGESGAGKTEATKIIMTYFAVHCGTGNNNLTnsesisppaspsrtTIEEQVLQSNPILEAFGNARTVRNDNSS 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  212 RFGKFVEIQFNHMGR-ISGAAIRTYLLERSRVCQVSDPERNYHCFYML------CAAPEQETERYQLGKPSTFHYLNQSN 284
Cdd:cd14899    163 RFGKFIELRFRDERRrLAGARIRTYLLEKIRVIKQAPHERNFHIFYELlsadnnCVSKEQKQVLALSGGPQSFRLLNQSL 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  285 CHAL-DAIDDSKEYLATRKAMDVVGISPEEQDAIFRVVAAILHLGNIEFAKSEESDGAEPKDDKSRF---------HLKV 354
Cdd:cd14899    243 CSKRrDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQIPHKGDDTVFADEARVmssttgafdHFTK 322

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  355 AAKLFMCDEKALENSLCNRVMVTRGESITKPLDPGSAALSRDALAKIVYSKLFDWLVTKINNSIGQDSSSKY-------- 426
Cdd:cd14899    323 AAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQASAPWgadesdvd 402

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  427 -------IIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKMEQEEYTKEEIDWSYIEFIDNQDVLDLIEKKPG 499
Cdd:cd14899    403 deedatdFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNNRACLELFEHRPI 482

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  500 GIIALLDEACMFPRSTHDTLAEKLYQTF---GSHKRF-TKPKLAR-TDFTICHYAGDVTYQTELFLDKNKDYVVGEHQSL 574
Cdd:cd14899    483 GIFSLTDQECVFPQGTDRALVAKYYLEFekkNSHPHFrSAPLIQRtTQFVVAHYAGCVTYTIDGFLAKNKDSFCESAAQL 562

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  575 MNSSDCSFVSSLFPKSREESSKSSKFSS------------------IGSQFKQQLQSLLETLNTTEPHYIRCVKPNNVLK 636
Cdd:cd14899    563 LAGSSNPLIQALAAGSNDEDANGDSELDgfggrtrrraksaiaavsVGTQFKIQLNELLSTVRATTPRYVRCIKPNDSHV 642

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|...
gi 1063705616  637 PEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFR 679
Cdd:cd14899    643 GSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRYR 685
MYSc_Myo13 cd14875
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ...
 90-718 3.06e-130

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: 422.68  E-value: 3.06e-130
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   90 YTYTGNILIAVNPFKRLPHLYGNEIMEQYKGTDFGELSPHPFAVADSAYRKMINEGV-SQAILVSGESGAGKTESTKMLM 168
Cdd:cd14875     18 YSLMGEMVLSVNPFRLMPFNSEEERKKYLALPDPRLLPPHIWQVAHKAFNAIFVQGLgNQSVVISGESGSGKTENAKMLI 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  169 QYL---AYMGGKAESEgRSVEQQVLE----SNPVLEAFGNAKTVRNNNSSRFGKFVEIQFNHM-GRISGAAIRTYLLERS 240
Cdd:cd14875     98 AYLgqlSYMHSSNTSQ-RSIADKIDEnlkwSNPVMESFGNARTVRNDNSSRFGKYIKLYFDPTsGVMVGGQTVTYLLEKS 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  241 RVCQVSDPERNYHCFYMLCA--APEQETERYQLGKPSTFHYLNQSNC---HALDA--IDDSKEYLATRKAMDVVGISPEE 313
Cdd:cd14875    177 RIIMQSPGERNYHIFYEMLAglSPEEKKELGGLKTAQDYKCLNGGNTfvrRGVDGktLDDAHEFQNVRHALSMIGVELET 256

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  314 QDAIFRVVAAILHLGNIEFaKSEESDGAEPKDDKSrfhLKVAAKLFMCDEKALENSLcnrVMVTRGESITKPLDPGSAAL 393
Cdd:cd14875    257 QNSIFRVLASILHLMEVEF-ESDQNDKAQIADETP---FLTACRLLQLDPAKLRECF---LVKSKTSLVTILANKTEAEG 329

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  394 SRDALAKIVYSKLFDWLVTKINNSI---GQDSSSKYIiGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKMEQE 470
Cdd:cd14875    330 FRNAFCKAIYVGLFDRLVEFVNASItpqGDCSGCKYI-GLLDIFGFENFTRNSFEQLCINYANESLQNHYNKYTFINDEE 408

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  471 EYTKEEIDWSYIEFIDNQDVLDLIEKKPGGIIALLDEACMFPRSTHDTLAEKLYQTF-GSHKRFTKPK-LARTDFTICHY 548
Cdd:cd14875    409 ECRREGIQIPKIEFPDNSECVNMFDQKRTGIFSMLDEECNFKGGTTERFTTNLWDQWaNKSPYFVLPKsTIPNQFGVNHY 488

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  549 AGDVTYQTELFLDKNKDYVVGE-HQSLMNSSDcSFVSSLFPksrEESSKSSKFSSIGSQFKQQLQSLLETLNTTEPHYIR 627
Cdd:cd14875    489 AAFVNYNTDEWLEKNTDALKEDmYECVSNSTD-EFIRTLLS---TEKGLARRKQTVAIRFQRQLTDLRTELESTETQFIR 564

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  628 CVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILAPEATERSF---DEVDACKKLLARVD 704
Cdd:cd14875    565 CIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFCRYFYLIMPRSTASLFkqeKYSEAAKDFLAYYQ 644

                          650       660
                   ....*....|....*....|
gi 1063705616  705 ------LKGFQIGKTKVFLR 718
Cdd:cd14875    645 rlygwaKPNYAVGKTKVFLR 664
MYSc_Myo17 cd14879
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ...
 80-717 1.21e-126

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: 411.94  E-value: 1.21e-126
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   80 LKARYNANEIYTYTG-NILIAVNPFKRLPHL---YGNEIMEQYKGTDFGE---LSPHPFAVADSAYRKMINEGVSQAILV 152
Cdd:cd14879     10 LASRFRSDLPYTRLGsSALVAVNPYKYLSSNsdaSLGEYGSEYYDTTSGSkepLPPHAYDLAARAYLRMRRRSEDQAVVF 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  153 SGESGAGKTESTKMLM-QYLAYmgGKAESEGRSVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFNHMGRISGAA 231
Cdd:cd14879     90 LGETGSGKSESRRLLLrQLLRL--SSHSKKGTKLSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQFNERGRLIGAK 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  232 IRTYLLERSRVCQVSDPERNYHCFYMLCA-APEQETERYQLGKPSTFHYLNQSNCHALDA---IDDSKEYLATRKAMDVV 307
Cdd:cd14879    168 VLDYRLERSRVASVPTGERNFHVFYYLLAgASPEERQHLGLDDPSDYALLASYGCHPLPLgpgSDDAEGFQELKTALKTL 247

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  308 GISPEEQDAIFRVVAAILHLGNIEFakseeSDGAEPKDD----KSRFHLKVAAKLFMCDEKALENSLCNR-VMVtRGESI 382
Cdd:cd14879    248 GFKRKHVAQICQLLAAILHLGNLEF-----TYDHEGGEEsavvKNTDVLDIVAAFLGVSPEDLETSLTYKtKLV-RKELC 321

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  383 TKPLDPGSAALSRDALAKIVYSKLFDWLVTKINNSI--GQDSSSKYiIGVLDIYGFESFKT---NSFEQFCINLTNEKLQ 457
Cdd:cd14879    322 TVFLDPEGAAAQRDELARTLYSLLFAWVVETINQKLcaPEDDFATF-ISLLDFPGFQNRSStggNSLDQFCVNFANERLH 400

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  458 QHFNQHVFKMEQEEYTKEEIDWSYIEFIDNQDVLDLIEKKPGGIIALLDEAC-MFPRSTHDTLAEKLYQTFGSHKRF-TK 535
Cdd:cd14879    401 NYVLRSFFERKAEELEAEGVSVPATSYFDNSDCVRLLRGKPGGLLGILDDQTrRMPKKTDEQMLEALRKRFGNHSSFiAV 480

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  536 PKLARTD----FTICHYAGDVTYQTELFLDKNKDYVVGEHQSLMNSSdcsfvsslfpksreessksskfssigSQFKQQL 611
Cdd:cd14879    481 GNFATRSgsasFTVNHYAGEVTYSVEGFLERNGDVLSPDFVNLLRGA--------------------------TQLNAAL 534

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  612 QSLLETLNTTEPHYIRCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFrilAPEATERSFD 691
Cdd:cd14879    535 SELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELAARLRVEYVVSLEHAEFCERY---KSTLRGSAAE 611

                          650       660
                   ....*....|....*....|....*.
gi 1063705616  692 EVDACKKLLARVDLKGFQIGKTKVFL 717
Cdd:cd14879    612 RIRQCARANGWWEGRDYVLGNTKVFL 637
MYSc_Myo26 cd14887
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ...
 74-718 9.70e-113

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: 375.53  E-value: 9.70e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   74 PGVLLNLKARY--------NANEIYTYTGNILIAVNPFkRLPHLYGNEIMEQYKGTDFGELSPHPFAVADSAYRKMINEG 145
Cdd:cd14887      1 PNLLENLYQRYnkayinkeNRNCIYTYTGTLLIAVNPY-RFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDR 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  146 VSQAILVSGESGAGKTESTKMLMQYLAYMGGK---AESEGrsVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFN 222
Cdd:cd14887     80 RSQSILISGESGAGKTETSKHVLTYLAAVSDRrhgADSQG--LEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFT 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  223 HMGRISGAAIRTYLLERSRVCQVSDPERNYHCFYMLCAAPEQETERyqlgKPSTFHYLNQSncHALDAIDdskeylatrK 302
Cdd:cd14887    158 GRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQ----KSSAGEGDPES--TDLRRIT---------A 222

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  303 AMDVVGISPEEQDAIFRVVAAILHLGNIEFAKSEE-----------------------SDGAEPKDDKS--------RFH 351
Cdd:cd14887    223 AMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEpetskkrkltsvsvgceetaadrSHSSEVKCLSSglkvteasRKH 302

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  352 LKVAAKLFMCDEKALENSLCNRVMVTRGESIT-KPLDPGSAALSRDALAKIVYSKLFDWLVTKINNSIGQDSSSKY---- 426
Cdd:cd14887    303 LKTVARLLGLPPGVEGEEMLRLALVSRSVRETrSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKPSEsdsd 382

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  427 ----------IIGVLDIYGFESFKT---NSFEQFCINLTNEKLQQHFNQHVFKMEQEEYTKEEIDWSYIEFIDN------ 487
Cdd:cd14887    383 edtpsttgtqTIGILDLFGFEDLRNhskNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDCSAFPfsfpla 462

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  488 -------QDVLDLI--------------EKKPGGIIALLDEACMFP-----RSTHDTLAEKLYQTFGSHKRFTKP----K 537
Cdd:cd14887    463 stltsspSSTSPFSptpsfrsssafatsPSLPSSLSSLSSSLSSSPpvwegRDNSDLFYEKLNKNIINSAKYKNItpalS 542

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  538 LARTDFTICHYAGDVTYQTELFLDKNKDYVVGEHQSLMNSsdCSFVSSL--FPKSREESSKSSKFSSIGSQFKQQLQSLL 615
Cdd:cd14887    543 RENLEFTVSHFACDVTYDARDFCRANREATSDELERLFLA--CSTYTRLvgSKKNSGVRAISSRRSTLSAQFASQLQQVL 620

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  616 ETLNTTEPHYIRCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILAPEATERSFDEVDA 695
Cdd:cd14887    621 KALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYETKLPMALREALTPKMF 700

                          730       740
                   ....*....|....*....|....*
gi 1063705616  696 CKKLLARVDLK--GFQIGKTKVFLR 718
Cdd:cd14887    701 CKIVLMFLEINsnSYTFGKTKIFFR 725
MYSc_Myo16 cd14878
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ...
 76-718 3.59e-112

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: 371.84  E-value: 3.59e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   76 VLLNLKARYNANEIYTYTGNILIAVNPFKRLPhLYGNEIMEQY---KGTDFGELSPHPFAVADSAYRKMINEGVSQAILV 152
Cdd:cd14878      3 LLYEIQKRFGNNQIYTFIGDILLLVNPYKELP-IYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFIL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  153 SGESGAGKTESTKMLMQYLAymgGKAESEGRSVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQF-NHMGRISGAA 231
Cdd:cd14878     82 SGERGSGKTEASKQIMKHLT---CRASSSRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKKHLTGAR 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  232 IRTYLLERSRVCQVSDPERNYHCFYMLCAAPEQEtERYQL--GKPSTFHYLNQSNCHALDAIDDS--KEYLATRK-AMDV 306
Cdd:cd14878    159 IYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAE-EKYGLhlNNLCAHRYLNQTMREDVSTAERSlnREKLAVLKqALNV 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  307 VGISPEEQDAIFRVVAAILHLGNIEFAKSEESDGAEPKDDKSrfhLKVAAKLFMCDEKALENSLCNRVMVTRGESITKPL 386
Cdd:cd14878    238 VGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQL---LEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRH 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  387 DPGSAALSRDALAKIVYSKLFDWLVTKINNSI-GQDSSSKY---IIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQ 462
Cdd:cd14878    315 TIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqSQDEQKSMqtlDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINE 394

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  463 HVFKMEQEEYTKEEIDWSYIEFIDNQD-VLDLIEKKPGGIIALLDEACMFPRSTHDTLAEKL------------YQTFGS 529
Cdd:cd14878    395 VLFLQEQTECVQEGVTMETAYSPGNQTgVLDFFFQKPSGFLSLLDEESQMIWSVEPNLPKKLqsllessntnavYSPMKD 474

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  530 HKRFTKPKLARTDFTICHYAGDVTYQTELFLDKNKDYVVGEHQSLMNSSDCSFVSSLFpksreesskSSKFSSIGSQFKQ 609
Cdd:cd14878    475 GNGNVALKDQGTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLF---------QSKLVTIASQLRK 545

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  610 QLQSLLETLNTTEPHYIRCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILAP--EATE 687
Cdd:cd14878    546 SLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADtlLGEK 625

                          650       660       670
                   ....*....|....*....|....*....|.
gi 1063705616  688 RSFDEVDACKKLLARVDLKGFQIGKTKVFLR 718
Cdd:cd14878    626 KKQSAEERCRLVLQQCKLQGWQMGVRKVFLK 656
MYSc_Myo37 cd14898
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ...
 80-687 2.40e-105

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: 349.58  E-value: 2.40e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   80 LKARYNANEIYTYTGNILIAVNPFKrlpHLYGNEIMEQYKGTDfGELSPHPFAVADSAYRKMINEGvSQAILVSGESGAG 159
Cdd:cd14898      7 LEKRYASGKIYTKSGLVFLALNPYE---TIYGAGAMKAYLKNY-SHVEPHVYDVAEASVQDLLVHG-NQTIVISGESGSG 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  160 KTESTKMLMQYLAYmgGKAESEgrSVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFNhmGRISGAAIRTYLLER 239
Cdd:cd14898     82 KTENAKLVIKYLVE--RTASTT--SIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITGAKFETYLLEK 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  240 SRVCQVSDPERNYHCFYMLCAapeqeTERYQLGKPSTFHYLNQSNCHALdaIDDSKEYLATRKAMDVVGISpeEQDAIFR 319
Cdd:cd14898    156 SRVTHHEKGERNFHIFYQFCA-----SKRLNIKNDFIDTSSTAGNKESI--VQLSEKYKMTCSAMKSLGIA--NFKSIED 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  320 VVAAILHLGNIEFAkseeSDGAEPKddKSRFHLKVAAKLFMCDEKALENSLCNRVMVTRGESITKPLDPGSAALSRDALA 399
Cdd:cd14898    227 CLLGILYLGSIQFV----NDGILKL--QRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQARTIRNSMA 300

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  400 KIVYSKLFDWLVTKINNSIGqdSSSKYIIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKMEQEEYTKEEIDW 479
Cdd:cd14898    301 RLLYSNVFNYITASINNCLE--GSGERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGMYKEEGIEW 378

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  480 SYIEFIDNQDVLDLIEkKPGGIIALLDEACMFPRSTHDTLAEKLyQTFGSHKRFTKpklARTDFTICHYAGDVTYQTELF 559
Cdd:cd14898    379 PDVEFFDNNQCIRDFE-KPCGLMDLISEESFNAWGNVKNLLVKI-KKYLNGFINTK---ARDKIKVSHYAGDVEYDLRDF 453

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  560 LDKNKDYvvgehqslmnssdcsfvSSLFPKSREESSKSSKFSSIGSQFKQQLQSLLETLNTTEPHYIRCVKPNNVLKPEI 639
Cdd:cd14898    454 LDKNREK-----------------GQLLIFKNLLINDEGSKEDLVKYFKDSMNKLLNSINETQAKYIKCIRPNEECRPWC 516

                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*...
gi 1063705616  640 FENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILAPEATE 687
Cdd:cd14898    517 FDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGITLFE 564
MYSc_Myo20 cd14881
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ...
 76-701 1.48e-98

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: 332.08  E-value: 1.48e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   76 VLLNLKARYNANEIYTYTGNILIAVNPFKRLphlyGNEImeQYKGTDFGELSPHPFAVADSAYRKMINEGVSQAILVSGE 155
Cdd:cd14881      3 VMKCLQARFYAKEFFTNVGPILLSVNPYRDV----GNPL--TLTSTRSSPLAPQLLKVVQEAVRQQSETGYPQAIILSGT 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  156 SGAGKT-ESTKMLMQYLAYMGGKAESEGRsveQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFNhmgriSGAAIRT 234
Cdd:cd14881     77 SGSGKTyASMLLLRQLFDVAGGGPETDAF---KHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQVT-----DGALYRT 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  235 ----YLLERSRVCQVSDPERNYHCFYMLCAAPEQEtERYQLG----KPSTFHYLNQSNcHALDAIDDSKEYLATRKAMDV 306
Cdd:cd14881    149 kihcYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQE-ERVKLHldgySPANLRYLSHGD-TRQNEAEDAARFQAWKACLGI 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  307 VGISPEEqdaIFRVVAAILHLGNIEFAKSEESDGaepkDDKSRFHLKVAAKLFMCDEKALENSLCNRVMVTRGESITKPL 386
Cdd:cd14881    227 LGIPFLD---VVRVLAAVLLLGNVQFIDGGGLEV----DVKGETELKSVAALLGVSGAALFRGLTTRTHNARGQLVKSVC 299

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  387 DPGSAALSRDALAKIVYSKLFDWLVTKIN-----NSIGQDSSSKYIIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFN 461
Cdd:cd14881    300 DANMSNMTRDALAKALYCRTVATIVRRANslkrlGSTLGTHATDGFIGILDMFGFEDPKPSQLEHLCINLCAETMQHFYN 379

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  462 QHVFKMEQEEYTKEEIDWSY-IEFIDNQDVLDLIEKKPGGIIALLDEACMfPRSTHDTLAEKLYQTFGSHKRF--TKPKL 538
Cdd:cd14881    380 THIFKSSIESCRDEGIQCEVeVDYVDNVPCIDLISSLRTGLLSMLDVECS-PRGTAESYVAKIKVQHRQNPRLfeAKPQD 458

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  539 ARTdFTICHYAGDVTYQTELFLDKNKDYVVGEHQSLMNSSDCSF--VSSLfpksreessksskfssigSQFKQQLQSLLE 616
Cdd:cd14881    459 DRM-FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQNCNFgfATHT------------------QDFHTRLDNLLR 519

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  617 TLNTTEPHYIRCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILAPEATERSFDE-VDA 695
Cdd:cd14881    520 TLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKAFNARYRLLAPFRLLRRVEEkALE 599


                   ....*.
gi 1063705616  696 CKKLLA 701
Cdd:cd14881    600 DCALIL 605
MYSc_Myo21 cd14882
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ...
 76-718 1.93e-96

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: 326.31  E-value: 1.93e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   76 VLLNLKARYNANEIYTYTGNILIAVNPfKRLPHLYGNEIMEQYKGTDFGELSPHPFAVADSAYRKMINEGVSQAILVSGE 155
Cdd:cd14882      3 ILEELRHRYLMGESYTFIGDILLSLNP-NEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  156 SGAGKTESTKMLMQYLAYMGgkaesEG-RSVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFNHMGRISGAAIRT 234
Cdd:cd14882     82 SYSGKTTNARLLIKHLCYLG-----DGnRGATGRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFWM 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  235 YLLERSRVCQVSDPERNYHCFYMLCAAPEQET--ERYQLGKPSTFHYL----NQSNCHALDAIDDS-------KEYLATR 301
Cdd:cd14882    157 YQLEKLRVSTTDGNQSNFHIFYYFYDFIEAQNrlKEYNLKAGRNYRYLrippEVPPSKLKYRRDDPegnveryKEFEEIL 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  302 KAMDvvgISPEEQDAIFRVVAAILHLGNIEFAKSEESDGAEPKDDKSRfhlkvAAKLFMCDEKALENSLCNRVMVTRGES 381
Cdd:cd14882    237 KDLD---FNEEQLETVRKVLAAILNLGEIRFRQNGGYAELENTEIASR-----VAELLRLDEKKFMWALTNYCLIKGGSA 308

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  382 ITKPLDPGSAALSRDALAKIVYSKLFDWLVTKINNSIGQDSS---SKYIIGVLDIYGFESFKTNSFEQFCINLTNEKLQQ 458
Cdd:cd14882    309 ERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSFPRAvfgDKYSISIHDMFGFECFHRNRLEQLMVNTLNEQMQY 388

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  459 HFNQHVFKMEQEEYTKEEIDWSYIEFIDNQDVLDLIEKKPGGIIALLDEAcmfPRSTHDtlAEKLYQTFGSHKR-FTKPK 537
Cdd:cd14882    389 HYNQRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPDGLFYIIDDA---SRSCQD--QNYIMDRIKEKHSqFVKKH 463

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  538 LArTDFTICHYAGDVTYQTELFLDKNKDYVVGEHQSLMNSSDCSFVSSLFpksreESSKSSKFSSIGSQFKQQLQSLLET 617
Cdd:cd14882    464 SA-HEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMF-----TNSQVRNMRTLAATFRATSLELLKM 537

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  618 L----NTTEPHYIRCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILAPEatersFDEV 693
Cdd:cd14882    538 LsigaNSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQEFLRRYQFLAFD-----FDET 612

                          650       660       670
                   ....*....|....*....|....*....|
gi 1063705616  694 -----DACKKLLARVDLKGFQIGKTKVFLR 718
Cdd:cd14882    613 vemtkDNCRLLLIRLKMEGWAIGKTKVFLK 642
MYSc_Myo23 cd14884
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ...
 74-718 2.17e-94

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: 321.86  E-value: 2.17e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   74 PGVLLNLKARYNANEIYTYTGNILIAVNPFKRLPHLYGNEIMEQY-------KGTDFGELSPHPFAVADSAYRKMINEGV 146
Cdd:cd14884      1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKELYDQDVMNVYlhkksnsAASAAPFPKAHIYDIANMAYKNMRGKLK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  147 SQAILVSGESGAGKTESTKMLMQYLAYMGGKAESEGRsvEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFNHM-- 224
Cdd:cd14884     81 RQTIVVSGHSGSGKTENCKFLFKYFHYIQTDSQMTER--IDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFEEVen 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  225 -------GRISGAAIRTYLLERSRVCQVSDPERNYHCFYMLC--AAPEQETER--------YQLGKPSTFHYLNQS--NC 285
Cdd:cd14884    159 tqknmfnGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLrgLSDEDLARRnlvrncgvYGLLNPDESHQKRSVkgTL 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  286 H-ALDAID--------DSKEYLATRKAMDVVGISPEEQDAIFRVVAAILHLGNiefakseesdgaepkddksrFHLKVAA 356
Cdd:cd14884    239 RlGSDSLDpseeekakDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGN--------------------RAYKAAA 298

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  357 KLFMCDEKALENSLCNRVMVTRGESITKPLDPGSAALSRDALAKIVYSKLFDWLVTKINNSIGQDSSSK----------- 425
Cdd:cd14884    299 ECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEKDesdnediysin 378

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  426 -YIIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKMEQEEYTKEEIDWSYIEFIDNQDVLDLIEKkpggIIAL 504
Cdd:cd14884    379 eAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAPSYSDTLIFIAK----IFRR 454

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  505 LDE-----ACMFPRS-----THDTLAEKLYQTFGSHKR-FTKPKLA----------RTDFTICHYAGDVTYQTELFLDKN 563
Cdd:cd14884    455 LDDitklkNQGQKKTddhffRYLLNNERQQQLEGKVSYgFVLNHDAdgtakkqnikKNIFFIRHYAGLVTYRINNWIDKN 534

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  564 KDYVVGEHQSLMNSSdcsfvSSLFPKSREESSKSSKFSSIGSQFKQQLQSLLETLNTTEPHYIRCVKPNNVLKPEIFENV 643
Cdd:cd14884    535 SDKIETSIETLISCS-----SNRFLREANNGGNKGNFLSVSKKYIKELDNLFTQLQSTDMYYIRCFLPNAKMLPNTFKRL 609

                          650       660       670       680       690       700       710
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063705616  644 NVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILAPEATERSFDEVDA-CKKLLARVDLKGFQIGKTKVFLR 718
Cdd:cd14884    610 LVYRQLKQCGSNEMIKILNRGLSHKIPKKETAAALKEQIAKELEKCNSNTDIeYQRRLAALDVQFIPDGRLYAFMK 685
MYSc_Myo18 cd01386
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ...
 75-718 1.15e-91

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: 313.86  E-value: 1.15e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   75 GVLLNLKARYNANEIYTYTGNILIAVNPFKRLPhLYGNEIMEQYKGTDFGELSPHPFAVADSAYRKMINEGVSQAILVSG 154
Cdd:cd01386      2 SVLHTLRQRYGANLIHTYAGPSLIVINPRHPLA-VYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  155 ESGAGKTESTKMLMQYLAYMGGkaeSEGRSVEQQVLES-NPVLEAFGNAKTVRNNNSSRFGKFVEIQFNHMGRISGAAIR 233
Cdd:cd01386     81 RSGSGKTTNCRHILEYLVTAAG---SVGGVLSVEKLNAaLTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASIQ 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  234 TYLLERSRVCQVSDPERNYHCFYML--CAAPEQETERY--QLGKPSTFhYLNQSNCHAlDAIDDSKEYLATRKAMDVVGI 309
Cdd:cd01386    158 TLLLERSRVARRPEGESNFNVFYYLlaGADAALRTELHlnQLAESNSF-GIVPLQKPE-DKQKAAAAFSKLQAAMKTLGI 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  310 SPEEQDAIFRVVAAILHLGNIEFAKSEESdgaePKDDKSRF-HLKVAAKLFMCDEKAL--------------ENSLCNRV 374
Cdd:cd01386    236 SEEEQRAIWSILAAIYHLGAAGATKAASA----GRKQFARPeWAQRAAYLLGCTLEELssaifkhhlsggpqQSTTSSGQ 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  375 MVTRGESITKPLDPGSAALsrDALAKIVYSKLFDWLVTKINNSIGQDSSSKYIIGVLDIYGFE------SFKTNSFEQFC 448
Cdd:cd01386    312 ESPARSSSGGPKLTGVEAL--EGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQnpahsgSQRGATFEDLC 389

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  449 INLTNEKLQQHFNQHVFKMEQEEYTKE--EIDWSYIEFIDNQDVlDLIEKKP--------------GGIIALLDEACMFP 512
Cdd:cd01386    390 HNYAQERLQLLFHERTFVAPLERYKQEnvEVDFDLPELSPGALV-ALIDQAPqqalvrsdlrdedrRGLLWLLDEEALYP 468

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  513 RSTHDTLAEKLYQTFGSHKRFTKPKLART-----DFTICHYAG--DVTYQTELFLDKNKDYVVGE--HQSLMNSSD---- 579
Cdd:cd01386    469 GSSDDTFLERLFSHYGDKEGGKGHSLLRRsegplQFVLGHLLGtnPVEYDVSGWLKAAKENPSAQnaTQLLQESQKetaa 548

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  580 ---CSFVsslfpksreessksskfssigSQFKQQLQSLLETLNTTEPHYIRCVKPN-NVLKPEIFE----------NVNV 645
Cdd:cd01386    549 vkrKSPC---------------------LQIKFQVDALIDTLRRTGLHFVHCLLPQhNAGKDERSTsspaagdellDVPL 607

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  646 LH-QLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILAPEATERSF------DEVDACKKLLARVDL--KGFQIGKTKVF 716
Cdd:cd01386    608 LRsQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGlnsevaDERKAVEELLEELDLekSSYRIGLSQVF 687


                   ..
gi 1063705616  717 LR 718
Cdd:cd01386    688 FR 689
MYSc_Myo24A cd14937
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ...
 76-718 3.87e-91

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: 310.79  E-value: 3.87e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   76 VLLNLKARYNANEIYTYTGNILIAVNPFKRLphlygNEIMEQYKGTDFGELSPHPFAVADSAYRKMINEGVSQAILVSGE 155
Cdd:cd14937      3 VLNMLALRYKKNYIYTIAEPMLISINPYQVI-----DVDINEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  156 SGAGKTESTKMLMQYlaYMGGKAESEgrSVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFNHMGRISGAAIRTY 235
Cdd:cd14937     78 SGSGKTEASKLVIKY--YLSGVKEDN--EISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSIEIF 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  236 LLERSRVCQVSDPERNYHCFYMLCAAPEQETE-RYQLGKPSTFHYLNQSNChALDAIDDSKEYLATRKAMDVVGISpEEQ 314
Cdd:cd14937    154 LLENIRVVSQEEEERGYHIFYQIFNGMSQELKnKYKIRSENEYKYIVNKNV-VIPEIDDAKDFGNLMISFDKMNMH-DMK 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  315 DAIFRVVAAILHLGNIEFAKSEE--SDGAEPKDDKSRFHLKVAAKLFMCDEKALENSLCNRVMVTRGESITKPLDPGSAA 392
Cdd:cd14937    232 DDLFLTLSGLLLLGNVEYQEIEKggKTNCSELDKNNLELVNEISNLLGINYENLKDCLVFTEKTIANQKIEIPLSVEESV 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  393 LSRDALAKIVYSKLFDWLVTKINNSIGQDSSSKYIIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKMEQEEY 472
Cdd:cd14937    312 SICKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYEKETELY 391

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  473 TKEEIDWSYIEFIDNQDVLDLIEKKPgGIIALLDEACMFPRSTHDTLAEKLYQTFGSHKRFTKPKLART-DFTICHYAGD 551
Cdd:cd14937    392 KAEDILIESVKYTTNESIIDLLRGKT-SIISILEDSCLGPVKNDESIVSVYTNKFSKHEKYASTKKDINkNFVIKHTVSD 470

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  552 VTYQTELFLDKNKDYVVGEHQSLMNSSDCSFVSSLFpKSREESSKSSKFSSIGSQFKQQLQSLLETLNTTEPHYIRCVKP 631
Cdd:cd14937    471 VTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLY-EDVEVSESLGRKNLITFKYLKNLNNIISYLKSTNIYFIKCIKP 549

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  632 NNVLKPEIFENVNVLHQLRCGGVMEAIRISCAgYPTRKPFNEFLTRFRIL-APEATERSFDEVDACKKLLAR-VDLKGFQ 709
Cdd:cd14937    550 NENKEKNNFNQKKVFPQLFSLSIIETLNISFF-FQYKYTFDVFLSYFEYLdYSTSKDSSLTDKEKVSMILQNtVDPDLYK 628


                   ....*....
gi 1063705616  710 IGKTKVFLR 718
Cdd:cd14937    629 VGKTMVFLK 637
MYSc_Myo12 cd14874
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ...
 75-718 1.47e-82

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: 285.61  E-value: 1.47e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   75 GVLLNLKARYNANEIYTYTGNILIAVNPFKRLPhLYGNEIMEQYkgtdfgelspHPFAVADSAYRKMI-NEGVSQAILVS 153
Cdd:cd14874      2 GIAQNLHERFKKGQTYTKASNVLVFVNDFNKLS-IQDQLVIKKC----------HISGVAENALDRIKsMSSNAESIVFG 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  154 GESGAGKTEStkmLMQYLAYMGGKAESEGRSVEQQVLESnpVLEAFGNAKTVRNNNSSRFGKFVEIQFNHmGRISGAAIR 233
Cdd:cd14874     71 GESGSGKSYN---AFQVFKYLTSQPKSKVTTKHSSAIES--VFKSFGCAKTLKNDEATRFGCSIDLLYKR-NVLTGLNLK 144

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  234 -TYLLERSRVCQVSDPERNYHCFYMLCAAPEQETE-RYQLGKPSTFHYLNQSNChALDAIDDSKEYLATRKAMDVVGISP 311
Cdd:cd14874    145 yTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKaKFGIKGLQKFFYINQGNS-TENIQSDVNHFKHLEDALHVLGFSD 223

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  312 EEQDAIFRVVAAILHLGNIEFAKSE----ESDGAEPKDDKsrfHLKVAAKLFMCDEKALENSLcnrvmvTRGESITKPLD 387
Cdd:cd14874    224 DHCISIYKIISTILHIGNIYFRTKRnpnvEQDVVEIGNMS---EVKWVAFLLEVDFDQLVNFL------LPKSEDGTTID 294

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  388 PGSAALSRDALAKIVYSKLFDWLVTKINNSIgQDSSSKYIIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKM 467
Cdd:cd14874    295 LNAALDNRDSFAMLIYEELFKWVLNRIGLHL-KCPLHTGVISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHSFHD 373

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  468 EQEEYTKEEI--DWSYIEFIDNQDVLDLIEKKPGGIIALLDEACMFPRSTHDTLAEKLYQTFGSHKRFTKPKLA-RTDFT 544
Cdd:cd14874    374 QLVDYAKDGIsvDYKVPNSIENGKTVELLFKKPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSSYGKARNKeRLEFG 453

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  545 ICHYAGDVTYQTELFLDKNKDYVVGEHQSLMNSSDCSFVSSLFpksreESSKSSKFSSIGSQFKQQL---QSLLETLNTT 621
Cdd:cd14874    454 VRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLF-----ESYSSNTSDMIVSQAQFILrgaQEIADKINGS 528

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  622 EPHYIRCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILAPEATERSFDEVDACKKLLA 701
Cdd:cd14874    529 HAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCLLPGDIAMCQNEKEIIQDILQ 608

                          650       660
                   ....*....|....*....|
gi 1063705616  702 RVDLK---GFQIGKTKVFLR 718
Cdd:cd14874    609 GQGVKyenDFKIGTEYVFLR 628
MYSc_Myo44 cd14905
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ...
 80-718 2.28e-80

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: 280.44  E-value: 2.28e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   80 LKARYNANEIYTYTGNILIAVNPFKRLPHLYGNEIMEQYKGTDfgELSPHPFAVADSAYRKMINEGVSQAILVSGESGAG 159
Cdd:cd14905      7 IQARYKKEIIYTYIGPILVSVNPLRYLPFLHSQELVRNYNQRR--GLPPHLFALAAKAISDMQDFRRDQLIFIGGESGSG 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  160 KTESTKMLMQYLAYMGgkaESEGRSVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFNHMGRISGAAIRTYLLER 239
Cdd:cd14905     85 KSENTKIIIQYLLTTD---LSRSKYLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKLYSYFLDE 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  240 SRVCQVSDPERNYHCFY-MLCAAPEQETERYQLGKPSTFHYLNQSNCHALDAIDDSKEYLATRKAMDVVGISPEEQDAIF 318
Cdd:cd14905    162 NRVTYQNKGERNFHIFYqFLKGITDEEKAAYQLGDINSYHYLNQGGSISVESIDDNRVFDRLKMSFVFFDFPSEKIDLIF 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  319 RVVAAILHLGNIEFAksEESDGAEPKDdksRFHLKVAAKLFMCDEKALENSLCNRVMVTRGESITkpldpgsaalSRDAL 398
Cdd:cd14905    242 KTLSFIIILGNVTFF--QKNGKTEVKD---RTLIESLSHNITFDSTKLENILISDRSMPVNEAVE----------NRDSL 306

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  399 AKIVYSKLFDWLVTKINNSIgQDSSSKYIIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKMEQEEYTKEEID 478
Cdd:cd14905    307 ARSLYSALFHWIIDFLNSKL-KPTQYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQREYQTERIP 385

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  479 W-SYIEFIDNQDVLDLIEKkpggIIALLDEACMFPRSTHDTLAEKLYQTFGSHKRFTKPKlarTDFTICHYAGDVTYQTE 557
Cdd:cd14905    386 WmTPISFKDNEESVEMMEK----IINLLDQESKNINSSDQIFLEKLQNFLSRHHLFGKKP---NKFGIEHYFGQFYYDVR 458

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  558 LFLDKNKDYVVGEHQSLMNSSDCSFVSS---LFPKSREESSKSSKFSSIGSQFKQQLqSLLETL---------NTTEP-- 623
Cdd:cd14905    459 GFIIKNRDEILQRTNVLHKNSITKYLFSrdgVFNINATVAELNQMFDAKNTAKKSPL-SIVKVLlscgsnnpnNVNNPnn 537

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  624 ---------------------------------------HYIRCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAG 664
Cdd:cd14905    538 nsgggggggnsgggsgsggstyttysstnkainnsncdfHFIRCIKPNSKKTHLTFDVKSVNEQIKSLCLLETTRIQRFG 617

                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1063705616  665 YPTRKPFNEFLTRFRILApeATERSFDEV-DACKKLLARVDL---KGFQIGKTKVFLR 718
Cdd:cd14905    618 YTIHYNNKIFFDRFSFFF--QNQRNFQNLfEKLKENDINIDSilpPPIQVGNTKIFLR 673
MYSc_Myo32 cd14893
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ...
 77-717 1.30e-70

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: 253.35  E-value: 1.30e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   77 LLNLKARYNANEIYTYTGNILIAVNPFKRLP-----HLygNEIMEQYKGTDFGELS------PHPFAVADSAYRKMINEG 145
Cdd:cd14893      4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPiytpdHM--QAYNKSREQTPLYEKDtvndapPHVFALAQNALRCMQDAG 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  146 VSQAILVSGESGAGKTESTKMLMQYLAYMGGKAE----SEGRSVE-----QQVLESNPVLEAFGNAKTVRNNNSSRFGKF 216
Cdd:cd14893     82 EDQAVILLGGMGAGKSEAAKLIVQYLCEIGDETEprpdSEGASGVlhpigQQILHAFTILEAFGNAATRQNRNSSRFAKM 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  217 VEIQFNHMGRISGAAIRTYLLERSRVCQVSDPERNYHCFYMLCAAPEQET---ERYQLGK-PSTFHYLNQSNCHALDAID 292
Cdd:cd14893    162 ISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHDPtlrDSLEMNKcVNEFVMLKQADPLATNFAL 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  293 DSKEYLATRKAMDVVGISPEEQDAIFRVVAAILHLGNIEF------AKSEESDGAEPKDDKSRFHLK------VAAKLFM 360
Cdd:cd14893    242 DARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpegGKSVGGANSTTVSDAQSCALKdpaqilLAAKLLE 321

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  361 CDEKALENSLCNRVMVTRGESIT----KPLDPGSAALSRDALAKIVYSKLFDWLVTKINNSIG----QDSSSKYIIG--- 429
Cdd:cd14893    322 VEPVVLDNYFRTRQFFSKDGNKTvsslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILGgifdRYEKSNIVINsqg 401

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  430 --VLDIYGFESFKT--NSFEQFCINLTNEKLQQHFNQHVFKM-------EQEEYTKEEIDWSYIEFIDNQD-VLDLIEKK 497
Cdd:cd14893    402 vhVLDMVGFENLTPsqNSFDQLCFNYWSEKVHHFYVQNTLAInfsfledESQQVENRLTVNSNVDITSEQEkCLQLFEDK 481

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  498 PGGIIALLDEACMFPRSTHDTLAEKLYQ-----------TFGS---HKRFTKPKLARTDFTICHYAGDVTYQTELFLDKN 563
Cdd:cd14893    482 PFGIFDLLTENCKVRLPNDEDFVNKLFSgneavgglsrpNMGAdttNEYLAPSKDWRLLFIVQHHCGKVTYNGKGLSSKN 561

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  564 ---------------KDYV---VGEHQSLMNSS---------DCSFVSSLFPKSREESSKSSKFSSIGSQFKQQLQSLLE 616
Cdd:cd14893    562 mlsisstcaaimqssKNAVlhaVGAAQMAAASSekaakqteeRGSTSSKFRKSASSARESKNITDSAATDVYNQADALLH 641

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  617 TLNTTEPHYIRCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFR-ILAPEATERSFDEVDA 695
Cdd:cd14893    642 ALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYKnVCGHRGTLESLLRSLS 721

                          730       740
                   ....*....|....*....|..
gi 1063705616  696 CKKLLARVDlkgFQIGKTKVFL 717
Cdd:cd14893    722 AIGVLEEEK---FVVGKTKVYL 740
MYSc_Myo24B cd14938
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ...
 74-717 3.35e-48

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: 185.42  E-value: 3.35e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   74 PGVLLNLKARYNANEIYTYTGNILIAVNPFKRLpHLYGNEIMEQYKGTD-FGELSPHPFAVADSAYRKMINEGVSQAILV 152
Cdd:cd14938      1 PSVLYHLKERFKNNKFYTKMGPLLIFINPKINN-NINNEETIEKYKCIDcIEDLSLNEYHVVHNALKNLNELKRNQSIII 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  153 SGESGAGKTESTKMLMQYLAY--MGGKAESEGRSVEQQVLES------------------NPVLEAFGNAKTVRNNNSSR 212
Cdd:cd14938     80 SGESGSGKSEIAKNIINFIAYqvKGSRRLPTNLNDQEEDNIHneentdyqfnmsemlkhvNVVMEAFGNAKTVKNNNSSR 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  213 FGKFVEIQFNHmGRISGAAIRTYLLERSRVCQVSDPERNYHCF-YMLCAAPEQETERYQLGKPSTFHYLNqsNCHALDAI 291
Cdd:cd14938    160 FSKFCTIHIEN-EEIKSFHIKKFLLDKERLINRKANENSFNIFyYIINGSSDKFKKMYFLKNIENYSMLN--NEKGFEKF 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  292 -DDSKEYLATRKAMDVVGISPEEQDAIFRVVAAILHLGNIEFAK---------------------SEESDGAEPKD---D 346
Cdd:cd14938    237 sDYSGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTEIVKafrkksllmgknqcgqninyeTILSELENSEDiglD 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  347 KSRFHLKVAAKLFMCDEKAL-----ENSLCNRVMVTRGESITKpldpgsAALSRDALAKIVYSKLFDWLVTKINNSIGQ- 420
Cdd:cd14938    317 ENVKNLLLACKLLSFDIETFvkyftTNYIFNDSILIKVHNETK------IQKKLENFIKTCYEELFNWIIYKINEKCTQl 390

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  421 ---DSSSKYiIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKMEQEEYTKEEIDWSY-IEFIDNQDVLD-LIE 495
Cdd:cd14938    391 qniNINTNY-INVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYnSENIDNEPLYNlLVG 469

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  496 KKPGGIIALLDEACMFPRSTHDTLAEKLYQTFGSHKRFTKPK---LARTDFTICHYAGDVTYQTELFLDKNKDYVVGEHQ 572
Cdd:cd14938    470 PTEGSLFSLLENVSTKTIFDKSNLHSSIIRKFSRNSKYIKKDditGNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFI 549

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  573 SLMNSSDC----SFVSSLFPKSREESSKSSKFSSIGSQFK------------------QQLQSLLETLNTTEPHYIRCVK 630
Cdd:cd14938    550 DMVKQSENeymrQFCMFYNYDNSGNIVEEKRRYSIQSALKlfkrrydtknqmavsllrNNLTELEKLQETTFCHFIVCMK 629

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  631 PnNVLKPEI--FENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILAPEATERsfdevdaCKKLLA--RVDLK 706
Cdd:cd14938    630 P-NESKRELcsFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNEDLKEK-------VEALIKsyQISNY 701

                          730
                   ....*....|.
gi 1063705616  707 GFQIGKTKVFL 717
Cdd:cd14938    702 EWMIGNNMIFL 712
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
 96-219 4.29e-36

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: 135.16  E-value: 4.29e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   96 ILIAVNPFKRLPHLYGNEIMEQYKGTDFGELSPHPFAVADSAYRKMINEGVSQAILVSGESGAGKTESTKMLMQYLA--- 172
Cdd:cd01363      1 VLVRVNPFKELPIYRDSKIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLAsva 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1063705616  173 ----------YMGGKAESEGRSvEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEI 219
Cdd:cd01363     81 fnginkgeteGWVYLTEITVTL-EDQILQANPILEAFGNAKTTRNENSSRFGKFIEI 136
MYSc_Myo33 cd14894
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ...
 80-665 1.09e-32

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: 138.34  E-value: 1.09e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616   80 LKARYNANEIYTYTGNILIAV-NPFK-----RLPHLYGNEIMEQYKGTDFGE--LSPHPFAVADSAYRKM---------- 141
Cdd:cd14894      7 LTSRFDDDRIYTYINHHTMAVmNPYRllqtaRFTSIYDEQVVLTYADTANAEtvLAPHPFAIAKQSLVRLffdnehtmpl 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  142 ---------INEGVSQAILVSGESGAGKTESTKMLMQYLAYMGGKAESEG------------------------------ 182
Cdd:cd14894     87 pstissnrsMTEGRGQSLFLCGESGSGKTELAKDLLKYLVLVAQPALSKGseetckvsgstrqpkiklftsstkstiqmr 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  183 ----RSV--------------------------------------------------------EQQ-------------- 188
Cdd:cd14894    167 teeaRTIalleakgvekyeivlldlhperwdemtsvsrskrlpqvhvdglffgfyeklehledEEQlrmyfknphaakkl 246

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  189 --VLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFNH-----MGRISGAAIRTYLLERSRVCQV------SDPERNYHCF 255
Cdd:cd14894    247 siVLDSNIVLEAFGHATTSMNLNSSRFGKMTTLQVAFglhpwEFQICGCHISPFLLEKSRVTSErgresgDQNELNFHIL 326

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  256 YMLCAAPEQETERYQLGKP--------STFHYLNQSNcHALDAI--------DDSKEYLATRKAMDVVGISPEEQDAIFR 319
Cdd:cd14894    327 YAMVAGVNAFPFMRLLAKElhldgidcSALTYLGRSD-HKLAGFvskedtwkKDVERWQQVIDGLDELNVSPDEQKTIFK 405

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  320 VVAAILHLGNIEFAKSEESdGAEPKDDKSRFHL--KVAAKLFMCDEKALENSLCNR--VMVTRGESITKPLDPGSAALSR 395
Cdd:cd14894    406 VLSAVLWLGNIELDYREVS-GKLVMSSTGALNApqKVVELLELGSVEKLERMLMTKsvSLQSTSETFEVTLEKGQVNHVR 484

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  396 DALAKIVYSKLFDWLVTKIN------------NSIGQDSSSK-----YIIGVLDIYGFESFKTNSFEQFCINLTNEKLqq 458
Cdd:cd14894    485 DTLARLLYQLAFNYVVFVMNeatkmsalstdgNKHQMDSNASapeavSLLKIVDVFGFEDLTHNSLDQLCINYLSEKL-- 562

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  459 hfnqhvFKMEQEEYTKEEIDWSYIEFIDNQDVLDLIEKKPGGIIALLDEAC------------------MFPRSTHDTLA 520
Cdd:cd14894    563 ------YAREEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASLEELTilhqsenmnaqqeekrnkLFVRNIYDRNS 636

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  521 EKLYQ---TFGSHKRFTKPKLARTDFTICHYAGDVTYQTELFLDKNKDYVVGEHQSLMNSSDCS-FVSSLFPKSREESSK 596
Cdd:cd14894    637 SRLPEpprVLSNAKRHTPVLLNVLPFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSShFCRMLNESSQLGWSP 716

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  597 SSKFSSIGS-------------QFKQQLQSLLETLNTTEPHYIRCVKPNNVLKPEIFENVNVLHQLRCGGV---MEAIRI 660
Cdd:cd14894    717 NTNRSMLGSaesrlsgtksfvgQFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLirqMEICRN 796


                   ....*
gi 1063705616  661 SCAGY 665
Cdd:cd14894    797 SSSSY 801
Myo5-like_CBD cd14945
Cargo binding domain of myosin 5 and similar proteins; Class V myosins are well studied ...
 1281-1699 1.22e-28

Cargo binding domain of myosin 5 and similar proteins; Class V myosins are well studied unconventional myosins, represented by three paralogs (Myo5 a,b,c) in vertebrates and two (myo2 and myo4) in fungi and related to plant class XI myosins. Their C-terminal cargo binding domains is important for the binding of a diverse set of cargos, including membrane vesicles, organelles, proteins and mRNA. MyoV-CBDs interact with several adaptor proteins that in turn interact with the cargo.


Pssm-ID: 271253 [Multi-domain]  Cd Length: 288  Bit Score: 117.50  E-value: 1.22e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1281 DVLLKCVSKNVGFSHG--KPVAAFTIYKCLIHWKLF--EAEKTSVFDRIVPIFGSAIENPEDDSN-LAYWLTNTSTLLFL 1355
Cdd:cd14945      4 DSLLRGIVTDFEPSSGdhKLTPAYILYLCIRHAASNglTGQSTSLLNKVLKTIQQVVQQHNDDMQlLAFWLSNASELLYF 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1356 LQRSLKSHSTTGASPKKPPQptsffgrmtqgfrspssaslsgdvvqQVDARYPALLFKQQLTAYIETIYGIFQENVKRKL 1435
Cdd:cd14945     84 LKQDSKLYGAAGEAPQKEEE--------------------------QKLTVSDLNELKQDLEAVSIKIYQQALKYLNKNL 137

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1436 APvlssciqglkdsshefsaetlsaesseqnspekpseenppeklsednssgklsedylaakpsednspakpseensqak 1515
Cdd:cd14945    138 QP------------------------------------------------------------------------------ 139

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1516 lsevnpqakpsaenslakpseenspteTWQDVIGLLNQLLGTLKKNYVPLFLAQKIFCQTFQDINVQLFNSLL-QRECCT 1594
Cdd:cd14945    140 ---------------------------KIRDIVKFLNSFLDLLKSFHVHPEIRSQVFTQLFSFINARLFNQLItKKDALS 192

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1595 FIMGKKVNVWLNELESWCSQATEDfvGSSWDELKNTRQALVLLVTEQKsTITYDDLTTNLCPALSTQQLYRICTLCKIDD 1674
Cdd:cd14945    193 WSRGMQIRANISRLEEWCEGRGLE--HLAVDFLSKLIQAVQLLQLKKY-TQEDIEILCELCPSLNPAQLQAILTQYQPAN 269

                          410       420
                   ....*....|....*....|....*
gi 1063705616 1675 HEdqnVSPDVISNLKllvTDEDEDS 1699
Cdd:cd14945    270 YG---ESPVPKEILR---TLAAEVS 288
DIL pfam01843
DIL domain; The DIL domain has no known function.
 1570-1674 8.78e-24

DIL domain; The DIL domain has no known function.


Pssm-ID: 460359 [Multi-domain]  Cd Length: 103  Bit Score: 97.28  E-value: 8.78e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1570 KIFCQTFQDINVQLFNSLLQR-ECCTFIMGKKVNVWLNELESWCSQAteDFVGSSWDELKNTRQALVLLVTeQKSTITYD 1648
Cdd:pfam01843    1 QLFSQLFYFINAELFNRLLLRkKYCSWSKGMQIRYNLSRLEEWARSN--GLESEARDHLAPLIQAAQLLQL-RKSTLEDL 77

                           90       100
                   ....*....|....*....|....*.
gi 1063705616 1649 DLTTNLCPALSTQQLYRICTLCKIDD 1674
Cdd:pfam01843   78 DSILQVCPALNPLQLHRLLTLYQPDD 103
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 885-1180 2.24e-11

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 68.89  E-value: 2.24e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  885 LQDAKTKLEKEVEELTS-CLELEKQMRMELEQVKT---------QEVEDLRSALNDMKLQLGETQVTKSEeilkLQSALQ 954
Cdd:TIGR04523  340 LNEQISQLKKELTNSESeNSEKQRELEEKQNEIEKlkkenqsykQEIKNLESQINDLESKIQNQEKLNQQ----KDEQIK 415

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  955 DMQLEFEELAKELEmtnDLAAENEQLKDLVSSLQRKIDESDSKYEETSKLSEErVKQEVPVIDqgviIKLEAENQKLKAL 1034
Cdd:TIGR04523  416 KLQQEKELLEKEIE---RLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES-LETQLKVLS----RSINKIKQNLEQK 487

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1035 VSTLEKK---IDSLDRKHDVTSSNISDqLKESASSDYEMLSNLAAENERLKALVSSLENE-NYENDGNDSPNeqkegpqm 1110
Cdd:TIGR04523  488 QKELKSKekeLKKLNEEKKELEEKVKD-LTKKISSLKEKIEKLESEKKEKESKISDLEDElNKDDFELKKEN-------- 558

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063705616 1111 LKEEILAEDFSIDD--EMTNKLAAENKDLYDLVDLLERKIDETEKKYEEASKLCEERLKQVVDTEKKYEEAS 1180
Cdd:TIGR04523  559 LEKEIDEKNKEIEElkQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLS 630
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
864-1227 2.83e-11

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 68.55  E-value: 2.83e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  864 RVKVAHRELRKLKM---------AAKETGALQDAKTKLEKEVEELTsclelekQMRMELEQvktqEVEDLRSALNDMKLQ 934
Cdd:PRK03918   366 EAKAKKEELERLKKrltgltpekLEKELEELEKAKEEIEEEISKIT-------ARIGELKK----EIKELKKAIEELKKA 434

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  935 LGETQVTK----------------------SEEILKLQSALQDMQLEFEELAKELEMTNDLAAEN---EQLKDLVSSLQR 989
Cdd:PRK03918   435 KGKCPVCGrelteehrkelleeytaelkriEKELKEIEEKERKLRKELRELEKVLKKESELIKLKelaEQLKELEEKLKK 514

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  990 -KIDESDSKYEETSKLSEERVKQEvpvidqGVIIKLEAENQKLKALVS---TLEKKIDSLDRKhdvtSSNISDQLKESAS 1065
Cdd:PRK03918   515 yNLEELEKKAEEYEKLKEKLIKLK------GEIKSLKKELEKLEELKKklaELEKKLDELEEE----LAELLKELEELGF 584

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1066 SDYEMLsnlaaeNERLKALvsslenENYENDGNDSPNEQKEGPQMLKE-EILAEDFSIDDEMTNKLAAENKDLYDLVDLL 1144
Cdd:PRK03918   585 ESVEEL------EERLKEL------EPFYNEYLELKDAEKELEREEKElKKLEEELDKAFEELAETEKRLEELRKELEEL 652

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1145 ERKIDETE-----KKYEEASKLCEERLKQVVDTEKKYEEASRLCEERLKQVVDTETKLIELKT------SMQRLEEKVSD 1213
Cdd:PRK03918   653 EKKYSEEEyeelrEEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKlekaleRVEELREKVKK 732

                          410
                   ....*....|....
gi 1063705616 1214 MEAEdkiLRQQALR 1227
Cdd:PRK03918   733 YKAL---LKERALS 743
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 871-1233 2.89e-11

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 68.51  E-value: 2.89e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  871 ELRKLKMAAKETGALQDAK----TKLEKEVEELTSCL-ELEKQMRmELEQVKTQ---EVEDLRSALNDMKLQLGETQ--- 939
Cdd:TIGR04523  125 ELNKLEKQKKENKKNIDKFlteiKKKEKELEKLNNKYnDLKKQKE-ELENELNLlekEKLNIQKNIDKIKNKLLKLElll 203

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  940 ---VTKSEEILKLQSALQDMQLEFEELAKELEMTNDlaaENEQLKDLVSSLQRKIDESDSKYEETSKLSEERVKQevpvI 1016
Cdd:TIGR04523  204 snlKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQ---EINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKE----L 276

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1017 DQ--GVIIKLEAENQKLKALVSTLEKK------------IDSLDRKHDVTSSNIS------DQLKESASSDYEMLSNLAA 1076
Cdd:TIGR04523  277 EQnnKKIKELEKQLNQLKSEISDLNNQkeqdwnkelkseLKNQEKKLEEIQNQISqnnkiiSQLNEQISQLKKELTNSES 356

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1077 EN----ERLKALVSSLENENYENDGNDSPNE---------------QKEGPQMLKEEI--LAEDFSIDDEMTNKLAAENK 1135
Cdd:TIGR04523  357 ENsekqRELEEKQNEIEKLKKENQSYKQEIKnlesqindleskiqnQEKLNQQKDEQIkkLQQEKELLEKEIERLKETII 436

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1136 DLYDLVDLLERKIDETEKKYEEASKLCEERLKQVVDTEKKYEEASRLCEERLKQVVDTETKLIELKTSMQRLEEKVSDME 1215
Cdd:TIGR04523  437 KNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLT 516

                          410       420
                   ....*....|....*....|
gi 1063705616 1216 AEDK--ILRQQALRNSASRK 1233
Cdd:TIGR04523  517 KKISslKEKIEKLESEKKEK 536
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 885-1228 6.52e-10

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 63.72  E-value: 6.52e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  885 LQDAKTKLEKEVEELTSCLELEKQMRMELEQVKtQEVEDLRSALNDMKLQLGETqvtkseeILKLQSALQDMQLEFEELA 964
Cdd:pfam06160   95 LDDIEEDIKQILEELDELLESEEKNREEVEELK-DKYRELRKTLLANRFSYGPA-------IDELEKQLAEIEEEFSQFE 166

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  965 KELEMTNDLAAEN--EQLKDLVSSLQRKIDESDSKYEETSKLSEERVKQevpvIDQGvIIKLEAENQKLKALvsTLEKKI 1042
Cdd:pfam06160  167 ELTESGDYLEAREvlEKLEEETDALEELMEDIPPLYEELKTELPDQLEE----LKEG-YREMEEEGYALEHL--NVDKEI 239

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1043 DSLDRKHDVTSSNISDQLKESASSDYEMLsnlaaeNERLKALVSSLENE----NY--ENDGN--DSPNEQKEGPQMLKEE 1114
Cdd:pfam06160  240 QQLEEQLEENLALLENLELDEAEEALEEI------EERIDQLYDLLEKEvdakKYveKNLPEieDYLEHAEEQNKELKEE 313

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1115 I--LAEDFSIDDEMTNKlaaenkdlydlVDLLERKIDETEKKYEEASKLCEErlKQVVDTE--KKYEEasrlCEERLKQV 1190
Cdd:pfam06160  314 LerVQQSYTLNENELER-----------VRGLEKQLEELEKRYDEIVERLEE--KEVAYSElqEELEE----ILEQLEEI 376

                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 1063705616 1191 vdtETKLIELKTSMQRLEEkvSDMEAEDKILR-QQALRN 1228
Cdd:pfam06160  377 ---EEEQEEFKESLQSLRK--DELEAREKLDEfKLELRE 410
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 867-1215 2.05e-09

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 62.78  E-value: 2.05e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  867 VAHRELRKLKMAAKETGALQDAKTKLEKEVEELTSCLElEKQMRMELEQVKTQEVEDLRSALNDMKLQLGETQVTKSEEI 946
Cdd:TIGR02169  668 FSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLD-ELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL 746

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  947 LKLQSALQDMQLEFEELAKEL-EMTNDLAAENEQLKDLVSSL-QRKIDESDskyEETSKLSEERVKQEvpvidqGVIIKL 1024
Cdd:TIGR02169  747 SSLEQEIENVKSELKELEARIeELEEDLHKLEEALNDLEARLsHSRIPEIQ---AELSKLEEEVSRIE------ARLREI 817

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1025 EAENQKLKALVSTLEKKIDSLDRKHDVTSSNISDqlkesassdyemlsnLAAENERLKALVSSLENEnyendgndspneq 1104
Cdd:TIGR02169  818 EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKS---------------IEKEIENLNGKKEELEEE------------- 869

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1105 kegpqmLKEeilaedfsiddemtnkLAAENKDLYDLVDLLERKIDETEKKYEEASKLCEErLKQVVDTEKKY----EEAS 1180
Cdd:TIGR02169  870 ------LEE----------------LEAALRDLESRLGDLKKERDELEAQLRELERKIEE-LEAQIEKKRKRlselKAKL 926

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 1063705616 1181 RLCEERLKQVVDTETKLIE----------LKTSMQRLEEKVSDME 1215
Cdd:TIGR02169  927 EALEEELSEIEDPKGEDEEipeeelsledVQAELQRVEEEIRALE 971
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
878-1227 3.10e-09

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 61.98  E-value: 3.10e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  878 AAKETGALQDAKTKLEKEVEELTSCLE-LEKQ------MRMELEQV------KTQEVEDLRSALNDMKLQLGETQVTK-- 942
Cdd:PRK02224   197 EEKEEKDLHERLNGLESELAELDEEIErYEEQreqareTRDEADEVleeheeRREELETLEAEIEDLRETIAETERERee 276

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  943 -SEEILKLQSALQDMQLEFEELAKELEMTN-----------DLAAENEQLKDLVS----SLQRKIDESDSKYEETSKLsE 1006
Cdd:PRK02224   277 lAEEVRDLRERLEELEEERDDLLAEAGLDDadaeavearreELEDRDEELRDRLEecrvAAQAHNEEAESLREDADDL-E 355

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1007 ERVKQEVPVIDQgviikLEAENQKLKALVSTLEKKIDSLDRKHDVTS---SNISDQLKESASSDYEMLSNLAAENERLKA 1083
Cdd:PRK02224   356 ERAEELREEAAE-----LESELEEAREAVEDRREEIEELEEEIEELRerfGDAPVDLGNAEDFLEELREERDELREREAE 430

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1084 LVSSLENEnyENDGNDSPNEQKEGP-----QMLKEEILAEDFSIDDEMTNKLAAENKDLYDLVDLLERKID------ETE 1152
Cdd:PRK02224   431 LEATLRTA--RERVEEAEALLEAGKcpecgQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLEraedlvEAE 508

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1153 KKYE---EASKLCEERLKQVVDT--------EKKYEEASRL-----------------CEERLKQVVDTETKLIELKTSM 1204
Cdd:PRK02224   509 DRIErleERREDLEELIAERRETieekreraEELRERAAELeaeaeekreaaaeaeeeAEEAREEVAELNSKLAELKERI 588

                          410       420
                   ....*....|....*....|....
gi 1063705616 1205 QRLEEKVSDMEA-EDKILRQQALR 1227
Cdd:PRK02224   589 ESLERIRTLLAAiADAEDEIERLR 612
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 864-1199 6.38e-09

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: 61.23  E-value: 6.38e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  864 RVKVAHRELRK----LKMAAKETGALQDAKTKLEkEVEELTSCLELEkQMRMELEQVKTQEvedlrSALNDMKLQLGETQ 939
Cdd:TIGR02168  190 RLEDILNELERqlksLERQAEKAERYKELKAELR-ELELALLVLRLE-ELREELEELQEEL-----KEAEEELEELTAEL 262

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  940 VTKSEEILKLQSALQDMQLEFEELAKEL--------EMTNDLAAENEQLKDLVSSLQRK---IDESDSKYEETSKLSEER 1008
Cdd:TIGR02168  263 QELEEKLEELRLEVSELEEEIEELQKELyalaneisRLEQQKQILRERLANLERQLEELeaqLEELESKLDELAEELAEL 342

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1009 VKQEVPVidQGVIIKLEAENQKLKALVSTLEKKIDSLDRKHDVTSSNIsDQLKESASSDYEMLSNLAAENERLKALVSSL 1088
Cdd:TIGR02168  343 EEKLEEL--KEELESLEAELEELEAELEELESRLEELEEQLETLRSKV-AQLELQIASLNNEIERLEARLERLEDRRERL 419

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1089 ENENYENDGNDSPNEQKEGPQML--KEEILAEDFSIDDEMTNKLAAenkdLYDLVDLLERKIDETEKKYEEASKLCE--E 1164
Cdd:TIGR02168  420 QQEIEELLKKLEEAELKELQAELeeLEEELEELQEELERLEEALEE----LREELEEAEQALDAAERELAQLQARLDslE 495

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 1063705616 1165 RLKQVVDTEKKYEEASRLCEERLKQVVDTETKLIE 1199
Cdd:TIGR02168  496 RLQENLEGFSEGVKALLKNQSGLSGILGVLSELIS 530
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 870-1221 6.91e-09

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 60.89  E-value: 6.91e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  870 RELRKLKMAAKETGALQDAktkLEKEVEELTSCL-----ELEKQMRmELEQVKT------QEVEDLRSALNDMkLQLGET 938
Cdd:pfam05483  296 KELEDIKMSLQRSMSTQKA---LEEDLQIATKTIcqlteEKEAQME-ELNKAKAahsfvvTEFEATTCSLEEL-LRTEQQ 370

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  939 QVTKSEEILKLQS-ALQDMQLEFEELAKeleMTNDLAAENEQLKDLVSSLQRKIDESdskyEETSKLSEErvkqevpvid 1017
Cdd:pfam05483  371 RLEKNEDQLKIITmELQKKSSELEEMTK---FKNNKEVELEELKKILAEDEKLLDEK----KQFEKIAEE---------- 433

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1018 qgviikLEAENQKLKALVSTLEKKIDSLDRKHDVTSSN----------ISDQLKESASSDYEMLSN---LAAENERLKAL 1084
Cdd:pfam05483  434 ------LKGKEQELIFLLQAREKEIHDLEIQLTAIKTSeehylkevedLKTELEKEKLKNIELTAHcdkLLLENKELTQE 507

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1085 VS--SLENENYENDGNdspNEQKEGPQMLKE-EILAEDfsiDDEMTNKLAAENKDLydlvdllERKIDETEKKYEEASKL 1161
Cdd:pfam05483  508 ASdmTLELKKHQEDII---NCKKQEERMLKQiENLEEK---EMNLRDELESVREEF-------IQKGDEVKCKLDKSEEN 574

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1162 CEERLKQVVDTEKKYEEASRLCEERLKQVVDTETKLIELKTSMQRLEEKVSdmeAEDKIL 1221
Cdd:pfam05483  575 ARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGS---AENKQL 631
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 885-1234 7.86e-09

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 60.85  E-value: 7.86e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  885 LQDAKTKLE---KEVEELTSCL-ELEKQM-RMELEQVKTQEVEDLRSALNDMKLQLGETQVTKSE-EILKLQSALQDMQL 958
Cdd:TIGR02169  172 KEKALEELEeveENIERLDLIIdEKRQQLeRLRREREKAERYQALLKEKREYEGYELLKEKEALErQKEAIERQLASLEE 251

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  959 EFEELAKELEmtnDLAAENEQLKDLVSSLQRKIDE--SDSKYEETSKLSEERVKQEVPvidQGVIIKLEAENQKLKALVS 1036
Cdd:TIGR02169  252 ELEKLTEEIS---ELEKRLEEIEQLLEELNKKIKDlgEEEQLRVKEKIGELEAEIASL---ERSIAEKERELEDAEERLA 325

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1037 TLEKKIDSLDRKHDVTSSNISDQLKESASSDYEmLSNLAAENERLKALVSSLENENYE-NDGNDSPNEQKEGPQMLKEEI 1115
Cdd:TIGR02169  326 KLEAEIDKLLAEIEELEREIEEERKRRDKLTEE-YAELKEELEDLRAELEEVDKEFAEtRDELKDYREKLEKLKREINEL 404

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1116 LAEDFSIDDE---MTNKLAAENKDLYDLVDLLERKIDETEKKYEEASKLcEERLKQVVDTEKKYEeasrlceerlKQVVD 1192
Cdd:TIGR02169  405 KRELDRLQEElqrLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ-EWKLEQLAADLSKYE----------QELYD 473

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 1063705616 1193 TETKLIELKTSMQRLEEKVSDMEAEDKILRQQALRNSASRKM 1234
Cdd:TIGR02169  474 LKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEV 515
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 870-1233 1.08e-08

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: 60.57  E-value: 1.08e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  870 RELRKLK----MAAKETGALQDAKTKLEKEVEELTSCLELEKQMRMELEQV------KTQEVEDLrsaLNDMKLQLGE-- 937
Cdd:pfam01576   12 EELQKVKerqqKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMrarlaaRKQELEEI---LHELESRLEEee 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  938 --TQVTKSEEiLKLQSALQDM--QLEFEELA---------------KELE--------MTNDLAAENEQLKDLVSSLQRK 990
Cdd:pfam01576   89 erSQQLQNEK-KKMQQHIQDLeeQLDEEEAArqklqlekvtteakiKKLEedillledQNSKLSKERKLLEERISEFTSN 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  991 IDESDSKYEETSKLseeRVKQEVpvidqgVIIKLEAENQKLKALVSTLEKkidsLDRKHDVTSSNISDQLKESASSDYEM 1070
Cdd:pfam01576  168 LAEEEEKAKSLSKL---KNKHEA------MISDLEERLKKEEKGRQELEK----AKRKLEGESTDLQEQIAELQAQIAEL 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1071 LSNLAAENERLKALVSSLENENyeNDGNDSPNEQKEGPQMLKEeiLAEDFSIDDEMTNKLAAENKDLYD----LVDLLER 1146
Cdd:pfam01576  235 RAQLAKKEEELQAALARLEEET--AQKNNALKKIRELEAQISE--LQEDLESERAARNKAEKQRRDLGEeleaLKTELED 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1147 KIDETEKKYEEASKLCEE--RLKQVVDTEKKYEEASrLCEERLK--QVVDTETKLIE--------LKTSMQRLEEKVSDM 1214
Cdd:pfam01576  311 TLDTTAAQQELRSKREQEvtELKKALEEETRSHEAQ-LQEMRQKhtQALEELTEQLEqakrnkanLEKAKQALESENAEL 389

                          410
                   ....*....|....*....
gi 1063705616 1215 EAEDKILRQQALRNSASRK 1233
Cdd:pfam01576  390 QAELRTLQQAKQDSEHKRK 408
PTZ00121 PTZ00121
MAEBL; Provisional
 868-1249 1.75e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 59.77  E-value: 1.75e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  868 AHRELRKLKMAAKETGALQDAKTK---LEKEVEELTSCLELEKQMRmelEQVKTQEV----EDLRSALNDMK----LQLG 936
Cdd:PTZ00121  1396 AKKKAEEDKKKADELKKAAAAKKKadeAKKKAEEKKKADEAKKKAE---EAKKADEAkkkaEEAKKAEEAKKkaeeAKKA 1472

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  937 ETQVTKSEEILKLQSALQdmqlEFEELAKELEMTNDLAAENEQLKDLVSSLQRKIDESDSKYEETSKLSEERVKQEVPVI 1016
Cdd:PTZ00121  1473 DEAKKKAEEAKKADEAKK----KAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKA 1548

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1017 DQgviIKLEAENQKLKALVSTLEKKIDSLDRKHDVTSSNISDQLKESASSDYEMLSNLA----------AENERLKALVS 1086
Cdd:PTZ00121  1549 DE---LKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEkkmkaeeakkAEEAKIKAEEL 1625

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1087 SLENE---NYENDGNDSPNEQKEGPQMLKEEilaEDFSIDDEMTNKLAAENKDLYDLVdlleRKIDETEKKYEEASKLCE 1163
Cdd:PTZ00121  1626 KKAEEekkKVEQLKKKEAEEKKKAEELKKAE---EENKIKAAEEAKKAEEDKKKAEEA----KKAEEDEKKAAEALKKEA 1698

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1164 ERLKQVVDTEKKYEEASRLCEERLKQVVDTETKLIELKTSMQRLEEKVSDMEAEDKILRQQALRNSASRKMSPQVSFTRP 1243
Cdd:PTZ00121  1699 EEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKE 1778


                   ....*.
gi 1063705616 1244 PPVENG 1249
Cdd:PTZ00121  1779 AVIEEE 1784
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
864-1233 3.51e-08

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 58.24  E-value: 3.51e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  864 RVKVAHRELRKLKMAAKETGALQDAKTKLEKEVEELTSCLELEKQMRMELEQVK-----TQEVEDLRSALNDMKLQLgET 938
Cdd:COG4717     72 ELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLqllplYQELEALEAELAELPERL-EE 150

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  939 QVTKSEEILKLQSALQDMQLEFEELAKELEMT-------------------NDLAAENEQLKDLVSSLQRKIDESDSKYE 999
Cdd:COG4717    151 LEERLEELRELEEELEELEAELAELQEELEELleqlslateeelqdlaeelEELQQRLAELEEELEEAQEELEELEEELE 230

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1000 ETSKLSE-----ERVKQE-----------------------------VPVIDQGVIIKLEAENQKLKALVSTLEKKIDSL 1045
Cdd:COG4717    231 QLENELEaaaleERLKEArlllliaaallallglggsllsliltiagVLFLVLGLLALLFLLLAREKASLGKEAEELQAL 310

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1046 DRKHDVTSSNISDQLKE---SASSDYEMLSNLAAENERLKALVSSLENENYENDGNDSPNEQKEgpqmLKEEILAEDfsi 1122
Cdd:COG4717    311 PALEELEEEELEELLAAlglPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAA----LLAEAGVED--- 383

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1123 DDEMTNKLAA--ENKDLYDLVDLLERKIDETEKKYEE-ASKLCEERLKQvvdTEKKYEEASRLCEERLKQVvdtETKLIE 1199
Cdd:COG4717    384 EEELRAALEQaeEYQELKEELEELEEQLEELLGELEElLEALDEEELEE---ELEELEEELEELEEELEEL---REELAE 457

                          410       420       430
                   ....*....|....*....|....*....|....
gi 1063705616 1200 LKTSMQRLEEKVSDMEAEDKILRQQALRNSASRK 1233
Cdd:COG4717    458 LEAELEQLEEDGELAELLQELEELKAELRELAEE 491
Myo5p-like_CBD_fungal cd15474
cargo binding domain of fungal myosin V -like proteins; Yeast myosin V travels along actin ...
 1517-1714 7.81e-08

cargo binding domain of fungal myosin V -like proteins; Yeast myosin V travels along actin cables, actin filaments that are bundled by fimbrin, in the presence of tropomyosin. This is in contrast to the other vertebrate class V myosins. Like other class V myosins, fungal myosin 2 and 4 contain a C-terminal cargo binding domain. In case of Myo4 it has been shown to bind to the adapter protein She3p (Swi5p-dependent HO expression 3), which in turn anchors myosin 4 to its cargos, zip-coded mRNP (messenger ribonucleoprotein particles) and tER (tubular endoplasmic reticulum). Myo 2 binds to Vac17, vacuole-specific cargo adaptor, and Mmr1, mitochondria-specific cargo adaptor. Both adaptors bind competitivly at the same site.


Pssm-ID: 271258  Cd Length: 352  Bit Score: 56.27  E-value: 7.81e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1517 SEVNPQAKPSAENSLAKPSEENSPTETWQDVIGLLNQLLGTLKKNYVPLFLAQKIFCQTFQDINVQLFNSLL-QRECCTF 1595
Cdd:cd15474    154 VLVLLTSLDLSELIDLNKEFFNKPKKKMADLITFLNEVYDLLQSFSVQPELLNAIVSSTLQYINVEAFNSLItKRSALSW 233

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1596 IMGKKVNVWLNELESWCSQATEDFVGSSWDELKNTrqalVLLVTEQKSTITYDDLTTNLCPALSTQQLYRICTLCKIDDH 1675
Cdd:cd15474    234 KRGSQISYNVSRLKEWCHQHGLSDANLQLEPLIQA----SKLLQLRKDDENDFKIILSVCYALNPAQIQKLLDKYQPANY 309

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1063705616 1676 EDQnVSPDVISNLKLLVTDEDEDsrSFLLDNNSSIPFAA 1714
Cdd:cd15474    310 EAP-VPKEFLNALEKLIKKENLS--LPGRKNNSKMEIPE 345
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
872-1217 9.77e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 57.00  E-value: 9.77e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  872 LRKLKMAAKETGALQDAKTKLEKEVEELTSCLELEKQMRMELEQVKtQEVEDLRSALNDMKLQLGET--QVTKSEEILKL 949
Cdd:PRK03918   206 LREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLE-GSKRKLEEKIRELEERIEELkkEIEELEEKVKE 284

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  950 QSALQDMQLEFEELAKELEMTND----LAAENEQLKDLVSSLQRKIDESDSKYEETSKLSEER--VKQEVPVIDQGV--- 1020
Cdd:PRK03918   285 LKELKEKAEEYIKLSEFYEEYLDelreIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLkeLEKRLEELEERHely 364

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1021 --IIKLEAENQKLKALVS-----TLEKKIDSLDRKhdvtssniSDQLKESASSDYEMLSNLAAENERLKALVSSLEN--- 1090
Cdd:PRK03918   365 eeAKAKKEELERLKKRLTgltpeKLEKELEELEKA--------KEEIEEEISKITARIGELKKEIKELKKAIEELKKakg 436

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1091 ------------------ENYENDGNDSPNEQKEGPQMLkEEILAEDFSIDDEMTN-KLAAENKDLYDLVDLLERK---- 1147
Cdd:PRK03918   437 kcpvcgrelteehrkellEEYTAELKRIEKELKEIEEKE-RKLRKELRELEKVLKKeSELIKLKELAEQLKELEEKlkky 515

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063705616 1148 -IDETEKKYEEAsklceERLKQVVDTEKKyeEASRLcEERLKQVVDTETKLIELKTSMQRLEEKVSDMEAE 1217
Cdd:PRK03918   516 nLEELEKKAEEY-----EKLKEKLIKLKG--EIKSL-KKELEKLEELKKKLAELEKKLDELEEELAELLKE 578
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 882-1225 1.05e-07

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 57.05  E-value: 1.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  882 TGALQDAKTKLE---KEVEELTSCLELEKQmrmELEQVKTQE--VEDLRSALNDMKLQLGETQvtKSEEILKLQ------ 950
Cdd:pfam15921  502 TASLQEKERAIEatnAEITKLRSRVDLKLQ---ELQHLKNEGdhLRNVQTECEALKLQMAEKD--KVIEILRQQienmtq 576

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  951 ------SALQDMQLEFEELAKELemtNDLAAENEQLKDLVSSLQRKIDESDSKyeeTSKLSEERVKqevpVIDQG----- 1019
Cdd:pfam15921  577 lvgqhgRTAGAMQVEKAQLEKEI---NDRRLELQEFKILKDKKDAKIRELEAR---VSDLELEKVK----LVNAGserlr 646

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1020 VIIKLEAENQKLKALVSTLEKKIDSLDRKHDVTSSNISDQlkesaSSDYEMLSNlaaeneRLKALVSSLENENYENDGND 1099
Cdd:pfam15921  647 AVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNK-----SEEMETTTN------KLKMQLKSAQSELEQTRNTL 715

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1100 SPNEQKEGPQMlkeeilaedfSIDDEMTNKLAAENKDlydlVDLLERKIDETEKKYEEASKlceerlkqvvdtEKKY--E 1177
Cdd:pfam15921  716 KSMEGSDGHAM----------KVAMGMQKQITAKRGQ----IDALQSKIQFLEEAMTNANK------------EKHFlkE 769

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1063705616 1178 EASRLCEErLKQVVDTETKL---IE-LKTSMQRLEEKVSDME-AEDKILRQQA 1225
Cdd:pfam15921  770 EKNKLSQE-LSTVATEKNKMageLEvLRSQERRLKEKVANMEvALDKASLQFA 821
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 870-1196 1.29e-07

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 56.67  E-value: 1.29e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  870 RELRKLKMAAKETGALQDAKTKLEKEVEELTSCLELEKQMR-----MELEQVKTQE------------------VEDLRS 926
Cdd:pfam05557  204 KELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYReeaatLELEKEKLEQelqswvklaqdtglnlrsPEDLSR 283

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  927 ---ALNDMKLQLGETQVTKSEEILKLQSALQDMQLEFEELAKELEmtnDLAAENEQLKDLVSSLQRK-------ID---- 992
Cdd:pfam05557  284 rieQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIE---DLNKKLKRHKALVRRLQRRvllltkeRDgyra 360

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  993 -----ESDSKYEETSKLSEERVK------QEVPVIDQGV---IIKLEAENQKLKALVSTLEKKIDSLDRKHDVTSSNISd 1058
Cdd:pfam05557  361 ilesyDKELTMSNYSPQLLERIEeaedmtQKMQAHNEEMeaqLSVAEEELGGYKQQAQTLERELQALRQQESLADPSYS- 439

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1059 qlKESASSDYEMLSNLAAENERLKALVSSLEN--ENYENDGNDSPNEQK-----EGPQMLKEEILAedfsiddEMTNKLA 1131
Cdd:pfam05557  440 --KEEVDSLRRKLETLELERQRLREQKNELEMelERRCLQGDYDPKKTKvlhlsMNPAAEAYQQRK-------NQLEKLQ 510

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063705616 1132 AENKDLYDLVDLLERKIDETEKKYEEASKLCEERLKQVvdteKKYEEASRLCEERLKQVVDTETK 1196
Cdd:pfam05557  511 AEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDL----RKELESAELKNQRLKEVFQAKIQ 571
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 873-1223 1.39e-07

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: 56.72  E-value: 1.39e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  873 RKLKMAAKETGALQDAKTKLEKEVEELTSCLElEKQMRME-LEQVKT---QEVEDLRSALNDMKlqlgetqvtkseeilK 948
Cdd:pfam01576  531 KKLEEDAGTLEALEEGKKRLQRELEALTQQLE-EKAAAYDkLEKTKNrlqQELDDLLVDLDHQR---------------Q 594

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  949 LQSALQDMQLEFEE-LAKELEMTNDLAAENEQLkdlvsslqrkidESDSKYEETSKLSEERVKQEVpvidQGVIIKLEAE 1027
Cdd:pfam01576  595 LVSNLEKKQKKFDQmLAEEKAISARYAEERDRA------------EAEAREKETRALSLARALEEA----LEAKEELERT 658

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1028 NQKLKA----LVSTlekKIDSLDRKHDVTSSN--ISDQLKESASSDYEMLSNL-AAENERLKALVS-SLENENYEND--G 1097
Cdd:pfam01576  659 NKQLRAemedLVSS---KDDVGKNVHELERSKraLEQQVEEMKTQLEELEDELqATEDAKLRLEVNmQALKAQFERDlqA 735

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1098 NDSPNEQKEgPQMLKE--EILAEdfsIDDEMTNK---LAAENKDLYDLVDlLERKIDETEKKYEEASKLCEERLKQVVDT 1172
Cdd:pfam01576  736 RDEQGEEKR-RQLVKQvrELEAE---LEDERKQRaqaVAAKKKLELDLKE-LEAQIDAANKGREEAVKQLKKLQAQMKDL 810

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1063705616 1173 EKKYEEASRLCEERLKQVVDTETKLIELKTSMQRLEEkvsDMEAEDKILRQ 1223
Cdd:pfam01576  811 QRELEEARASRDEILAQSKESEKKLKNLEAELLQLQE---DLAASERARRQ 858
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 872-1209 2.05e-07

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 56.21  E-value: 2.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  872 LRKLKMAAKETGALQDAKTKLEKEVEELTSCLELEKQMRM----------ELEQVKTQEVEDLRSALNDM--KLQLGETQ 939
Cdd:TIGR00606  500 KKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMltkdkmdkdeQIRKIKSRHSDELTSLLGYFpnKKQLEDWL 579

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  940 VTKSEEILKLQSALQDMQLEfeeLAKELEMTNDLAAENEQLKDLVSSLQRKIDESDSKYEETSKLseERVKQEVP----- 1014
Cdd:TIGR00606  580 HSKSKEINQTRDRLAKLNKE---LASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDL--ERLKEEIEksskq 654

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1015 ---------VIDQgVIIKLEAENQ--------------KLKALVSTLEKKIDSLDRKHDVTSSNISDQLKES------AS 1065
Cdd:TIGR00606  655 ramlagataVYSQ-FITQLTDENQsccpvcqrvfqteaELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRdemlglAP 733

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1066 SDYEMLSNLAAENERLKALVSSLENENYENDGNDSPNEQKEGPQMLKEEiLAEDFSIDDEMTNKLAAENKDLYDLVDLLE 1145
Cdd:TIGR00606  734 GRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEE-SAKVCLTDVTIMERFQMELKDVERKIAQQA 812

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063705616 1146 RKID--ETEKKYEEASKLCEERLKQVVDTEKKYEEASRLCEERLKQVVDTETKLIELKTSMQRLEE 1209
Cdd:TIGR00606  813 AKLQgsDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGT 878
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
864-1233 3.54e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 55.46  E-value: 3.54e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  864 RVKVAHRELRKLKMAAKETgalqdakTKLEKEVEELTSCLELEKQMRMELEQVKtQEVEDLRSALNDMKLQL--GETQVT 941
Cdd:PRK03918   267 RIEELKKEIEELEEKVKEL-------KELKEKAEEYIKLSEFYEEYLDELREIE-KRLSRLEEEINGIEERIkeLEEKEE 338

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  942 KSEEILKLQSALQDMQLEFEELAKELEMTNDLAAENEQLKDLVSSLQrkIDESDSKYEETSKLSEERVKQEVPVIDQgvI 1021
Cdd:PRK03918   339 RLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLT--PEKLEKELEELEKAKEEIEEEISKITAR--I 414

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1022 IKLEAENQKLKALVSTLEK----------KIDSLDRKHDVTS-----SNISDQLKESASSDYEMLSNL-----AAENER- 1080
Cdd:PRK03918   415 GELKKEIKELKKAIEELKKakgkcpvcgrELTEEHRKELLEEytaelKRIEKELKEIEEKERKLRKELrelekVLKKESe 494

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1081 ----------LKALVSSLENENYENDGNDSPN--EQKEGPQMLKEEI--LAEDFSIDDEMTNKLAAENKDLYDL------ 1140
Cdd:PRK03918   495 liklkelaeqLKELEEKLKKYNLEELEKKAEEyeKLKEKLIKLKGEIksLKKELEKLEELKKKLAELEKKLDELeeelae 574

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1141 ------------VDLLERKIDETEKKYEEASKLCEERlKQVVDTEKKYEEASRLCEERLKQVVDTETKLIELKTSMQRLE 1208
Cdd:PRK03918   575 llkeleelgfesVEELEERLKELEPFYNEYLELKDAE-KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELE 653

                          410       420
                   ....*....|....*....|....*
gi 1063705616 1209 EKVSDMEAEDKILRQQALRNSASRK 1233
Cdd:PRK03918   654 KKYSEEEYEELREEYLELSRELAGL 678
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 874-1235 3.76e-07

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: 55.18  E-value: 3.76e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  874 KLKMAAKETGALQDAKTKLEKEVEELTSCLELEKQMRMELE-------------QVKTQEVEDLRSALND--MKLQL--- 935
Cdd:pfam01576  364 QLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEhkrkklegqlqelQARLSESERQRAELAEklSKLQSele 443

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  936 --------GETQVTK-SEEILKLQSALQDMQlefEELAKELEMTNDLAAENEQLKDLVSSLQRKIDESDSKYEETSK--- 1003
Cdd:pfam01576  444 svssllneAEGKNIKlSKDVSSLESQLQDTQ---ELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERqls 520

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1004 -----LSEERVKQEVpviDQGVIIKLEAENQKLK----ALVSTLEKKIDSLDRkhdvtssnisdqLKESASSDYEMLSNL 1074
Cdd:pfam01576  521 tlqaqLSDMKKKLEE---DAGTLEALEEGKKRLQreleALTQQLEEKAAAYDK------------LEKTKNRLQQELDDL 585

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1075 AAENERLKALVSSLEnenyendgndspNEQKEGPQMLKEEILAEDFSIDDEMTNKLAAENKDLYDLVdlLERKIDE---T 1151
Cdd:pfam01576  586 LVDLDHQRQLVSNLE------------KKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALS--LARALEEaleA 651

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1152 EKKYEEASKLCEERLKQVV----DTEKKYEEAsrlceERLKQVVdtETKLIELKTSMQRLEEKVSdmEAEDKILR----Q 1223
Cdd:pfam01576  652 KEELERTNKQLRAEMEDLVsskdDVGKNVHEL-----ERSKRAL--EQQVEEMKTQLEELEDELQ--ATEDAKLRlevnM 722

                          410
                   ....*....|..
gi 1063705616 1224 QALRNSASRKMS 1235
Cdd:pfam01576  723 QALKAQFERDLQ 734
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 880-1225 5.20e-07

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 54.73  E-value: 5.20e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  880 KETGALQDAKT-KLEKEVEEltsclelEKQMRMELeqvkTQEVEDLRSALNDMKLQLG----ETQVTKSEEILKLQSALQ 954
Cdd:pfam05483  161 KETCARSAEKTkKYEYEREE-------TRQVYMDL----NNNIEKMILAFEELRVQAEnarlEMHFKLKEDHEKIQHLEE 229

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  955 DMQLEFEELAKELEMTNDLAAENE-QLKDLVSSLQRKIDESDsKYEETSKLSEERVKQEVPVIDQgviIKLEAENQKLKA 1033
Cdd:pfam05483  230 EYKKEINDKEKQVSLLLIQITEKEnKMKDLTFLLEESRDKAN-QLEEKTKLQDENLKELIEKKDH---LTKELEDIKMSL 305

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1034 LVSTLEKKidSLDRKHDVTSSNISdQLKESASSDYEMLSNLAAENE----RLKALVSSLEN---------ENYENDGNDS 1100
Cdd:pfam05483  306 QRSMSTQK--ALEEDLQIATKTIC-QLTEEKEAQMEELNKAKAAHSfvvtEFEATTCSLEEllrteqqrlEKNEDQLKII 382

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1101 PNE-QKEGPQMLKEEILAEDFSIDDEMTNKLAAENKDLYDLVDLLERKIDETEKKYEEASKLCEERLKQVVDTEKKYEEA 1179
Cdd:pfam05483  383 TMElQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAI 462

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 1063705616 1180 SRLCEERLKQVVDTETKLIELKTSMQRLEEKVSDMEAEDKILRQQA 1225
Cdd:pfam05483  463 KTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEA 508
Myosin_N pfam02736
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ...
 7-50 5.93e-07

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


Pssm-ID: 460670  Cd Length: 45  Bit Score: 47.43  E-value: 5.93e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1063705616    7 TVGSQVWVEDPDEAWLDGEVVEANGQEIKVNCQT-KTVVAKVNAV 50
Cdd:pfam02736    1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVETEDgKTVTVKKDDV 45
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 881-1216 6.30e-07

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: 54.41  E-value: 6.30e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  881 ETGALQDAKTKLEKEVEELTSCLELEKQMRMEL-EQVKTQEVEDLRsalnDMKLQLGETQVTKSEEIlklqSALQDMQLE 959
Cdd:pfam01576  707 ELQATEDAKLRLEVNMQALKAQFERDLQARDEQgEEKRRQLVKQVR----ELEAELEDERKQRAQAV----AAKKKLELD 778

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  960 FEELAKELEMTNDLAAEN-EQLKDL---VSSLQRKIDESDSKYEE---TSKLSEERVKQevpvidqgviikLEAENQKLK 1032
Cdd:pfam01576  779 LKELEAQIDAANKGREEAvKQLKKLqaqMKDLQRELEEARASRDEilaQSKESEKKLKN------------LEAELLQLQ 846

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1033 ALVSTLEKkidsLDRKHDVTSSNISDQLKESASSDyemlSNLAAENERLKALVSSLENENYENDGNdspneqkegpqmlk 1112
Cdd:pfam01576  847 EDLAASER----ARRQAQQERDELADEIASGASGK----SALQDEKRRLEARIAQLEEELEEEQSN-------------- 904

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1113 EEILAEDF----SIDDEMTNKLAAE-----------------NKDLY---------------DLVDLLERKIDETEKKYE 1156
Cdd:pfam01576  905 TELLNDRLrkstLQVEQLTTELAAErstsqksesarqqlerqNKELKaklqemegtvkskfkSSIAALEAKIAQLEEQLE 984

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063705616 1157 EASKLCEERLKQVVDTEKKYEEASRLCEERLK-------QVVDTETKLIELKTSMQRLEEKVSDMEA 1216
Cdd:pfam01576  985 QESRERQAANKLVRRTEKKLKEVLLQVEDERRhadqykdQAEKGNSRMKQLKRQLEEAEEEASRANA 1051
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 880-1231 9.25e-07

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 53.98  E-value: 9.25e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  880 KETGALQDAKTKLEKEVEELTSCLElEKQMRMELEQVKTQEVEDLRSALN-------DMKLQLGE------TQVTKSEEI 946
Cdd:pfam05557  111 NELSELRRQIQRAELELQSTNSELE-ELQERLDLLKAKASEAEQLRQNLEkqqsslaEAEQRIKElefeiqSQEQDSEIV 189

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  947 LKLQSALQ---DMQLEFEELAKELEMTNDLAAENEQLKDLVSSLQRKIDEsdskyeetsklsEERVKQEVpvidqgviIK 1023
Cdd:pfam05557  190 KNSKSELAripELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLER------------EEKYREEA--------AT 249

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1024 LEAENQKLKALVSTLEKkidsLDRKHDVTSSNisdqlKESASSDYEMLSNlaaENERLKALVSSLEnenyendgNDSPNE 1103
Cdd:pfam05557  250 LELEKEKLEQELQSWVK----LAQDTGLNLRS-----PEDLSRRIEQLQQ---REIVLKEENSSLT--------SSARQL 309

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1104 QKEGPQmLKEEILAEDFSIDDEMTnklaaENKDLYDLVDLLERKIdetekkyeeaSKLCEER--LKQVV---DTEKKYEE 1178
Cdd:pfam05557  310 EKARRE-LEQELAQYLKKIEDLNK-----KLKRHKALVRRLQRRV----------LLLTKERdgYRAILesyDKELTMSN 373

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063705616 1179 ASRLCEERLKQVVD----TETKLIELKTSMQRLEEKV-------SDMEAEDKILRQQALRNSAS 1231
Cdd:pfam05557  374 YSPQLLERIEEAEDmtqkMQAHNEEMEAQLSVAEEELggykqqaQTLERELQALRQQESLADPS 437
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
 885-1232 1.24e-06

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 53.90  E-value: 1.24e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  885 LQDAKTKLEKEVEELTSclelekqmrMELEQVKTQ--EVEDLRSALNDMKLQLgeTQVTKSEEILKLQSALQDMQLEFEE 962
Cdd:TIGR01612  698 LDDLKSKIDKEYDKIQN---------METATVELHlsNIENKKNELLDIIVEI--KKHIHGEINKDLNKILEDFKNKEKE 766

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  963 LAKELemtNDLAAENEQLKDLVSslqrKIDESDSKYEETSKL---SEERVKQEVpviDQG--VIIKLEAENQKLKALVST 1037
Cdd:TIGR01612  767 LSNKI---NDYAKEKDELNKYKS----KISEIKNHYNDQINIdniKDEDAKQNY---DKSkeYIKTISIKEDEIFKIINE 836

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1038 LEKKIDSLDRKHDVTSsNISDQLKESASSDYEMLSNLAaenERLKALVSSLENENYENDGNDSPneqkegpqmlkeeila 1117
Cdd:TIGR01612  837 MKFMKDDFLNKVDKFI-NFENNCKEKIDSEHEQFAELT---NKIKAEISDDKLNDYEKKFNDSK---------------- 896

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1118 edfSIDDEMTNKLAAENKDLydlvdllerkidETEKKYEEASKLCEERLKQVvdteKKYEEASRLCEERLKQVVDT--ET 1195
Cdd:TIGR01612  897 ---SLINEINKSIEEEYQNI------------NTLKKVDEYIKICENTKESI----EKFHNKQNILKEILNKNIDTikES 957

                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1063705616 1196 KLIElKTSMQRLEEKVSDMEAE-DKILRQQALRNSASR 1232
Cdd:TIGR01612  958 NLIE-KSYKDKFDNTLIDKINElDKAFKDASLNDYEAK 994
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 870-1079 2.47e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 2.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  870 RELRKLKMAAKETGALQDAKTKLEKEVEELTSCLELEKQMRMELEQVKTQEVEDLRSALNDMKLQLGETQVTKSEEILKL 949
Cdd:COG1196    299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  950 QSALQDMQLEFEELAKELEMTNDLAAENEQLKDLVSSLQRKIDESDSKYEETSKLSEERVKQEVPVID-QGVIIKLEAEN 1028
Cdd:COG1196    379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEaAEEEAELEEEE 458

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1063705616 1029 QKLKALVSTLEKKIDSLDRKHDVTssnisDQLKESASSDYEMLSNLAAENE 1079
Cdd:COG1196    459 EALLELLAELLEEAALLEAALAEL-----LEELAEAAARLLLLLEAEADYE 504
PTZ00121 PTZ00121
MAEBL; Provisional
 870-1209 2.52e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.84  E-value: 2.52e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  870 RELRKLKMAAKETGALQDAKTKLE---KEVEELTSCLELEK---QMRMELEQVKTQEVEDLRSALNDMKLQLGET----- 938
Cdd:PTZ00121  1470 KKADEAKKKAEEAKKADEAKKKAEeakKKADEAKKAAEAKKkadEAKKAEEAKKADEAKKAEEAKKADEAKKAEEkkkad 1549

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  939 QVTKSEEILKLQSALQDMQLEFEELAKELEMTNDLAAENEQLKDLVSSLQRKIDESDSKYEETSKLSEERVKQEVpvidq 1018
Cdd:PTZ00121  1550 ELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE----- 1624

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1019 gvIIKLEAENQKLKALVSTLEKKIDSLD--RKHDVTSSNISDQLKESASSDYEMLSNL--AAENERLKALVSSLENE--- 1091
Cdd:PTZ00121  1625 --LKKAEEEKKKVEQLKKKEAEEKKKAEelKKAEEENKIKAAEEAKKAEEDKKKAEEAkkAEEDEKKAAEALKKEAEeak 1702

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1092 NYENDGNDSPNEQKEGPQMLKEEilaEDFSIDDEMTNKLAAENKDLYDlvdllERKIDETEKKYEEASKLCEERLKQVVD 1171
Cdd:PTZ00121  1703 KAEELKKKEAEEKKKAEELKKAE---EENKIKAEEAKKEAEEDKKKAE-----EAKKDEEEKKKIAHLKKEEEKKAEEIR 1774

                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1063705616 1172 TEKKYEEASRLCEERLKQVVDTETKLIELKTSMQRLEE 1209
Cdd:PTZ00121  1775 KEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIE 1812
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
919-1227 2.66e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 51.83  E-value: 2.66e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  919 QEVEDLRSALNDMKLQLGETQVTKSEEILKLQSALQDMQLEFEELAKELE-MTNDLAAENEQLKDLVSSLQRKIDESDSK 997
Cdd:COG4372      6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEqAREELEQLEEELEQARSELEQLEEELEEL 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  998 YEETSKLSEERVKQEvpviDQgvIIKLEAENQKLKALVSTLEKKIDSLDRKHDVTSSNISDQLKESASSDYEM------L 1071
Cdd:COG4372     86 NEQLQAAQAELAQAQ----EE--LESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELkeleeqL 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1072 SNLAAENERLKALVSSLENENYENDGN---DSPNEQKEGPQMLKEEILAEDFSIDDEMTNKLAAENKDLYDLVDLLERKI 1148
Cdd:COG4372    160 ESLQEELAALEQELQALSEAEAEQALDellKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALL 239

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063705616 1149 DETEKKYEEASKLCEERLKQVVDTEKKYEEASRLCEERLKQVVDTETKLIELKTSMQRLEEKVSDMEAEDKILRQQALR 1227
Cdd:COG4372    240 DALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALL 318
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
873-1224 2.90e-06

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.08  E-value: 2.90e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  873 RKLKMAAKETGALQDAKTKLEKEVEELTSCLELEKQMRMELEQVKtQEVEDLRSALNDMKLQLGetQVTKSEEILKLQSA 952
Cdd:COG4717     64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELE-AELEELREELEKLEKLLQ--LLPLYQELEALEAE 140

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  953 LQDMQLEFEELAKELEMTNDLAAENEQLKDLVSSLQRKIDESDSKYEETSKLSEERVKQEVPVIDQGvIIKLEAENQKLK 1032
Cdd:COG4717    141 LAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQR-LAELEEELEEAQ 219

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1033 ALVSTLEKKIDSLDRKHdvTSSNISDQLKE-------------------SASSDYEMLSNLAAENERLKALVSSLENENY 1093
Cdd:COG4717    220 EELEELEEELEQLENEL--EAAALEERLKEarlllliaaallallglggSLLSLILTIAGVLFLVLGLLALLFLLLAREK 297

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1094 ENDGND-SPNEQKEGPQMLKEEILAE---DFSIDDEMTNKLAAENKDLYDLVDLLERKIDETEKK------YEEASKLCE 1163
Cdd:COG4717    298 ASLGKEaEELQALPALEELEEEELEEllaALGLPPDLSPEELLELLDRIEELQELLREAEELEEElqleelEQEIAALLA 377

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1164 --------------ERLKQVVDTEKKYEEASRLCEERLKQVV---------DTETKLIELKTSMQRLEEKVSDMEAEDKI 1220
Cdd:COG4717    378 eagvedeeelraalEQAEEYQELKEELEELEEQLEELLGELEellealdeeELEEELEELEEELEELEEELEELREELAE 457


                   ....
gi 1063705616 1221 LRQQ 1224
Cdd:COG4717    458 LEAE 461
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 921-1225 3.11e-06

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: 52.37  E-value: 3.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  921 VEDLRSALNDMK-LQLGETQVT-------------------------KSEEILKLQSALQDMQLEFEELAKELemtNDLA 974
Cdd:TIGR02168  628 VDDLDNALELAKkLRPGYRIVTldgdlvrpggvitggsaktnssileRRREIEELEEKIEELEEKIAELEKAL---AELR 704

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  975 AENEQLKDLVSSLQRKIDESDSKYEETSK-LSEERVKQEvpvidqgviiKLEAENQKLKALVSTLEKKIDSLDRKHDVTS 1053
Cdd:TIGR02168  705 KELEELEEELEQLRKELEELSRQISALRKdLARLEAEVE----------QLEERIAQLSKELTELEAEIEELEERLEEAE 774

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1054 SNISDQLKESASSDyEMLSNLAAENERLKALVSSLENEnyENDGNDSPNEQKEGPQMLKEEIlaedfsiddemtnklaae 1133
Cdd:TIGR02168  775 EELAEAEAEIEELE-AQIEQLKEELKALREALDELRAE--LTLLNEEAANLRERLESLERRI------------------ 833

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1134 nkdlydlvDLLERKIDETEKKYEEASKLCEERLKQVVDTEKKYEEASRLCEERLKQVVDTETKLIELKTSMQRLEEKVSD 1213
Cdd:TIGR02168  834 --------AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRE 905

                          330
                   ....*....|..
gi 1063705616 1214 MEAEDKILRQQA 1225
Cdd:TIGR02168  906 LESKRSELRREL 917
Myo5_CBD cd15470
Cargo binding domain of myosin 5; Class V myosins are well studied unconventional myosins, ...
 1543-1704 3.17e-06

Cargo binding domain of myosin 5; Class V myosins are well studied unconventional myosins, represented by three paralogs (Myo5a,b,c) in vertebrates. Their C-terminal cargo binding domains (CBDs) are important for the binding of a diverse set of cargos, including membrane vesicles, organelles, proteins and mRNA. The MyoV-CBDs directly interact with several adaptor proteins, in case of Myo5a, melanophilin (MLPH), Rab interacting lysosomal protein-like 2 (RILPL2), and granuphilin, and in case of Myo5b, Rab11-family interacting protein 2.


Pssm-ID: 271254 [Multi-domain]  Cd Length: 332  Bit Score: 51.06  E-value: 3.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1543 TWQDVIGLLNQLLGTLKKNYVPLFLAQKIFCQTFQDINVQLFNSLLQR-ECCTFIMGKKVNVWLNELESWCSQA--TEDF 1619
Cdd:cd15470    142 TLDSLLQQLNSFHTTLTQHGLDPELIKQVFRQLFYLICASTLNNLLLRkDLCSWSKGMQIRYNVSQLEEWLRDKglQDSG 221

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1620 VGSSWDELKntrQALVLLvteQKSTITYDDLTT--NLCPALSTQQLYRICTLCKIDDHEDQNVSPDVISNLKLLVTDEDE 1697
Cdd:cd15470    222 ARETLEPLI---QAAQLL---QVKKTTEEDAQSicEMCTKLTTAQIVKILNLYTPVDDFEERVTPSFIRKVQARLNERAD 295


                   ....*..
gi 1063705616 1698 DSRSFLL 1704
Cdd:cd15470    296 SNQLQLL 302
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 974-1247 3.81e-06

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 51.30  E-value: 3.81e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  974 AAENEQLKDLVSSLQRKIDESDSKYEETSKlSEERVKQEVPVIDQGvIIKLEAENQKLKALVSTLEKKIDSLDRKHDVTS 1053
Cdd:COG4942     19 ADAAAEAEAELEQLQQEIAELEKELAALKK-EEKALLKQLAALERR-IAALARRIRALEQELAALEAELAELEKEIAELR 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1054 SNISDQLKESAssdyEMLSNL--AAENERLKALVSSlenenyendgnDSPNEQKEGPQMLKEEILAedfsiDDEMTNKLA 1131
Cdd:COG4942     97 AELEAQKEELA----ELLRALyrLGRQPPLALLLSP-----------EDFLDAVRRLQYLKYLAPA-----RREQAEELR 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1132 AENKDLYDLVDLLERKIDETEKKYEEAsklcEERLKQVVDTEKKYEEASRLCEERLKQvvdTETKLIELKTSMQRLEEKV 1211
Cdd:COG4942    157 ADLAELAALRAELEAERAELEALLAEL----EEERAALEALKAERQKLLARLEKELAE---LAAELAELQQEAEELEALI 229

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1063705616 1212 SDMEAEDKilrqqalrnsASRKMSPQVSFTR-----PPPVE 1247
Cdd:COG4942    230 ARLEAEAA----------AAAERTPAAGFAAlkgklPWPVS 260
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 906-1248 3.94e-06

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: 51.66  E-value: 3.94e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  906 EKQMRMELEQVKTQEVEDLRSAlnDMKLQLGETQVTKSEEILKlQSALQdmqLEFEELAKELEMTNDLAAENEQLKDLVS 985
Cdd:pfam17380  291 EKFEKMEQERLRQEKEEKAREV--ERRRKLEEAEKARQAEMDR-QAAIY---AEQERMAMERERELERIRQEERKRELER 364

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  986 SLQRKIDESDSKYEETSKLSEERVKQevpviDQGVIIKLEAEnQKLKALVSTLEKKIDSLDRKHDVTSsnisdqlKESAS 1065
Cdd:pfam17380  365 IRQEEIAMEISRMRELERLQMERQQK-----NERVRQELEAA-RKVKILEEERQRKIQQQKVEMEQIR-------AEQEE 431

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1066 SDYEMLSNLAAENERLKALVSSLENENyendgndspNEQKEGPQMLKEEILAEDFSIDDEMTNKLAAENkdlydlvdlLE 1145
Cdd:pfam17380  432 ARQREVRRLEEERAREMERVRLEEQER---------QQQVERLRQQEEERKRKKLELEKEKRDRKRAEE---------QR 493

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1146 RKIDETEKKYEEASKLCEERLKQVVDTEKK------YEEASRLC--EERLKQVVDTETKLIE---LKTSMQRleEKVSDM 1214
Cdd:pfam17380  494 RKILEKELEERKQAMIEEERKRKLLEKEMEerqkaiYEEERRREaeEERRKQQEMEERRRIQeqmRKATEER--SRLEAM 571

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 1063705616 1215 EAEDKILRqQALRNSASRK--------------MSPQVSFTRPPPVEN 1248
Cdd:pfam17380  572 EREREMMR-QIVESEKARAeyeattpittikpiYRPRISEYQPPDVES 618
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 885-1150 5.39e-06

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 51.28  E-value: 5.39e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  885 LQDAKTKLEKEVEELTSCLELEKQMRMELEQVK---TQEVEDLRSALN--DMKLQLGETQVTKSEEILKLQSALQDMQLE 959
Cdd:pfam05557  316 LEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVlllTKERDGYRAILEsyDKELTMSNYSPQLLERIEEAEDMTQKMQAH 395

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  960 FEELAKELEMtndLAAENEQLKDLVSSLQRKID--ESDSKYEETSKLSEE--RVKQEVPvidqgviiKLEAENQKLKALV 1035
Cdd:pfam05557  396 NEEMEAQLSV---AEEELGGYKQQAQTLERELQalRQQESLADPSYSKEEvdSLRRKLE--------TLELERQRLREQK 464

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1036 STLEKKIDSLDRKHDvtsSNISD----QLKESASSDY-----EMLSNLAAENERLKALVSSLENENyendgndspneqkE 1106
Cdd:pfam05557  465 NELEMELERRCLQGD---YDPKKtkvlHLSMNPAAEAyqqrkNQLEKLQAEIERLKRLLKKLEDDL-------------E 528

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1063705616 1107 GPQMLKEEILAEDFSIDDEMTNKLAAENKDLYDLVDLLERKIDE 1150
Cdd:pfam05557  529 QVLRLPETTSTMNFKEVLDLRKELESAELKNQRLKEVFQAKIQE 572
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 877-1091 5.73e-06

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 50.53  E-value: 5.73e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  877 MAAKETGALQDAKTKLEKEVEELTSCLELEKQMRMELEQVKT---QEVEDLRSALNDMKLQLGETQvtksEEILKLQSAL 953
Cdd:COG4942     10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKallKQLAALERRIAALARRIRALE----QELAALEAEL 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  954 QDMQLEFEELAKELEmtndlaAENEQLKDLVSSLQRK--------------IDESDSKYEETSKLSEERVKQevpvIDQ- 1018
Cdd:COG4942     86 AELEKEIAELRAELE------AQKEELAELLRALYRLgrqpplalllspedFLDAVRRLQYLKYLAPARREQ----AEEl 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1019 -GVIIKLEAENQKLKALVSTLEKKIDSLDRKHDVTSSNISDQ------LKESASSDYEMLSNLAAENERLKALVSSLENE 1091
Cdd:COG4942    156 rADLAELAALRAELEAERAELEALLAELEEERAALEALKAERqkllarLEKELAELAAELAELQQEAEELEALIARLEAE 235
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
905-1225 6.31e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 51.19  E-value: 6.31e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  905 LEKQMRMELEQVKTQ----EVEDLRSALNDMKLQLGETQvtksEEILKLQS----------ALQDMQLEFEELAKELE-- 968
Cdd:PRK02224   181 VLSDQRGSLDQLKAQieekEEKDLHERLNGLESELAELD----EEIERYEEqreqaretrdEADEVLEEHEERREELEtl 256

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  969 ------MTNDLAA---ENEQLKDLVSSLQRKIDESDSKYEET------SKLSEERVKQEVPVIDQ--------------- 1018
Cdd:PRK02224   257 eaeiedLRETIAEterEREELAEEVRDLRERLEELEEERDDLlaeaglDDADAEAVEARREELEDrdeelrdrleecrva 336

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1019 ------------GVIIKLEAENQKLKALVSTLEKKIDSLDRKHDVTSSNISD-----------------QLKESASSDYE 1069
Cdd:PRK02224   337 aqahneeaeslrEDADDLEERAEELREEAAELESELEEAREAVEDRREEIEEleeeieelrerfgdapvDLGNAEDFLEE 416

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1070 MLSNLAAENERLKALVSSLENEnyENDGNDSPNEQKEGP-----QMLKEEILAEDFSIDDEMTNKLAAENKDLYDLVDLL 1144
Cdd:PRK02224   417 LREERDELREREAELEATLRTA--RERVEEAEALLEAGKcpecgQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEV 494

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1145 ERKIDETEKKYEEASKLceERLKQvvdtekKYEEASRLCEERLKQVVDTETKLIELKTSMQRLEEKVSDMEAEDKILRQQ 1224
Cdd:PRK02224   495 EERLERAEDLVEAEDRI--ERLEE------RREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEE 566


                   .
gi 1063705616 1225 A 1225
Cdd:PRK02224   567 A 567
PTZ00121 PTZ00121
MAEBL; Provisional
 853-1219 9.45e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.91  E-value: 9.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  853 KKAAITTQCGWRVKVAHRELRK---LKMAAKETGALQDAKTKLE--KEVEELTSCLElEKQMRMELEQvKTQE---VEDL 924
Cdd:PTZ00121  1411 KKAAAAKKKADEAKKKAEEKKKadeAKKKAEEAKKADEAKKKAEeaKKAEEAKKKAE-EAKKADEAKK-KAEEakkADEA 1488

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  925 RSALNDMK-----LQLGETQVTKSEEILKLQSALQDMQLEFEELAKELEMTNDlAAENEQLKDLVSSLQRKIDESDSKYE 999
Cdd:PTZ00121  1489 KKKAEEAKkkadeAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKK-AEEKKKADELKKAEELKKAEEKKKAE 1567

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1000 ETSKLSEERvkqEVPVIDQGVIIKLEAENQKLKALVSTLEKKIDSLDRKHDVTSSNISDQLK--ESASSDYEMLSNLAAE 1077
Cdd:PTZ00121  1568 EAKKAEEDK---NMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKkaEEEKKKVEQLKKKEAE 1644

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1078 NERLKALVSSLENENY---ENDGNDSPNEQKEGPQMLKEEilaEDFSIDDEMTNKLAAENKDLYDLVDLLERKIDETE-- 1152
Cdd:PTZ00121  1645 EKKKAEELKKAEEENKikaAEEAKKAEEDKKKAEEAKKAE---EDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEel 1721

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063705616 1153 KKYEEASKLCEERLKQVVDTEKKYEEASRLCEERLKQVVDTETKLIELKTSMQRLEEKVSDMEAEDK 1219
Cdd:PTZ00121  1722 KKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEE 1788
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 918-1229 9.89e-06

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 50.50  E-value: 9.89e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  918 TQEVEDLRSALNDMKlQLGETQ-VTKSEEILKLQSALQDMQLEFEELA----KELEMTNDLaaeNEQLKDLVSSLQRK-- 990
Cdd:pfam15921   84 SHQVKDLQRRLNESN-ELHEKQkFYLRQSVIDLQTKLQEMQMERDAMAdirrRESQSQEDL---RNQLQNTVHELEAAkc 159

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  991 -----IDESDSKYEETSK--LSEERVKQEVpvidQGVIIKLEAENQK------------LKALVSTLEKKIDSLDRKHDV 1051
Cdd:pfam15921  160 lkedmLEDSNTQIEQLRKmmLSHEGVLQEI----RSILVDFEEASGKkiyehdsmstmhFRSLGSAISKILRELDTEISY 235

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1052 TSSNI---SDQ---LKESASSDYEMLsnLAAENERLKALVSSLENENYENDGNDSPNEQKEGPQMLKEEILAEDFSIDDE 1125
Cdd:pfam15921  236 LKGRIfpvEDQleaLKSESQNKIELL--LQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNS 313

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1126 MTNKlaaENKDLYDLVDLLERKIDETEKKYEEAsklCEERLKQVVDTEKKYEEASRLCEERLKQVVDTETKLIELKTSMQ 1205
Cdd:pfam15921  314 MYMR---QLSDLESTVSQLRSELREAKRMYEDK---IEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLH 387

                          330       340
                   ....*....|....*....|....
gi 1063705616 1206 RLEEKVSDMEAEDKILRQQALRNS 1229
Cdd:pfam15921  388 KREKELSLEKEQNKRLWDRDTGNS 411
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 882-1222 9.90e-06

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: 50.56  E-value: 9.90e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  882 TGALQDAKTKLEKEVEELTSCLELEKQMRmeleqvkTQEVEDLR----SALNDMKLQLGETQVTKSeeilKLQSALQDMQ 957
Cdd:pfam01576  315 TAAQQELRSKREQEVTELKKALEEETRSH-------EAQLQEMRqkhtQALEELTEQLEQAKRNKA----NLEKAKQALE 383

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  958 LEFEELAKELEMTNDLAAENEQLKdlvSSLQRKIDESDSKYEETsklseERVKQEVpvidQGVIIKLEAENQKLKALVST 1037
Cdd:pfam01576  384 SENAELQAELRTLQQAKQDSEHKR---KKLEGQLQELQARLSES-----ERQRAEL----AEKLSKLQSELESVSSLLNE 451

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1038 LEKKIDSLDRKHDVTSSNISD---QLKESASSDYEMLSNLAAENERLKALVSSLENENyENDGNDSPNEQKEGPQML--- 1111
Cdd:pfam01576  452 AEGKNIKLSKDVSSLESQLQDtqeLLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEE-EAKRNVERQLSTLQAQLSdmk 530

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1112 -KEEILAEDFSIDDEMTNKLAaenKDLYDLVDLLERKIDETEKKYEEASKLCEE---------RLKQVVDT-EKKY---- 1176
Cdd:pfam01576  531 kKLEEDAGTLEALEEGKKRLQ---RELEALTQQLEEKAAAYDKLEKTKNRLQQElddllvdldHQRQLVSNlEKKQkkfd 607

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1063705616 1177 ----EE---ASRLCEERLKQVVDT---ETKLIELKTSMQRLEEKVSDMEAEDKILR 1222
Cdd:pfam01576  608 qmlaEEkaiSARYAEERDRAEAEArekETRALSLARALEEALEAKEELERTNKQLR 663
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 744-1171 1.50e-05

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: 50.06  E-value: 1.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  744 VITYLSRKKYLLLQSASTEIqAFCRGHIARVQFKATRREAASVRIQKQARTYicQTAFKKLCASAISIQSGLRAMAARVE 823
Cdd:TIGR02168  660 VITGGSAKTNSSILERRREI-EELEEKIEELEEKIAELEKALAELRKELEEL--EEELEQLRKELEELSRQISALRKDLA 736

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  824 FQYRTKRKAAiiiqSQIRRCLCRRRYLRTKKAAITTQCGWRVKVAHRELRKLKMAAKETGALQDAKTKLEKEVEELTSCL 903
Cdd:TIGR02168  737 RLEAEVEQLE----ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL 812

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  904 ELEKqmrmELEQVKTQEVEDLRSALNDMKLQLGETQ---VTKSEEILKLQSALQDMQLEFEELAKELemtndlaaenEQL 980
Cdd:TIGR02168  813 TLLN----EEAANLRERLESLERRIAATERRLEDLEeqiEELSEDIESLAAEIEELEELIEELESEL----------EAL 878

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  981 KDLVSSLQRKIDESDSKYEETSKlseervkqevpvidqgVIIKLEAENQKLKALVSTLEKKIDSLDRKHDVTSSNIsDQL 1060
Cdd:TIGR02168  879 LNERASLEEALALLRSELEELSE----------------ELRELESKRSELRRELEELREKLAQLELRLEGLEVRI-DNL 941

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1061 KESASSDYEML--------SNLAAENERLKALVSSLENEnYENDGN---DSPNEQKEgpqmLKEEIlaeDFsiddemtnk 1129
Cdd:TIGR02168  942 QERLSEEYSLTleeaealeNKIEDDEEEARRRLKRLENK-IKELGPvnlAAIEEYEE----LKERY---DF--------- 1004

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|..
gi 1063705616 1130 LAAENKDLYDLVDLLERKIdetekkyEEASKLCEERLKQVVD 1171
Cdd:TIGR02168 1005 LTAQKEDLTEAKETLEEAI-------EEIDREARERFKDTFD 1039
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 865-1217 3.01e-05

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 48.74  E-value: 3.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  865 VKVAHRELRKLKMAAKETGALQDAKTK-----LEKEVEELTSCLELEKQMRMELEQVKTQEVE--DLRSALNDMKLQLGE 937
Cdd:pfam07888   89 LRQSREKHEELEEKYKELSASSEELSEekdalLAQRAAHEARIRELEEDIKTLTQRVLERETEleRMKERAKKAGAQRKE 168

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  938 TQVTKSEeilkLQSALQDMQLEFEELAKELEMTNDLAAENE----QLKDLVSSLQRKIDESDSKYEETSKLSEE-RVKQE 1012
Cdd:pfam07888  169 EEAERKQ----LQAKLQQTEEELRSLSKEFQELRNSLAQRDtqvlQLQDTITTLTQKLTTAHRKEAENEALLEElRSLQE 244

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1013 VpvidqgviikLEAENQKLKALVSTLEKKIDSLDRKHD------VTSSNISDQLKESASSDYEMLSNLAAENERLKalvs 1086
Cdd:pfam07888  245 R----------LNASERKVEGLGEELSSMAAQRDRTQAelhqarLQAAQLTLQLADASLALREGRARWAQERETLQ---- 310

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1087 slenENYENDgndspneqKEGPQMLKEEILAEDFSIDDEMTNKLAAE-----NKDLyDLVDLLERKIDETEKKyeeASKL 1161
Cdd:pfam07888  311 ----QSAEAD--------KDRIEKLSAELQRLEERLQEERMEREKLEvelgrEKDC-NRVQLSESRRELQELK---ASLR 374

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1063705616 1162 CEERLKQVVDTEKK-YEEASRLCEERLKQVVDTETKLIELkTSMQRLEEKVSDMEAE 1217
Cdd:pfam07888  375 VAQKEKEQLQAEKQeLLEYIRQLEQRLETVADAKWSEAAL-TSTERPDSPLSDSEDE 430
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
866-1231 3.08e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 48.36  E-value: 3.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  866 KVAHRELRKLKMAAKETGALQDAKTKLEKEVEELTSCLELEKQMRMELEQvKTQEVEDLRSALNDMKLQLGETQvtksEE 945
Cdd:COG4372      7 KVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQ-AREELEQLEEELEQARSELEQLE----EE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  946 ILKLQSALQDMQLEFEELAKELEMTNDlaaENEQLKDLVSSLQRKIDesdskyeetsklseervkqevpvidqgviiKLE 1025
Cdd:COG4372     82 LEELNEQLQAAQAELAQAQEELESLQE---EAEELQEELEELQKERQ------------------------------DLE 128

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1026 AENQKLKALVSTLEKKIDSLDRKHDVTSSNISDQLKESASSDYEMLSNLAAE-NERLKALVSSLeNENYENDGNDSPNEQ 1104
Cdd:COG4372    129 QQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEaEQALDELLKEA-NRNAEKEEELAEAEK 207

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1105 KEGPQMLKEEILAEDFSIDDEMtNKLAAENKDLYDLVDLLERKIDETEKKYEEASKLCEERLKQVVDTEKKYEEASRLCE 1184
Cdd:COG4372    208 LIESLPRELAEELLEAKDSLEA-KLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELE 286

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 1063705616 1185 ERLKQVVDTETKLIELKTSMQRLEEKVSDMEAEDKILRQQALRNSAS 1231
Cdd:COG4372    287 ALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALA 333
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 873-1158 3.14e-05

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 48.86  E-value: 3.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  873 RKLKMAAKETGALQDAKTKLEKEVEELTSCLELEKQMRMELEQVKTQ---EVEDLRSALNDMKLQLGETQVTKseEILKL 949
Cdd:TIGR04523  489 KELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEkesKISDLEDELNKDDFELKKENLEK--EIDEK 566

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  950 QSALQDMQLEFEELAKElemtndlaaeNEQLKDLVSSLQRKIDESDSKYEETSKLSEERVKQevpvidqgvIIKLEAENQ 1029
Cdd:TIGR04523  567 NKEIEELKQTQKSLKKK----------QEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKE---------LEKAKKENE 627

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1030 KLkalvSTLEKKIDSLDRKHDVTSSNISDQLKESASSdyemLSNLAAENERLKALVSSLENENYENDGNDSPNEQKEgpq 1109
Cdd:TIGR04523  628 KL----SSIIKNIKSKKNKLKQEVKQIKETIKEIRNK----WPEIIKKIKESKTKIDDIIELMKDWLKELSLHYKKY--- 696

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1063705616 1110 mLKEEILAEDFSIDDEMTNKLAAENKDLYDLVDLLERKIDETEKKYEEA 1158
Cdd:TIGR04523  697 -ITRMIRIKDLPKLEEKYKEIEKELKKLDEFSKELENIIKNFNKKFDDA 744
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 884-1150 3.30e-05

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 48.80  E-value: 3.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  884 ALQDAKTKLEKEVEELTSCLELEKQMRMELeqVKTQEVEDLRSALNDMKLQLgetQVTKSEEILKLQSALQDMQLEFEEL 963
Cdd:COG5185    337 GIQNLTAEIEQGQESLTENLEAIKEEIENI--VGEVELSKSSEELDSFKDTI---ESTKESLDEIPQNQRGYAQEILATL 411

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  964 AKELEMtNDLAAENeqlkdlvssLQRKIDESDSKYEETSKLSEERVKQEVPVIDQGVIIKLEAENQKLKALVSTLEKKID 1043
Cdd:COG5185    412 EDTLKA-ADRQIEE---------LQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRSVRSKKE 481

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1044 SLDRKHdvtssnisDQLKESASSDYEMLSNLAAENERLKALVSSLENEnYENDGNDSPNEQKEgpqmlKEEILAEDFSID 1123
Cdd:COG5185    482 DLNEEL--------TQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQ-VAESLKDFMRARGY-----AHILALENLIPA 547

                          250       260
                   ....*....|....*....|....*..
gi 1063705616 1124 DEMtnKLAAENKDLYDLVDLLERKIDE 1150
Cdd:COG5185    548 SEL--IQASNAKTDGQAANLRTAVIDE 572
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 909-1252 3.32e-05

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 49.07  E-value: 3.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  909 MRMELEQVKTQEVEDLRSALNDMKLQLGETQVTKSEEILKLQSALQDMQLEFEELAKELEmtndLAAENEQLKDLvsSLQ 988
Cdd:pfam12128  583 VKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREET----FARTALKNARL--DLR 656

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  989 RKIDEsdskyeetsKLSEERVKQEvpvidqgviiKLEAENQKLKALVSTLEKKIDSLDRKHDVTSSNISDQLKEsassdy 1068
Cdd:pfam12128  657 RLFDE---------KQSEKDKKNK----------ALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKRE------ 711

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1069 emlsNLAAENERLKALVSSLENenyendgndspneqKEGpqMLKEEILAEDFS-------IDDEMTNKLAAENKDLYDLV 1141
Cdd:pfam12128  712 ----ARTEKQAYWQVVEGALDA--------------QLA--LLKAAIAARRSGakaelkaLETWYKRDLASLGVDPDVIA 771

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1142 DLlERKIDETEKKYEEasklCEERLKQVVDTEKKYEEASRLCEERLK-QVVDTETKLIELKTSMQRLEEKV----SDMEA 1216
Cdd:pfam12128  772 KL-KREIRTLERKIER----IAVRRQEVLRYFDWYQETWLQRRPRLAtQLSNIERAISELQQQLARLIADTklrrAKLEM 846

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 1063705616 1217 EDKILRQQALRNSASRK-----MSPQVSFTRPPPVENGHHE 1252
Cdd:pfam12128  847 ERKASEKQQVRLSENLRglrceMSKLATLKEDANSEQAQGS 887
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 870-1071 4.26e-05

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: 46.84  E-value: 4.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  870 RELRKLKmaaKETGALQDAKTKLEKEVEELTSclELEKqMRMELEQVKtQEVEDLRSALNDMKLQLGETQVTKseeilkl 949
Cdd:COG1579     24 HRLKELP---AELAELEDELAALEARLEAAKT--ELED-LEKEIKRLE-LEIEEVEARIKKYEEQLGNVRNNK------- 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  950 qsalqdmqlEFEELAKELEMtndLAAENEQLKDLVSSLQRKIDESDSKYEETSKLSEERVKQevpvidqgviikLEAENQ 1029
Cdd:COG1579     90 ---------EYEALQKEIES---LKRRISDLEDEILELMERIEELEEELAELEAELAELEAE------------LEEKKA 145

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1063705616 1030 KLKALVSTLEKKIDSLDRKHDVTSSNISDQLKESassdYEML 1071
Cdd:COG1579    146 ELDEELAELEAELEELEAEREELAAKIPPELLAL----YERI 183
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
885-1218 4.65e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.52  E-value: 4.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  885 LQDAKTKLEKEVEELTSCLElekqmrmeleqvKTQEVEDLrsaLNDMKLQLGETqvtkSEEILKLQSALQDMQLEFEELA 964
Cdd:PRK03918   167 LGEVIKEIKRRIERLEKFIK------------RTENIEEL---IKEKEKELEEV----LREINEISSELPELREELEKLE 227

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  965 KELEMTNDLAAENEQLKDLVSS-------LQRKIDESDSKYEETSKLSEE------RVKQEVPVIDQGVII-----KLEA 1026
Cdd:PRK03918   228 KEVKELEELKEEIEELEKELESlegskrkLEEKIRELEERIEELKKEIEEleekvkELKELKEKAEEYIKLsefyeEYLD 307

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1027 ENQKLKALVSTLEKKIDSLDRKHDVTSSNIS-----DQLKESASSDYEMLSNLAAENERLKALVSSLENENYENDGNdSP 1101
Cdd:PRK03918   308 ELREIEKRLSRLEEEINGIEERIKELEEKEErleelKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGL-TP 386

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1102 NEQKEGPQML---KEEILAEDFSIDDEMtNKLAAENKDLYDLVDLLE----------RKIDETEKK-----YEEASKLCE 1163
Cdd:PRK03918   387 EKLEKELEELekaKEEIEEEISKITARI-GELKKEIKELKKAIEELKkakgkcpvcgRELTEEHRKelleeYTAELKRIE 465

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1063705616 1164 ERLKQVVDTEKKYEEAsrlcEERLKQVVDTETKLIELKT---SMQRLEEKVSDMEAED 1218
Cdd:PRK03918   466 KELKEIEEKERKLRKE----LRELEKVLKKESELIKLKElaeQLKELEEKLKKYNLEE 519
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 1021-1245 6.19e-05

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 47.52  E-value: 6.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1021 IIKLEAENQKLKALVSTLEKKIDSLDRKHDVTSSNISDQLKESASSDYEMLSN---LAAENERLKALVSSLEN---ENYE 1094
Cdd:COG3883     18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLqaeIAEAEAEIEERREELGErarALYR 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1095 NDGNDSPNEqkegpqMLkeeILAEDFS--IDD-EMTNKLAAENKDLYDLVDLLERKIDETEKKYEEASKLCEERLKQVvd 1171
Cdd:COG3883     98 SGGSVSYLD------VL---LGSESFSdfLDRlSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAEL-- 166

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063705616 1172 tEKKYEEASRLCEERLKQVVDTETKLIELKTSMQRLEEKVSDMEAEDKILRQQALRNSASRKMSPQVSFTRPPP 1245
Cdd:COG3883    167 -EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
PTZ00121 PTZ00121
MAEBL; Provisional
 871-1219 6.71e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.21  E-value: 6.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  871 ELRKLKMAAKETGALQDAKTKLEKEVEELTSCLELEKQMRMElEQVKTQEVEDLRSALNDMKLQLGEtQVTKSEEILKLQ 950
Cdd:PTZ00121  1126 DARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAE-EARKAEDAKKAEAARKAEEVRKAE-ELRKAEDARKAE 1203

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  951 SALQdmqleFEELAKELEMTNdlaAENEQLKDLVsslqRKIDESDSKYEETSKLSEERVKQEVPVIDQGVIIKLEAENQK 1030
Cdd:PTZ00121  1204 AARK-----AEEERKAEEARK---AEDAKKAEAV----KKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAA 1271

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1031 LKAlvsTLEKKIDSLDRKHDVTSSN---------ISDQLKESA--SSDYEMLSNLAAENERLKALVSSLENENYENDGND 1099
Cdd:PTZ00121  1272 IKA---EEARKADELKKAEEKKKADeakkaeekkKADEAKKKAeeAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAA 1348

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1100 SPNEQKEGPQMLKEEILAEDFSIDDEMTNKLAAENKDLYDLVdlleRKIDETEKKYEEASKLCEErLKQVVDTEKKYEEA 1179
Cdd:PTZ00121  1349 KAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEK----KKADEAKKKAEEDKKKADE-LKKAAAAKKKADEA 1423

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 1063705616 1180 SRLCEER-----LKQVVDTETKLIELKtsmQRLEEKVSDMEAEDK 1219
Cdd:PTZ00121  1424 KKKAEEKkkadeAKKKAEEAKKADEAK---KKAEEAKKAEEAKKK 1465
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
873-1092 7.43e-05

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.99  E-value: 7.43e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  873 RKLKMAAKETGALQDAKTKLEKEVEELTSCLELEKQMRMEL--------EQVKTQEVEDLRSALNDMKLQLGETqvtkSE 944
Cdd:COG4913    610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALqrlaeyswDEIDVASAEREIAELEAELERLDAS----SD 685

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  945 EILKLQSALQDMQLEFEELAKELEMTND----LAAENEQLKDLVSSLQRKIDESDSKYEETSKLS-EERVKQEVP----- 1014
Cdd:COG4913    686 DLAALEEQLEELEAELEELEEELDELKGeigrLEKELEQAEEELDELQDRLEAAEDLARLELRALlEERFAAALGdaver 765

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1015 VIDQGVIIKLEAENQKLKALVSTLEKKIDSLDRKHDVTSSNISDQLkESASSDYEMLSNLAAEN-----ERLKALVSSLE 1089
Cdd:COG4913    766 ELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADL-ESLPEYLALLDRLEEDGlpeyeERFKELLNENS 844


                   ...
gi 1063705616 1090 NEN 1092
Cdd:COG4913    845 IEF 847
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 871-1234 7.86e-05

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 47.52  E-value: 7.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  871 ELRKLKMaakeTGALQDAKTKLEKEVEELT--SCLELEKQmrmeleqvktqeVEDLRSALNDMKLQLGETQVTKSEEILK 948
Cdd:PRK04778    52 KVKKLNL----TGQSEEKFEEWRQKWDEIVtnSLPDIEEQ------------LFEAEELNDKFRFRKAKHEINEIESLLD 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  949 L-QSALQDMQLEFEELaKELEMTNDlaAENEQLKDLVSSLQRKIDESDSKYEETSKLSEERVKQEVPVIDQ--------- 1018
Cdd:PRK04778   116 LiEEDIEQILEELQEL-LESEEKNR--EEVEQLKDLYRELRKSLLANRFSFGPALDELEKQLENLEEEFSQfveltesgd 192

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1019 -----GVIIKLEAENQKLK-------ALVSTLEKKI------------DSLDRKHDVTSSNIS---DQLKESASSDYEML 1071
Cdd:PRK04778   193 yvearEILDQLEEELAALEqimeeipELLKELQTELpdqlqelkagyrELVEEGYHLDHLDIEkeiQDLKEQIDENLALL 272

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1072 SNL---AAE------NERLKALVSSLENE---NYENDGNDSP-----NEQKEGPQMLKEEI--LAEDFSIDD---EMTNK 1129
Cdd:PRK04778   273 EELdldEAEekneeiQERIDQLYDILEREvkaRKYVEKNSDTlpdflEHAKEQNKELKEEIdrVKQSYTLNEselESVRQ 352

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1130 LAAENKDLYDLVDLLERKIDETEKKYEEAsklcEERLKQvvdtekkyeeasrlCEERLKQVvdtETKLIELKTSMQRLEE 1209
Cdd:PRK04778   353 LEKQLESLEKQYDEITERIAEQEIAYSEL----QEELEE--------------ILKQLEEI---EKEQEKLSEMLQGLRK 411

                          410       420
                   ....*....|....*....|....*.
gi 1063705616 1210 kvSDMEAEDKILR-QQALRNSAsRKM 1234
Cdd:PRK04778   412 --DELEAREKLERyRNKLHEIK-RYL 434
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 907-1094 9.89e-05

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 46.75  E-value: 9.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  907 KQMRMELEQVKtQEVEDLRSALNDMKLQLGETQvtksEEILKLQSALQDMQLEFEELAKELEMTN-DLAAENEQLKDLVS 985
Cdd:COG3883     19 QAKQKELSELQ-AELEAAQAELDALQAELEELN----EEYNELQAELEALQAEIDKLQAEIAEAEaEIEERREELGERAR 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  986 SLQRK---------IDESDS------KYEETSKLSEErvkqevpviDQGVIIKLEAENQKLKALVSTLEKKIDSLDRKHD 1050
Cdd:COG3883     94 ALYRSggsvsyldvLLGSESfsdfldRLSALSKIADA---------DADLLEELKADKAELEAKKAELEAKLAELEALKA 164

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1063705616 1051 VTSSNISDqlKESASSDYE-MLSNLAAENERLKALVSSLENENYE 1094
Cdd:COG3883    165 ELEAAKAE--LEAQQAEQEaLLAQLSAEEAAAEAQLAELEAELAA 207
Myo5b_CBD cd15477
Cargo binding domain of myosin 5b; Class V myosins are well studied unconventional myosins, ...
 1509-1711 1.01e-04

Cargo binding domain of myosin 5b; Class V myosins are well studied unconventional myosins, represented by three paralogs (Myo5a,b,c) in vertebrates. Their C-terminal cargo binding domains (CBDs) are important for the binding of a diverse set of cargos, including membrane vesicles, organelles, proteins and mRNA. They interact with several adaptor proteins, in case of Myo5b-CBD, Rab11-family interacting protein 2.


Pssm-ID: 271261  Cd Length: 372  Bit Score: 46.78  E-value: 1.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1509 EENSQAKLSEVNPQAKPSAENSLAkpseENSPTETWQDVIGLLNQLLGTLKKNYVPLFLAQKIFCQTFQDIN-VQLFNSL 1587
Cdd:cd15477    150 ENESIQGLSGVKPMGYRKRSSSMA----DGDNSYTLEALIRQLNTFHSIMCDQGLDPEIIQQVFKQLFYMINaVTLNNLL 225

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1588 LQRECCTFIMGKKVNVWLNELESWCSQATEDFVGSSwDELKNTRQALVLLVTEQKSTITYDDLTTnLCPALSTQQLYRIC 1667
Cdd:cd15477    226 LRKDVCSWSTGMQLRYNISQLEEWLRGRNLHQSGAA-QTMEPLIQAAQLLQLKKKTSEDAEAICS-LCTALSTQQIVKIL 303

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1063705616 1668 TLCKIDDHEDQNVSPDVISNLKLLVTDEDeDSRSFLLDNNSSIP 1711
Cdd:cd15477    304 NLYTPLNEFEERVTVSFIRTIQAQLQERN-DPPQLLLDTKHMFP 346
PRK12704 PRK12704
phosphodiesterase; Provisional
 872-1013 1.14e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 46.69  E-value: 1.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  872 LRKLKMAAKETGALQDAKTKLE---KEVEELTSCLELE-----KQMRMELEQvktqEVEDLRSalndmKLQLGETQVTKS 943
Cdd:PRK12704    24 VRKKIAEAKIKEAEEEAKRILEeakKEAEAIKKEALLEakeeiHKLRNEFEK----ELRERRN-----ELQKLEKRLLQK 94

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063705616  944 EEIL-KLQSALQDMQLEFEELAKELEmtndlaAENEQLKDLVSSLQRKIDESDSKYEETSKLSEERVKQEV 1013
Cdd:PRK12704    95 EENLdRKLELLEKREEELEKKEKELE------QKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEIL 159
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 878-1223 1.43e-04

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 45.96  E-value: 1.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  878 AAKETGALQDAKTKLEKEVEELTSCLELEKQMRMELEQVKTQevedlrsalnDMKLQLGETQVTKSEEilKLQSALQDmq 957
Cdd:pfam15905   51 ATARKVKSLELKKKSQKNLKESKDQKELEKEIRALVQERGEQ----------DKRLQALEEELEKVEA--KLNAAVRE-- 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  958 lefeelakELEMTNDLAAENEQLKDLVSS---LQRKIDEsDSKYEETSKLSEERVKQEVpvidqgviiKLEAENQKLKAL 1034
Cdd:pfam15905  117 --------KTSLSASVASLEKQLLELTRVnelLKAKFSE-DGTQKKMSSLSMELMKLRN---------KLEAKMKEVMAK 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1035 VSTLEKKIDSLDRKHDVTSSNISdQLKESASSDYEMLSNLAAENERLKALVSSLENENyendgndspnEQKEgpqMLKEE 1114
Cdd:pfam15905  179 QEGMEGKLQVTQKNLEHSKGKVA-QLEEKLVSTEKEKIEEKSETEKLLEYITELSCVS----------EQVE---KYKLD 244

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1115 IlaedfsidDEMTNKLAAENKDLYDLVDLLERKIDETEKKYEEASKLCEErlkqvvdtekkyeeasrLCEERLKQVVDTE 1194
Cdd:pfam15905  245 I--------AQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKL-----------------LESEKEELLREYE 299

                          330       340
                   ....*....|....*....|....*....
gi 1063705616 1195 TKLIELKTSMQRLEEKVSDMEAEDKILRQ 1223
Cdd:pfam15905  300 EKEQTLNAELEELKEKLTLEEQEHQKLQQ 328
Leu_zip pfam15294
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ...
 877-989 1.82e-04

Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).


Pssm-ID: 464620 [Multi-domain]  Cd Length: 276  Bit Score: 45.47  E-value: 1.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  877 MAAKETGALQDaKTKLEKEVEELTSCLELEKqmrmeLEQVKTQEVEDLRSALNDMKLQLGETQVTKSEEILKLQSALQDM 956
Cdd:pfam15294  152 LESQATQALDE-KSKLEKALKDLQKEQGAKK-----DVKSNLKEISDLEEKMAALKSDLEKTLNASTALQKSLEEDLAST 225

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1063705616  957 ---------QLEFEElaKELE-----------MTNDLAAENEQLKDLVSSLQR 989
Cdd:pfam15294  226 khellkvqeQLEMAE--KELEkkfqqtaayrnMKEMLTKKNEQIKELRKRLSK 276
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 874-1094 1.95e-04

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 45.57  E-value: 1.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  874 KLKMAAKETGALQDAKTKLEKEVEELTSCLEL----------EKQMR---MELEQ------VKTQEVEDLRSALnDMKLQ 934
Cdd:pfam15905  109 KLNAAVREKTSLSASVASLEKQLLELTRVNELlkakfsedgtQKKMSslsMELMKlrnkleAKMKEVMAKQEGM-EGKLQ 187

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  935 LGETQVTKSEEILklqSALQDMQLEFEELakelemTNDLAAENEQLKDLVSSLQRKIDESDsKYEETSKLSEERVKQEvp 1014
Cdd:pfam15905  188 VTQKNLEHSKGKV---AQLEEKLVSTEKE------KIEEKSETEKLLEYITELSCVSEQVE-KYKLDIAQLEELLKEK-- 255

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1015 viDQgviiKLEAENQKLKALVSTLEKKIDSLDRKHDVTSSNISDQLKEsassDYEMLSNLAAENERLKALVSSLENENYE 1094
Cdd:pfam15905  256 --ND----EIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEELLRE----YEEKEQTLNAELEELKEKLTLEEQEHQK 325
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 892-1239 2.15e-04

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 46.35  E-value: 2.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  892 LEKEVEELTSCLELEKQM---RME-------------LEQVKTQEVEDLRSALNDMKLQLGEtqvtkseeilkLQSALQD 955
Cdd:pfam10174  135 LRKTLEEMELRIETQKQTlgaRDEsikkllemlqskgLPKKSGEEDWERTRRIAEAEMQLGH-----------LEVLLDQ 203

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  956 MQLEFEELAKELEMTNDLAAENEQLKDL----------VSSLQRKIDESDSKYEET-------SKLSEERVKQ-EV---- 1013
Cdd:pfam10174  204 KEKENIHLREELHRRNQLQPDPAKTKALqtviemkdtkISSLERNIRDLEDEVQMLktngllhTEDREEEIKQmEVyksh 283

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1014 -----PVIDQgviikLEAENQKLKALVSTLEKKIDSLDRKHDVTSSNIsDQLKESassdyemlsnLAAENERLKALVSsl 1088
Cdd:pfam10174  284 skfmkNKIDQ-----LKQELSKKESELLALQTKLETLTNQNSDCKQHI-EVLKES----------LTAKEQRAAILQT-- 345

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1089 enenyENDGNDSPNEQKEgpQMLKEEILAEDFSIDDEMTnkLAAENKDLYDLVDLLERKIDETEKKYEEASKLCEERLKQ 1168
Cdd:pfam10174  346 -----EVDALRLRLEEKE--SFLNKKTKQLQDLTEEKST--LAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQ 416

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1169 V----------------VDT-----EKKYEEASRLCeERLKQVVDTETKlielktsmQRLEEkVSDMEAEDKILRQQAlr 1227
Cdd:pfam10174  417 LaglkervkslqtdssnTDTalttlEEALSEKERII-ERLKEQREREDR--------ERLEE-LESLKKENKDLKEKV-- 484

                          410
                   ....*....|..
gi 1063705616 1228 NSASRKMSPQVS 1239
Cdd:pfam10174  485 SALQPELTEKES 496
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 872-1214 2.17e-04

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 45.98  E-value: 2.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  872 LRKLKMAAKETGA-LQDAKTKLEKEVEELTSCLELEKQMRMELEQVKTQeVEDLRSALNDMKLQLGETqvtkseeILKLQ 950
Cdd:PRK04778   100 FRKAKHEINEIESlLDLIEEDIEQILEELQELLESEEKNREEVEQLKDL-YRELRKSLLANRFSFGPA-------LDELE 171

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  951 SALQDMQLEFEELAKELEMTNDLAAEN--EQLKDLVSSLQRKIDE--------------------------SDSKY---- 998
Cdd:PRK04778   172 KQLENLEEEFSQFVELTESGDYVEAREilDQLEEELAALEQIMEEipellkelqtelpdqlqelkagyrelVEEGYhldh 251

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  999 ---EETSKLSEERVKQEVPVIDQGVIIKLEAENQ----KLKALVSTLEKKIDSldrKHDV--TSSNISDQLKESAssdyE 1069
Cdd:PRK04778   252 ldiEKEIQDLKEQIDENLALLEELDLDEAEEKNEeiqeRIDQLYDILEREVKA---RKYVekNSDTLPDFLEHAK----E 324

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1070 MLSNLAAENERLKalvsslenENYENDGNDSPNEQKEGPQMlkEEILAEDFSIDDEMTNKLAAENkDLYDLVDLLERKID 1149
Cdd:PRK04778   325 QNKELKEEIDRVK--------QSYTLNESELESVRQLEKQL--ESLEKQYDEITERIAEQEIAYS-ELQEELEEILKQLE 393

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1150 ETEKKYEEAS---------------KLceERLKQVVDTEKKYEEASRL-------------CEERLKQVVDT-------- 1193
Cdd:PRK04778   394 EIEKEQEKLSemlqglrkdeleareKL--ERYRNKLHEIKRYLEKSNLpglpedylemffeVSDEIEALAEEleekpinm 471

                          410       420
                   ....*....|....*....|....
gi 1063705616 1194 ---ETKLIELKTSMQRLEEKVSDM 1214
Cdd:PRK04778   472 eavNRLLEEATEDVETLEEETEEL 495
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 951-1203 2.61e-04

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 45.69  E-value: 2.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  951 SALQDMQL-EFEELAKEL--EMTNDLAAENEQLKDLVSSLQR--------KIDESDSKYEETSKLSEErVKQEVPVIDQg 1019
Cdd:PRK05771    23 EALHELGVvHIEDLKEELsnERLRKLRSLLTKLSEALDKLRSylpklnplREEKKKVSVKSLEELIKD-VEEELEKIEK- 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1020 VIIKLEAENQKLKALVSTLEKKIDSLDRKHDVTSSnisdqlkesassdyemLSNLAaENERLKALVSSLENENYENDGND 1099
Cdd:PRK05771   101 EIKELEEEISELENEIKELEQEIERLEPWGNFDLD----------------LSLLL-GFKYVSVFVGTVPEDKLEELKLE 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1100 SPNEQKEGPQMLKEE------ILAEDFSIDDEMTNKLAAENKDLYDLVDLLERkIDETEKKYEEASKLCEERLKQVVDTE 1173
Cdd:PRK05771   164 SDVENVEYISTDKGYvyvvvvVLKELSDEVEEELKKLGFERLELEEEGTPSEL-IREIKEELEEIEKERESLLEELKELA 242

                          250       260       270
                   ....*....|....*....|....*....|
gi 1063705616 1174 KKYEEASRLCEERLKQVVDTETKLIELKTS 1203
Cdd:PRK05771   243 KKYLEELLALYEYLEIELERAEALSKFLKT 272
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
 867-1227 2.82e-04

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 45.77  E-value: 2.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  867 VAHRELRKLKMAAKETGALQDAKTKLEKEVEE-LTSCLElekQMRMELEQVKTQEVEDLRSALNDMKLQ-LGETQVTKSE 944
Cdd:NF033838    34 VVHAEEVRGGNNPTVTSSGNESQKEHAKEVEShLEKILS---EIQKSLDKRKHTQNVALNKKLSDIKTEyLYELNVLKEK 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  945 EILKLQSALQ-DMQLEFEELAKELEMTNDLAAENEqlKDLVSSLQRKIDESDSKYEETSKLSEERVKQEVPVIDQGVIiK 1023
Cdd:NF033838   111 SEAELTSKTKkELDAAFEQFKKDTLEPGKKVAEAT--KKVEEAEKKAKDQKEEDRRNYPTNTYKTLELEIAESDVEVK-K 187

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1024 LEAENQKLKALVSTLEKKIDSLDRKhdvtssnisdqlKESASSDYEMLSNLAAENERLK--ALVSSLENENYENDGNDSP 1101
Cdd:NF033838   188 AELELVKEEAKEPRDEEKIKQAKAK------------VESKKAEATRLEKIKTDREKAEeeAKRRADAKLKEAVEKNVAT 255

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1102 NEQKEGPQMLKEEILAE----DFSIDDEMTNKLAAENKDLYDLVDLLERKIDETEKKYEEASKLC-----EERLKQVVDT 1172
Cdd:NF033838   256 SEQDKPKRRAKRGVLGEpatpDKKENDAKSSDSSVGEETLPSPSLKPEKKVAEAEKKVEEAKKKAkdqkeEDRRNYPTNT 335

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1063705616 1173 EKKYEeaSRLCEERLKqVVDTETKLIELKTSMQRLEEKVSDMEAEDKILRQQALR 1227
Cdd:NF033838   336 YKTLE--LEIAESDVK-VKEAELELVKEEAKEPRNEEKIKQAKAKVESKKAEATR 387
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
870-1045 6.47e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.67  E-value: 6.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  870 RELRKLKMAAKETGALQDAKTKLEKEVEELTSCLELEKQMRMELEQVKTqEVEDLRSALNDMKLQLG-ETQVTKSEEILK 948
Cdd:PRK03918   592 ERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEK-RLEELRKELEELEKKYSeEEYEELREEYLE 670

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  949 LQSALQDMQLEFEELAKELEmtnDLAAENEQLKDLVSSLQRKIDESDS-------------KYEETSKLSEERVKQEVPV 1015
Cdd:PRK03918   671 LSRELAGLRAELEELEKRRE---EIKKTLEKLKEELEEREKAKKELEKlekalerveelreKVKKYKALLKERALSKVGE 747

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1063705616 1016 ID------------QGVIIKLEAENQKLKALVSTLEKKIDSL 1045
Cdd:PRK03918   748 IAseifeeltegkySGVRVKAEENKVKLFVVYQGKERPLTFL 789
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
948-1215 8.21e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.28  E-value: 8.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  948 KLQSALQDMQLEFEELAKELEMTNDLaaeNEQLKDLVSSLQRKIDESDSKYEETSKLSEER--VKQEVPVIDQ--GVIIK 1023
Cdd:PRK03918   166 NLGEVIKEIKRRIERLEKFIKRTENI---EELIKEKEKELEEVLREINEISSELPELREELekLEKEVKELEElkEEIEE 242

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1024 LEAENQKLKALVSTLEKKIDSLDRKHDVTSSNISDqLKESAsSDYEMLSNLAAENERLKALVSSLENENYENDGNDSPNE 1103
Cdd:PRK03918   243 LEKELESLEGSKRKLEEKIRELEERIEELKKEIEE-LEEKV-KELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLE 320

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1104 QKEgpQMLKEEIlaEDFSIDDEMTNKLAAENKDLYDLVDLLErkidETEKKYEEASKLCE--ERLKQ------VVDTEKK 1175
Cdd:PRK03918   321 EEI--NGIEERI--KELEEKEERLEELKKKLKELEKRLEELE----ERHELYEEAKAKKEelERLKKrltgltPEKLEKE 392

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1063705616 1176 YEEASRLCEERLKQVVDTETKLIELKTSMQRLEEKVSDME 1215
Cdd:PRK03918   393 LEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK 432
PTZ00121 PTZ00121
MAEBL; Provisional
 890-1233 1.02e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 1.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  890 TKLEKEVEELTSclELEKQMRMELEQVKTQEVEDLRSALNDMKlqlgetqvtKSEEILKLQSALQDMQLEFEELAKElem 969
Cdd:PTZ00121  1082 DAKEDNRADEAT--EEAFGKAEEAKKTETGKAEEARKAEEAKK---------KAEDARKAEEARKAEDARKAEEARK--- 1147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  970 tndlaAENEQLKDLVSSLQ--RKIDESdSKYEETSKLSEERVKQEVPVIDQgvIIKLEAENQKLKALVSTLEKKIDSLDR 1047
Cdd:PTZ00121  1148 -----AEDAKRVEIARKAEdaRKAEEA-RKAEDAKKAEAARKAEEVRKAEE--LRKAEDARKAEAARKAEEERKAEEARK 1219

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1048 KHDVTSSNISDQLKESASSDYEMLSnlaAENERLKALVSSLENENYENDGNDSPNEQKEGPQMLKEEILAEDFSIDDEMt 1127
Cdd:PTZ00121  1220 AEDAKKAEAVKKAEEAKKDAEEAKK---AEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEA- 1295

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1128 nKLAAENKDlydlVDLLERKIDEtEKKYEEASKLCEERLKQVVDTEKKYEEASRLCEERLKQvvdTETKLIELKTSMQRL 1207
Cdd:PTZ00121  1296 -KKAEEKKK----ADEAKKKAEE-AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAE---AEAAADEAEAAEEKA 1366

                          330       340
                   ....*....|....*....|....*.
gi 1063705616 1208 EEKVSDMEAEDKilRQQALRNSASRK 1233
Cdd:PTZ00121  1367 EAAEKKKEEAKK--KADAAKKKAEEK 1390
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
942-1225 1.09e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 42.98  E-value: 1.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  942 KSEEILKLQSALQDMQLEFEELAKELemTNDLAAENEQLKDLVSSLQRKIDESDSKYEETSKLSEER--VKQEVPVIDQG 1019
Cdd:COG1340     16 KIEELREEIEELKEKRDELNEELKEL--AEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERdeLNEKLNELREE 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1020 V--IIKLEAENQKLKALVSTLEKKIDSLDRKHDVTSsnisdqlkesassdyemlSNLAAENE---RLKALVSSLENENYE 1094
Cdd:COG1340     94 LdeLRKELAELNKAGGSIDKLRKEIERLEWRQQTEV------------------LSPEEEKElveKIKELEKELEKAKKA 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1095 NDGNDSPNEQKEGPQMLKEEilAEDFSidDEMTNkLAAENKDLYDLVDLLERKIDETEKKYEEASklceerlKQVVDTEK 1174
Cdd:COG1340    156 LEKNEKLKELRAELKELRKE--AEEIH--KKIKE-LAEEAQELHEEMIELYKEADELRKEADELH-------KEIVEAQE 223

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1063705616 1175 KYEEASRLCEERLKQVVDTETKLielktSMQRLEEKVSDMEAEDKILRQQA 1225
Cdd:COG1340    224 KADELHEEIIELQKELRELRKEL-----KKLRKKQRALKREKEKEELEEKA 269
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 895-1219 1.12e-03

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 43.52  E-value: 1.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  895 EVEELTS-CLELEKQMR--MELEQVKTQEVEDLRSALN------------DMKLQLGETQVTK-SEEILKLQSALQDMQL 958
Cdd:pfam05622    8 EKDELAQrCHELDQQVSllQEEKNSLQQENKKLQERLDqlesgddsgtpgGKKYLLLQKQLEQlQEENFRLETARDDYRI 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  959 EFEELAK---ELEMTND----LAAENEQLKD-----------------LVSSLQRKI-DESDSK---------------- 997
Cdd:pfam05622   88 KCEELEKevlELQHRNEeltsLAEEAQALKDemdilressdkvkkleaTVETYKKKLeDLGDLRrqvklleernaeymqr 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  998 ---YEETS----------------------KLSEERVKQEvpvidqgviiKLEAENQKLKALVSTLEKKIDSLDRKHDV- 1051
Cdd:pfam05622  168 tlqLEEELkkanalrgqletykrqvqelhgKLSEESKKAD----------KLEFEYKKLEEKLEALQKEKERLIIERDTl 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1052 -----------TSSNISDQLKESASSDYEMLSNLAAE---NErLKALVSSLENEnyendgNDSPNEQKEGPQMLKEEILA 1117
Cdd:pfam05622  238 retneelrcaqLQQAELSQADALLSPSSDPGDNLAAEimpAE-IREKLIRLQHE------NKMLRLGQEGSYRERLTELQ 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1118 EDFSIDDEMTNKLAAENKDLYDLVDLLERKIDETEKKYEEA-----------SKLcEERLKQVVDTEKKYEEASRLCEER 1186
Cdd:pfam05622  311 QLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQgskaedssllkQKL-EEHLEKLHEAQSELQKKKEQIEEL 389

                          410       420       430
                   ....*....|....*....|....*....|....
gi 1063705616 1187 -LKQVVDTETKLIELKTSMQRLEEKVSDMEAEDK 1219
Cdd:pfam05622  390 ePKQDSNLAQKIDELQEALRKKDEDMKAMEERYK 423
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 879-1089 1.69e-03

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: 43.42  E-value: 1.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  879 AKETGALQDAKTKLEKEVEELTSCLELEKQMRMELEQVKTQEVEDLRSALND--MKLQLGETQVTKSEEILKLQSALQDM 956
Cdd:pfam02463  254 ESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLerRKVDDEEKLKESEKEKKKAEKELKKE 333

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  957 QLEFEELAKEL---------------EMTNDLAAENEQLKDLVSSLQRKIDESDSKYEETSKLSEERVK-----QEVPVI 1016
Cdd:pfam02463  334 KEEIEELEKELkeleikreaeeeeeeELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEeekeaQLLLEL 413

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063705616 1017 DQGVIIKLEAENQKLKALVSTLEKKIDSLDRKHDVTSSNISDQ-LKESASSDYEMLSNLAAENERLKALVSSLE 1089
Cdd:pfam02463  414 ARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQeLKLLKDELELKKSEDLLKETQLVKLQEQLE 487
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1005-1225 1.70e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 1.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1005 SEERVKQEVPVIDqgviiKLEAENQKLKALVSTLEKKIDSLdRKHDVTSSNISDQLKESASSDYEMLSNLAAENERLKAL 1084
Cdd:PRK03918   146 SREKVVRQILGLD-----DYENAYKNLGEVIKEIKRRIERL-EKFIKRTENIEELIKEKEKELEEVLREINEISSELPEL 219

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1085 VSSLENENYENDGNDSPNEQKEGPQMLKEEI------LAEDFSIDDEMTNKLAAENKDLYDLVDLLErKIDETEKKYEEA 1158
Cdd:PRK03918   220 REELEKLEKEVKELEELKEEIEELEKELESLegskrkLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKL 298

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063705616 1159 SKLCEERLKQVVDTEKkyeEASRLcEERLKQVVDTETKLIELKTSMQRLEEKVSDMEAEDKILRQQA 1225
Cdd:PRK03918   299 SEFYEEYLDELREIEK---RLSRL-EEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERH 361
AAA_13 pfam13166
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 935-1231 2.02e-03

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.


Pssm-ID: 463796 [Multi-domain]  Cd Length: 712  Bit Score: 43.13  E-value: 2.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  935 LGETQVTKSEEILKLQSALQDMQLEFEELAKELEMTN--DLAAENEQLKDLVSSLQRKIDESDS------KYEET--SKL 1004
Cdd:pfam13166   87 LGEESIEIQEKIAKLKKEIKDHEEKLDAAEANLQKLDkeKEKLEADFLDECWKKIKRKKNSALSealngfKYEANfkSRL 166

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1005 SEERVKQEVpviDQGVIIKLEaenqKLKALVSTLEKkidslDRKHDVTSSNISDQLKESASSDYEMLSNLAAENERLKAL 1084
Cdd:pfam13166  167 LREIEKDNF---NAGVLLSDE----DRKAALATVFS-----DNKPEIAPLTFNVIDFDALEKAEILIQKVIGKSSAIEEL 234

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1085 VSSLENEN--------YENDGNDSPNEQKEGPQMLKEEiLAEDFsiDDEMTnklaaenkdlyDLVDLLERKIDetekKYE 1156
Cdd:pfam13166  235 IKNPDLADwveqglelHKAHLDTCPFCGQPLPAERKAA-LEAHF--DDEFT-----------EFQNRLQKLIE----KVE 296

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063705616 1157 EASKLCEERLKQVVDTEKKYEEASRLCEERLKQvvdTETKLIELKTSMQRLEEKVSDMEAEDKILRQQALRNSAS 1231
Cdd:pfam13166  297 SAISSLLAQLPAVSDLASLLSAFELDVEDIESE---AEVLNSQLDGLRRALEAKRKDPFKSIELDSVDAKIESIN 368
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
871-1081 3.36e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 41.43  E-value: 3.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  871 ELRKLKMAAKETGALQDAKTKLEKEVEEL-----TSCLELEKQMRMeleqvkTQEVEDLRSALNDMKlqlgeTQVTKSEE 945
Cdd:COG1340     93 ELDELRKELAELNKAGGSIDKLRKEIERLewrqqTEVLSPEEEKEL------VEKIKELEKELEKAK-----KALEKNEK 161

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  946 ILKLQSALQDMQLEFEELAKELemtNDLAAENEQLKDLVSSLQRKIDESdskYEETSKLSEERVKQEVpvidqgviiKLE 1025
Cdd:COG1340    162 LKELRAELKELRKEAEEIHKKI---KELAEEAQELHEEMIELYKEADEL---RKEADELHKEIVEAQE---------KAD 226

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1026 AENQKLKAL---VSTLEKKIDSL-DRKHDVTSSNISDQLKESASSDYEMLSNlaaeNERL 1081
Cdd:COG1340    227 ELHEEIIELqkeLRELRKELKKLrKKQRALKREKEKEELEEKAEEIFEKLKK----GEKL 282
PRK01156 PRK01156
chromosome segregation protein; Provisional
 872-1217 3.65e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 42.20  E-value: 3.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  872 LRKLKMAAKETGALQDAKTKLEKEVEELTSCLELEKQMRMEL------------EQVKTQEVEDL------------RSA 927
Cdd:PRK01156   217 LKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIktaesdlsmeleKNNYYKELEERhmkiindpvyknRNY 296

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  928 LND---MKLQLG---------ETQVTKSEEILKLQSALQDMQLEFEELAKELEMTNDLAAENEQLKDLVSSLQRKIDESD 995
Cdd:PRK01156   297 INDyfkYKNDIEnkkqilsniDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLK 376

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  996 SKYEETSKlSEERVKQEVP------VIDQGVIIKLEAE-NQKLKAL---VSTLEKKIDSLDRKHDVTSSNIS-------- 1057
Cdd:PRK01156   377 KKIEEYSK-NIERMSAFISeilkiqEIDPDAIKKELNEiNVKLQDIsskVSSLNQRIRALRENLDELSRNMEmlngqsvc 455

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1058 ----DQLKESASSDyeMLSNLAAENERLKALVSSLENEnyendgNDSPNEQKEGPQMLKEEILAEDFSIDDEMTNKLAAE 1133
Cdd:PRK01156   456 pvcgTTLGEEKSNH--IINHYNEKKSRLEEKIREIEIE------VKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESA 527

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1134 NKDLYDLVDLLERkIDETEKKYEEASKlcEERLKQVVDTEKKYEEASRLCEERLKQVVDT-ETKLIELKTSMQRLEEKVS 1212
Cdd:PRK01156   528 RADLEDIKIKINE-LKDKHDKYEEIKN--RYKSLKLEDLDSKRTSWLNALAVISLIDIETnRSRSNEIKKQLNDLESRLQ 604


                   ....*
gi 1063705616 1213 DMEAE 1217
Cdd:PRK01156   605 EIEIG 609
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
 883-1226 3.76e-03

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: 42.05  E-value: 3.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  883 GALQDAKTKLEKEVEELTscLELEKQMRMELEQVKTQeVEDLRSALNDmklqlGETQVTKSEEilklqSALQDMQLEFEE 962
Cdd:pfam09731  128 KALEEVLKEAISKAESAT--AVAKEAKDDAIQAVKAH-TDSLKEASDT-----AEISREKATD-----SALQKAEALAEK 194

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  963 LAKELemTNDLAAENEQLKDLVSSLQRKIdESDSKYEETSKLSEERVKQEVPVIDQGVIIKLEAENQKLKALVSTLEKKI 1042
Cdd:pfam09731  195 LKEVI--NLAKQSEEEAAPPLLDAAPETP-PKLPEHLDNVEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIFPDII 271

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1043 DSLdrKHDVTSSNisDQLKESASSDYEMLSNLAAENERLKAlvsslenenyendgndspNEQKEGPQMLKEEILAEDFSI 1122
Cdd:pfam09731  272 PVL--KEDNLLSN--DDLNSLIAHAHREIDQLSKKLAELKK------------------REEKHIERALEKQKEELDKLA 329

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1123 DDEMTNKLAAENKDLYDLVDLLERKIDETEKKYEE--------ASKLCEERLKQVVDTEKkyEEASRLCEERLKQVVDTE 1194
Cdd:pfam09731  330 EELSARLEEVRAADEAQLRLEFEREREEIRESYEEklrtelerQAEAHEEHLKDVLVEQE--IELQREFLQDIKEKVEEE 407

                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1063705616 1195 -----TKLIELKTSMQRLEEKVSD-MEAEDKILRQQAL 1226
Cdd:pfam09731  408 ragrlLKLNELLANLKGLEKATSShSEVEDENRKAQQL 445
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 879-1031 4.38e-03

Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.


Pssm-ID: 462536 [Multi-domain]  Cd Length: 176  Bit Score: 39.92  E-value: 4.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  879 AKETGALQDAKTKLEKEVEELTSCLELEKQMRMELEQVKTQEVEDLRSALNDmklQLGETQVTKSE---EILKLQSALQD 955
Cdd:pfam08614   13 LDRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLRE---ELAELYRSRGElaqRLVDLNEELQE 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  956 MQLEFEELAKELEmtnDLAAENEQLKDLVSSLQRKI-----------DESDSKYEETSKLsEERVKqevpvidqgviiKL 1024
Cdd:pfam08614   90 LEKKLREDERRLA---ALEAERAQLEEKLKDREEELrekrklnqdlqDELVALQLQLNMA-EEKLR------------KL 153


                   ....*..
gi 1063705616 1025 EAENQKL 1031
Cdd:pfam08614  154 EKENREL 160
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
862-1060 4.58e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 4.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  862 GWRVKVAHRELRKLKMA----AKETGALQDAKTKLEKEVEEL-TSCLELEKQMRmeleQVKTQEVEDLRSALNDMKLQLG 936
Cdd:COG4913    280 ALRLWFAQRRLELLEAEleelRAELARLEAELERLEARLDALrEELDELEAQIR----GNGGDRLEQLEREIERLERELE 355

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  937 EtqvtKSEEILKLQSALQDMQLEFEELAKELemtndlAAENEQLKDLVSSLQrkidesdskyEETSKLSEERVKqevpvi 1016
Cdd:COG4913    356 E----RERRRARLEALLAALGLPLPASAEEF------AALRAEAAALLEALE----------EELEALEEALAE------ 409

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1063705616 1017 dqgviikLEAENQKLKALVSTLEKKIDSLDRKHdvtsSNISDQL 1060
Cdd:COG4913    410 -------AEAALRDLRRELRELEAEIASLERRK----SNIPARL 442
PRK01156 PRK01156
chromosome segregation protein; Provisional
 867-1217 5.81e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 41.43  E-value: 5.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  867 VAHRELRKLKMAAKETGALQDAKTKLEKEVEELTSCLELE-------KQMRMELEQVKTQEVEDLRSALND---MKLQLG 936
Cdd:PRK01156   229 NAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMEleknnyyKELEERHMKIINDPVYKNRNYINDyfkYKNDIE 308

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  937 ---------ETQVTKSEEILKLQSALQDMQLEFEELAKELEMTNDLAAENEQLKDLVSSLQRKIDESDSKYEETSKlSEE 1007
Cdd:PRK01156   309 nkkqilsniDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSK-NIE 387

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1008 RVKQEVP------VIDQGVIIKLEAE-NQKLKAL---VSTLEKKIDSLDRKHDVTSSNIS------------DQLKESAS 1065
Cdd:PRK01156   388 RMSAFISeilkiqEIDPDAIKKELNEiNVKLQDIsskVSSLNQRIRALRENLDELSRNMEmlngqsvcpvcgTTLGEEKS 467

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1066 SDyeMLSNLAAENERLKALVSSLENEnyENDGNDSPNEQKEGPQMLKEEILAEDFSIDDEMTNKLAAENKDLYDLVDLLE 1145
Cdd:PRK01156   468 NH--IINHYNEKKSRLEEKIREIEIE--VKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKD 543

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1146 R--------------KIDETEKKYEEASKLC---------------EERLKQVVDTEKKYEEAS--------------RL 1182
Cdd:PRK01156   544 KhdkyeeiknrykslKLEDLDSKRTSWLNALavislidietnrsrsNEIKKQLNDLESRLQEIEigfpddksyidksiRE 623

                          410       420       430
                   ....*....|....*....|....*....|....*
gi 1063705616 1183 CEERLKQVVDTETKLIELKTSMQRLEEKVSDMEAE 1217
Cdd:PRK01156   624 IENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQ 658
PLN02939 PLN02939
transferase, transferring glycosyl groups
 877-1217 8.64e-03

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 41.04  E-value: 8.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  877 MAAKETGALQDAKTKLEKEVEELTSCLELEKQMRM---------ELEQVKTQEVEDLRSALNDM-----KLQLGETQVTK 942
Cdd:PLN02939   102 MQRDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGMiqnaeknilLLNQARLQALEDLEKILTEKealqgKINILEMRLSE 181

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  943 SEEILKLQSA------LQDMQLE----------------FEELAKELEmtnDLAAENEQLKDLVSSLQRKIDEsdskYEE 1000
Cdd:PLN02939   182 TDARIKLAAQekihveILEEQLEklrnellirgateglcVHSLSKELD---VLKEENMLLKDDIQFLKAELIE----VAE 254

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1001 TsklsEERVkqevpvidqgviIKLEAENQKLKALVSTLEKKIdsLDRKHDVTSsniSDQLKESAssdyemlsnLAAENER 1080
Cdd:PLN02939   255 T----EERV------------FKLEKERSLLDASLRELESKF--IVAQEDVSK---LSPLQYDC---------WWEKVEN 304

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1081 LKALVSSLENEnyendgndspneqkegpqmlkeeilAEDFSIddemtnkLAAENKDLYDLVDLLERKIDETeKKYEEAS- 1159
Cdd:PLN02939   305 LQDLLDRATNQ-------------------------VEKAAL-------VLDQNQDLRDKVDKLEASLKEA-NVSKFSSy 351

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063705616 1160 ---------KLCEERLkQVVDTEkkYEEASRLCEERLKQVVDTETKLIElKTSMQRLEEKVSDMEAE 1217
Cdd:PLN02939   352 kvellqqklKLLEERL-QASDHE--IHSYIQLYQESIKEFQDTLSKLKE-ESKKRSLEHPADDMPSE 414
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
913-1048 9.58e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 40.61  E-value: 9.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  913 LEQVKTQEVEDLRSALNDMKLQLGETQVTKSEEILKLqsalqdmqlefEELAKELEmtndlaAENEQLKDLVSSLQRKID 992
Cdd:COG2433    382 LEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRL-----------EEQVERLE------AEVEELEAELEEKDERIE 444

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1063705616  993 ESDSKYEETSKLSEERVKQEvpvidqGVIIKLEAENQKLKALVSTLEKKIDSLDRK 1048
Cdd:COG2433    445 RLERELSEARSEERREIRKD------REISRLDREIERLERELEEERERIEELKRK 494
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 871-1179 9.77e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 40.80  E-value: 9.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  871 ELRKL-KMAAKETGALQDAKTKLEKEVEELTSCLELEKQMRMELEQvKTQEVEDLRSALNDMKlqlgetqvtksEEILKL 949
Cdd:TIGR00606  847 LNRKLiQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVE-LSTEVQSLIREIKDAK-----------EQDSPL 914

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616  950 QSALQDMQLEFEELAKELEMTNDLAaeNEQLKDLVSSLQRKIDESDSKYEETSKLSEERVKQEVPVIDqGVIIKLEAENQ 1029
Cdd:TIGR00606  915 ETFLEKDQQEKEELISSKETSNKKA--QDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELN-TVNAQLEECEK 991

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705616 1030 KLKALVSTLEKKIDSLDRKHdVTSSNISDQLkesassdyemlsNLAAENERLKALVSSLENENYENdGNDSPNEQKEGPQ 1109
Cdd:TIGR00606  992 HQEKINEDMRLMRQDIDTQK-IQERWLQDNL------------TLRKRENELKEVEEELKQHLKEM-GQMQVLQMKQEHQ 1057

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063705616 1110 MLKEEIlaedfsiddemtnklaaenkdlyDLVDLLERKIDETEKKYEEASKLCEERL--KQVVDTEKKYEEA 1179
Cdd:TIGR00606 1058 KLEENI-----------------------DLIKRNHVLALGRQKGYEKEIKHFKKELrePQFRDAEEKYREM 1106
 
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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