NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1836165656|ref|NP_001369278|]
View 

unconventional myosin-Va isoform 5 [Homo sapiens]

Protein Classification

kinesin family protein( domain architecture ID 12917866)

kinesin family protein is a microtubule-dependent molecular motor that plays an important role in intracellular transport and in cell division and has ATPase-containing motor domain; similar to carboxy-terminal kinesins that contains a C-terminal domain responsible for the motor activity (it hydrolyzes ATP and binds microtubules)

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
MYSc_Myo5 cd01380
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ...
 107-775 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: 1319.85  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  107 PAVLHNLRVRFIDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 186
Cdd:cd01380      1 PAVLHNLKVRFCQRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  187 GESGAGKTVSAKYAMRYFATVSGSAS-EANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRT 265
Cdd:cd01380     81 GESGAGKTVSAKYAMRYFATVGGSSSgETQVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANMRT 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  266 YLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQACTLLGISESH 345
Cdd:cd01380    161 YLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPVIDGVDDAAEFEETRKALTLLGISEEE 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  346 QMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNARD 425
Cdd:cd01380    241 QMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQAIVARD 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  426 ALAKHIYAKLFNWIVDNVNQALHSAV--KQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMK 503
Cdd:cd01380    321 ALAKHIYAQLFDWIVDRINKALASPVkeKQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQEEYVK 400

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  504 EQIPWTLIDFYDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNK-CALFEKPRLSNKAFIIQHFADKVE 582
Cdd:cd01380    401 EEIEWSFIDFYDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKpNKHFKKPRFSNTAFIVKHFADDVE 480

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  583 YQCEGFLEKNKDTVFEEQIKVLKSSKFkmlpelfqddekaisptsatssgrtpltrtpakptkgrpgqmakeHKKTVGHQ 662
Cdd:cd01380    481 YQVEGFLEKNRDTVSEEHLNVLKASKN---------------------------------------------RKKTVGSQ 515

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  663 FRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMKQKD 742
Cdd:cd01380    516 FRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSKE 595

                          650       660       670
                   ....*....|....*....|....*....|....
gi 1836165656  743 VL-SDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 775
Cdd:cd01380    596 WLrDDKKKTCENILENLILDPDKYQFGKTKIFFR 629
Myo5a_CBD cd15478
Cargo binding domain of myosin 5a; Class V myosins are well studied unconventional myosins, ...
 1505-1879 0e+00

Cargo binding domain of myosin 5a; 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 Myo5a-CBD, melanophilin (MLPH), Rab interacting lysosomal protein-like 2 (RILPL2), and granuphilin. Mutations in human Myo5a (many of which map to the cargo binding domain) lead to Griscelli syndrome, a severe neurological disease.


:

Pssm-ID: 271262  Cd Length: 375  Bit Score: 720.66  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1505 KEDEQKLVKNLILELKPRGVAVNLIPGLPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSN 1584
Cdd:cd15478      1 KEDEQKLVKNLILELKPRGVAVNLIPGLPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1585 TCRFLHCLKQYSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPMIVSGMLEHETIQGVSG 1664
Cdd:cd15478     81 TCRFLHCLKQYSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPMIVSGMLEHETIQGVSG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1665 VKPTGLRKRTSSIADEGTYTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQIR 1744
Cdd:cd15478    161 VKPTGLRKRTSSIADEGTYTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQIR 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1745 YNVSQLEEWLRDKNLMNSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERVSVSF 1824
Cdd:cd15478    241 YNVSQLEEWLRDKNLMNSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERVSVSF 320

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1836165656 1825 IRTIQMRLRDRKDSPQLLMDAKHIFPVTFPFNPSSLALETIQIPASLGLGFISRV 1879
Cdd:cd15478    321 IRTIQMRLRDRKDSPQLLMDAKHIFPVTFPFNPSSLALETIQIPASLGLGFISRV 375
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 926-1468 5.01e-18

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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 91.27  E-value: 5.01e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  926 KRELKKLKIEARSVERYKKLHigmeNKIMQLQRKVdeQNKDYKCLVEKLTNLEGIYNSETEKLRSDLERLQLSEEEAKVA 1005
Cdd:TIGR02168  199 ERQLKSLERQAEKAERYKELK----AELRELELAL--LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEEL 272

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1006 TGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQekealnhriVQQAKEMTETMEKKLV 1085
Cdd:TIGR02168  273 RLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE---------LESKLDELAEELAELE 343

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1086 EETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTlmvhvpkpghKRTDSTHSSNESEYIFSSEI----AEMEDIP 1161
Cdd:TIGR02168  344 EKLEELKEELESLEAELEELEAELEELESRLEELEEQLE----------TLRSKVAQLELQIASLNNEIerleARLERLE 413

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1162 SRTEEPSEKKVPLDMSL----FLKLQKRVTELEQEKQVMQDELDRKEEQvlrskaKEEERPQIRGAELEYESLKRQELES 1237
Cdd:TIGR02168  414 DRRERLQQEIEELLKKLeeaeLKELQAELEELEEELEELQEELERLEEA------LEELREELEEAEQALDAAERELAQL 487

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1238 ENKK--LKNELNELRKALSEKSAPEVTAPGAPAYRVLMEQLTSVSEELDVRKEEVLILRSQLV------SQKEAIQ---- 1305
Cdd:TIGR02168  488 QARLdsLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVvvenlnAAKKAIAflkq 567

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1306 -------------PKDDKNTMTDSTIL---------LEDVQKMKDKGEIAQAYI--------GLKE-TNRSSALDYHELN 1354
Cdd:TIGR02168  568 nelgrvtflpldsIKGTEIQGNDREILkniegflgvAKDLVKFDPKLRKALSYLlggvlvvdDLDNaLELAKKLRPGYRI 647

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1355 --EDGELW-----LVYEGLKQANRLLE-----SQLQSQKRSHENEAEALRGEIQSLKEENNRQQQLLAQNLQLPPEARIE 1422
Cdd:TIGR02168  648 vtLDGDLVrpggvITGGSAKTNSSILErrreiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQ 727

                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*..
gi 1836165656 1423 -ASLQHEITRLTNENLDLMEQLEKQDKTVRKLKKQLKVFAKKIGELE 1468
Cdd:TIGR02168  728 iSALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAE 774
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 837-859 1.65e-06

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.


:

Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 45.78  E-value: 1.65e-06
                            10        20
                    ....*....|....*....|...
gi 1836165656   837 RRTKAATIIQKYWRMYVVRRRYK 859
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRYK 23
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 812-834 1.85e-03

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.


:

Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 37.31  E-value: 1.85e-03
                            10        20
                    ....*....|....*....|...
gi 1836165656   812 RMRKAAITMQRYVRGYQARCYAK 834
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRYK 23
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 789-810 2.06e-03

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.


:

Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 37.31  E-value: 2.06e-03
                            10        20
                    ....*....|....*....|..
gi 1836165656   789 KLRAACIRIQKTIRGWLLRKKY 810
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRY 22
CBD_MYO6-like super family cl41207
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, ...
 853-886 3.66e-03

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


The actual alignment was detected with superfamily member cd21759:

Pssm-ID: 409646 [Multi-domain]  Cd Length: 149  Bit Score: 39.80  E-value: 3.66e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1836165656  853 VVRRRYKI--RRAATIVLQSYLRGFLARNRYRKILR 886
Cdd:cd21759     34 VIKLKNKIlyRREALIKIQKTVRGYLARKKHRPRIK 69
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 886-907 6.69e-03

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.


:

Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 35.76  E-value: 6.69e-03
                            10        20
                    ....*....|....*....|..
gi 1836165656   886 REHKAVIIQKRVRGWLARTHYK 907
Cdd:smart00015    2 LTRAAIIIQAAWRGYLARKRYK 23
 
Name Accession Description Interval E-value
MYSc_Myo5 cd01380
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ...
 107-775 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: 1319.85  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  107 PAVLHNLRVRFIDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 186
Cdd:cd01380      1 PAVLHNLKVRFCQRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  187 GESGAGKTVSAKYAMRYFATVSGSAS-EANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRT 265
Cdd:cd01380     81 GESGAGKTVSAKYAMRYFATVGGSSSgETQVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANMRT 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  266 YLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQACTLLGISESH 345
Cdd:cd01380    161 YLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPVIDGVDDAAEFEETRKALTLLGISEEE 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  346 QMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNARD 425
Cdd:cd01380    241 QMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQAIVARD 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  426 ALAKHIYAKLFNWIVDNVNQALHSAV--KQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMK 503
Cdd:cd01380    321 ALAKHIYAQLFDWIVDRINKALASPVkeKQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQEEYVK 400

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  504 EQIPWTLIDFYDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNK-CALFEKPRLSNKAFIIQHFADKVE 582
Cdd:cd01380    401 EEIEWSFIDFYDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKpNKHFKKPRFSNTAFIVKHFADDVE 480

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  583 YQCEGFLEKNKDTVFEEQIKVLKSSKFkmlpelfqddekaisptsatssgrtpltrtpakptkgrpgqmakeHKKTVGHQ 662
Cdd:cd01380    481 YQVEGFLEKNRDTVSEEHLNVLKASKN---------------------------------------------RKKTVGSQ 515

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  663 FRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMKQKD 742
Cdd:cd01380    516 FRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSKE 595

                          650       660       670
                   ....*....|....*....|....*....|....
gi 1836165656  743 VL-SDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 775
Cdd:cd01380    596 WLrDDKKKTCENILENLILDPDKYQFGKTKIFFR 629
Myosin_head pfam00063
Myosin head (motor domain);
96-775 0e+00

Myosin head (motor domain);


Pssm-ID: 395017 [Multi-domain]  Cd Length: 674  Bit Score: 1079.61  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656   96 NDLTALSYLHEPAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMA 175
Cdd:pfam00063    2 EDMVELSYLNEPSVLHNLKKRY-KSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  176 RDERNQSIIVSGESGAGKTVSAKYAMRYFATVSGSASEAN---VEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGF 252
Cdd:pfam00063   81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGNvgrLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQF 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  253 DKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHT 332
Cdd:pfam00063  161 DAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQSGCYTIDGIDDSEEFKIT 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  333 RQACTLLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATETYI 412
Cdd:pfam00063  241 DKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGRETVS 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  413 KPISKLQATNARDALAKHIYAKLFNWIVDNVNQALHS-AVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNM 491
Cdd:pfam00063  321 KPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVkTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQFFNH 400

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  492 HVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNTHlNKCALFEKPRL-SN 569
Cdd:pfam00063  401 HMFKLEQEEYVREGIEWTFIDFGDNQPCIDLIEKKpLGILSLLDEECLFPKATDQTFLDKLYSTF-SKHPHFQKPRLqGE 479

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  570 KAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGRTPltrtpaKPTKgrpg 649
Cdd:pfam00063  480 THFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGKSTP------KRTK---- 549

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  650 qmaKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQE 729
Cdd:pfam00063  550 ---KKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQE 626

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*...
gi 1836165656  730 FFSRYRVLMKQKDV--LSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 775
Cdd:pfam00063  627 FVQRYRILAPKTWPkwKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
MYSc smart00242
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...
 88-786 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: 1018.63  E-value: 0e+00
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656    88 NPDILVGENDLTALSYLHEPAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVA 167
Cdd:smart00242    1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRY-LKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIA 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656   168 EEAYKQMARDERNQSIIVSGESGAGKTVSAKYAMRYFATVSGSASEAN-VEEKVLASNPIMESIGNAKTTRNDNSSRFGK 246
Cdd:smart00242   80 DNAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEVGsVEDQILESNPILEAFGNAKTLRNNNSSRFGK 159

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656   247 YIEIGFDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDA 326
Cdd:smart00242  160 FIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQGGCLTVDGIDDA 239

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656   327 KEMAHTRQACTLLGISESHQMGIFRILAGILHLGNVGFTSRDAD-SCTIPPKHEPLCIFCELMGVDYEEMCHWLCHRKLA 405
Cdd:smart00242  240 EEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDnAASTVKDKEELSNAAELLGVDPEELEKALTKRKIK 319

                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656   406 TATETYIKPISKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKL 485
Cdd:smart00242  320 TGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSFEQLCINYANEKL 399

                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656   486 QQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEK 564
Cdd:smart00242  400 QQFFNQHVFKLEQEEYEREGIDWTFIDFFDNQDCIDLIEKKpPGILSLLDEECRFPKGTDQTFLEKLNQHHKKHPHFSKP 479

                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656   565 PRLSNKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEkaispTSATSSGRtpltrtpakpt 644
Cdd:smart00242  480 KKKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGV-----SNAGSKKR----------- 543

                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656   645 kgrpgqmakehKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSR 724
Cdd:smart00242  544 -----------FQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYR 612

                           650       660       670       680       690       700
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1836165656   725 WTYQEFFSRYRVLMKQK--DVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFRAGQVAYLEKLR 786
Cdd:smart00242  613 LPFDEFLQRYRVLLPDTwpPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELR 676
COG5022 COG5022
Myosin heavy chain [General function prediction only];
35-1257 0e+00

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 969.93  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656   35 ARVWIPDPEEVWKSAELLK-DYKPGDKVLLLHLEEGK--DLEYHLDPKTKelphlRNPDILVGENDLTALSYLHEPAVLH 111
Cdd:COG5022     10 SGCWIPDEEKGWIWAEIIKeAFNKGKVTEEGKKEDGEsvSVKKKVLGNDR-----IKLPKFDGVDDLTELSYLNEPAVLH 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  112 NLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSGESGA 191
Cdd:COG5022     85 NLEKRY-NNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGA 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  192 GKTVSAKYAMRYFATVSGSASE--ANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYLLE 269
Cdd:COG5022    164 GKTENAKRIMQYLASVTSSSTVeiSSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLE 243

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  270 KSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQACTLLGISESHQMGI 349
Cdd:COG5022    244 KSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDKIDGIDDAKEFKITLDALKTIGIDEEEQDQI 323

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  350 FRILAGILHLGNVGFTSrDADSCTIPPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNARDALAK 429
Cdd:COG5022    324 FKILAAILHIGNIEFKE-DRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAK 402

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  430 HIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWT 509
Cdd:COG5022    403 ALYSNLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWS 482

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  510 LIDFYDNQPCINLIESK--LGILDLLDEECKMPKGTDDTWAQKLYNT-HLNKCALFEKPRLSNKAFIIQHFADKVEYQCE 586
Cdd:COG5022    483 FIDYFDNQPCIDLIEKKnpLGILSLLDEECVMPHATDESFTSKLAQRlNKNSNPKFKKSRFRDNKFVVKHYAGDVEYDVE 562

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  587 GFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKaisptsatssgrtpltrtpaKPTKGRPgqmakehkKTVGHQFRNS 666
Cdd:COG5022    563 GFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEEN--------------------IESKGRF--------PTLGSRFKES 614

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  667 LHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMKQK----- 741
Cdd:COG5022    615 LNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKswtge 694

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  742 -DVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFRAGQVAYLEKLRADKLRAACIRIQKTIRGWLLRKKYLRMRKAAITM 820
Cdd:COG5022    695 yTWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKI 774

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  821 QRYVRGYQARCYAKFLRRTKAATIIQKYWRMYVVRRRYKIRRAATIVLQSYL-RGFLARNRYRKILREHKAVIIQKRVRG 899
Cdd:COG5022    775 QVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIkREKKLRETEEVEFSLKAEVLIQKFGRS 854

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  900 WLARTHYKRSMHAIIYLQCCFRRMMAKRELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQ-NKDYKCLVEKLTNLE 978
Cdd:COG5022    855 LKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKKSLSSDlIENLEFKTELIARLK 934

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  979 GIYNSETEKLRSDLERLQLSEeeakvatgrVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLL 1058
Cdd:COG5022    935 KLLNNIDLEEGPSIEYVKLPE---------LNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELS 1005

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1059 KQ------EKEALNHRIVQQAKEMTETMEKKLVEETKQLELDLNDERlryQNLLNEFSRLEERYDDLKeemtlmvhVPKP 1132
Cdd:COG5022   1006 KQygalqeSTKQLKELPVEVAELQSASKIISSESTELSILKPLQKLK---GLLLLENNQLQARYKALK--------LRRE 1074

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1133 GHKRTDSTHSSNESEYIFSSEI----AEMEDIPSRTEEPSEKKVPLDMSLFLKLQKRVTELEQ-----EKQVMQDELDRK 1203
Cdd:COG5022   1075 NSLLDDKQLYQLESTENLLKTInvkdLEVTNRNLVKPANVLQFIVAQMIKLNLLQEISKFLSQlvntlEPVFQKLSVLQL 1154

                         1210      1220      1230      1240      1250
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1836165656 1204 EEQVLRSKAKEEERPQIRGAELEYESLKRQE--LESENKKLKNELNELRKALSEKS 1257
Cdd:COG5022   1155 ELDGLFWEANLEALPSPPPFAALSEKRLYQSalYDEKSKLSSSEVNDLKNELIALF 1210
Myo5a_CBD cd15478
Cargo binding domain of myosin 5a; Class V myosins are well studied unconventional myosins, ...
 1505-1879 0e+00

Cargo binding domain of myosin 5a; 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 Myo5a-CBD, melanophilin (MLPH), Rab interacting lysosomal protein-like 2 (RILPL2), and granuphilin. Mutations in human Myo5a (many of which map to the cargo binding domain) lead to Griscelli syndrome, a severe neurological disease.


Pssm-ID: 271262  Cd Length: 375  Bit Score: 720.66  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1505 KEDEQKLVKNLILELKPRGVAVNLIPGLPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSN 1584
Cdd:cd15478      1 KEDEQKLVKNLILELKPRGVAVNLIPGLPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1585 TCRFLHCLKQYSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPMIVSGMLEHETIQGVSG 1664
Cdd:cd15478     81 TCRFLHCLKQYSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPMIVSGMLEHETIQGVSG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1665 VKPTGLRKRTSSIADEGTYTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQIR 1744
Cdd:cd15478    161 VKPTGLRKRTSSIADEGTYTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQIR 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1745 YNVSQLEEWLRDKNLMNSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERVSVSF 1824
Cdd:cd15478    241 YNVSQLEEWLRDKNLMNSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERVSVSF 320

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1836165656 1825 IRTIQMRLRDRKDSPQLLMDAKHIFPVTFPFNPSSLALETIQIPASLGLGFISRV 1879
Cdd:cd15478    321 IRTIQMRLRDRKDSPQLLMDAKHIFPVTFPFNPSSLALETIQIPASLGLGFISRV 375
PTZ00014 PTZ00014
myosin-A; Provisional
 58-822 1.72e-141

myosin-A; Provisional


Pssm-ID: 240229 [Multi-domain]  Cd Length: 821  Bit Score: 460.65  E-value: 1.72e-141
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656   58 GDKVLLLHLEEGKDLEYHLDPKtkelpHLRNPDILVGEN---DLTALSYLHEPAVLHNLRVRFIdSKLIYTYCGIVLVAI 134
Cdd:PTZ00014    63 GEKLTLKQIDPPTNSTFEVKPE-----HAFNANSQIDPMtygDIGLLPHTNIPCVLDFLKHRYL-KNQIYTTADPLLVAI 136

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  135 NPYEQLPIYGEDIINAY-SGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSGESGAGKTVSAKYAMRYFATVSGSASE 213
Cdd:PTZ00014   137 NPFKDLGNTTNDWIRRYrDAKDSDKLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFASSKSGNMD 216

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  214 ANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLC--A 291
Cdd:PTZ00014   217 LKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLkgA 296

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  292 SAKLPE-FKMLRLGNADNFNytkqGGSPVIEGVDDAKEMAHTRQACTLLGISESHQMGIFRILAGILHLGNVGFTSRDAD 370
Cdd:PTZ00014   297 NDEMKEkYKLKSLEEYKYIN----PKCLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEG 372

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  371 -----SCTIPPKHEPLCIFCELMGVDYEEMCHWLchrklaTATETYI------KPISKLQATNARDALAKHIYAKLFNWI 439
Cdd:PTZ00014   373 gltdaAAISDESLEVFNEACELLFLDYESLKKEL------TVKVTYAgnqkieGPWSKDESEMLKDSLSKAVYEKLFLWI 446

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  440 VDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPC 519
Cdd:PTZ00014   447 IRNLNATIEPPGGFKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGISTEELEYTSNESV 526

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  520 INLIESKL-GILDLLDEECKMPKGTDD----TWAQKLYNthlNKCALFEKpRLSNKAFIIQHFADKVEYQCEGFLEKNKD 594
Cdd:PTZ00014   527 IDLLCGKGkSVLSILEDQCLAPGGTDEkfvsSCNTNLKN---NPKYKPAK-VDSNKNFVIKHTIGDIQYCASGFLFKNKD 602

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  595 TVFEEQIKVLKSSKFKMLPELFQDDEkaisptsatssgrtpLTRtpakptkgrpGQMAKehKKTVGHQFRNSLHLLMETL 674
Cdd:PTZ00014   603 VLRPELVEVVKASPNPLVRDLFEGVE---------------VEK----------GKLAK--GQLIGSQFLNQLDSLMSLI 655

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  675 NATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRV--LMKQKDVLSDRKQTCK 752
Cdd:PTZ00014   656 NSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYldLAVSNDSSLDPKEKAE 735

                          730       740       750       760       770       780       790
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1836165656  753 NVLEKLILDKDKYQFGKTKIFFRAGQVAYLEKLRADKLRA--ACIRIqktIRGWLLRKKYLR-MRKAAITMQR 822
Cdd:PTZ00014   736 KLLERSGLPKDSYAIGKTMVFLKKDAAKELTQIQREKLAAwePLVSV---LEALILKIKKKRkVRKNIKSLVR 805
DIL pfam01843
DIL domain; The DIL domain has no known function.
 1711-1814 4.26e-42

DIL domain; The DIL domain has no known function.


Pssm-ID: 460359 [Multi-domain]  Cd Length: 103  Bit Score: 149.66  E-value: 4.26e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1711 QVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQIRYNVSQLEEWLRDKNLmNSGAKETLEPLIQAAQLLQVKKKTDDDAEA 1790
Cdd:pfam01843    1 QLFSQLFYFINAELFNRLLLRKKYCSWSKGMQIRYNLSRLEEWARSNGL-ESEARDHLAPLIQAAQLLQLRKSTLEDLDS 79

                           90       100
                   ....*....|....*....|....
gi 1836165656 1791 ICSMCNALTTAQIVKVLNLYTPVN 1814
Cdd:pfam01843   80 ILQVCPALNPLQLHRLLTLYQPDD 103
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 926-1468 5.01e-18

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: 91.27  E-value: 5.01e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  926 KRELKKLKIEARSVERYKKLHigmeNKIMQLQRKVdeQNKDYKCLVEKLTNLEGIYNSETEKLRSDLERLQLSEEEAKVA 1005
Cdd:TIGR02168  199 ERQLKSLERQAEKAERYKELK----AELRELELAL--LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEEL 272

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1006 TGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQekealnhriVQQAKEMTETMEKKLV 1085
Cdd:TIGR02168  273 RLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE---------LESKLDELAEELAELE 343

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1086 EETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTlmvhvpkpghKRTDSTHSSNESEYIFSSEI----AEMEDIP 1161
Cdd:TIGR02168  344 EKLEELKEELESLEAELEELEAELEELESRLEELEEQLE----------TLRSKVAQLELQIASLNNEIerleARLERLE 413

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1162 SRTEEPSEKKVPLDMSL----FLKLQKRVTELEQEKQVMQDELDRKEEQvlrskaKEEERPQIRGAELEYESLKRQELES 1237
Cdd:TIGR02168  414 DRRERLQQEIEELLKKLeeaeLKELQAELEELEEELEELQEELERLEEA------LEELREELEEAEQALDAAERELAQL 487

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1238 ENKK--LKNELNELRKALSEKSAPEVTAPGAPAYRVLMEQLTSVSEELDVRKEEVLILRSQLV------SQKEAIQ---- 1305
Cdd:TIGR02168  488 QARLdsLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVvvenlnAAKKAIAflkq 567

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1306 -------------PKDDKNTMTDSTIL---------LEDVQKMKDKGEIAQAYI--------GLKE-TNRSSALDYHELN 1354
Cdd:TIGR02168  568 nelgrvtflpldsIKGTEIQGNDREILkniegflgvAKDLVKFDPKLRKALSYLlggvlvvdDLDNaLELAKKLRPGYRI 647

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1355 --EDGELW-----LVYEGLKQANRLLE-----SQLQSQKRSHENEAEALRGEIQSLKEENNRQQQLLAQNLQLPPEARIE 1422
Cdd:TIGR02168  648 vtLDGDLVrpggvITGGSAKTNSSILErrreiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQ 727

                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*..
gi 1836165656 1423 -ASLQHEITRLTNENLDLMEQLEKQDKTVRKLKKQLKVFAKKIGELE 1468
Cdd:TIGR02168  728 iSALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAE 774
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 951-1458 1.41e-13

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: 76.30  E-value: 1.41e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  951 NKIMQLQRKVDEQNKDYKCLVEKLTNLegiyNSETEKLRSDLER----LQLSEEEAKVATGRVLSLQEEIAKLRKDLEQT 1026
Cdd:pfam05483  268 DKANQLEEKTKLQDENLKELIEKKDHL----TKELEDIKMSLQRsmstQKALEEDLQIATKTICQLTEEKEAQMEELNKA 343

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1027 RSEKKCIeehADRYKQETEQLVSNLKEENTLLKQEKEALNHRIVQQAKEMTETMEKKLVEETKQLELD------LNDERL 1100
Cdd:pfam05483  344 KAAHSFV---VTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEelkkilAEDEKL 420

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1101 RYQNllNEFSRLEERYDDLKEEMTLMVHV-PKPGHKRTDSTHSSNESEYIFSSEIAEMedipsRTEEPSEKKVPLDMSLF 1179
Cdd:pfam05483  421 LDEK--KQFEKIAEELKGKEQELIFLLQArEKEIHDLEIQLTAIKTSEEHYLKEVEDL-----KTELEKEKLKNIELTAH 493

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1180 L-KLQKRVTELEQEKQVMQDELDRKEEQVLRSKaKEEER--PQIRGAElEYESLKRQELESENKKLKNELNELRKAL--S 1254
Cdd:pfam05483  494 CdKLLLENKELTQEASDMTLELKKHQEDIINCK-KQEERmlKQIENLE-EKEMNLRDELESVREEFIQKGDEVKCKLdkS 571

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1255 EKSAPEV---TAPGAPAYRVLMEQLTSVSEELDVRKEEVlilrSQLVSQKEAIQPKDDKNTMTDSTILLEdVQKMKDKGE 1331
Cdd:pfam05483  572 EENARSIeyeVLKKEKQMKILENKCNNLKKQIENKNKNI----EELHQENKALKKKGSAENKQLNAYEIK-VNKLELELA 646

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1332 IAQAYIGLKETNRSSALDYHELNEDGELWLVYEGLKQANRLLESQLQSQKRSHENEAEAL----RGEIQSLKEENNRQQQ 1407
Cdd:pfam05483  647 SAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMValmeKHKHQYDKIIEERDSE 726

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1836165656 1408 LLAQNLQLPPEARIEASLQHEITRLTNENLDLMEQLEKQDKTVRKLKKQLK 1458
Cdd:pfam05483  727 LGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAK 777
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 926-1310 1.28e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 73.43  E-value: 1.28e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  926 KRELKKLKIEARSVERYKKLHIGMEnkimqlQRKVDEQNKDYKCLVEKLTNLEGIYNSETEKLRSDLERLQLSEEEAKVA 1005
Cdd:COG1196    199 ERQLEPLERQAEKAERYRELKEELK------ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEEL 272

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1006 TGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEentlLKQEKEALNHRIVQQAKEMTETMEKKLV 1085
Cdd:COG1196    273 RLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE----LEEELAELEEELEELEEELEELEEELEE 348

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1086 EETK--QLELDLNDERLRYQNLLNEFSRLEERYDDLKEEmtlmvhvpkpghkrtdsthssneseyiFSSEIAEMEDIPSR 1163
Cdd:COG1196    349 AEEEleEAEAELAEAEEALLEAEAELAEAEEELEELAEE---------------------------LLEALRAAAELAAQ 401

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1164 TEEPSEKKvpldmslfLKLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEErpqiRGAELEYESLKRQELESENKKLK 1243
Cdd:COG1196    402 LEELEEAE--------EALLERLERLEEELEELEEALAELEEEEEEEEEALEE----AAEEEAELEEEEEALLELLAELL 469

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1836165656 1244 NELNELRKALSEKSAPEVTApgAPAYRVLMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQPKDDK 1310
Cdd:COG1196    470 EEAALLEAALAELLEELAEA--AARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEA 534
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
966-1468 1.59e-12

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 72.79  E-value: 1.59e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  966 DYKCLVEKLTNLEGIYNSETEKLRSDLERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKqETE 1045
Cdd:PRK03918   159 DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE-ELK 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1046 QLVSNLKEENTLLKQEKEALNHRIVQqakemTETMEKKLVEETKQLEldlndERLRYqnlLNEFSRLEERYDDLKEEMTL 1125
Cdd:PRK03918   238 EEIEELEKELESLEGSKRKLEEKIRE-----LEERIEELKKEIEELE-----EKVKE---LKELKEKAEEYIKLSEFYEE 304

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1126 MVHVPKPGHKRTDSTHSSNESeyiFSSEIAEMEDIPSRTEEPSEKKVpldmslflKLQKRVTELEQEKQVMQDELDRKEE 1205
Cdd:PRK03918   305 YLDELREIEKRLSRLEEEING---IEERIKELEEKEERLEELKKKLK--------ELEKRLEELEERHELYEEAKAKKEE 373

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1206 -QVLRSKAKEEERPQIRgAELEYESLKRQELESENKK-------LKNELNELRKALSEKSAPEVTAPgapayrVLMEQLT 1277
Cdd:PRK03918   374 lERLKKRLTGLTPEKLE-KELEELEKAKEEIEEEISKitarigeLKKEIKELKKAIEELKKAKGKCP------VCGRELT 446

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1278 SvSEELDVRKEEVLILRSQLVSQKEAI-QPKDDKNTMTDSTILLEDVQKMKDKGEIAQAYIGLKEtnRSSALDYHELNED 1356
Cdd:PRK03918   447 E-EHRKELLEEYTAELKRIEKELKEIEeKERKLRKELRELEKVLKKESELIKLKELAEQLKELEE--KLKKYNLEELEKK 523

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1357 GELwlvYEGLKQANRLLESQLQSQKRS------HENEAEALRGEIQSLKEEN---NRQQQLLAQNLQLPPEARIEA--SL 1425
Cdd:PRK03918   524 AEE---YEKLKEKLIKLKGEIKSLKKElekleeLKKKLAELEKKLDELEEELaelLKELEELGFESVEELEERLKElePF 600

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|...
gi 1836165656 1426 QHEITRLTNENLDLMEQLEKQDKTVRKLKKQLKVFAKKIGELE 1468
Cdd:PRK03918   601 YNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLE 643
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 837-859 1.65e-06

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 45.78  E-value: 1.65e-06
                            10        20
                    ....*....|....*....|...
gi 1836165656   837 RRTKAATIIQKYWRMYVVRRRYK 859
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRYK 23
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
 839-859 5.76e-05

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 459869  Cd Length: 21  Bit Score: 41.53  E-value: 5.76e-05
                           10        20
                   ....*....|....*....|.
gi 1836165656  839 TKAATIIQKYWRMYVVRRRYK 859
Cdd:pfam00612    1 RKAAIKIQAAWRGYLARKRYK 21
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
 833-863 2.14e-04

IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory complex protein 10 (DRC10), belongs to the IQ motif-containing protein family which contains a C-terminal conserved IQ motif domain and two coiled-coil domains. The IQ motif ([ILV]QxxxRxxxx[RK]), where x stands for any amino-acid residue, interacts with calmodulin (CaM) in a calcium-independent manner and is present in proteins with a wide diversity of biological functions. The IQCD protein was found to primarily accumulate in the acrosome area of round and elongating spermatids of the testis during late stage of spermiogenesis and was then localized to the acrosome and tail regions of mature spermatozoa. The expression of IQCD follows the trajectory of acrosome development during spermatogenesis. IQCD is associated with neuroblastoma and neurodegenerative diseases, and is reported to interact with the nuclear retinoid X receptor in the presence of 9-cis-retinoic acid, thereby activating the transcriptional activity of the receptor.


Pssm-ID: 467745 [Multi-domain]  Cd Length: 37  Bit Score: 40.22  E-value: 2.14e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1836165656  833 AKFLRRTKAATIIQKYWRMYVVRRRYKIRRA 863
Cdd:cd23767      3 EELQRMNRAATLIQALWRGYKVRKELKKKKK 33
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 812-834 1.85e-03

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 37.31  E-value: 1.85e-03
                            10        20
                    ....*....|....*....|...
gi 1836165656   812 RMRKAAITMQRYVRGYQARCYAK 834
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRYK 23
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 789-810 2.06e-03

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 37.31  E-value: 2.06e-03
                            10        20
                    ....*....|....*....|..
gi 1836165656   789 KLRAACIRIQKTIRGWLLRKKY 810
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRY 22
CBD_MYO6-like cd21759
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, ...
 791-818 3.36e-03

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


Pssm-ID: 409646 [Multi-domain]  Cd Length: 149  Bit Score: 39.80  E-value: 3.36e-03
                           10        20
                   ....*....|....*....|....*...
gi 1836165656  791 RAACIRIQKTIRGWLLRKKYlRMRKAAI 818
Cdd:cd21759     45 REALIKIQKTVRGYLARKKH-RPRIKGL 71
CBD_MYO6-like cd21759
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, ...
 853-886 3.66e-03

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


Pssm-ID: 409646 [Multi-domain]  Cd Length: 149  Bit Score: 39.80  E-value: 3.66e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1836165656  853 VVRRRYKI--RRAATIVLQSYLRGFLARNRYRKILR 886
Cdd:cd21759     34 VIKLKNKIlyRREALIKIQKTVRGYLARKKHRPRIK 69
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 967-1109 5.57e-03

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


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 41.02  E-value: 5.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  967 YKCLVEKLTNLEGIYNSETEKLRSDLERLQL------SEEEAKVATGRVLSLQE-EIAKLRKDLEQTRSEKKCIEEHADR 1039
Cdd:cd16269    144 YQLYLEDREKLVEKYRQVPRKGVKAEEVLQEflqskeAEAEAILQADQALTEKEkEIEAERAKAEAAEQERKLLEEQQRE 223

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1040 YKQETEQLVSNLKEENTLLKQEKEAlnhRIVQQAKEMTETMEKKLVEETKQLELDLNDERLRYQNLLNEF 1109
Cdd:cd16269    224 LEQKLEDQERSYEEHLRQLKEKMEE---ERENLLKEQERALESKLKEQEALLEEGFKEQAELLQEEIRSL 290
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 886-907 6.69e-03

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 35.76  E-value: 6.69e-03
                            10        20
                    ....*....|....*....|..
gi 1836165656   886 REHKAVIIQKRVRGWLARTHYK 907
Cdd:smart00015    2 LTRAAIIIQAAWRGYLARKRYK 23
 
Name Accession Description Interval E-value
MYSc_Myo5 cd01380
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ...
 107-775 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: 1319.85  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  107 PAVLHNLRVRFIDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 186
Cdd:cd01380      1 PAVLHNLKVRFCQRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  187 GESGAGKTVSAKYAMRYFATVSGSAS-EANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRT 265
Cdd:cd01380     81 GESGAGKTVSAKYAMRYFATVGGSSSgETQVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANMRT 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  266 YLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQACTLLGISESH 345
Cdd:cd01380    161 YLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPVIDGVDDAAEFEETRKALTLLGISEEE 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  346 QMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNARD 425
Cdd:cd01380    241 QMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQAIVARD 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  426 ALAKHIYAKLFNWIVDNVNQALHSAV--KQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMK 503
Cdd:cd01380    321 ALAKHIYAQLFDWIVDRINKALASPVkeKQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQEEYVK 400

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  504 EQIPWTLIDFYDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNK-CALFEKPRLSNKAFIIQHFADKVE 582
Cdd:cd01380    401 EEIEWSFIDFYDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKpNKHFKKPRFSNTAFIVKHFADDVE 480

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  583 YQCEGFLEKNKDTVFEEQIKVLKSSKFkmlpelfqddekaisptsatssgrtpltrtpakptkgrpgqmakeHKKTVGHQ 662
Cdd:cd01380    481 YQVEGFLEKNRDTVSEEHLNVLKASKN---------------------------------------------RKKTVGSQ 515

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  663 FRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMKQKD 742
Cdd:cd01380    516 FRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSKE 595

                          650       660       670
                   ....*....|....*....|....*....|....
gi 1836165656  743 VL-SDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 775
Cdd:cd01380    596 WLrDDKKKTCENILENLILDPDKYQFGKTKIFFR 629
Myosin_head pfam00063
Myosin head (motor domain);
96-775 0e+00

Myosin head (motor domain);


Pssm-ID: 395017 [Multi-domain]  Cd Length: 674  Bit Score: 1079.61  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656   96 NDLTALSYLHEPAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMA 175
Cdd:pfam00063    2 EDMVELSYLNEPSVLHNLKKRY-KSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  176 RDERNQSIIVSGESGAGKTVSAKYAMRYFATVSGSASEAN---VEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGF 252
Cdd:pfam00063   81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGNvgrLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQF 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  253 DKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHT 332
Cdd:pfam00063  161 DAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQSGCYTIDGIDDSEEFKIT 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  333 RQACTLLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATETYI 412
Cdd:pfam00063  241 DKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGRETVS 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  413 KPISKLQATNARDALAKHIYAKLFNWIVDNVNQALHS-AVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNM 491
Cdd:pfam00063  321 KPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVkTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQFFNH 400

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  492 HVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNTHlNKCALFEKPRL-SN 569
Cdd:pfam00063  401 HMFKLEQEEYVREGIEWTFIDFGDNQPCIDLIEKKpLGILSLLDEECLFPKATDQTFLDKLYSTF-SKHPHFQKPRLqGE 479

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  570 KAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGRTPltrtpaKPTKgrpg 649
Cdd:pfam00063  480 THFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGKSTP------KRTK---- 549

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  650 qmaKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQE 729
Cdd:pfam00063  550 ---KKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQE 626

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*...
gi 1836165656  730 FFSRYRVLMKQKDV--LSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 775
Cdd:pfam00063  627 FVQRYRILAPKTWPkwKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
MYSc smart00242
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...
 88-786 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: 1018.63  E-value: 0e+00
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656    88 NPDILVGENDLTALSYLHEPAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVA 167
Cdd:smart00242    1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRY-LKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIA 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656   168 EEAYKQMARDERNQSIIVSGESGAGKTVSAKYAMRYFATVSGSASEAN-VEEKVLASNPIMESIGNAKTTRNDNSSRFGK 246
Cdd:smart00242   80 DNAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEVGsVEDQILESNPILEAFGNAKTLRNNNSSRFGK 159

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656   247 YIEIGFDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDA 326
Cdd:smart00242  160 FIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQGGCLTVDGIDDA 239

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656   327 KEMAHTRQACTLLGISESHQMGIFRILAGILHLGNVGFTSRDAD-SCTIPPKHEPLCIFCELMGVDYEEMCHWLCHRKLA 405
Cdd:smart00242  240 EEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDnAASTVKDKEELSNAAELLGVDPEELEKALTKRKIK 319

                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656   406 TATETYIKPISKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKL 485
Cdd:smart00242  320 TGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSFEQLCINYANEKL 399

                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656   486 QQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEK 564
Cdd:smart00242  400 QQFFNQHVFKLEQEEYEREGIDWTFIDFFDNQDCIDLIEKKpPGILSLLDEECRFPKGTDQTFLEKLNQHHKKHPHFSKP 479

                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656   565 PRLSNKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEkaispTSATSSGRtpltrtpakpt 644
Cdd:smart00242  480 KKKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGV-----SNAGSKKR----------- 543

                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656   645 kgrpgqmakehKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSR 724
Cdd:smart00242  544 -----------FQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYR 612

                           650       660       670       680       690       700
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1836165656   725 WTYQEFFSRYRVLMKQK--DVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFRAGQVAYLEKLR 786
Cdd:smart00242  613 LPFDEFLQRYRVLLPDTwpPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELR 676
COG5022 COG5022
Myosin heavy chain [General function prediction only];
35-1257 0e+00

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 969.93  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656   35 ARVWIPDPEEVWKSAELLK-DYKPGDKVLLLHLEEGK--DLEYHLDPKTKelphlRNPDILVGENDLTALSYLHEPAVLH 111
Cdd:COG5022     10 SGCWIPDEEKGWIWAEIIKeAFNKGKVTEEGKKEDGEsvSVKKKVLGNDR-----IKLPKFDGVDDLTELSYLNEPAVLH 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  112 NLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSGESGA 191
Cdd:COG5022     85 NLEKRY-NNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGA 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  192 GKTVSAKYAMRYFATVSGSASE--ANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYLLE 269
Cdd:COG5022    164 GKTENAKRIMQYLASVTSSSTVeiSSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLE 243

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  270 KSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQACTLLGISESHQMGI 349
Cdd:COG5022    244 KSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDKIDGIDDAKEFKITLDALKTIGIDEEEQDQI 323

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  350 FRILAGILHLGNVGFTSrDADSCTIPPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNARDALAK 429
Cdd:COG5022    324 FKILAAILHIGNIEFKE-DRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAK 402

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  430 HIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWT 509
Cdd:COG5022    403 ALYSNLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWS 482

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  510 LIDFYDNQPCINLIESK--LGILDLLDEECKMPKGTDDTWAQKLYNT-HLNKCALFEKPRLSNKAFIIQHFADKVEYQCE 586
Cdd:COG5022    483 FIDYFDNQPCIDLIEKKnpLGILSLLDEECVMPHATDESFTSKLAQRlNKNSNPKFKKSRFRDNKFVVKHYAGDVEYDVE 562

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  587 GFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKaisptsatssgrtpltrtpaKPTKGRPgqmakehkKTVGHQFRNS 666
Cdd:COG5022    563 GFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEEN--------------------IESKGRF--------PTLGSRFKES 614

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  667 LHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMKQK----- 741
Cdd:COG5022    615 LNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKswtge 694

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  742 -DVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFRAGQVAYLEKLRADKLRAACIRIQKTIRGWLLRKKYLRMRKAAITM 820
Cdd:COG5022    695 yTWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKI 774

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  821 QRYVRGYQARCYAKFLRRTKAATIIQKYWRMYVVRRRYKIRRAATIVLQSYL-RGFLARNRYRKILREHKAVIIQKRVRG 899
Cdd:COG5022    775 QVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIkREKKLRETEEVEFSLKAEVLIQKFGRS 854

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  900 WLARTHYKRSMHAIIYLQCCFRRMMAKRELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQ-NKDYKCLVEKLTNLE 978
Cdd:COG5022    855 LKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKKSLSSDlIENLEFKTELIARLK 934

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  979 GIYNSETEKLRSDLERLQLSEeeakvatgrVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLL 1058
Cdd:COG5022    935 KLLNNIDLEEGPSIEYVKLPE---------LNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELS 1005

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1059 KQ------EKEALNHRIVQQAKEMTETMEKKLVEETKQLELDLNDERlryQNLLNEFSRLEERYDDLKeemtlmvhVPKP 1132
Cdd:COG5022   1006 KQygalqeSTKQLKELPVEVAELQSASKIISSESTELSILKPLQKLK---GLLLLENNQLQARYKALK--------LRRE 1074

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1133 GHKRTDSTHSSNESEYIFSSEI----AEMEDIPSRTEEPSEKKVPLDMSLFLKLQKRVTELEQ-----EKQVMQDELDRK 1203
Cdd:COG5022   1075 NSLLDDKQLYQLESTENLLKTInvkdLEVTNRNLVKPANVLQFIVAQMIKLNLLQEISKFLSQlvntlEPVFQKLSVLQL 1154

                         1210      1220      1230      1240      1250
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1836165656 1204 EEQVLRSKAKEEERPQIRGAELEYESLKRQE--LESENKKLKNELNELRKALSEKS 1257
Cdd:COG5022   1155 ELDGLFWEANLEALPSPPPFAALSEKRLYQSalYDEKSKLSSSEVNDLKNELIALF 1210
MYSc cd00124
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ...
 107-775 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: 880.39  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  107 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMG-DMDPHIFAVAEEAYKQMARDERNQSIIV 185
Cdd:cd00124      1 AAILHNLRERY-ARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  186 SGESGAGKTVSAKYAMRYFATVSGSAS------EANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRII 259
Cdd:cd00124     80 SGESGAGKTETTKLVLKYLAALSGSGSskssssASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLV 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  260 GANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADN----FNYTKQGGSPVIEGVDDAKEMAHTRQA 335
Cdd:cd00124    160 GASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSyyylNDYLNSSGCDRIDGVDDAEEFQELLDA 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  336 CTLLGISESHQMGIFRILAGILHLGNVGFTSR--DADSCTIPPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATETYIK 413
Cdd:cd00124    240 LDVLGFSDEEQDSIFRILAAILHLGNIEFEEDeeDEDSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETITK 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  414 PISKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQH--SFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNM 491
Cdd:cd00124    320 PLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAEstSFIGILDIFGFENFEVNSFEQLCINYANEKLQQFFNQ 399

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  492 HVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRLSNK 570
Cdd:cd00124    400 HVFKLEQEEYEEEGIDWSFIDFPDNQDCLDLIEGKpLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKRKAKL 479

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  571 AFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKfkmlpelfqddekaisptsatssgrtpltrtpakptkgrpgq 650
Cdd:cd00124    480 EFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGS------------------------------------------ 517

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  651 makehkktvghQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEF 730
Cdd:cd00124    518 -----------QFRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEF 586

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*..
gi 1836165656  731 FSRYRVLMKQKDVLSDR--KQTCKNVLEKLILDKDKYQFGKTKIFFR 775
Cdd:cd00124    587 LKRYRILAPGATEKASDskKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
MYSc_class_II cd01377
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ...
 107-775 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: 799.37  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  107 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 186
Cdd:cd01377      1 ASVLHNLRERY-YSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILIT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  187 GESGAGKTVSAKYAMRYFATVSGSA--------SEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRI 258
Cdd:cd01377     80 GESGAGKTENTKKVIQYLASVAASSkkkkesgkKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKI 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  259 IGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQACTL 338
Cdd:cd01377    160 AGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAFDI 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  339 LGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKPISKL 418
Cdd:cd01377    240 LGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKE 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  419 QATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQ 498
Cdd:cd01377    320 QVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQ 399

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  499 EEYMKEQIPWTLIDF-YDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPR--LSNKAFII 574
Cdd:cd01377    400 EEYKKEGIEWTFIDFgLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKPKpkKSEAHFIL 479

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  575 QHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGRTPLtrtpakptkgrpgqmake 654
Cdd:cd01377    480 KHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEESGGGGGKKKKKGGSF------------------ 541

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  655 hkKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRY 734
Cdd:cd01377    542 --RTVSQLHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRY 619

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|...
gi 1836165656  735 RVLMKQ--KDVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 775
Cdd:cd01377    620 SILAPNaiPKGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
MYSc_Myo11 cd01384
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ...
 107-775 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: 762.99  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  107 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLP-IYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIV 185
Cdd:cd01384      1 PGVLHNLKVRY-ELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  186 SGESGAGKTVSAKYAMRYFATVSGSAS--EANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANM 263
Cdd:cd01384     80 SGESGAGKTETTKMLMQYLAYMGGRAVteGRSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAAI 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  264 RTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQACTLLGISE 343
Cdd:cd01384    160 RTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNQSKCFELDGVDDAEEYRATRRAMDVVGISE 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  344 SHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEP---LCIFCELMGVDYEEMCHWLCHRKLATATETYIKPISKLQA 420
Cdd:cd01384    240 EEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKSefhLKAAAELLMCDEKALEDALCKRVIVTPDGIITKPLDPDAA 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  421 TNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEE 500
Cdd:cd01384    320 TLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQHVFKMEQEE 399

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  501 YMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNThLNKCALFEKPRLSNKAFIIQHFAD 579
Cdd:cd01384    400 YTKEEIDWSYIEFVDNQDVLDLIEKKpGGIIALLDEACMFPRSTHETFAQKLYQT-LKDHKRFSKPKLSRTDFTIDHYAG 478

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  580 KVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELF--QDDEKAISPTSATSsgrtpltrtpakptkgrpgqmakehkk 657
Cdd:cd01384    479 DVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFppLPREGTSSSSKFSS--------------------------- 531

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  658 tVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVL 737
Cdd:cd01384    532 -IGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLL 610

                          650       660       670
                   ....*....|....*....|....*....|....*....
gi 1836165656  738 MKQKDVLS-DRKQTCKNVLEKLILdkDKYQFGKTKIFFR 775
Cdd:cd01384    611 APEVLKGSdDEKAACKKILEKAGL--KGYQIGKTKVFLR 647
MYSc_Myo7 cd01381
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ...
 108-775 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: 754.86  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  108 AVLHNLRVRFIDsKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 187
Cdd:cd01381      2 GILRNLLIRYRE-KLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  188 ESGAGKTVSAKYAMRYFATVSGSASEanVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYL 267
Cdd:cd01381     81 ESGAGKTESTKLILQYLAAISGQHSW--IEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKIEQYL 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  268 LEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQACTLLGISESHQM 347
Cdd:cd01381    159 LEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGNCLTCEGRDDAAEFADIRSAMKVLMFTDEEIW 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  348 GIFRILAGILHLGNVGFTSRDA---DSCTIpPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNAR 424
Cdd:cd01381    239 DIFKLLAAILHLGNIKFEATVVdnlDASEV-RDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAEQALDVR 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  425 DALAKHIYAKLFNWIVDNVNQALHSAVKQHSF---IGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEY 501
Cdd:cd01381    318 DAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtsIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFKLEQEEY 397

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  502 MKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNTHLNKcALFEKPR-LSNKAFIIQHFAD 579
Cdd:cd01381    398 DKEGINWQHIEFVDNQDVLDLIALKpMNIMSLIDEESKFPKGTDQTMLEKLHSTHGNN-KNYLKPKsDLNTSFGINHFAG 476

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  580 KVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEkaisPTSATSSGRTPltrtpakptkgrpgqmakehkkTV 659
Cdd:cd01381    477 VVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDI----SMGSETRKKSP----------------------TL 530

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  660 GHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMK 739
Cdd:cd01381    531 SSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVP 610

                          650       660       670
                   ....*....|....*....|....*....|....*...
gi 1836165656  740 --QKDVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 775
Cdd:cd01381    611 giPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
MYSc_Myo8 cd01383
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ...
 107-775 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: 732.58  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  107 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDmdPHIFAVAEEAYKQMARDERNQSIIVS 186
Cdd:cd01383      1 PSVLHNLEYRY-SQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYRQKLLDS--PHVYAVADTAYREMMRDEINQSIIIS 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  187 GESGAGKTVSAKYAMRYFATVSGSASeaNVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTY 266
Cdd:cd01383     78 GESGAGKTETAKIAMQYLAALGGGSS--GIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQTY 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  267 LLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQACTLLGISESHQ 346
Cdd:cd01383    156 LLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNQSNCLTIDGVDDAKKFHELKEALDTVGISKEDQ 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  347 MGIFRILAGILHLGNVGFTSRDADSCTIPPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNARDA 426
Cdd:cd01383    236 EHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAIDARDA 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  427 LAKHIYAKLFNWIVDNVNQALHSAVKQHS-FIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQ 505
Cdd:cd01383    316 LAKAIYASLFDWLVEQINKSLEVGKRRTGrSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEEYELDG 395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  506 IPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLyNTHLNKCALFEKPRlsNKAFIIQHFADKVEYQ 584
Cdd:cd01383    396 IDWTKVDFEDNQECLDLIEKKpLGLISLLDEESNFPKATDLTFANKL-KQHLKSNSCFKGER--GGAFTIRHYAGEVTYD 472

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  585 CEGFLEKNKDTVFEEQIKVLKSSKFKmLPELFQddekaispTSATSSGRTPLTRTPAkptkGRPGQMakehKKTVGHQFR 664
Cdd:cd01383    473 TSGFLEKNRDLLHSDLIQLLSSCSCQ-LPQLFA--------SKMLDASRKALPLTKA----SGSDSQ----KQSVATKFK 535

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  665 NSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLM-KQKDV 743
Cdd:cd01383    536 GQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLpEDVSA 615

                          650       660       670
                   ....*....|....*....|....*....|..
gi 1836165656  744 LSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 775
Cdd:cd01383    616 SQDPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
Myo5a_CBD cd15478
Cargo binding domain of myosin 5a; Class V myosins are well studied unconventional myosins, ...
 1505-1879 0e+00

Cargo binding domain of myosin 5a; 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 Myo5a-CBD, melanophilin (MLPH), Rab interacting lysosomal protein-like 2 (RILPL2), and granuphilin. Mutations in human Myo5a (many of which map to the cargo binding domain) lead to Griscelli syndrome, a severe neurological disease.


Pssm-ID: 271262  Cd Length: 375  Bit Score: 720.66  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1505 KEDEQKLVKNLILELKPRGVAVNLIPGLPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSN 1584
Cdd:cd15478      1 KEDEQKLVKNLILELKPRGVAVNLIPGLPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1585 TCRFLHCLKQYSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPMIVSGMLEHETIQGVSG 1664
Cdd:cd15478     81 TCRFLHCLKQYSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPMIVSGMLEHETIQGVSG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1665 VKPTGLRKRTSSIADEGTYTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQIR 1744
Cdd:cd15478    161 VKPTGLRKRTSSIADEGTYTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQIR 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1745 YNVSQLEEWLRDKNLMNSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERVSVSF 1824
Cdd:cd15478    241 YNVSQLEEWLRDKNLMNSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERVSVSF 320

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1836165656 1825 IRTIQMRLRDRKDSPQLLMDAKHIFPVTFPFNPSSLALETIQIPASLGLGFISRV 1879
Cdd:cd15478    321 IRTIQMRLRDRKDSPQLLMDAKHIFPVTFPFNPSSLALETIQIPASLGLGFISRV 375
MYSc_Myo22 cd14883
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ...
 108-775 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: 719.11  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  108 AVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 187
Cdd:cd14883      2 GINTNLKVRY-KKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  188 ESGAGKTVSAKYAMRYFATVSGSASEanVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYL 267
Cdd:cd14883     81 ESGAGKTETTKLILQYLCAVTNNHSW--VEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGAIIQDYL 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  268 LEKSRVVFQAEEERNYHIFYQLCASAKL-PEFK-MLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQACTLLGISESH 345
Cdd:cd14883    159 LEQSRITFQAPGERNYHVFYQLLAGAKHsKELKeKLKLGEPEDYHYLNQSGCIRIDNINDKKDFDHLRLAMNVLGIPEEM 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  346 QMGIFRILAGILHLGNVGFTSRDADSCTIPPKH-EPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNAR 424
Cdd:cd14883    239 QEGIFSVLSAILHLGNLTFEDIDGETGALTVEDkEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQEARDNR 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  425 DALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKE 504
Cdd:cd14883    319 DAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKLEQEEYEKE 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  505 QIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNTHlNKCALFEKP--RLSNKAFIIQHFADKV 581
Cdd:cd14883    399 GINWSHIVFTDNQECLDLIEKPpLGILKLLDEECRFPKGTDLTYLEKLHAAH-EKHPYYEKPdrRRWKTEFGVKHYAGEV 477

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  582 EYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQ-DDEKAISPTSATSSGRTPLTRTpakpTKGRPgqmakehkkTVG 660
Cdd:cd14883    478 TYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTyPDLLALTGLSISLGGDTTSRGT----SKGKP---------TVG 544

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  661 HQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMKQ 740
Cdd:cd14883    545 DTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPR 624

                          650       660       670
                   ....*....|....*....|....*....|....*..
gi 1836165656  741 KDVLSDRKQ--TCKNVLEKLILDKDKYQFGKTKIFFR 775
Cdd:cd14883    625 ARSADHKETcgAVRALMGLGGLPEDEWQVGKTKVFLR 661
MYSc_Myo1 cd01378
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ...
 108-775 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: 717.40  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  108 AVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 187
Cdd:cd01378      2 AINENLKKRF-ENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  188 ESGAGKTVSAKYAMRYFATVSGSaSEANVE---EKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMR 264
Cdd:cd01378     81 ESGAGKTEASKRIMQYIAAVSGG-SESEVErvkDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGHIT 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  265 TYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQACTLLGISES 344
Cdd:cd01378    160 NYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVIGFTEE 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  345 HQMGIFRILAGILHLGNVGFTSRDADSCTIPPKhEPLCIFCELMGVDYEEMCHWLCHRKLATATE---TYIKPISKLQAT 421
Cdd:cd01378    240 EQDSIFRILAAILHLGNIQFAEDEEGNAAISDT-SVLDFVAYLLGVDPDQLEKALTHRTIETGGGgrsVYEVPLNVEQAA 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  422 NARDALAKHIYAKLFNWIVDNVNQALHSAVKQHS-FIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEE 500
Cdd:cd01378    319 YARDALAKAIYSRLFDWIVERINKSLAAKSGGKKkVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELTLKAEQEE 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  501 YMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECK-MPKGTDDTWAQKLyNTHLNKCALFEKP----RLSNKAFII 574
Cdd:cd01378    399 YVREGIEWTPIKYFNNKIICDLIEEKpPGIFAILDDACLtAGDATDQTFLQKL-NQLFSNHPHFECPsghfELRRGEFRI 477

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  575 QHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDekaisptsatssgrtpltrtPAKPTKGRPgqmake 654
Cdd:cd01378    478 KHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEG--------------------VDLDSKKRP------ 531

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  655 hkKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRY 734
Cdd:cd01378    532 --PTAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERY 609

                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1836165656  735 RVLMK----------QKDVLSDRKQTCknvlekliLDKDKYQFGKTKIFFR 775
Cdd:cd01378    610 KLLSPktwpawdgtwQGGVESILKDLN--------IPPEEYQMGKTKIFIR 652
Myo5b_CBD cd15477
Cargo binding domain of myosin 5b; Class V myosins are well studied unconventional myosins, ...
 1505-1876 0e+00

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: 646.53  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1505 KEDEQKLVKNLILELKPRGVAVNlIPGLPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSN 1584
Cdd:cd15477      1 KEDEALLIRNLVTDLKPQAVSAT-VPCLPAYILYMCIRHADYINDDQKVHSLLTSTINGIKKVLKKHNDDFEMTSFWLAN 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1585 TCRFLHCLKQYSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPMIVSGMLEHETIQGVSG 1664
Cdd:cd15477     80 TCRLLHCLKQYSGDEGFMTQNTAKQNEHCLKNFDLTEYRQVLSDLSIQIYQQLIKIAEGILQPMIVSAMLENESIQGLSG 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1665 VKPTGLRKRTSSIAD-EGTYTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQI 1743
Cdd:cd15477    160 VKPMGYRKRSSSMADgDNSYTLEALIRQLNTFHSIMCDQGLDPEIIQQVFKQLFYMINAVTLNNLLLRKDVCSWSTGMQL 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1744 RYNVSQLEEWLRDKNLMNSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERVSVS 1823
Cdd:cd15477    240 RYNISQLEEWLRGRNLHQSGAAQTMEPLIQAAQLLQLKKKTSEDAEAICSLCTALSTQQIVKILNLYTPLNEFEERVTVS 319

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1836165656 1824 FIRTIQMRLRDRKDSPQLLMDAKHIFPVTFPFNPSSLALETIQIPASLGLGFI 1876
Cdd:cd15477    320 FIRTIQAQLQERNDPPQLLLDTKHMFPVLFPFNPSALTLDSIHIPASLNLDFL 372
MYSc_Myo42 cd14903
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ...
 107-775 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: 641.83  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  107 PAVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLP-IYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIV 185
Cdd:cd14903      1 AAILYNVKKRFL-RKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  186 SGESGAGKTVSAKYAMRYFATVSGSASEANVEeKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRT 265
Cdd:cd14903     80 SGESGAGKTETTKILMNHLATIAGGLNDSTIK-KIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLVGAKCRT 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  266 YLLEKSRVVFQAEEERNYHIFYQLCASAKLPEfkMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQACTLLGISESH 345
Cdd:cd14903    159 YLLEKTRVISHERPERNYHIFYQLLASPDVEE--RLFLDSANECAYTGANKTIKIEGMSDRKHFARTKEALSLIGVSEEK 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  346 QMGIFRILAGILHLGNVGFTSRDAD--SCTIPPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNA 423
Cdd:cd14903    237 QEVLFEVLAGILHLGQLQIQSKPNDdeKSAIAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKKDQAEDC 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  424 RDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMK 503
Cdd:cd14903    317 RDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFKTVQIEYEE 396

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  504 EQIPWTLIDFYDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRLSNKAFIIQHFADKVEY 583
Cdd:cd14903    397 EGIRWAHIDFADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFPRTSRTQFTIKHYAGPVTY 476

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  584 QCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFqdDEKAISPTSATSSGRTPltrtpakptkGRPGQMAKEHKKTVGHQF 663
Cdd:cd14903    477 ESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLF--KEKVESPAAASTSLARG----------ARRRRGGALTTTTVGTQF 544

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  664 RNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMKQK-D 742
Cdd:cd14903    545 KDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFLPEGrN 624

                          650       660       670
                   ....*....|....*....|....*....|....
gi 1836165656  743 VLSDRKQTCKNVLEKLILDK-DKYQFGKTKIFFR 775
Cdd:cd14903    625 TDVPVAERCEALMKKLKLESpEQYQMGLTRIYFQ 658
MYSc_Myo6 cd01382
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ...
 110-775 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: 630.05  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  110 LHNLRVRFIDSKlIYTYCGIVLVAINPYEQLP-IYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSGE 188
Cdd:cd01382      4 LNNIRVRYSKDK-IYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVSGE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  189 SGAGKTVSAKYAMRYFATVSGSASeANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYLL 268
Cdd:cd01382     83 SGAGKTESTKYILRYLTESWGSGA-GPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYLL 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  269 EKSRVVFQAEEERNYHIFYQLCASAklPE---FKMLRLGNadnfnytkqggspviegVDDAKEMAHTRQACTLLGISESH 345
Cdd:cd01382    162 EKSRICVQSKEERNYHIFYRLCAGA--PEdlrEKLLKDPL-----------------LDDVGDFIRMDKAMKKIGLSDEE 222

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  346 QMGIFRILAGILHLGNVGFTSRDADS---CTIPPKHEPLCIFC-ELMGVDYEEMCHWLCHRKLATATE----TYIK-PIS 416
Cdd:cd01382    223 KLDIFRVVAAVLHLGNIEFEENGSDSgggCNVKPKSEQSLEYAaELLGLDQDELRVSLTTRVMQTTRGgakgTVIKvPLK 302

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  417 KLQATNARDALAKHIYAKLFNWIVDNVNQAL---HSAvkqhSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHV 493
Cdd:cd01382    303 VEEANNARDALAKAIYSKLFDHIVNRINQCIpfeTSS----YFIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQFFNERI 378

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  494 FKLEQEEYMKEQIPWTLIDFYDNQPCINLIESKL-GILDLLDEECKMPKGTDDTWAQKLYNTHLNKcALFEKPRLS---- 568
Cdd:cd01382    379 LKEEQELYEKEGLGVKEVEYVDNQDCIDLIEAKLvGILDLLDEESKLPKPSDQHFTSAVHQKHKNH-FRLSIPRKSklki 457

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  569 ------NKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAiSPTSATSSGRTPLtrtpak 642
Cdd:cd01382    458 hrnlrdDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNN-NKDSKQKAGKLSF------ 530

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  643 ptkgrpgqmakehkKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFP 722
Cdd:cd01382    531 --------------ISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFP 596

                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1836165656  723 SRWTYQEFFSRYRVLMKQKDVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 775
Cdd:cd01382    597 SRTSFHDLYNMYKKYLPPKLARLDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
MYSc_Myo4 cd14872
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ...
 107-775 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: 623.72  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  107 PAVLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 186
Cdd:cd14872      1 AMIVHNLRKRFKNDQ-IYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILIS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  187 GESGAGKTVSAKYAMRYFATVSGSASeaNVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTY 266
Cdd:cd14872     80 GESGAGKTEATKQCLSFFAEVAGSTN--GVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGASTENY 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  267 LLEKSRVVFQAEEERNYHIFYQLCASAklPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQACTLLGISESHQ 346
Cdd:cd14872    158 LLEKSRVVYQIKGERNFHIFYQLLASP--DPASRGGWGSSAAYGYLSLSGCIEVEGVDDVADFEEVVLAMEQLGFDDADI 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  347 MGIFRILAGILHLGNVGFTS----RDADSCTIPPKHEpLCIFCELMGVDYEEMCHWLCHRKLAT-ATETYIKPISKLQAT 421
Cdd:cd14872    236 NNVMSLIAAILKLGNIEFASgggkSLVSGSTVANRDV-LKEVATLLGVDAATLEEALTSRLMEIkGCDPTRIPLTPAQAT 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  422 NARDALAKHIYAKLFNWIVDNVNQALHSA-VKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEE 500
Cdd:cd14872    315 DACDALAKAAYSRLFDWLVKKINESMRPQkGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTFKLEEAL 394

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  501 YMKEQIPWTLIDFYDNQPCINLIESKL-GILDLLDEECKMPKGTDDTWAQKLYNTH-LNKCALFEKPRLSNKAFIIQHFA 578
Cdd:cd14872    395 YQSEGVKFEHIDFIDNQPVLDLIEKKQpGLMLALDDQVKIPKGSDATFMIAANQTHaAKSTFVYAEVRTSRTEFIVKHYA 474

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  579 DKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEkaisptsatssgrtpltrtPAKPTKgrpgqmakehKKT 658
Cdd:cd14872    475 GDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPPSE-------------------GDQKTS----------KVT 525

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  659 VGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLM 738
Cdd:cd14872    526 LGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFLV 605

                          650       660       670
                   ....*....|....*....|....*....|....*....
gi 1836165656  739 K--QKDVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 775
Cdd:cd14872    606 KtiAKRVGPDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
MYSc_Myo9 cd01385
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ...
 110-775 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: 622.09  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  110 LHNLRVRFIDSKlIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSGES 189
Cdd:cd01385      4 LENLRARFKHGK-IYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISGES 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  190 GAGKTVSAKYAMRYFATVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYLLE 269
Cdd:cd01385     83 GSGKTESTNFLLHHLTALSQKGYGSGVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVEKYLLE 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  270 KSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQACTLLGISESHQMGI 349
Cdd:cd01385    163 KSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNQSDCYTLEGEDEKYEFERLKQAMEMVGFLPETQRQI 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  350 FRILAGILHLGNVGFTSRDA---DSCTIPPKhEPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNARDA 426
Cdd:cd01385    243 FSVLSAVLHLGNIEYKKKAYhrdESVTVGNP-EVLDIISELLRVKEETLLEALTTKKTVTVGETLILPYKLPEAIATRDA 321

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  427 LAKHIYAKLFNWIVDNVNQAL----HSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYM 502
Cdd:cd01385    322 MAKCLYSALFDWIVLRINHALlnkkDLEEAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIFKLEQEEYK 401

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  503 KEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKlYNTHLNKCALFEKPRLSNKAFIIQHFADKV 581
Cdd:cd01385    402 KEGISWHNIEYTDNTGCLQLISKKpTGLLCLLDEESNFPGATNQTLLAK-FKQQHKDNKYYEKPQVMEPAFIIAHYAGKV 480

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  582 EYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAI-----------------SPTSATSSGRT-PLTRTPAKP 643
Cdd:cd01385    481 KYQIKDFREKNLDLMRPDIVAVLRSSSSAFVRELIGIDPVAVfrwavlrafframaafrEAGRRRAQRTAgHSLTLHDRT 560

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  644 TKGRPGQMAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPS 723
Cdd:cd01385    561 TKSLLHLHKKKKPPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTGMLETVRIRRSGYSV 640

                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1836165656  724 RWTYQEFFSRYRVLMKqKDVLSdRKQTCKNVLEKLILDKDKYQFGKTKIFFR 775
Cdd:cd01385    641 RYTFQEFITQFQVLLP-KGLIS-SKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
Myo5_CBD cd15470
Cargo binding domain of myosin 5; Class V myosins are well studied unconventional myosins, ...
 1506-1872 0e+00

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: 614.99  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1506 EDEQKLVKNLILELKPRGvAVNLIPGLPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSNT 1585
Cdd:cd15470      1 EDESRLIKNLITDLKPRG-AVGLLPGLPAYILFMCIRHADYVNDEAKVRSLLTATINAIKKVLKKHSEDFEMLSFWLVNT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1586 CRFLHCLKQYSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPmivsgmlehetiqgvsgv 1665
Cdd:cd15470     80 CRLLNCLKQYSGEEEFMKHNTPKQNEHCLKNFDLSEYRQVLSDLAIQIYQQLIKRAEEILQP------------------ 141

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1666 kptglrkrtssiadegtyTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQIRY 1745
Cdd:cd15470    142 ------------------TLDSLLQQLNSFHTTLTQHGLDPELIKQVFRQLFYLICASTLNNLLLRKDLCSWSKGMQIRY 203

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1746 NVSQLEEWLRDKNLMNSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERVSVSFI 1825
Cdd:cd15470    204 NVSQLEEWLRDKGLQDSGARETLEPLIQAAQLLQVKKTTEEDAQSICEMCTKLTTAQIVKILNLYTPVDDFEERVTPSFI 283

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1836165656 1826 RTIQMRLRDRKDSP--QLLMDAKHIFPVTFPFNPSSLALETIQIPASLG 1872
Cdd:cd15470    284 RKVQARLNERADSNqlQLLMDTKYIFPVTFPFNPSPVALEELQIPPSLH 332
MYSc_Myo15 cd01387
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ...
 108-775 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: 604.82  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  108 AVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 187
Cdd:cd01387      2 TVLWNLKTRY-ERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  188 ESGAGKTVSAKYAMRYFATVSGSAsEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFdKRYRIIGANMRTYL 267
Cdd:cd01387     81 ESGSGKTEATKLIMQYLAAVNQRR-NNLVTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-EGGVIVGAITSQYL 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  268 LEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQACTLLGISESHQM 347
Cdd:cd01387    159 LEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGGNCEIAGKSDADDFRRLLAAMQVLGFSSEEQD 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  348 GIFRILAGILHLGNVGFTSRDA----DSCTIPPKHEPLCIfCELMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNA 423
Cdd:cd01387    239 SIFRILASVLHLGNVYFHKRQLrhgqEGVSVGSDAEIQWV-AHLLQISPEGLQKALTFKVTETRRERIFTPLTIDQALDA 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  424 RDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMK 503
Cdd:cd01387    318 RDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVFKLEQEEYIR 397

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  504 EQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKL-YNTHLNKcaLFEKPRLSNKAFIIQHFADKV 581
Cdd:cd01387    398 EQIDWTEIAFADNQPVINLISKKpVGILHILDDECNFPQATDHSFLEKChYHHALNE--LYSKPRMPLPEFTIKHYAGQV 475

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  582 EYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDekaisptsatssgRTPLTRTPAKPTKGRPGQMaKEHKKTVGH 661
Cdd:cd01387    476 WYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSH-------------RAQTDKAPPRLGKGRFVTM-KPRTPTVAA 541

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  662 QFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMKQK 741
Cdd:cd01387    542 RFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVALK 621

                          650       660       670
                   ....*....|....*....|....*....|....*.
gi 1836165656  742 DVLSDRKQTCKNVLEKL--ILDKDKYQFGKTKIFFR 775
Cdd:cd01387    622 LPRPAPGDMCVSLLSRLctVTPKDMYRLGATKVFLR 657
MYSc_Myo29 cd14890
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ...
 108-775 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: 598.30  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  108 AVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLP-IYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMAR----DERNQS 182
Cdd:cd14890      2 SLLHTLRLRY-ERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  183 IIVSGESGAGKTVSAKYAMRYFATVS-----------------GSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFG 245
Cdd:cd14890     81 IIISGESGAGKTEATKIIMQYLARITsgfaqgasgegeaaseaIEQTLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  246 KYIEIGFDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNA-DNFNYTKQGGSpvIEGVD 324
Cdd:cd14890    161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPvEYFYLRGECSS--IPSCD 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  325 DAKEMAHTRQACTLLGISESHQMGIFRILAGILHLGNVGFTS-RDADSCTIPPKHEPLCIFCELMGVDYEEMCHWLCHRK 403
Cdd:cd14890    239 DAKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESeNDTTVLEDATTLQSLKLAAELLGVNEDALEKALLTRQ 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  404 LATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANE 483
Cdd:cd14890    319 LFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYANE 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  484 KLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESKL----GILDLLDeECKMPKGTDdtwAQKLYNTHLNkc 559
Cdd:cd14890    399 KLQRHFNQHMFEVEQVEYSNEGIDWQYITFNDNQACLELIEGKVngkpGIFITLD-DCWRFKGEE---ANKKFVSQLH-- 472

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  560 ALFEKPRLSNKA--------------------FIIQHFADKVEYQCEGFLEKNKDTVFEEqikvlksskfkmLPELFQDD 619
Cdd:cd14890    473 ASFGRKSGSGGTrrgssqhphfvhpkfdadkqFGIKHYAGDVIYDASGFNEKNNETLNAE------------MKELIKQS 540

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  620 EKAISPTSatssgrtpltrtpakptkgrpgqmakehkktVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEK 699
Cdd:cd14890    541 RRSIREVS-------------------------------VGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGL 589

                          650       660       670       680       690       700       710
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1836165656  700 RAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMKQKDVLsdrKQTCKNVLEKLILDKDKYQFGKTKIFFR 775
Cdd:cd14890    590 DCLRQLKYSGMMEAIQIRQQGFALREEHDSFFYDFQVLLPTAENI---EQLVAVLSKMLGLGKADWQIGSSKIFLK 662
MYSc_Myo10 cd14873
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ...
 108-775 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: 594.47  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  108 AVLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLP-IYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 186
Cdd:cd14873      2 SIMYNLFQRYKRNQ-IYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  187 GESGAGKTVSAKYAMRYFATVS-------GSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRII 259
Cdd:cd14873     81 GESGAGKTESTKLILKFLSVISqqslelsLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQ 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  260 GANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQACTLL 339
Cdd:cd14873    161 GGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNQSGCVEDKTISDQESFREVITAMEVM 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  340 GISESHQMGIFRILAGILHLGNVGFTSrdADSCTIPPKhEPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKPISKLQ 419
Cdd:cd14873    241 QFSKEEVREVSRLLAGILHLGNIEFIT--AGGAQVSFK-TALGRSAELLGLDPTQLTDALTQRSMFLRGEEILTPLNVQQ 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  420 ATNARDALAKHIYAKLFNWIVDNVNQALHSAvKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQE 499
Cdd:cd14873    318 AVDSRDSLAMALYARCFEWVIKKINSRIKGK-EDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLEQL 396

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  500 EYMKEQIPWTLIDFYDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKcALFEKPRLSNKAFIIQHFAD 579
Cdd:cd14873    397 EYSREGLVWEDIDWIDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQHANN-HFYVKPRVAVNNFGVKHYAG 475

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  580 KVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDekaisptSATSSGRTPltrtpakptkgrpgQMAKEHKK-T 658
Cdd:cd14873    476 EVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHV-------SSRNNQDTL--------------KCGSKHRRpT 534

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  659 VGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLM 738
Cdd:cd14873    535 VSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLM 614

                          650       660       670
                   ....*....|....*....|....*....|....*..
gi 1836165656  739 KQKDVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 775
Cdd:cd14873    615 RNLALPEDVRGKCTSLLQLYDASNSEWQLGKTKVFLR 651
MYSc_Myo40 cd14901
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ...
 107-773 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: 586.37  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  107 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAY---SGQNMGD---MDPHIFAVAEEAYKQMARDER- 179
Cdd:cd14901      1 PSILHVLRRRF-AHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehGERRAAGerkLPPHVYAVADKAFRAMLFASRg 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  180 ---NQSIIVSGESGAGKTVSAKYAMRYFATVS-------GSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIE 249
Cdd:cd14901     80 qkcDQSILVSGESGAGKTETTKIIMNYLASVSsatthgqNATERENVRDRVLESNPILEAFGNARTNRNNNSSRFGKFIR 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  250 IGFDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPV-IEGVDDAKE 328
Cdd:cd14901    160 LGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLNSSQCYDrRDGVDDSVQ 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  329 MAHTRQACTLLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEP-LCIFCELMGVDYEEMCHWLCHRKLATA 407
Cdd:cd14901    240 YAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGGTFSMSSLAnVRAACDLLGLDMDVLEKTLCTREIRAG 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  408 TETYIKPISKLQATNARDALAKHIYAKLFNWIVDNVNQAL--HSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKL 485
Cdd:cd14901    320 GEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIaySESTGASRFIGIVDIFGFEIFATNSLEQLCINFANEKL 399

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  486 QQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNThLNKCALFEK 564
Cdd:cd14901    400 QQLFGKFVFEMEQDEYVAEAIPWTFVEYPNNDACVAMFEARpTGLFSLLDEQCLLPRGNDEKLANKYYDL-LAKHASFSV 478

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  565 PRLSN--KAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPelfqddekaisptsatssgrtpltrtpak 642
Cdd:cd14901    479 SKLQQgkRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLS----------------------------- 529

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  643 ptkgrpgqmakehkKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFP 722
Cdd:cd14901    530 --------------STVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYP 595

                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1836165656  723 SRWTYQEFFSRYRVLMKQK-------DVLSDRKQTCKNVLEKLILDKDKYQFGKTKIF 773
Cdd:cd14901    596 VRFPHDAFVHTYSCLAPDGasdtwkvNELAERLMSQLQHSELNIEHLPPFQVGKTKVF 653
MYSc_Myo27 cd14888
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ...
 107-775 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: 568.55  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  107 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLP-IYGEDIINAYSgQNMGDMDPHIFAVAEEAYKQMARDERNQSIIV 185
Cdd:cd14888      1 ASILHSLNLRF-DIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILI 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  186 SGESGAGKTVSAKYAMRYFATVsGSASE---ANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDK-------- 254
Cdd:cd14888     79 SGESGAGKTESTKYVMKFLACA-GSEDIkkrSLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSKlkskrmsg 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  255 -RYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCA-----------------------SAKLPEFKMLRLGNADNFN 310
Cdd:cd14888    158 dRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAaareakntglsyeendeklakgaDAKPISIDMSSFEPHLKFR 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  311 YTKQGGSPVIEGVDDAKEMAHTRQACTLLGISESHQMGIFRILAGILHLGNVGF-TSRDADSCTI--PPKHEPLCIFCEL 387
Cdd:cd14888    238 YLTKSSCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFeNNEACSEGAVvsASCTDDLEKVASL 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  388 MGVDYEEMCHWLCHRKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDNVNQAL-HSAVKQHSFIGVLDIYGFE 466
Cdd:cd14888    318 LGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIgYSKDNSLLFCGVLDIFGFE 397

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  467 TFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDD 545
Cdd:cd14888    398 CFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFPDNQDCVDLLQEKpLGIFCMLDEECFVPGGKDQ 477

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  546 TWAQKLYNTHLNKcALFEKPRLSNKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQddekaisp 625
Cdd:cd14888    478 GLCNKLCQKHKGH-KRFDVVKTDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNLFS-------- 548

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  626 tsatssgrtpltrtpAKPTKGRPGQMAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQL 705
Cdd:cd14888    549 ---------------AYLRRGTDGNTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQL 613

                          650       660       670       680       690       700       710
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  706 RACGVLETIRISAAGFPSRWTYQEFFSRYRVLMkqkdvlsdRKQTCKNVLEklildkdkYQFGKTKIFFR 775
Cdd:cd14888    614 KYGGVLQAVQVSRAGYPVRLSHAEFYNDYRILL--------NGEGKKQLSI--------WAVGKTLCFFK 667
MYSc_Myo3 cd01379
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ...
 107-775 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: 564.21  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  107 PAVLHNLRVRFIDSkLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 186
Cdd:cd01379      1 DTIVSQLQKRYSRD-QIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVIS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  187 GESGAGKTVSAKYAMRYFaTVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTY 266
Cdd:cd01379     80 GESGAGKTESANLLVQQL-TVLGKANNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEY 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  267 LLEKSRVVFQAEEERNYHIFYQLCA----SAKLPEFKmlrLGNADNFNYTKQGGspviEGVDDAKEMAHTR------QAC 336
Cdd:cd01379    159 LLEKSRVVHQAIGERNFHIFYYIYAglaeDKKLAKYK---LPENKPPRYLQNDG----LTVQDIVNNSGNRekfeeiEQC 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  337 -TLLGISESHQMGIFRILAGILHLGNVGFTS-----RDADSCTIpPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATET 410
Cdd:cd01379    232 fKVIGFTKEEVDSVYSILAAILHIGDIEFTEvesnhQTDKSSRI-SNPEALNNVAKLLGIEADELQEALTSHSVVTRGET 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  411 YIKPISKLQATNARDALAKHIYAKLFNWIVDNVNQAL----HSAVKQHSfIGVLDIYGFETFEINSFEQFCINYANEKLQ 486
Cdd:cd01379    311 IIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpdrSASDEPLS-IGILDIFGFENFQKNSFEQLCINIANEQIQ 389

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  487 QQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNthlN-KCALFEK 564
Cdd:cd01379    390 YYFNQHIFAWEQQEYLNEGIDVDLIEYEDNRPLLDMFLQKpMGLLALLDEESRFPKATDQTLVEKFHN---NiKSKYYWR 466

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  565 PRLSNKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLpelfqddekaisptsatssgrtpltrtpakpt 644
Cdd:cd01379    467 PKSNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLV-------------------------------- 514

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  645 kgrpgqmakehKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSR 724
Cdd:cd01379    515 -----------RQTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHR 583

                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1836165656  725 WTYQEFFSRYRVL---MKQKDVLSdrKQTCKNVLEKLILdkDKYQFGKTKIFFR 775
Cdd:cd01379    584 ILFADFLKRYYFLafkWNEEVVAN--RENCRLILERLKL--DNWALGKTKVFLK 633
MYSc_Myh15_mammals cd14929
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ...
 107-775 1.35e-179

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: 558.82  E-value: 1.35e-179
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  107 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 186
Cdd:cd14929      1 ASVLHTLRRRY-DHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  187 GESGAGKTVSAKYAMRYFATVSGSASE----ANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGAN 262
Cdd:cd14929     80 GESGAGKTVNTKHIIQYFATIAAMIESkkklGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSAD 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  263 MRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPViEGVDDAKEMAHTRQACTLLGIS 342
Cdd:cd14929    160 IDIYLLEKSRVIFQQPGERNYHIFYQILSGKKELRDLLLVSANPSDFHFCSCGAVAV-ESLDDAEELLATEQAMDILGFL 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  343 ESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKPISKLQATN 422
Cdd:cd14929    239 PDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIEQVTY 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  423 ARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYM 502
Cdd:cd14929    319 AVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLEQEEYR 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  503 KEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRLSNKAFIIQ----HF 577
Cdd:cd14929    399 KEGIDWVSIDFgLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKPDKKKFEAHfelvHY 478

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  578 ADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDekaISPTSATSSGRtpltrtpakptkgrpgqmaKEHKK 657
Cdd:cd14929    479 AGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENY---ISTDSAIQFGE-------------------KKRKK 536

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  658 TVGHQFRNSLH-----LLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFS 732
Cdd:cd14929    537 GASFQTVASLHkenlnKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQ 616

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*...
gi 1836165656  733 RY-----RVLMKQKDVlSDRKQTcKNVLEKLILDKDKYQFGKTKIFFR 775
Cdd:cd14929    617 RYcilnpRTFPKSKFV-SSRKAA-EELLGSLEIDHTQYRFGITKVFFK 662
MYSc_Myo31 cd14892
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ...
 113-775 2.15e-179

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: 557.84  E-value: 2.15e-179
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  113 LRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGE--DIINAYSGQNMGDMD-PHIFAVAEEAYKQMARD----ERNQSIIV 185
Cdd:cd14892      7 LRRRY-ERDAIYTFTADILISINPYKSIPLLYDvpGFDSQRKEEATASSPpPHVFSIAERAYRAMKGVgkgqGTPQSIVV 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  186 SGESGAGKTVSAKYAMRYFATVSGSASEA-----------NVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDK 254
Cdd:cd14892     86 SGESGAGKTEASKYIMKYLATASKLAKGAstskgaanaheSIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQIHYNS 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  255 RYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQ 334
Cdd:cd14892    166 DGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGNCVEVDGVDDATEFKQLRD 245

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  335 ACTLLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEP--LCIFCELMGVDYEEMCHWLCHRKLATATETYI 412
Cdd:cd14892    246 AMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDVFAQSADGvnVAKAAGLLGVDAAELMFKLVTQTTSTARGSVL 325

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  413 K-PISKLQATNARDALAKHIYAKLFNWIVDNVNqALHSAV-----------KQHSFIGVLDIYGFETFEINSFEQFCINY 480
Cdd:cd14892    326 EiKLTAREAKNALDALCKYLYGELFDWLISRIN-ACHKQQtsgvtggaaspTFSPFIGILDIFGFEIMPTNSFEQLCINF 404

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  481 ANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMP-KGTDDTWAQKLYNTHLNK 558
Cdd:cd14892    405 TNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQDNQDCLDLIQKKpLGLLPLLEEQMLLKrKTTDKQLLTIYHQTHLDK 484

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  559 CALFEKPRLSNKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKfkmlpelfqddekaisptsatssgrtpltr 638
Cdd:cd14892    485 HPHYAKPRFECDEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSS------------------------------ 534

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  639 tpakptkgrpgqmakehkktvghQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISA 718
Cdd:cd14892    535 -----------------------KFRTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRR 591

                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1836165656  719 AGFPSRWTYQEFFSRYRVLMKQKDVLSDRKQTCKNVLE--------KLILDKDKYQFGKTKIFFR 775
Cdd:cd14892    592 EGFPIRRQFEEFYEKFWPLARNKAGVAASPDACDATTArkkceeivARALERENFQLGRTKVFLR 656
MYSc_Myh3 cd14913
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ...
 107-775 8.91e-179

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: 556.59  E-value: 8.91e-179
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  107 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 186
Cdd:cd14913      1 PAVLYNLKDRY-TSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  187 GESGAGKTVSAKYAMRYFATVSG---------SASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYR 257
Cdd:cd14913     80 GESGAGKTVNTKRVIQYFATIAAtgdlakkkdSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  258 IIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLG-NADNFNYTKQGgSPVIEGVDDAKEMAHTRQAC 336
Cdd:cd14913    160 LASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITtNPYDYPFISQG-EILVASIDDAEELLATDSAI 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  337 TLLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKPIS 416
Cdd:cd14913    239 DILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQT 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  417 KLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKL 496
Cdd:cd14913    319 VDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVL 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  497 EQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPR-LSNKA--- 571
Cdd:cd14913    399 EQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKvVKGRAeah 478

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  572 FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFqddekaisPTSATSSGrtPLTRTPAKPTKGRPGQm 651
Cdd:cd14913    479 FSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLY--------ATFATADA--DSGKKKVAKKKGSSFQ- 547

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  652 akehkkTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFF 731
Cdd:cd14913    548 ------TVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFK 621

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*..
gi 1836165656  732 SRYRVLMKQ---KDVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 775
Cdd:cd14913    622 QRYRVLNASaipEGQFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
MYSc_Myo43 cd14904
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ...
 107-775 1.21e-176

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: 550.32  E-value: 1.21e-176
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  107 PAVLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLP-IYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIV 185
Cdd:cd14904      1 PSILFNLKKRFAASK-PYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  186 SGESGAGKTVSAKYAMRYFATVSGSASEANVEeKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRT 265
Cdd:cd14904     80 SGESGAGKTETTKIVMNHLASVAGGRKDKTIA-KVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAKCET 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  266 YLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQG-GSPVIEGVDDAKEMAHTRQACTLLGISES 344
Cdd:cd14904    159 YLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLGDSlAQMQIPGLDDAKLFASTQKSLSLIGLDND 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  345 HQMGIFRILAGILHLGNVGFTSRDADSCTIPpKHEPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNAR 424
Cdd:cd14904    239 AQRTLFKILSGVLHLGEVMFDKSDENGSRIS-NGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLAPVEAEENR 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  425 DALAKHIYAKLFNWIVDNVNQAL---HSAVKQHsfIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEY 501
Cdd:cd14904    318 DALAKAIYSKLFDWMVVKINAAIstdDDRIKGQ--IGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKTVEEEY 395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  502 MKEQIPWTLIDFYDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHL----NKCALFekPRLSNKAFIIQHF 577
Cdd:cd14904    396 IREGLQWDHIEYQDNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHQtkkdNESIDF--PKVKRTQFIINHY 473

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  578 ADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEkAISPTSATSSGRtpltrtpakptkgrpgqmAKEHKK 657
Cdd:cd14904    474 AGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSE-APSETKEGKSGK------------------GTKAPK 534

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  658 TVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVL 737
Cdd:cd14904    535 SLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIM 614

                          650       660       670
                   ....*....|....*....|....*....|....*....
gi 1836165656  738 MKQKDVLSDRKQTCKNVLEKLILDKD-KYQFGKTKIFFR 775
Cdd:cd14904    615 FPPSMHSKDVRRTCSVFMTAIGRKSPlEYQIGKSLIYFK 653
MYSc_Myh7b cd14927
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ...
 108-775 9.29e-176

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: 548.79  E-value: 9.29e-176
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  108 AVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 187
Cdd:cd14927      2 SVLHNLRRRY-SRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  188 ESGAGKTVSAKYAMRYFATVS-------------GSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDK 254
Cdd:cd14927     81 ESGAGKTVNTKRVIQYFAIVAalgdgpgkkaqflATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  255 RYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKlPEFK--MLRLGNADNFNYTKQGGSPViEGVDDAKEMAHT 332
Cdd:cd14927    161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKK-PELQdmLLVSMNPYDYHFCSQGVTTV-DNMDDGEELMAT 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  333 RQACTLLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATETYI 412
Cdd:cd14927    239 DHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVT 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  413 KPISKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMH 492
Cdd:cd14927    319 KGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHH 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  493 VFKLEQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRLSNKA 571
Cdd:cd14927    399 MFILEQEEYKREGIEWVFIDFgLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPDKKR 478

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  572 -----FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFqddEKAISPTSATSsgrtPLTRTPAKPTKG 646
Cdd:cd14927    479 kyeahFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLY---ENYVGSDSTED----PKSGVKEKRKKA 551

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  647 RPGQmakehkkTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWT 726
Cdd:cd14927    552 ASFQ-------TVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRIL 624

                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1836165656  727 YQEFFSRYRVLMKQ---KDVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 775
Cdd:cd14927    625 YADFKQRYRILNPSaipDDKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
MYSc_Myh10 cd14920
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ...
 108-775 1.94e-173

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: 542.68  E-value: 1.94e-173
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  108 AVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 187
Cdd:cd14920      2 SVLHNLKDRYY-SGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  188 ESGAGKTVSAKYAMRYFATVSGS-------ASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIG 260
Cdd:cd14920     81 ESGAGKTENTKKVIQYLAHVASShkgrkdhNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  261 ANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPvIEGVDDAKEMAHTRQACTLLG 340
Cdd:cd14920    161 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIP-IPGQQDKDNFQETMEAMHIMG 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  341 ISESHQMGIFRILAGILHLGNVGF-TSRDADSCTIpPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKPISKLQ 419
Cdd:cd14920    240 FSHEEILSMLKVVSSVLQFGNISFkKERNTDQASM-PENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQ 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  420 ATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQ-HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQ 498
Cdd:cd14920    319 ADFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQ 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  499 EEYMKEQIPWTLIDF-YDNQPCINLIESKL---GILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRLSNKA-FI 573
Cdd:cd14920    399 EEYQREGIEWNFIDFgLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKAdFC 478

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  574 IQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKaISPTSATSSGRTPLTRTPAKPTKGRpgqmak 653
Cdd:cd14920    479 IIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDR-IVGLDQVTGMTETAFGSAYKTKKGM------ 551

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  654 ehKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSR 733
Cdd:cd14920    552 --FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQR 629

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....
gi 1836165656  734 YRVLMKQK--DVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 775
Cdd:cd14920    630 YEILTPNAipKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
MYSc_Myh1_insects_crustaceans cd14909
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ...
 107-775 7.00e-171

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: 535.57  E-value: 7.00e-171
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  107 PAVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 186
Cdd:cd14909      1 ASVLHNLRQRYY-AKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLIT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  187 GESGAGKTVSAKYAMRYFATVSGS-------ASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRII 259
Cdd:cd14909     80 GESGAGKTENTKKVIAYFATVGASkktdeaaKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLA 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  260 GANMRTYLLEKSRVVFQAEEERNYHIFYQLcASAKLPEFKMLRL--GNADNFNYTKQGGSpVIEGVDDAKEMAHTRQACT 337
Cdd:cd14909    160 GADIETYLLEKARVISQQSLERSYHIFYQI-MSGSVPGVKEMCLlsDNIYDYYIVSQGKV-TVPNVDDGEEFSLTDQAFD 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  338 LLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKPISK 417
Cdd:cd14909    238 ILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNV 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  418 LQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLE 497
Cdd:cd14909    318 QQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLE 397

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  498 QEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRLSNKA----- 571
Cdd:cd14909    398 QEEYKREGIDWAFIDFgMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKPGqqaah 477

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  572 FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGRTpltrtpakpTKGrpGQM 651
Cdd:cd14909    478 FAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGEQAKGGRG---------KKG--GGF 546

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  652 AkehkkTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFF 731
Cdd:cd14909    547 A-----TVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFK 621

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*
gi 1836165656  732 SRYRVLM-KQKDVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 775
Cdd:cd14909    622 MRYKILNpAGIQGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
MYSc_Myo46 cd14907
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ...
 109-775 4.65e-170

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: 533.07  E-value: 4.65e-170
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  109 VLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLP---------IYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDER 179
Cdd:cd14907      3 LLINLKKRYQQDK-IFTYVGPTLIVMNPYKQIDnlfseevmqMYKEQIIQNGEYFDIKKEPPHIYAIAALAFKQLFENNK 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  180 NQSIIVSGESGAGKTVSAKYAMRYFATVSG------------------SASEANVEEKVLASNPIMESIGNAKTTRNDNS 241
Cdd:cd14907     82 KQAIVISGESGAGKTENAKYAMKFLTQLSQqeqnseevltltssiratSKSTKSIEQKILSCNPILEAFGNAKTVRNDNS 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  242 SRFGKYIEIGFDKRYR-IIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAK---LPEFKMLRLGNADNFNYTKQGGS 317
Cdd:cd14907    162 SRFGKYVSILVDKKKRkILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADqqlLQQLGLKNQLSGDRYDYLKKSNC 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  318 PVIEGVDDAKEMAHTRQACTLLGISESHQMGIFRILAGILHLGNVGFTSR--DADSCTIPPKHEPLCIFCELMGVDYEEM 395
Cdd:cd14907    242 YEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDStlDDNSPCCVKNKETLQIIAKLLGIDEEEL 321

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  396 CHWLCHRKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDNVNQAL--HSAVKQHSF------IGVLDIYGFET 467
Cdd:cd14907    322 KEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpKDEKDQQLFqnkylsIGLLDIFGFEV 401

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  468 FEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTL--IDFYDNQPCINLIES-KLGILDLLDEECKMPKGTD 544
Cdd:cd14907    402 FQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSYTDNQDVIDLLDKpPIGIFNLLDDSCKLATGTD 481

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  545 DTWAQKLYNTHLNKCALFEKPRLSNKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAis 624
Cdd:cd14907    482 EKLLNKIKKQHKNNSKLIFPNKINKDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFSGEDGS-- 559

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  625 ptsaTSSGRTPLTRTPAKptkgrpgqmakehKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQ 704
Cdd:cd14907    560 ----QQQNQSKQKKSQKK-------------DKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQ 622

                          650       660       670       680       690       700       710
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1836165656  705 LRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMkqkdvlsdrkqtcKNVLeklildkdkyqFGKTKIFFR 775
Cdd:cd14907    623 IRYLGVLESIRVRKQGYPYRKSYEDFYKQYSLLK-------------KNVL-----------FGKTKIFMK 669
Myo5c_CBD cd15476
Cargo binding domain of myosin 5C; Class V myosins are well studied unconventional myosins, ...
 1506-1873 7.08e-169

Cargo binding domain of myosin 5C; 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.MyoVb and myoVc areprimarily expressed in epithelial cells, and have been implicated as motors involved in recycling endosomes.


Pssm-ID: 271260 [Multi-domain]  Cd Length: 332  Bit Score: 516.64  E-value: 7.08e-169
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1506 EDEQKLVKNLILELKPRGVAVNLIPGLPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSNT 1585
Cdd:cd15476      1 EDEAKLIQNLILDLKPRGVVVNMIPGLPAHILFMCVRHADYLNDANKLKSLMNAIITGVKQVIKEHQEDFEMLSFWLSNT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1586 CRFLHCLKQYSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPmivsgmlehetiqgvsgv 1665
Cdd:cd15476     81 YHFLNCLKQYSGEEEFMKHNTPRQNKNCLKNFDLSEHRQILSDLAIRIYHQFISVMENNLQP------------------ 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1666 kptglrkrtssiadegtyTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQIRY 1745
Cdd:cd15476    143 ------------------TISSILQQLSYFYSTMCQHGMDPELIKQAVKQLFFLIGAVTLNSIFLRKDMCSCRKGMQIRC 204

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1746 NVSQLEEWLRDKNLMNSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERVSVSFI 1825
Cdd:cd15476    205 NISYLEEWLKEKNLQNSNAKETLEPLSQAAWLLQVNKTTDDDAKEICERCTELSAVQIVKILNSYTPIDDFEKRVTPSFV 284

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 1836165656 1826 RTIQMRLRDRKDSPQLLMDAKHIFPVTFPFNPSSLALETIQIPASLGL 1873
Cdd:cd15476    285 RKVQSLLQNREGSSQLMLDTKYRFQVTFPFCPSPQALEMLQVPSSLKL 332
MYSc_Myh2_insects_mollusks cd14911
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ...
 108-775 4.36e-167

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: 525.32  E-value: 4.36e-167
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  108 AVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 187
Cdd:cd14911      2 SVLHNIKDRYY-SGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  188 ESGAGKTVSAKYAMRYFATVSGSASEAN----------------VEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIG 251
Cdd:cd14911     81 ESGAGKTENTKKVIQFLAYVAASKPKGSgavphpavnpavligeLEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  252 FDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPViEGVDDAKEMAH 331
Cdd:cd14911    161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPV-PGVDDYAEFQA 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  332 TRQACTLLGISESHQMGIFRILAGILHLGNVGF-TSRDADSCTIPPKHEPLCIfCELMGVDYEEMCHWLCHRKLATATET 410
Cdd:cd14911    240 TVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFrQERNNDQATLPDNTVAQKI-AHLLGLSVTDMTRAFLTPRIKVGRDF 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  411 YIKPISKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQ-HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQF 489
Cdd:cd14911    319 VTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQgASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLF 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  490 NMHVFKLEQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHlNKCALFEKPRLS 568
Cdd:cd14911    399 NHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAH-SMHPKFMKTDFR 477

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  569 NKA-FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSgrtplTRTPAKPTKGR 647
Cdd:cd14911    478 GVAdFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIVGMAQQALTD-----TQFGARTRKGM 552

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  648 pgqmakehKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTY 727
Cdd:cd14911    553 --------FRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPF 624

                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|
gi 1836165656  728 QEFFSRYRVLMKQ--KDVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 775
Cdd:cd14911    625 QEFRQRYELLTPNviPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
MYSc_Myo47 cd14908
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ...
 107-775 1.30e-166

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: 524.47  E-value: 1.30e-166
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  107 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAY------SGQNM---GDMDPHIFAVAEEAYKQMARD 177
Cdd:cd14908      1 PAILHSLSRRF-FRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYrqegllRSQGIespQALGPHVFAIADRSYRQMMSE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  178 ER-NQSIIVSGESGAGKTVSAKYAMRYFATV----------SGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGK 246
Cdd:cd14908     80 IRaSQSILISGESGAGKTESTKIVMLYLTTLgngeegapneGEELGKLSIMDRVLQSNPILEAFGNARTLRNDNSSRFGK 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  247 YIEIGFDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASA--------KLPEFKMLRLGNADNFNYTKQGGSP 318
Cdd:cd14908    160 FIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGdeeehekyEFHDGITGGLQLPNEFHYTGQGGAP 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  319 VIEGVDDAKEMAHTRQACTLLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPK---HEPLCIFCELMGVDYEEM 395
Cdd:cd14908    240 DLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEegnEKCLARVAKLLGVDVDKL 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  396 CHWLCHRKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQ--HSFIGVLDIYGFETFEINSF 473
Cdd:cd14908    320 LRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKdiRSSVGVLDIFGFECFAHNSF 399

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  474 EQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIES-KLGILDLLDEECKMP-KGTDDTWAQKL 551
Cdd:cd14908    400 EQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFPDNQDCLDTIQAkKKGILTMLDDECRLGiRGSDANYASRL 479

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  552 YNTHLNKC--ALFEKPRLSNKA-------FIIQHFADKVEYQCE-GFLEKNKDtvfeeqiKVLKSSKfkmlpELFQDdek 621
Cdd:cd14908    480 YETYLPEKnqTHSENTRFEATSiqktkliFAVRHFAGQVQYTVEtTFCEKNKD-------EIPLTAD-----SLFES--- 544

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  622 aisptsatssgrtpltrtpakptkgrpgqmakehkktvGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRA 701
Cdd:cd14908    545 --------------------------------------GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRV 586

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  702 VQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMK--QKDVLS------DRKQTCKNVLEKLI-------------- 759
Cdd:cd14908    587 TEQLRYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLLPliPEVVLSwsmerlDPQKLCVKKMCKDLvkgvlspamvsmkn 666

                          730
                   ....*....|....*.
gi 1836165656  760 LDKDKYQFGKTKIFFR 775
Cdd:cd14908    667 IPEDTMQLGKSKVFMR 682
MYSc_Myh7 cd14917
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ...
 107-775 7.66e-165

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: 519.27  E-value: 7.66e-165
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  107 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 186
Cdd:cd14917      1 PAVLYNLKERY-ASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  187 GESGAGKTVSAKYAMRYFATVSG---------SASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYR 257
Cdd:cd14917     80 GESGAGKTVNTKRVIQYFAVIAAigdrskkdqTPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  258 IIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRL-GNADNFNYTKQGGSPViEGVDDAKEMAHTRQAC 336
Cdd:cd14917    160 LASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLItNNPYDYAFISQGETTV-ASIDDAEELMATDNAF 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  337 TLLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKPIS 416
Cdd:cd14917    239 DVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQN 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  417 KLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKL 496
Cdd:cd14917    319 VQQVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  497 EQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPR-LSNKA--- 571
Cdd:cd14917    399 EQEEYKKEGIEWTFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPRnIKGKPeah 478

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  572 FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDdekaisptsaTSSGRTPLTRTPAKPTKGRPGQm 651
Cdd:cd14917    479 FSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFAN----------YAGADAPIEKGKGKAKKGSSFQ- 547

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  652 akehkkTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFF 731
Cdd:cd14917    548 ------TVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFR 621

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*..
gi 1836165656  732 SRYRVLMKQ---KDVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 775
Cdd:cd14917    622 QRYRILNPAaipEGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
MYSc_Myh6 cd14916
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ...
 107-775 2.94e-162

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: 512.30  E-value: 2.94e-162
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  107 PAVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 186
Cdd:cd14916      1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  187 GESGAGKTVSAKYAMRYFATVSG----------SASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRY 256
Cdd:cd14916     80 GESGAGKTVNTKRVIQYFASIAAigdrskkenpNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  257 RIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRL-GNADNFNYTKQGgSPVIEGVDDAKEMAHTRQA 335
Cdd:cd14916    160 KLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVtNNPYDYAFVSQG-EVSVASIDDSEELLATDSA 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  336 CTLLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKPI 415
Cdd:cd14916    239 FDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  416 SKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFK 495
Cdd:cd14916    319 SVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  496 LEQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPR----LSNK 570
Cdd:cd14916    399 LEQEEYKKEGIEWEFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRnvkgKQEA 478

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  571 AFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAisptSATSSGrtpltrtpakptKGRPGQ 650
Cdd:cd14916    479 HFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASA----DTGDSG------------KGKGGK 542

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  651 MAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEF 730
Cdd:cd14916    543 KKGSSFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDF 622

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*....
gi 1836165656  731 FSRYRVL----MKQKDVLSDRKQTCKnVLEKLILDKDKYQFGKTKIFFR 775
Cdd:cd14916    623 RQRYRILnpaaIPEGQFIDSRKGAEK-LLGSLDIDHNQYKFGHTKVFFK 670
MYSc_Myh16 cd14934
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ...
 108-775 2.74e-161

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: 509.18  E-value: 2.74e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  108 AVLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 187
Cdd:cd14934      2 SVLDNLRQRYTNMR-IYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  188 ESGAGKTVSAKYAMRYFATVSGSASEA-----NVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGAN 262
Cdd:cd14934     81 ESGAGKTENTKKVIQYFANIGGTGKQSsdgkgSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGAD 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  263 MRTYLLEKSRVVFQAEEERNYHIFYQLCASAKlPEF--KMLRLGNADNFNYTKQGGSpVIEGVDDAKEMAHTRQACTLLG 340
Cdd:cd14934    161 IESYLLEKSRVISQQAAERGYHIFYQILSNKK-PELieSLLLVPNPKEYHWVSQGVT-VVDNMDDGEELQITDVAFDVLG 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  341 ISESHQMGIFRILAGILHLGNVGFTSR------DADSCTIPPKheplciFCELMGVDYEEMCHWLCHRKLATATETYIKP 414
Cdd:cd14934    239 FSAEEKIGVYKLTGGIMHFGNMKFKQKpreeqaEVDTTEVADK------VAHLMGLNSGELQKGITRPRVKVGNEFVQKG 312

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  415 ISKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVF 494
Cdd:cd14934    313 QNMEQCNNSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMF 392

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  495 KLEQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKP-----RLS 568
Cdd:cd14934    393 VLEQEEYKREGIEWVFIDFgLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKPkggkgKGP 472

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  569 NKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFkMLPELFQDDEKAISPTSATSSGRTPLtrtpakptkgrp 648
Cdd:cd14934    473 EAHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSL-GLLALLFKEEEAPAGSKKQKRGSSFM------------ 539

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  649 gqmakehkkTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQ 728
Cdd:cd14934    540 ---------TVSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYP 610

                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1836165656  729 EFFSRYRVLmkQKDVLS----DRKQTCKNVLEKLILDKDKYQFGKTKIFFR 775
Cdd:cd14934    611 EFKQRYQVL--NPNVIPqgfvDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
MYSc_Myh2_mammals cd14912
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ...
 107-775 4.46e-160

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: 506.58  E-value: 4.46e-160
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  107 PAVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 186
Cdd:cd14912      1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  187 GESGAGKTVSAKYAMRYFATVSGSAS-----------EANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKR 255
Cdd:cd14912     80 GESGAGKTVNTKRVIQYFATIAVTGEkkkeeitsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  256 YRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLG-NADNFNYTKQGGSPViEGVDDAKEMAHTRQ 334
Cdd:cd14912    160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITtNPYDYPFVSQGEISV-ASIDDQEELMATDS 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  335 ACTLLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKP 414
Cdd:cd14912    239 AIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKG 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  415 ISKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVF 494
Cdd:cd14912    319 QTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  495 KLEQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRL----SN 569
Cdd:cd14912    399 VLEQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVvkgkAE 478

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  570 KAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSgrtpltrtpakpTKGrpG 649
Cdd:cd14912    479 AHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEGASAGGGA------------KKG--G 544

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  650 QMAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQE 729
Cdd:cd14912    545 KKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYAD 624

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*....
gi 1836165656  730 FFSRYRVLMKQ---KDVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 775
Cdd:cd14912    625 FKQRYKVLNASaipEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
MYSc_Myh13 cd14923
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ...
 107-775 2.58e-159

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: 504.22  E-value: 2.58e-159
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  107 PAVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 186
Cdd:cd14923      1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILIT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  187 GESGAGKTVSAKYAMRYFATVS----------GSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRY 256
Cdd:cd14923     80 GESGAGKTVNTKRVIQYFATIAvtgdkkkeqqPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  257 RIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKlPEFKMLRL--GNADNFNYTKQGgSPVIEGVDDAKEMAHTRQ 334
Cdd:cd14923    160 KLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKK-PELIDLLLisTNPFDFPFVSQG-EVTVASIDDSEELLATDN 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  335 ACTLLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKP 414
Cdd:cd14923    238 AIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKG 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  415 ISKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVF 494
Cdd:cd14923    318 QNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 397

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  495 KLEQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPR-LSNKA- 571
Cdd:cd14923    398 VLEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKpAKGKAe 477

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  572 --FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFqddekaiSPTSATSSGRTPLTRTPAKpTKGRPG 649
Cdd:cd14923    478 ahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLF-------SNYAGAEAGDSGGSKKGGK-KKGSSF 549

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  650 QmakehkkTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQE 729
Cdd:cd14923    550 Q-------TVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYAD 622

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*....
gi 1836165656  730 FFSRYRVLMKQ---KDVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 775
Cdd:cd14923    623 FKQRYRILNASaipEGQFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
MYSc_Myo28 cd14889
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ...
 109-775 2.60e-159

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: 503.67  E-value: 2.60e-159
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  109 VLHNLRVRFIDSkLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQM----ARDERNQSII 184
Cdd:cd14889      3 LLEVLKVRFMQS-NIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMlgrlARGPKNQCIV 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  185 VSGESGAGKTVSAKYAMRYFATVSGSASEanVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFdKRYRIIGANMR 264
Cdd:cd14889     82 ISGESGAGKTESTKLLLRQIMELCRGNSQ--LEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RNGHVKGAKIN 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  265 TYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQACTLLGISES 344
Cdd:cd14889    159 EYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLLDPGKYRYLNNGAGCKREVQYWKKKYDEVCNAMDMVGFTEQ 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  345 HQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHE-PLCIFCELMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNA 423
Cdd:cd14889    239 EEVDMFTILAGILSLGNITFEMDDDEALKVENDSNgWLKAAAGQFGVSEEDLLKTLTCTVTFTRGEQIQRHHTKQQAEDA 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  424 RDALAKHIYAKLFNWIVDNVNQALHSAVK---QHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEE 500
Cdd:cd14889    319 RDSIAKVAYGRVFGWIVSKINQLLAPKDDssvELREIGILDIFGFENFAVNRFEQACINLANEQLQYFFNHHIFLMEQKE 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  501 YMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLyNTHLNKCALFEKPRLSNKAFIIQHFAD 579
Cdd:cd14889    399 YKKEGIDWKEITYKDNKPILDLFLNKpIGILSLLDEQSHFPQATDESFVDKL-NIHFKGNSYYGKSRSKSPKFTVNHYAG 477

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  580 KVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFqddekaisptsATSSGRTPLTRTPAKPTKGRPGQMAKEHKKTV 659
Cdd:cd14889    478 KVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLF-----------TATRSRTGTLMPRAKLPQAGSDNFNSTRKQSV 546

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  660 GHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMK 739
Cdd:cd14889    547 GAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAERYKILLC 626

                          650       660       670
                   ....*....|....*....|....*....|....*.
gi 1836165656  740 QKDvLSDRKQTCKNVLEKliLDKDKYQFGKTKIFFR 775
Cdd:cd14889    627 EPA-LPGTKQSCLRILKA--TKLVGWKCGKTRLFFK 659
MYSc_Myh8 cd14918
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ...
 107-775 4.62e-159

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: 503.50  E-value: 4.62e-159
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  107 PAVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 186
Cdd:cd14918      1 PGVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  187 GESGAGKTVSAKYAMRYFATVSGSAS---------EANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYR 257
Cdd:cd14918     80 GESGAGKTVNTKRVIQYFATIAVTGEkkkeesgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  258 IIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLG-NADNFNYTKQGgSPVIEGVDDAKEMAHTRQAC 336
Cdd:cd14918    160 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITtNPYDYAFVSQG-EITVPSIDDQEELMATDSAI 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  337 TLLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKPIS 416
Cdd:cd14918    239 DILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  417 KLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKL 496
Cdd:cd14918    319 VQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  497 EQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRL----SNKA 571
Cdd:cd14918    399 EQEEYKKEGIEWTFIDFgMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVvkgkAEAH 478

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  572 FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGRtpltrtpakpTKGRPGQm 651
Cdd:cd14918    479 FSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSGAKKGAK----------KKGSSFQ- 547

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  652 akehkkTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFF 731
Cdd:cd14918    548 ------TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFK 621

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*..
gi 1836165656  732 SRYRVLMKQ---KDVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 775
Cdd:cd14918    622 QRYKVLNASaipEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
MYSc_Myo36 cd14897
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ...
 109-775 6.33e-158

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: 499.22  E-value: 6.33e-158
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  109 VLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDM-DPHIFAVAEEAYKQMARDERNQSIIVSG 187
Cdd:cd14897      3 IVQTLKSRYNKDK-FYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSVRSQrPPHLFWIADQAYRRLLETGRNQCILVSG 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  188 ESGAGKTVSAKYAMRYFATVSGSASEaNVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYL 267
Cdd:cd14897     82 ESGAGKTESTKYMIKHLMKLSPSDDS-DLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAKIDDYL 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  268 LEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNyTKQGGSPVIEGVDDAKEMAHTRQACT-------LLG 340
Cdd:cd14897    161 LEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHR-ILRDDNRNRPVFNDSEELEYYRQMFHdltnimkLIG 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  341 ISESHQMGIFRILAGILHLGNVGF-TSRDADSCTIPPKHePLCIFCELMGVDYEEMCHWLCHRKLATATETYIKPISKLQ 419
Cdd:cd14897    240 FSEEDISVIFTILAAILHLTNIVFiPDEDTDGVTVADEY-PLHAVAKLLGIDEVELTEALISNVNTIRGERIQSWKSLRQ 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  420 ATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQH-----SFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVF 494
Cdd:cd14897    319 ANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDFQimtrgPSIGILDMSGFENFKINSFDQLCINLSNERLQQYFNDYVF 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  495 KLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLyNTHLNKCALFEKPRLSNKAFI 573
Cdd:cd14897    399 PRERSEYEIEGIEWRDIEYHDNDDVLELFFKKpLGILPLLDEESTFPQSTDSSLVQKL-NKYCGESPRYVASPGNRVAFG 477

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  574 IQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFqddekaispTSatssgrtpltrtpakptkgrpgqmak 653
Cdd:cd14897    478 IRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLF---------TS-------------------------- 522

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  654 ehkktvghQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSR 733
Cdd:cd14897    523 --------YFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKR 594

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|...
gi 1836165656  734 YRVLM-KQKDVLSDRKQTCKNVLEklILDKDKYQFGKTKIFFR 775
Cdd:cd14897    595 YKEICdFSNKVRSDDLGKCQKILK--TAGIKGYQFGKTKVFLK 635
MYSc_Myh1_mammals cd14910
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ...
 107-775 5.43e-157

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: 498.10  E-value: 5.43e-157
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  107 PAVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 186
Cdd:cd14910      1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  187 GESGAGKTVSAKYAMRYFATVSGSAS-----------EANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKR 255
Cdd:cd14910     80 GESGAGKTVNTKRVIQYFATIAVTGEkkkeeatsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  256 YRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLG-NADNFNYTKQGgSPVIEGVDDAKEMAHTRQ 334
Cdd:cd14910    160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITtNPYDYAFVSQG-EITVPSIDDQEELMATDS 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  335 ACTLLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKP 414
Cdd:cd14910    239 AIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKG 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  415 ISKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVF 494
Cdd:cd14910    319 QTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  495 KLEQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRLSNKA-- 571
Cdd:cd14910    399 VLEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKve 478

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  572 --FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFqddekaisptsatsSGRTPLTRTPAKPTKGrpG 649
Cdd:cd14910    479 ahFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLF--------------SGAAAAEAEEGGGKKG--G 542

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  650 QMAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQE 729
Cdd:cd14910    543 KKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYAD 622

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*....
gi 1836165656  730 FFSRYRVLMKQ---KDVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 775
Cdd:cd14910    623 FKQRYKVLNASaipEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
MYSc_Myh18 cd14932
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ...
 108-775 1.10e-156

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: 497.24  E-value: 1.10e-156
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  108 AVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 187
Cdd:cd14932      2 SVLHNLKERYY-SGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  188 ESGAGKTVSAKYAMRYFATVSGSA-----------SEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRY 256
Cdd:cd14932     81 ESGAGKTENTKKVIQYLAYVASSFktkkdqssialSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  257 RIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQgGSPVIEGVDDAKEMAHTRQAC 336
Cdd:cd14932    161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSN-GNVTIPGQQDKELFAETMEAF 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  337 TLLGISESHQMGIFRILAGILHLGNVGF-TSRDADSCTIPPKHEPLCIfCELMGVDYEEMCHWLCHRKLATATETYIKPI 415
Cdd:cd14932    240 RIMSIPEEEQTGLLKVVSAVLQLGNMSFkKERNSDQASMPDDTAAQKV-CHLLGMNVTDFTRAILSPRIKVGRDYVQKAQ 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  416 SKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQ-HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVF 494
Cdd:cd14932    319 TQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  495 KLEQEEYMKEQIPWTLIDF-YDNQPCINLIESKL---GILDLLDEECKMPKGTDDTWAQKLYNTHLNKcALFEKP-RLSN 569
Cdd:cd14932    399 ILEQEEYQREGIEWSFIDFgLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVVQEQGNN-PKFQKPkKLKD 477

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  570 KA-FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSsgrtpLTRTPAKPTKGRP 648
Cdd:cd14932    478 DAdFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRIVGLDKVAG-----MGESLHGAFKTRK 552

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  649 GQMakehkKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQ 728
Cdd:cd14932    553 GMF-----RTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 627

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*....
gi 1836165656  729 EFFSRYRVLMKQK--DVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 775
Cdd:cd14932    628 EFRQRYEILTPNAipKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
MYSc_Myh4 cd14915
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ...
 107-775 1.70e-156

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: 496.56  E-value: 1.70e-156
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  107 PAVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 186
Cdd:cd14915      1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  187 GESGAGKTVSAKYAMRYFATVSGSAS-----------EANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKR 255
Cdd:cd14915     80 GESGAGKTVNTKRVIQYFATIAVTGEkkkeeaasgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  256 YRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLG-NADNFNYTKQGgSPVIEGVDDAKEMAHTRQ 334
Cdd:cd14915    160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITtNPYDFAFVSQG-EITVPSIDDQEELMATDS 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  335 ACTLLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKP 414
Cdd:cd14915    239 AVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKG 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  415 ISKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVF 494
Cdd:cd14915    319 QTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  495 KLEQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRLSN-KA- 571
Cdd:cd14915    399 VLEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKgKAe 478

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  572 --FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGrtpltrtpakptkgrpG 649
Cdd:cd14915    479 ahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQTAEAEGGGGKKG----------------G 542

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  650 QMAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQE 729
Cdd:cd14915    543 KKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYAD 622

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*....
gi 1836165656  730 FFSRYRVLMKQ---KDVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 775
Cdd:cd14915    623 FKQRYKVLNASaipEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
MYSc_Myh11 cd14921
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ...
 108-775 3.38e-156

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: 495.69  E-value: 3.38e-156
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  108 AVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 187
Cdd:cd14921      2 SVLHNLRERYF-SGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  188 ESGAGKTVSAKYAMRYFATVSGS-------ASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIG 260
Cdd:cd14921     81 ESGAGKTENTKKVIQYLAVVASShkgkkdtSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  261 ANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPvIEGVDDAKEMAHTRQACTLLG 340
Cdd:cd14921    161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVP-IPAAQDDEMFQETLEAMSIMG 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  341 ISESHQMGIFRILAGILHLGNVGF-TSRDADSCTIPPKHEPLCIfCELMGVDYEEMCHWLCHRKLATATETYIKPISKLQ 419
Cdd:cd14921    240 FSEEEQLSILKVVSSVLQLGNIVFkKERNTDQASMPDNTAAQKV-CHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQ 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  420 ATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQ-HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQ 498
Cdd:cd14921    319 ADFAIEALAKATYERLFRWILTRVNKALDKTHRQgASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQ 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  499 EEYMKEQIPWTLIDF-YDNQPCINLIE---SKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKcALFEKPR-LSNKA-F 572
Cdd:cd14921    399 EEYQREGIEWNFIDFgLDLQPCIELIErpnNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNH-PKFQKPKqLKDKTeF 477

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  573 IIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGRTPLTrTPAKPTKGRpgqma 652
Cdd:cd14921    478 SIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSLP-SASKTKKGM----- 551

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  653 kehKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFS 732
Cdd:cd14921    552 ---FRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 628

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*
gi 1836165656  733 RYRVLMKQK--DVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 775
Cdd:cd14921    629 RYEILAANAipKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
MYSc_Myo30 cd14891
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ...
 107-775 3.21e-155

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: 492.25  E-value: 3.21e-155
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  107 PAVLHNLRVRF-IDSKLIYTYCGIVLVAINPYEQLPiygEDIINAYSGQNMGDMDPHIFAVAEEAYKQM---ARDERNQS 182
Cdd:cd14891      1 AGILHNLEERSkLDNQRPYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMclgSGRMQNQS 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  183 IIVSGESGAGKTVSAKYAMRYFATVS-----------------GSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFG 245
Cdd:cd14891     78 IVISGESGAGKTETSKIILRFLTTRAvggkkasgqdieqsskkRKLSVTSLDERLMDTNPILESFGNAKTLRNHNSSRFG 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  246 KYIEIGFDKR-YRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVD 324
Cdd:cd14891    158 KFMKLQFTKDkFKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNQSGCVSDDNID 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  325 DAKEMAHTRQACTLLGISESHQMGIFRILAGILHLGNVGFTSRD-----ADSCTIPPKhEPLCIFCELMGVDYEEMCHWL 399
Cdd:cd14891    238 DAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDtsegeAEIASESDK-EALATAAELLGVDEEALEKVI 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  400 CHRKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEI-NSFEQFCI 478
Cdd:cd14891    317 TQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFETkNDFEQLLI 396

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  479 NYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESKL-GILDLLDEECKMPKGTDDTWAQKLYNTHL- 556
Cdd:cd14891    397 NYANEALQATFNQQVFIAEQELYKSEGIDVGVITWPDNRECLDLIASKPnGILPLLDNEARNPNPSDAKLNETLHKTHKr 476

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  557 NKCALFEKPRLSNKAFIIQHFADKVEYQCEGFLEKNKDTVfeeqikvlksskfkmlPELFQDdekaisptsatssgrtpL 636
Cdd:cd14891    477 HPCFPRPHPKDMREMFIVKHYAGTVSYTIGSFIDKNNDII----------------PEDFED-----------------L 523

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  637 TRTPAKptkgrpgqmakehkktvghqFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRI 716
Cdd:cd14891    524 LASSAK--------------------FSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEV 583

                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1836165656  717 SAAGFPSRWTYQEFFSRYRVLM----KQKDVLSDRKQTcKNVLEKLILDKDKYQFGKTKIFFR 775
Cdd:cd14891    584 LKVGLPTRVTYAELVDVYKPVLppsvTRLFAENDRTLT-QAILWAFRVPSDAYRLGRTRVFFR 645
MYSc_Myo19 cd14880
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ...
 109-773 1.08e-153

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: 488.59  E-value: 1.08e-153
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  109 VLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLP-IYGEDIINAY-SGQNMGDMDPHIFAVAEEAYK--QMARDERNQSII 184
Cdd:cd14880      3 VLRCLQARYT-ADTFYTNAGCTLVALNPFKPVPqLYSPELMREYhAAPQPQKLKPHIFTVGEQTYRnvKSLIEPVNQSIV 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  185 VSGESGAGKTVSAKYAMRYFATVSGSAS--EAN-----VEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYR 257
Cdd:cd14880     82 VSGESGAGKTWTSRCLMKFYAVVAASPTswESHkiaerIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQQ 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  258 IIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTkqggsPVIEGVDDAKEMAHTRQACT 337
Cdd:cd14880    162 MTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWL-----PNPERNLEEDCFEVTREAML 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  338 LLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEPLC---IFCELMGVDYEEMCHWLCHRKLATATE--TYI 412
Cdd:cd14880    237 HLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTKEsvrTSALLLKLPEDHLLETLQIRTIRAGKQqqVFK 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  413 KPISKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQ-HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNM 491
Cdd:cd14880    317 KPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSwTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQHFVA 396

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  492 HVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIE-SKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRLSNK 570
Cdd:cd14880    397 HYLRAQQEEYAVEGLEWSFINYQDNQTCLDLIEgSPISICSLINEECRLNRPSSAAQLQTRIESALAGNPCLGHNKLSRE 476

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  571 -AFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGRTPLTrtpakptkgrpg 649
Cdd:cd14880    477 pSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEKTQEEPSGQSRAPVL------------ 544

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  650 qmakehkkTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQE 729
Cdd:cd14880    545 --------TVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQN 616

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....
gi 1836165656  730 FFSRYRVLMKqkdvLSDRKQTCKNVLEKLILDKDKYQFGKTKIF 773
Cdd:cd14880    617 FVERYKLLRR----LRPHTSSGPHSPYPAKGLSEPVHCGRTKVF 656
MYSc_Myh9 cd14919
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ...
 108-775 2.91e-151

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: 482.29  E-value: 2.91e-151
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  108 AVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 187
Cdd:cd14919      2 SVLHNLKERYY-SGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  188 ESGAGKTVSAKYAMRYFATVSGS----ASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANM 263
Cdd:cd14919     81 ESGAGKTENTKKVIQYLAHVASShkskKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  264 RTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQgGSPVIEGVDDAKEMAHTRQACTLLGISE 343
Cdd:cd14919    161 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSN-GHVTIPGQQDKDMFQETMEAMRIMGIPE 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  344 SHQMGIFRILAGILHLGNVGF-TSRDADSCTIPPKHEPLCIfCELMGVDYEEMCHWLCHRKLATATETYIKPISKLQATN 422
Cdd:cd14919    240 EEQMGLLRVISGVLQLGNIVFkKERNTDQASMPDNTAAQKV-SHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADF 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  423 ARDALAKHIYAKLFNWIVDNVNQALHSAVKQ-HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEY 501
Cdd:cd14919    319 AIEALAKATYERMFRWLVLRINKALDKTKRQgASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEY 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  502 MKEQIPWTLIDF-YDNQPCINLIESKL---GILDLLDEECKMPKGTDDTWAQKLYN---THLNkcalFEKPR-LSNKA-F 572
Cdd:cd14919    399 QREGIEWNFIDFgLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQeqgTHPK----FQKPKqLKDKAdF 474

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  573 IIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGRTPLtrtpAKPTKGRPGQMa 652
Cdd:cd14919    475 CIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETAL----PGAFKTRKGMF- 549

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  653 kehkKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFS 732
Cdd:cd14919    550 ----RTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQ 625

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*
gi 1836165656  733 RYRVLMKQK--DVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 775
Cdd:cd14919    626 RYEILTPNSipKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
MYSc_Myo41 cd14902
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ...
 107-775 1.04e-150

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: 482.47  E-value: 1.04e-150
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  107 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLP-IYGEDIINAY--------SGQNMGDMDPHIFAVAEEAYKQMARD 177
Cdd:cd14902      1 AALLQALSERF-EHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYkasmtstsPVSQLSELPPHVFAIGGKAFGGLLKP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  178 ER-NQSIIVSGESGAGKTVSAKYAMRYFATVSGSASEANVE--------EKVLASNPIMESIGNAKTTRNDNSSRFGKYI 248
Cdd:cd14902     80 ERrNQSILVSGESGSGKTESTKFLMQFLTSVGRDQSSTEQEgsdaveigKRILQTNPILESFGNAQTIRNDNSSRFGKFI 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  249 EIGFDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGS----PVIEGVD 324
Cdd:cd14902    160 KIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELLNSYGPsfarKRAVADK 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  325 DAKEMAHTRQACTLLGISESHQMGIFRILAGILHLGNVGFT---SRDADSCTIPPKHEPLCIFCELMGVDYEEMCHWLCH 401
Cdd:cd14902    240 YAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTaenGQEDATAVTAASRFHLAKCAELMGVDVDKLETLLSS 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  402 RKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSF---------IGVLDIYGFETFEINS 472
Cdd:cd14902    320 REIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINYFDSAVSIsdedeelatIGILDIFGFESLNRNG 399

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  473 FEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESKL-GILDLLDEECKMPKGTDDTWAQKL 551
Cdd:cd14902    400 FEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYPSNAACLALFDDKSnGLFSLLDQECLMPKGSNQALSTKF 479

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  552 YNTHLNKcalfekprlsnKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEK--AISPTSAT 629
Cdd:cd14902    480 YRYHGGL-----------GQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGADENRdsPGADNGAA 548

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  630 SSGRTPLTRTPakptkgrpgqmakehkkTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACG 709
Cdd:cd14902    549 GRRRYSMLRAP-----------------SVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVG 611

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  710 VLETIRISAAGFPSRWTYQEF---FSRYRVLMKQKD----------------------VLSDRKQTCKNVLEKLILDKDK 764
Cdd:cd14902    612 VLEAVRIARHGYSVRLAHASFielFSGFKCFLSTRDraakmnnhdlaqalvtvlmdrvLLEDGVEREEKNPGALTAVTGD 691

                          730       740
                   ....*....|....*....|....*
gi 1836165656  765 Y--------------QFGKTKIFFR 775
Cdd:cd14902    692 GsgtafendcrrkdvQVGRTLVFCK 716
MYSc_Myo34 cd14895
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ...
 107-775 2.20e-149

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: 478.29  E-value: 2.20e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  107 PAVLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLP-IYGediINAYSGQNMGDMD--PHIFAVAEEAYKQMAR------- 176
Cdd:cd14895      1 PAFVDYLAQRYGVDQ-VYCRSGAVLIAVNPFKHIPgLYD---LHKYREEMPGWTAlpPHVFSIAEGAYRSLRRrlhepga 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  177 DERNQSIIVSGESGAGKTVSAKYAMRYFA--------TVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYI 248
Cdd:cd14895     77 SKKNQTILVSGESGAGKTETTKFIMNYLAesskhttaTSSSKRRRAISGSELLSANPILESFGNARTLRNDNSSRFGKFV 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  249 EIGF-----DKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLG--NADNFNYTKQGGSPVI- 320
Cdd:cd14895    157 RMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLEllSAQEFQYISGGQCYQRn 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  321 EGVDDAKEMAHTRQACTLLGISESHQMGIFRILAGILHLGNVGFTS-------RDADSCTIPPK-----------HEPLC 382
Cdd:cd14895    237 DGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVAssedegeEDNGAASAPCRlasaspssltvQQHLD 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  383 IFCELMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDNVNQAlhSAVKQHS------- 455
Cdd:cd14895    317 IVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSA--SPQRQFAlnpnkaa 394

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  456 ------FIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LG 528
Cdd:cd14895    395 nkdttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDNSVCLEMLEQRpSG 474

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  529 ILDLLDEECKMPKGTDDTWAQKLYNThLNKCALFEKPRL--SNKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKS 606
Cdd:cd14895    475 IFSLLDEECVVPKGSDAGFARKLYQR-LQEHSNFSASRTdqADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAELFSVLGK 553

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  607 SKFKMLPELFqdDEKAISPTSATSSGRTPLTRtpakptkgRPGQMAkehKKTVGHQFRNSLHLLMETLNATTPHYVRCIK 686
Cdd:cd14895    554 TSDAHLRELF--EFFKASESAELSLGQPKLRR--------RSSVLS---SVGIGSQFKQQLASLLDVVQQTQTHYIRCIK 620

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  687 PNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMKQKDVLSdrkQTCKNVLEKliLDKDKYQ 766
Cdd:cd14895    621 PNDESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKNASD---ATASALIET--LKVDHAE 695


                   ....*....
gi 1836165656  767 FGKTKIFFR 775
Cdd:cd14895    696 LGKTRVFLR 704
MYSc_Myo39 cd14900
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ...
 109-749 3.03e-149

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: 475.18  E-value: 3.03e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  109 VLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLP-IYGEDIINAY---------SGQNMGD--MDPHIFAVAEEAYKQMAR 176
Cdd:cd14900      3 ILSALETRFYAQK-IYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssSTRNKGSdpMPPHIYQVAGEAYKAMML 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  177 ----DERNQSIIVSGESGAGKTVSAKYAMRYFA---------TVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSR 243
Cdd:cd14900     82 glngVMSDQSILVSGESGSGKTESTKFLMEYLAqagdnnlaaSVSMGKSTSGIAAKVLQTNILLESFGNARTLRNDNSSR 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  244 FGKYIEIGFDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKmlrlgnADNFNYtkqggspviegV 323
Cdd:cd14900    162 FGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARK------RDMYRR-----------V 224

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  324 DDAKEMahtrqactlLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHE--PLCIF-----CELMGVDYEEMC 396
Cdd:cd14900    225 MDAMDI---------IGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSDlaPSSIWsrdaaATLLSVDATKLE 295

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  397 HWLCHRKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDNVNQALH--SAVKQHS---FIGVLDIYGFETFEIN 471
Cdd:cd14900    296 KALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLKmdDSSKSHGglhFIGILDIFGFEVFPKN 375

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  472 SFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQK 550
Cdd:cd14900    376 SFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFCDNQDCVNLISQRpTGILSLIDEECVMPKGSDTTLASK 455

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  551 LYnTHLNKCALFEKPRL--SNKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIkvlksskfkmlpELFQDdekaisptsa 628
Cdd:cd14900    456 LY-RACGSHPRFSASRIqrARGLFTIVHYAGHVEYSTDGFLEKNKDVLHQEAV------------DLFVY---------- 512

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  629 tssgrtpltrtpakptkgrpgqmakehkktvGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRAC 708
Cdd:cd14900    513 -------------------------------GLQFKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCN 561

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|.
gi 1836165656  709 GVLETIRISAAGFPSRWTYQEFFSRYRVLMKQKDVLSDRKQ 749
Cdd:cd14900    562 GVMEAVRVARAGFPIRLLHDEFVARYFSLARAKNRLLAKKQ 602
MYSc_Myh19 cd15896
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ...
 108-775 4.08e-149

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: 476.48  E-value: 4.08e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  108 AVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 187
Cdd:cd15896      2 SVLHNLKERYY-SGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  188 ESGAGKTVSAKYAMRYFATVSGS-----------ASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRY 256
Cdd:cd15896     81 ESGAGKTENTKKVIQYLAHVASShktkkdqnslaLSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  257 RIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQgGSPVIEGVDDAKEMAHTRQAC 336
Cdd:cd15896    161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSN-GNVTIPGQQDKDLFTETMEAF 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  337 TLLGISESHQMGIFRILAGILHLGNVGF-TSRDADSCTIPPKHEPLCIfCELMGVDYEEMCHWLCHRKLATATETYIKPI 415
Cdd:cd15896    240 RIMGIPEDEQIGMLKVVASVLQLGNMSFkKERHTDQASMPDNTAAQKV-CHLMGMNVTDFTRAILSPRIKVGRDYVQKAQ 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  416 SKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQ-HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVF 494
Cdd:cd15896    319 TQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  495 KLEQEEYMKEQIPWTLIDF-YDNQPCINLIE---SKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRLSNK 570
Cdd:cd15896    399 ILEQEEYQREGIEWSFIDFgLDLQPCIDLIEkpaSPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKKLKDE 478

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  571 A-FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGRTPltrtpaKPTKGRPG 649
Cdd:cd15896    479 AdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVGLDKVSGMSEMP------GAFKTRKG 552

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  650 QMakehkKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQE 729
Cdd:cd15896    553 MF-----RTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 627

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*...
gi 1836165656  730 FFSRYRVLMKQK--DVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 775
Cdd:cd15896    628 FRQRYEILTPNAipKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
MYSc_Myh14_mammals cd14930
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ...
 108-775 6.18e-147

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: 470.35  E-value: 6.18e-147
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  108 AVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 187
Cdd:cd14930      2 SVLHNLRERYY-SGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  188 ESGAGKTVSAKYAMRYFATVSGSAS-------EANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIG 260
Cdd:cd14930     81 ESGAGKTENTKKVIQYLAHVASSPKgrkepgvPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  261 ANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGgsPVIEGVDDAKEMAHTRQACTLLG 340
Cdd:cd14930    161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNG--PSSSPGQERELFQETLESLRVLG 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  341 ISESHQMGIFRILAGILHLGNVGF-TSRDADSCTIpPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKPISKLQ 419
Cdd:cd14930    239 FSHEEITSMLRMVSAVLQFGNIVLkRERNTDQATM-PDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQ 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  420 ATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQ-HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQ 498
Cdd:cd14930    318 ADFALEALAKATYERLFRWLVLRLNRALDRSPRQgASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQ 397

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  499 EEYMKEQIPWTLIDF-YDNQPCINLIESKL---GILDLLDEECKMPKGTDDTWAQKLYNTHlNKCALFEKPR-LSNKA-F 572
Cdd:cd14930    398 EEYQREGIPWTFLDFgLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRPRhLRDQAdF 476

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  573 IIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGRtpltrtpaKPTKGRPgqmA 652
Cdd:cd14930    477 SVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGD--------GPPGGRP---R 545

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  653 KEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFS 732
Cdd:cd14930    546 RGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQ 625

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*
gi 1836165656  733 RYRVLMKQK--DVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 775
Cdd:cd14930    626 RYEILTPNAipKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
PTZ00014 PTZ00014
myosin-A; Provisional
 58-822 1.72e-141

myosin-A; Provisional


Pssm-ID: 240229 [Multi-domain]  Cd Length: 821  Bit Score: 460.65  E-value: 1.72e-141
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656   58 GDKVLLLHLEEGKDLEYHLDPKtkelpHLRNPDILVGEN---DLTALSYLHEPAVLHNLRVRFIdSKLIYTYCGIVLVAI 134
Cdd:PTZ00014    63 GEKLTLKQIDPPTNSTFEVKPE-----HAFNANSQIDPMtygDIGLLPHTNIPCVLDFLKHRYL-KNQIYTTADPLLVAI 136

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  135 NPYEQLPIYGEDIINAY-SGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSGESGAGKTVSAKYAMRYFATVSGSASE 213
Cdd:PTZ00014   137 NPFKDLGNTTNDWIRRYrDAKDSDKLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFASSKSGNMD 216

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  214 ANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLC--A 291
Cdd:PTZ00014   217 LKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLkgA 296

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  292 SAKLPE-FKMLRLGNADNFNytkqGGSPVIEGVDDAKEMAHTRQACTLLGISESHQMGIFRILAGILHLGNVGFTSRDAD 370
Cdd:PTZ00014   297 NDEMKEkYKLKSLEEYKYIN----PKCLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEG 372

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  371 -----SCTIPPKHEPLCIFCELMGVDYEEMCHWLchrklaTATETYI------KPISKLQATNARDALAKHIYAKLFNWI 439
Cdd:PTZ00014   373 gltdaAAISDESLEVFNEACELLFLDYESLKKEL------TVKVTYAgnqkieGPWSKDESEMLKDSLSKAVYEKLFLWI 446

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  440 VDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPC 519
Cdd:PTZ00014   447 IRNLNATIEPPGGFKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGISTEELEYTSNESV 526

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  520 INLIESKL-GILDLLDEECKMPKGTDD----TWAQKLYNthlNKCALFEKpRLSNKAFIIQHFADKVEYQCEGFLEKNKD 594
Cdd:PTZ00014   527 IDLLCGKGkSVLSILEDQCLAPGGTDEkfvsSCNTNLKN---NPKYKPAK-VDSNKNFVIKHTIGDIQYCASGFLFKNKD 602

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  595 TVFEEQIKVLKSSKFKMLPELFQDDEkaisptsatssgrtpLTRtpakptkgrpGQMAKehKKTVGHQFRNSLHLLMETL 674
Cdd:PTZ00014   603 VLRPELVEVVKASPNPLVRDLFEGVE---------------VEK----------GKLAK--GQLIGSQFLNQLDSLMSLI 655

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  675 NATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRV--LMKQKDVLSDRKQTCK 752
Cdd:PTZ00014   656 NSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYldLAVSNDSSLDPKEKAE 735

                          730       740       750       760       770       780       790
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1836165656  753 NVLEKLILDKDKYQFGKTKIFFRAGQVAYLEKLRADKLRA--ACIRIqktIRGWLLRKKYLR-MRKAAITMQR 822
Cdd:PTZ00014   736 KLLERSGLPKDSYAIGKTMVFLKKDAAKELTQIQREKLAAwePLVSV---LEALILKIKKKRkVRKNIKSLVR 805
MYSc_Myo35 cd14896
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ...
 107-775 5.44e-139

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: 447.30  E-value: 5.44e-139
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  107 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 186
Cdd:cd14896      1 SSVLLCLKKRF-HLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  187 GESGAGKTVSAKYAMRYFATVSGSASEANVE--EKVLasnPIMESIGNAKTTRNDNSSRFGKYIEIGFdKRYRIIGANMR 264
Cdd:cd14896     80 GHSGSGKTEAAKKIVQFLSSLYQDQTEDRLRqpEDVL---PILESFGHAKTILNANASRFGQVLRLHL-QHGVIVGASVS 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  265 TYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQACTLLGISES 344
Cdd:cd14896    156 HYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGACRLQGKEDAQDFEGLLKALQGLGLCAE 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  345 HQMGIFRILAGILHLGNVGFTSRDADSctippkHEPLCIFCE--------LMGVDYEEMCHWLCHRKLATATETYIKPIS 416
Cdd:cd14896    236 ELTAIWAVLAAILQLGNICFSSSERES------QEVAAVSSWaeihtaarLLQVPPERLEGAVTHRVTETPYGRVSRPLP 309

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  417 KLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSF--IGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVF 494
Cdd:cd14896    310 VEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESDatIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLL 389

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  495 KLEQEEYMKEQIPWTLIDFYDNQPCINLIESKL-GILDLLDEECKMPKGTDDTWAQKLYNTHLNKcALFEKPRLSNKAFI 573
Cdd:cd14896    390 AQEEEECQRELLPWVPIPQPPRESCLDLLVDQPhSLLSILDDQTWLSQATDHTFLQKCHYHHGDH-PSYAKPQLPLPVFT 468

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  574 IQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDdekaisptsatssgrtpltrtpAKPTKGRpgqmaK 653
Cdd:cd14896    469 VRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQE----------------------AEPQYGL-----G 521

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  654 EHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSR 733
Cdd:cd14896    522 QGKPTLASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLAR 601

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....
gi 1836165656  734 YRVLMKQK-DVLSDRKQtCKNVLEKLI-LDKDKYQFGKTKIFFR 775
Cdd:cd14896    602 FGALGSERqEALSDRER-CGAILSQVLgAESPLYHLGATKVLLK 644
MYSc_Myo45 cd14906
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ...
 109-773 1.58e-137

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


Pssm-ID: 276871 [Multi-domain]  Cd Length: 715  Bit Score: 445.96  E-value: 1.58e-137
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  109 VLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLP-IYGEDIINAYSGQN-MGDMDPHIFAVAEEAYKQMARDERNQSIIVS 186
Cdd:cd14906      3 ILNNLGKRYK-SDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINqNKSPIPHIYAVALRAYQSMVSEKKNQSIIIS 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  187 GESGAGKTVSAKYAMRYFATVSGSASEAN---------VEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKR-Y 256
Cdd:cd14906     82 GESGSGKTEASKTILQYLINTSSSNQQQNnnnnnnnnsIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSdG 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  257 RIIGANMRTYLLEKSRVVFQAEEER-NYHIFYQLCASAKLPEFKMLRLGN--------------ADNFNYTKQGGSPVIE 321
Cdd:cd14906    162 KIDGASIETYLLEKSRISHRPDNINlSYHIFYYLVYGASKDERSKWGLNNdpskyryldarddvISSFKSQSSNKNSNHN 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  322 GVDDAKE-MAHTRQACTLLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTI---PPKHEPLCIFCELMGVDYEEMCH 397
Cdd:cd14906    242 NKTESIEsFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAyqkDKVTASLESVSKLLGYIESVFKQ 321

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  398 WLCHRKLATATE--TYIKPISKLQATNARDALAKHIYAKLFNWIVDNVNQ-----------ALHSAVKQHSFIGVLDIYG 464
Cdd:cd14906    322 ALLNRNLKAGGRgsVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRkfnqntqsndlAGGSNKKNNLFIGVLDIFG 401

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  465 FETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGT 543
Cdd:cd14906    402 FENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNFIDNKECIELIEKKsDGILSLLDDECIMPKGS 481

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  544 DDTWAQKlYNTHLNKCALFEKPRLSNKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAI 623
Cdd:cd14906    482 EQSLLEK-YNKQYHNTNQYYQRTLAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLFQQQITST 560

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  624 SPTSATSSGRTpltrtpakptkgrpgqmakehkkTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQ 703
Cdd:cd14906    561 TNTTKKQTQSN-----------------------TVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLS 617

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  704 QLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMKQKDVLSDRKQTCKNVLEKLIL----------------------- 760
Cdd:cd14906    618 QLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDMYNRKNNNNPKLASQLILQNIqsklktmgisnnkkknnsnsnsn 697

                          730
                   ....*....|....*.
gi 1836165656  761 ---DKDKYQFGKTKIF 773
Cdd:cd14906    698 ttnDKPLFQIGKTKIF 713
MYSc_Myo14 cd14876
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ...
 107-773 9.67e-137

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: 441.35  E-value: 9.67e-137
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  107 PAVLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLPIYGEDIINAYSG-QNMGDMDPHIFAVAEEAYKQMARDERNQSIIV 185
Cdd:cd14876      1 PCVLDFLKHRYLKNQ-IYTTADPLLVAINPFKDLGNATDEWIRKYRDaPDLTKLPPHVFYTARRALENLHGVNKSQTIIV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  186 SGESGAGKTVSAKYAMRYFATVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRT 265
Cdd:cd14876     80 SGESGAGKTEATKQIMRYFASAKSGNMDLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIRYGSVVA 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  266 YLLEKSRVVFQAEEERNYHIFYQLC--ASAKLPE-FKMLRLGNADNFNytkqGGSPVIEGVDDAKEMAHTRQACTLLGIS 342
Cdd:cd14876    160 FLLEKSRIVTQDDNERSYHIFYQLLkgADSEMKSkYHLLGLKEYKFLN----PKCLDVPGIDDVADFEEVLESLKSMGLT 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  343 ESHQMGIFRILAGILHLGNVGFTSRDA----DSCTIPPkhEPLCIF---CELMGVDYEEMCHWLChRKLATATETYIK-P 414
Cdd:cd14876    236 EEQIDTVFSIVSGVLLLGNVKITGKTEqgvdDAAAISN--ESLEVFkeaCSLLFLDPEALKRELT-VKVTKAGGQEIEgR 312

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  415 ISKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVF 494
Cdd:cd14876    313 WTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFIDIVF 392

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  495 KLEQEEYMKEQIPWTLIDFYDNQPCIN-LIESKLGILDLLDEECKMPKGTDD----TWAQKLYNthlNKCALFEKpRLSN 569
Cdd:cd14876    393 ERESKLYKDEGIPTAELEYTSNAEVIDvLCGKGKSVLSILEDQCLAPGGSDEkfvsACVSKLKS---NGKFKPAK-VDSN 468

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  570 KAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDdekaisptsatssgrTPLTRtpakptkgrpG 649
Cdd:cd14876    469 INFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEG---------------VVVEK----------G 523

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  650 QMAKehKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQE 729
Cdd:cd14876    524 KIAK--GSLIGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEE 601

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*.
gi 1836165656  730 FFSRYRVL-MKQKDVLSDRKQT-CKNVLEKLILDKDKYQFGKTKIF 773
Cdd:cd14876    602 FLYQFKFLdLGIANDKSLDPKVaALKLLESSGLSEDEYAIGKTMVF 647
MYSc_Myo38 cd14899
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ...
 108-760 1.10e-128

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: 421.43  E-value: 1.10e-128
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  108 AVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLP-IYGEDIINAYS---GQNMGDM-------DPHIFAVAEEAYKQMAR 176
Cdd:cd14899      2 SILNALRLRY-ERHAIYTHIGDILISINPFQDLPqLYGDEILRGYAydhNSQFGDRvtstdprEPHLFAVARAAYIDIVQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  177 DERNQSIIVSGESGAGKTVSAKYAMRYFATVSG----------------SASEANVEEKVLASNPIMESIGNAKTTRNDN 240
Cdd:cd14899     81 NGRSQSILISGESGAGKTEATKIIMTYFAVHCGtgnnnltnsesisppaSPSRTTIEEQVLQSNPILEAFGNARTVRNDN 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  241 SSRFGKYIEIGF-DKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQL------CASAKLPEFKMLRlGNADNFNYTK 313
Cdd:cd14899    161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELlsadnnCVSKEQKQVLALS-GGPQSFRLLN 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  314 QG-GSPVIEGVDDAKEMAHTRQACTLLGISESHQMGIFRILAGILHLGNVGFT--------------SRDADSCTIPPKH 378
Cdd:cd14899    240 QSlCSKRRDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEqiphkgddtvfadeARVMSSTTGAFDH 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  379 epLCIFCELMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVK------ 452
Cdd:cd14899    320 --FTKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQASapwgad 397

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  453 ---------QHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLI 523
Cdd:cd14899    398 esdvddeedATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNNRACLELF 477

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  524 ESK-LGILDLLDEECKMPKGTDDTWAQKLY--------NTHLNKCALFEKprlsNKAFIIQHFADKVEYQCEGFLEKNKD 594
Cdd:cd14899    478 EHRpIGIFSLTDQECVFPQGTDRALVAKYYlefekknsHPHFRSAPLIQR----TTQFVVAHYAGCVTYTIDGFLAKNKD 553

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  595 TVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGRTPLTRTPAKPTKGrpgqmakehKKTVGHQFRNSLHLLMETL 674
Cdd:cd14899    554 SFCESAAQLLAGSSNPLIQALAAGSNDEDANGDSELDGFGGRTRRRAKSAIA---------AVSVGTQFKIQLNELLSTV 624

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  675 NATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYR----VLMKQKDVLSDRKQT 750
Cdd:cd14899    625 RATTPRYVRCIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRYRrvllSLYKWGDNDFERQMR 704

                          730
                   ....*....|
gi 1836165656  751 CKNVLEKLIL 760
Cdd:cd14899    705 CGVSLGKTRV 714
MYSc_Myo25 cd14886
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ...
 109-775 1.90e-124

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: 406.96  E-value: 1.90e-124
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  109 VLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLP-IYGEDIINAYSGQNMG-----DMDPHIFAVAEEAYKQMARDERNQS 182
Cdd:cd14886      3 VIDILRDRFAKDK-IYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQS 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  183 IIVSGESGAGKTVSAKYAMRYFAtVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGAN 262
Cdd:cd14886     82 CIVSGESGAGKTETAKQLMNFFA-YGHSTSSTDVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGLKGGK 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  263 MRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQACTLLgIS 342
Cdd:cd14886    161 ITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCYDAPGIDDQKEFAPVRSQLEKL-FS 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  343 ESHQMGIFRILAGILHLGNVGF---TSRDADSCTIPPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKPISKLQ 419
Cdd:cd14886    240 KNEIDSFYKCISGILLAGNIEFseeGDMGVINAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNETIISPVTQAQ 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  420 ATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQE 499
Cdd:cd14886    320 AEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFINQVFKSEIQ 399

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  500 EYMKEQIPWTLIDFYDNQPCINLIES-KLGILDLLDEECKMPKGTDDTWAQKLyNTHLNKcALFEKPRLSNKAFIIQHFA 578
Cdd:cd14886    400 EYEIEGIDHSMITFTDNSNVLAVFDKpNLSIFSFLEEQCLIQTGSSEKFTSSC-KSKIKN-NSFIPGKGSQCNFTIVHTA 477

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  579 DKVEYQCEGFLEKNKDTVFEEQIKVLKSSKfkmlpelfqddekaisptsatssgrTPLTRTPAKPTKGRPGQMAKehkKT 658
Cdd:cd14886    478 ATVTYNTEEFVDKNKHKLSVDILELLMGST-------------------------NPIVNKAFSDIPNEDGNMKG---KF 529

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  659 VGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLM 738
Cdd:cd14886    530 LGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILI 609

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|.
gi 1836165656  739 KQKDVL----SDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 775
Cdd:cd14886    610 SHNSSSqnagEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
MYSc_Myo13 cd14875
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ...
 109-775 2.03e-122

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: 401.88  E-value: 2.03e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  109 VLHNLRVRFIDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAY-SGQNMGDMDPHIFAVAEEAYKQM-ARDERNQSIIVS 186
Cdd:cd14875      3 LLHCIKERFEKLHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYlALPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVVIS 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  187 GESGAGKTVSAKYAMRYFATVS----GSASEANVEEKVLA----SNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRI 258
Cdd:cd14875     83 GESGSGKTENAKMLIAYLGQLSymhsSNTSQRSIADKIDEnlkwSNPVMESFGNARTVRNDNSSRFGKYIKLYFDPTSGV 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  259 -IGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKML-RLGNADNFNYTKQGGSPVIEGVD-----DAKEMAH 331
Cdd:cd14875    163 mVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKCLNGGNTFVRRGVDgktldDAHEFQN 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  332 TRQACTLLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPpKHEPLCIFCELMGVDYEEM--CHWLchrKLATATE 409
Cdd:cd14875    243 VRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQNDKAQIA-DETPFLTACRLLQLDPAKLreCFLV---KSKTSLV 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  410 TYIKpiSKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHS--FIGVLDIYGFETFEINSFEQFCINYANEKLQQ 487
Cdd:cd14875    319 TILA--NKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITPQGDCSGckYIGLLDIFGFENFTRNSFEQLCINYANESLQN 396

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  488 QFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPR 566
Cdd:cd14875    397 HYNKYTFINDEEECRREGIQIPKIEFPDNSECVNMFDQKrTGIFSMLDEECNFKGGTTERFTTNLWDQWANKSPYFVLPK 476

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  567 --LSNKaFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDekaisptsatssgrtpltrtpakpt 644
Cdd:cd14875    477 stIPNQ-FGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTE------------------------- 530

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  645 kgrpgQMAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSR 724
Cdd:cd14875    531 -----KGLARRKQTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVR 605

                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  725 WTYQEFFSRYRVLM--------KQKDvLSDRKQTCKNVLEKLI-LDKDKYQFGKTKIFFR 775
Cdd:cd14875    606 RPIEQFCRYFYLIMprstaslfKQEK-YSEAAKDFLAYYQRLYgWAKPNYAVGKTKVFLR 664
MYSc_Myo37 cd14898
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ...
 108-737 6.12e-114

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: 374.62  E-value: 6.12e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  108 AVLHNLRVRFIDSKlIYTYCGIVLVAINPYEQlpIYGEDIINAYSgQNMGDMDPHIFAVAEEAYKQMARdERNQSIIVSG 187
Cdd:cd14898      2 ATLEILEKRYASGK-IYTKSGLVFLALNPYET--IYGAGAMKAYL-KNYSHVEPHVYDVAEASVQDLLV-HGNQTIVISG 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  188 ESGAGKTVSAKYAMRYFatVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRyrIIGANMRTYL 267
Cdd:cd14898     77 ESGSGKTENAKLVIKYL--VERTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFDGK--ITGAKFETYL 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  268 LEKSRVVFQAEEERNYHIFYQLCASaklpefKMLRLGNaDNFNYTKQGGSPViEGVDDAKEMAHTRQACTLLGISESHQm 347
Cdd:cd14898    153 LEKSRVTHHEKGERNFHIFYQFCAS------KRLNIKN-DFIDTSSTAGNKE-SIVQLSEKYKMTCSAMKSLGIANFKS- 223

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  348 gIFRILAGILHLGNVGFTSrdaDSCTIPPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATEtYIKPISKL-QATNARDA 426
Cdd:cd14898    224 -IEDCLLGILYLGSIQFVN---DGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGE-TIEVFNTLkQARTIRNS 298

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  427 LAKHIYAKLFNWIVDNVNQALhSAVKQHSfIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQI 506
Cdd:cd14898    299 MARLLYSNVFNYITASINNCL-EGSGERS-ISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGMYKEEGI 376

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  507 PWTLIDFYDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKL--YNTHlnkcalFEKPRLSNKaFIIQHFADKVEYQ 584
Cdd:cd14898    377 EWPDVEFFDNNQCIRDFEKPCGLMDLISEESFNAWGNVKNLLVKIkkYLNG------FINTKARDK-IKVSHYAGDVEYD 449

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  585 CEGFLEKNKDtvfEEQIKVLKSskfkmlpelfqddekaisptsatssgrtpltrtpakptkgrPGQMAKEHKKTVGHQFR 664
Cdd:cd14898    450 LRDFLDKNRE---KGQLLIFKN-----------------------------------------LLINDEGSKEDLVKYFK 485

                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1836165656  665 NSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVL 737
Cdd:cd14898    486 DSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRIL 558
MYSc_Myo17 cd14879
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ...
 108-774 1.43e-106

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: 356.09  E-value: 1.43e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  108 AVLHNLRVRFIdSKLIYTYCGI-VLVAINPYEQLPI--------YGEDIINAYSGQNMGDMdPHIFAVAEEAYKQMARDE 178
Cdd:cd14879      5 AITSHLASRFR-SDLPYTRLGSsALVAVNPYKYLSSnsdaslgeYGSEYYDTTSGSKEPLP-PHAYDLAARAYLRMRRRS 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  179 RNQSIIVSGESGAGKTVSAKYAMRYFATVSGSAS-EANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYR 257
Cdd:cd14879     83 EDQAVVFLGETGSGKSESRRLLLRQLLRLSSHSKkGTKLSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQFNERGR 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  258 IIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGG---SPVIEGVDDAKEMAHTRQ 334
Cdd:cd14879    163 LIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLASYGchpLPLGPGSDDAEGFQELKT 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  335 ACTLLGISESHQMGIFRILAGILHLGNVGFT---SRDADSCTIPPKHEpLCIFCELMGVDYEEmchwlchrkLATATeTY 411
Cdd:cd14879    243 ALKTLGFKRKHVAQICQLLAAILHLGNLEFTydhEGGEESAVVKNTDV-LDIVAAFLGVSPED---------LETSL-TY 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  412 iKpiSKL-------------QATNARDALAKHIYAKLFNWIVDNVNQALhSAVKQ--HSFIGVLDIYGFETF---EINSF 473
Cdd:cd14879    312 -K--TKLvrkelctvfldpeGAAAQRDELARTLYSLLFAWVVETINQKL-CAPEDdfATFISLLDFPGFQNRsstGGNSL 387

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  474 EQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECK-MPKGTDDTWAQKL 551
Cdd:cd14879    388 DQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSYFDNSDCVRLLRGKpGGLLGILDDQTRrMPKKTDEQMLEAL 467

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  552 YNTHLNKCALFEKPRLSNK----AFIIQHFADKVEYQCEGFLEKNKDTVfeeqikvlkSSKFKMLpelfqddekaISPTs 627
Cdd:cd14879    468 RKRFGNHSSFIAVGNFATRsgsaSFTVNHYAGEVTYSVEGFLERNGDVL---------SPDFVNL----------LRGA- 527

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  628 atssgrtpltrtpakptkgrpgqmakehkktvgHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRA 707
Cdd:cd14879    528 ---------------------------------TQLNAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRS 574

                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1836165656  708 CGVLETIRISAAGFPSRWTYQEFFSRYrvlmKQKDVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFF 774
Cdd:cd14879    575 LGLPELAARLRVEYVVSLEHAEFCERY----KSTLRGSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
MYSc_Myo16 cd14878
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ...
 108-775 5.73e-98

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: 331.39  E-value: 5.73e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  108 AVLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLPIYGEDIINAY---SGQNMGDMDPHIFAVAEEAYKQMARDERNQSII 184
Cdd:cd14878      2 SLLYEIQKRFGNNQ-IYTFIGDILLLVNPYKELPIYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  185 VSGESGAGKTVSAKYAMRYFATVSGSaSEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGF-DKRYRIIGANM 263
Cdd:cd14878     81 LSGERGSGKTEASKQIMKHLTCRASS-SRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKKHLTGARI 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  264 RTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQG---GSPVIEGVDDAKEMAHTRQACTLLG 340
Cdd:cd14878    160 YTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTmreDVSTAERSLNREKLAVLKQALNVVG 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  341 ISESHQMGIFRILAGILHLGNVGFTS-RDADSCTIppkhEPLCIFCELMG---VDYEEMCHWLCHRKLATATETYIKPIS 416
Cdd:cd14878    240 FSSLEVENLFVILSAILHLGDIRFTAlTEADSAFV----SDLQLLEQVAGmlqVSTDELASALTTDIQYFKGDMIIRRHT 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  417 KLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSF----IGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMH 492
Cdd:cd14878    316 IQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLQSQDEQKSMqtldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEV 395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  493 VFKLEQEEYMKEQIPW----------TLIDFYDNQPcinlieskLGILDLLDEECKMPKGTDDTWAQKLY----NTHLNK 558
Cdd:cd14878    396 LFLQEQTECVQEGVTMetayspgnqtGVLDFFFQKP--------SGFLSLLDEESQMIWSVEPNLPKKLQslleSSNTNA 467

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  559 CALFEK-------PRLSNKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQddekaisptsatss 631
Cdd:cd14878    468 VYSPMKdgngnvaLKDQGTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQ-------------- 533

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  632 grTPLTrtpakptkgrpgqmakehkkTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVL 711
Cdd:cd14878    534 --SKLV--------------------TIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVL 591

                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1836165656  712 ETIRISAAGFPSRWTYQEFFSRYRVLMKQkdVLSDRKQT-----CKNVLEKLILdkDKYQFGKTKIFFR 775
Cdd:cd14878    592 EMVKIFRYGYPVRLSFSDFLSRYKPLADT--LLGEKKKQsaeerCRLVLQQCKL--QGWQMGVRKVFLK 656
MYSc_Myo18 cd01386
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ...
 109-775 1.42e-96

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: 328.50  E-value: 1.42e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  109 VLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSGE 188
Cdd:cd01386      3 VLHTLRQRY-GANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLGR 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  189 SGAGKTVSAKYAMRYFATVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYLL 268
Cdd:cd01386     82 SGSGKTTNCRHILEYLVTAAGSVGGVLSVEKLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASIQTLLL 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  269 EKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGN-ADNFNYtkqGGSPVIEGVD---DAKEMAHTRQACTLLGISES 344
Cdd:cd01386    162 ERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQlAESNSF---GIVPLQKPEDkqkAAAAFSKLQAAMKTLGISEE 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  345 HQMGIFRILAGILHLGNVGftsrdadSCTIPP-------KHEPLCIFCELMGVDYEEMCHWLCHRKL------ATATETY 411
Cdd:cd01386    239 EQRAIWSILAAIYHLGAAG-------ATKAASagrkqfaRPEWAQRAAYLLGCTLEELSSAIFKHHLsggpqqSTTSSGQ 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  412 IKPIS------KLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFE------INSFEQFCIN 479
Cdd:cd01386    312 ESPARsssggpKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPAhsgsqrGATFEDLCHN 391

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  480 YANEKLQQQFNMHVFKLEQEEYMKEQIPwtlIDFYDNQPC----INLI---------------ESKLGILDLLDEECKMP 540
Cdd:cd01386    392 YAQERLQLLFHERTFVAPLERYKQENVE---VDFDLPELSpgalVALIdqapqqalvrsdlrdEDRRGLLWLLDEEALYP 468

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  541 KGTDDTWAQKLYnTHLNKCALFEKPRLSNKA-----FIIQHF--ADKVEYQCEGFLEKNKDTVFEEQikvlksskfkmLP 613
Cdd:cd01386    469 GSSDDTFLERLF-SHYGDKEGGKGHSLLRRSegplqFVLGHLlgTNPVEYDVSGWLKAAKENPSAQN-----------AT 536

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  614 ELFQDDEKaisptsatssgrtpltrtpakptkgrpgQMAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPN----- 688
Cdd:cd01386    537 QLLQESQK----------------------------ETAAVKRKSPCLQIKFQVDALIDTLRRTGLHFVHCLLPQhnagk 588

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  689 -DFKFPFTFDEKRAVQ------QLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMK-------QKDVLSDRKQTCKNV 754
Cdd:cd01386    589 dERSTSSPAAGDELLDvpllrsQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPpltkklgLNSEVADERKAVEEL 668

                          730       740
                   ....*....|....*....|.
gi 1836165656  755 LEKLILDKDKYQFGKTKIFFR 775
Cdd:cd01386    669 LEELDLEKSSYRIGLSQVFFR 689
MYSc_Myo26 cd14887
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ...
 107-775 3.06e-95

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: 325.83  E-value: 3.06e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  107 PAVLHNLRVRFI-------DSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDER 179
Cdd:cd14887      1 PNLLENLYQRYNkayinkeNRNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  180 NQSIIVSGESGAGKTVSAKYAMRYFATVS---GSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRY 256
Cdd:cd14887     81 SQSILISGESGAGKTETSKHVLTYLAAVSdrrHGADSQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGRG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  257 RIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYtkqggspviegvddakEMAHTRQAC 336
Cdd:cd14887    161 KLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSSAGEGDPEST----------------DLRRITAAM 224

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  337 TLLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEPLCIFCELMGVDYEEMCHWLCHR---KLATATETYIK 413
Cdd:cd14887    225 KTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKLTSVSVGCEETAADRSHSSEVKCLSsglKVTEASRKHLK 304

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  414 PISKL--------------------------------QATNARDALAKHIYAKLFNWIVDNVNQALHSAVK--------- 452
Cdd:cd14887    305 TVARLlglppgvegeemlrlalvsrsvretrsffdldGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKpsesdsded 384

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  453 -----QHSFIGVLDIYGFETFE---INSFEQFCINYANEKLqqqfnmHVFKLEQ-----------EEYMKEQI------- 506
Cdd:cd14887    385 tpsttGTQTIGILDLFGFEDLRnhsKNRLEQLCINYANERL------HCFLLEQlilnehmlytqEGVFQNQDcsafpfs 458

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  507 ----------PWTLIDF-----------YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCAL-FEK 564
Cdd:cd14887    459 fplastltssPSSTSPFsptpsfrsssaFATSPSLPSSLSSLSSSLSSSPPVWEGRDNSDLFYEKLNKNIINSAKYkNIT 538

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  565 PRLS--NKAFIIQHFADKVEYQCEGFLEKNKDTVFEEqikvlksskfkmLPELFqddekaisptsatSSGRTPLTRTPAK 642
Cdd:cd14887    539 PALSreNLEFTVSHFACDVTYDARDFCRANREATSDE------------LERLF-------------LACSTYTRLVGSK 593

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  643 PTKGRpgQMAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFP 722
Cdd:cd14887    594 KNSGV--RAISSRRSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFP 671

                          730       740       750       760       770
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1836165656  723 SRWTYQEFFSRY--RVLMKQKDVLSDrKQTCKNVLEKLILDKDKYQFGKTKIFFR 775
Cdd:cd14887    672 CRLPYVELWRRYetKLPMALREALTP-KMFCKIVLMFLEINSNSYTFGKTKIFFR 725
MYSc_Myo24A cd14937
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ...
 109-775 1.09e-94

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


Pssm-ID: 276897  Cd Length: 637  Bit Score: 321.19  E-value: 1.09e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  109 VLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYgediINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSGE 188
Cdd:cd14937      3 VLNMLALRY-KKNYIYTIAEPMLISINPYQVIDVD----INEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  189 SGAGKTVSAKYAMRYFatVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYLL 268
Cdd:cd14937     78 SGSGKTEASKLVIKYY--LSGVKEDNEISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSIEIFLL 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  269 EKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGgSPVIEGVDDAKEMAHTRQACTLLGISESHQmG 348
Cdd:cd14937    156 ENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNK-NVVIPEIDDAKDFGNLMISFDKMNMHDMKD-D 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  349 IFRILAGILHLGNVGFTSRDA---DSCTIPPKH--EPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNA 423
Cdd:cd14937    234 LFLTLSGLLLLGNVEYQEIEKggkTNCSELDKNnlELVNEISNLLGINYENLKDCLVFTEKTIANQKIEIPLSVEESVSI 313

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  424 RDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMK 503
Cdd:cd14937    314 CKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYEKETELYKA 393

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  504 EQIPWTLIDFYDNQPCINLIESKLGILDLLDEECKMPKGTDDTwaqkLYNTHLNKCALFEK----PRLSNKAFIIQHFAD 579
Cdd:cd14937    394 EDILIESVKYTTNESIIDLLRGKTSIISILEDSCLGPVKNDES----IVSVYTNKFSKHEKyastKKDINKNFVIKHTVS 469

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  580 KVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEkaisptSATSSGRtpltrtpakptkgrpgqmakehKKTV 659
Cdd:cd14937    470 DVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVE------VSESLGR----------------------KNLI 521

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  660 GHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAgFPSRWTYQEFFSRYRVL-- 737
Cdd:cd14937    522 TFKYLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNISFF-FQYKYTFDVFLSYFEYLdy 600

                          650       660       670
                   ....*....|....*....|....*....|....*...
gi 1836165656  738 MKQKDVLSDRKQTCKNVLEKLIlDKDKYQFGKTKIFFR 775
Cdd:cd14937    601 STSKDSSLTDKEKVSMILQNTV-DPDLYKVGKTMVFLK 637
MYSc_Myo20 cd14881
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ...
 108-774 2.91e-91

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: 311.28  E-value: 2.91e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  108 AVLHNLRVRFIDSKLiYTYCGIVLVAINPYEqlpiygeDIINAY---SGQNMGDMdPHIFAVAEEAYKQMARDERNQSII 184
Cdd:cd14881      2 AVMKCLQARFYAKEF-FTNVGPILLSVNPYR-------DVGNPLtltSTRSSPLA-PQLLKVVQEAVRQQSETGYPQAII 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  185 VSGESGAGKTVSAKYAMRYFATVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKryriiGANMR 264
Cdd:cd14881     73 LSGTSGSGKTYASMLLLRQLFDVAGGGPETDAFKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQVTD-----GALYR 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  265 T----YLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLG--NADNFNYTkQGGSPVIEGVDDAKEMAHTRQACTL 338
Cdd:cd14881    148 TkihcYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDgySPANLRYL-SHGDTRQNEAEDAARFQAWKACLGI 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  339 LGISESHQMgifRILAGILHLGNVGFTsrDADSCTIPPKHE-PLCIFCELMGVDYEEMchwlcHRKLATATET----YIK 413
Cdd:cd14881    227 LGIPFLDVV---RVLAAVLLLGNVQFI--DGGGLEVDVKGEtELKSVAALLGVSGAAL-----FRGLTTRTHNargqLVK 296

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  414 PISKLQATNA-RDALAKHIYAKLFNWIVDNVN--QALHSAVKQHS---FIGVLDIYGFETFEINSFEQFCINYANEKLQQ 487
Cdd:cd14881    297 SVCDANMSNMtRDALAKALYCRTVATIVRRANslKRLGSTLGTHAtdgFIGILDMFGFEDPKPSQLEHLCINLCAETMQH 376

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  488 QFNMHVFKLEQEEYMKEQIPWTL-IDFYDNQPCINLIES-KLGILDLLDEECKmPKGTDDTWAQKLYNTHLNKCALFEKP 565
Cdd:cd14881    377 FYNTHIFKSSIESCRDEGIQCEVeVDYVDNVPCIDLISSlRTGLLSMLDVECS-PRGTAESYVAKIKVQHRQNPRLFEAK 455

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  566 RLSNKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVL--KSSKFKMLPELfQDdekaisptsatssgrtpltrtpakp 643
Cdd:cd14881    456 PQDDRMFGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFykQNCNFGFATHT-QD------------------------- 509

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  644 tkgrpgqmakehkktvghqFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPS 723
Cdd:cd14881    510 -------------------FHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPH 570

                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1836165656  724 RWTYQEFFSRYRVL--MKQKDVLSDRKQTCKNVLEKLILDKDK---------YQFGKTKIFF 774
Cdd:cd14881    571 RMRFKAFNARYRLLapFRLLRRVEEKALEDCALILQFLEAQPPsklssvstsWALGKRHIFL 632
MYSc_Myo23 cd14884
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ...
 107-774 6.52e-90

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: 308.76  E-value: 6.52e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  107 PAVLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLP-IYGEDIINAYS-------GQNMGDMDPHIFAVAEEAYKQMARDE 178
Cdd:cd14884      1 PNVLQNLKNRYLKNK-IYTFHASLLLALNPYKPLKeLYDQDVMNVYLhkksnsaASAAPFPKAHIYDIANMAYKNMRGKL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  179 RNQSIIVSGESGAGKTVSAKYAMRYFATVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKR--- 255
Cdd:cd14884     80 KRQTIVVSGHSGSGKTENCKFLFKYFHYIQTDSQMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFEEVent 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  256 ------YRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQL---CASAKLPEFKMLR------LGNADNFNYTKQGGSPVI 320
Cdd:cd14884    160 qknmfnGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVlrgLSDEDLARRNLVRncgvygLLNPDESHQKRSVKGTLR 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  321 EGVD-----------DAKEMAHTRQACTLLGISESHQMGIFRILAGILHLGNvgftsrDADSCTippkheplcifCELMG 389
Cdd:cd14884    240 LGSDsldpseeekakDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGN------RAYKAA-----------AECLQ 302

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  390 VDYEEMCHWLCHRKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDNVNQAL------------HSAVKQHSFI 457
Cdd:cd14884    303 IEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVlkckekdesdneDIYSINEAII 382

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  458 GVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESklgILDLLDEEC 537
Cdd:cd14884    383 SILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAPSYSDTLIFIAK---IFRRLDDIT 459

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  538 KMP----KGTDDTWAQKLYNTHlNKCALFEK-------PRL---SNKA-------FIIQHFADKVEYQCEGFLEKNKDTV 596
Cdd:cd14884    460 KLKnqgqKKTDDHFFRYLLNNE-RQQQLEGKvsygfvlNHDadgTAKKqnikkniFFIRHYAGLVTYRINNWIDKNSDKI 538

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  597 feeqikvlksskfkmlpelfqddEKAISPTSATSSGRTpLTRTPAKPTKGrpgqmakeHKKTVGHQFRNSLHLLMETLNA 676
Cdd:cd14884    539 -----------------------ETSIETLISCSSNRF-LREANNGGNKG--------NFLSVSKKYIKELDNLFTQLQS 586

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  677 TTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMkQKDVLSDRKQTCKNVLE 756
Cdd:cd14884    587 TDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKETAAALKEQI-AKELEKCNSNTDIEYQR 665

                          730
                   ....*....|....*...
gi 1836165656  757 KLILDKDKYQFGKTKIFF 774
Cdd:cd14884    666 RLAALDVQFIPDGRLYAF 683
Myo5-like_CBD cd14945
Cargo binding domain of myosin 5 and similar proteins; Class V myosins are well studied ...
 1506-1829 6.57e-86

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: 282.75  E-value: 6.57e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1506 EDEQKLVKNLILELKPRGVAVNLipgLPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSNT 1585
Cdd:cd14945      1 SEEDSLLRGIVTDFEPSSGDHKL---TPAYILYLCIRHAASNGLTGQSTSLLNKVLKTIQQVVQQHNDDMQLLAFWLSNA 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1586 CRFLHCLKQYSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPmivsgmlehetiqgvsgv 1665
Cdd:cd14945     78 SELLYFLKQDSKLYGAAGEAPQKEEEQKLTVSDLNELKQDLEAVSIKIYQQALKYLNKNLQP------------------ 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1666 kptglrkrtssiadegtyTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQIRY 1745
Cdd:cd14945    140 ------------------KIRDIVKFLNSFLDLLKSFHVHPEIRSQVFTQLFSFINARLFNQLITKKDALSWSRGMQIRA 201

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1746 NVSQLEEWLRDKNLmNSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERVSVSFI 1825
Cdd:cd14945    202 NISRLEEWCEGRGL-EHLAVDFLSKLIQAVQLLQLKKYTQEDIEILCELCPSLNPAQLQAILTQYQPANYGESPVPKEIL 280


                   ....
gi 1836165656 1826 RTIQ 1829
Cdd:cd14945    281 RTLA 284
MYSc_Myo44 cd14905
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ...
 121-775 9.53e-86

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: 296.23  E-value: 9.53e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  121 KLIYTYCGIVLVAINPYEQLP-IYGEDIINAYSgQNMGdMDPHIFAVAEEAYKQMARDERNQSIIVSGESGAGKTVSAKY 199
Cdd:cd14905     14 EIIYTYIGPILVSVNPLRYLPfLHSQELVRNYN-QRRG-LPPHLFALAAKAISDMQDFRRDQLIFIGGESGSGKSENTKI 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  200 AMRYFATVSGSASEAnVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYLLEKSRVVFQAEE 279
Cdd:cd14905     92 IIQYLLTTDLSRSKY-LRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKLYSYFLDENRVTYQNKG 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  280 ERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQACTLLGISESHQMGIFRILAGILHL 359
Cdd:cd14905    171 ERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQGGSISVESIDDNRVFDRLKMSFVFFDFPSEKIDLIFKTLSFIIIL 250

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  360 GNVGFTSRDADSctippkheplcifcelmGVDYEEMCHWLCHRKLATATETYIKPISKL-----QATNARDALAKHIYAK 434
Cdd:cd14905    251 GNVTFFQKNGKT-----------------EVKDRTLIESLSHNITFDSTKLENILISDRsmpvnEAVENRDSLARSLYSA 313

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  435 LFNWIVDNVNQALHSAVKQHSfIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPW-TLIDF 513
Cdd:cd14905    314 LFHWIIDFLNSKLKPTQYSHT-LGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQREYQTERIPWmTPISF 392

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  514 YDNQPCINLIESklgILDLLDEECKMPKGTDDTWAQKLYNtHLNKCALF-EKPrlsNKaFIIQHFADKVEYQCEGFLEKN 592
Cdd:cd14905    393 KDNEESVEMMEK---IINLLDQESKNINSSDQIFLEKLQN-FLSRHHLFgKKP---NK-FGIEHYFGQFYYDVRGFIIKN 464

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  593 KDTVFEEQIKVLKSSKFKMLpeLFQDDEKAISPTSA---------TSSGRTPLT----------------RTPAKPTKGR 647
Cdd:cd14905    465 RDEILQRTNVLHKNSITKYL--FSRDGVFNINATVAelnqmfdakNTAKKSPLSivkvllscgsnnpnnvNNPNNNSGGG 542

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  648 PGQMAKEHKKTVGHQFRNSLHLLMETLNATTP--HYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRW 725
Cdd:cd14905    543 GGGGNSGGGSGSGGSTYTTYSSTNKAINNSNCdfHFIRCIKPNSKKTHLTFDVKSVNEQIKSLCLLETTRIQRFGYTIHY 622

                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1836165656  726 TYQEFFSRYRVLMKQkdvlsdrKQTCKNVLEKLI---LDKDK-----YQFGKTKIFFR 775
Cdd:cd14905    623 NNKIFFDRFSFFFQN-------QRNFQNLFEKLKendINIDSilpppIQVGNTKIFLR 673
MYSc_Myo12 cd14874
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ...
 108-775 8.49e-80

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: 277.52  E-value: 8.49e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  108 AVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYsgqnmgdmdpHIFAVAEEAYKQMARDERN-QSIIVS 186
Cdd:cd14874      2 GIAQNLHERF-KKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  187 GESGAGKTVSAKYAMRYFATVSGSASEAnveEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFdKRYRIIGANMR-T 265
Cdd:cd14874     71 GESGSGKSYNAFQVFKYLTSQPKSKVTT---KHSSAIESVFKSFGCAKTLKNDEATRFGCSIDLLY-KRNVLTGLNLKyT 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  266 YLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSpvIEGV-DDAKEMAHTRQACTLLGISES 344
Cdd:cd14874    147 VPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNS--TENIqSDVNHFKHLEDALHVLGFSDD 224

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  345 HQMGIFRILAGILHLGNVGFTSR-----DADSCTIPPKHEPLCIfCELMGVDYEEMCHWLchrklaTATETYIKPISKLQ 419
Cdd:cd14874    225 HCISIYKIISTILHIGNIYFRTKrnpnvEQDVVEIGNMSEVKWV-AFLLEVDFDQLVNFL------LPKSEDGTTIDLNA 297

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  420 ATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSfIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQE 499
Cdd:cd14874    298 ALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGV-ISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHSFHDQLV 376

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  500 EYMKEQIPwtlIDF-----YDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCAlFEKPRLSNK-AF 572
Cdd:cd14874    377 DYAKDGIS---VDYkvpnsIENGKTVELLFKKpYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSS-YGKARNKERlEF 452

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  573 IIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQddekaiSPTSATSsgrtpltrtpakptkgrpgqma 652
Cdd:cd14874    453 GVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFE------SYSSNTS---------------------- 504

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  653 kEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFS 732
Cdd:cd14874    505 -DMIVSQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFAR 583

                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1836165656  733 RYRVLM--------KQKDVLSDRKQTCKNVLEklildkDKYQFGKTKIFFR 775
Cdd:cd14874    584 QYRCLLpgdiamcqNEKEIIQDILQGQGVKYE------NDFKIGTEYVFLR 628
MYSc_Myo32 cd14893
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ...
 110-774 1.32e-75

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: 268.38  E-value: 1.32e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  110 LHNLRVRF-IDSklIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQN----------MGDMDPHIFAVAEEAYKQMARDE 178
Cdd:cd14893      4 LYTLRARYrMEQ--VYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSReqtplyekdtVNDAPPHVFALAQNALRCMQDAG 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  179 RNQSIIVSGESGAGKTVSAKYAMRYFATVSGSASEAN-----------VEEKVLASNPIMESIGNAKTTRNDNSSRFGKY 247
Cdd:cd14893     82 EDQAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPdsegasgvlhpIGQQILHAFTILEAFGNAATRQNRNSSRFAKM 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  248 IEIGFDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKL-PEFK-MLRLGN-ADNFNYTKQGGSPVIEGVD 324
Cdd:cd14893    162 ISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHdPTLRdSLEMNKcVNEFVMLKQADPLATNFAL 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  325 DAKEMAHTRQACTLLGISESHQMGIFRILAGILHLGNVGF----------------TSRDADSCTIPPKHEPLcIFCELM 388
Cdd:cd14893    242 DARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpeggksvgganstTVSDAQSCALKDPAQIL-LAAKLL 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  389 GVDYEEMCHWLCHRKL----ATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDNVNQAL---------HSAVKQHS 455
Cdd:cd14893    321 EVEPVVLDNYFRTRQFfskdGNKTVSSLKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifdryekSNIVINSQ 400

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  456 FIGVLDIYGFETFE--INSFEQFCINYANEKLQQQF-------NMHVFKLEQEEYMKEQIPWTLIDF-YDNQPCINLIES 525
Cdd:cd14893    401 GVHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYvqntlaiNFSFLEDESQQVENRLTVNSNVDItSEQEKCLQLFED 480

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  526 K-LGILDLLDEECKMPKGTDDTWAQKLYN--------THLNKCALFEKPRLSNKA-----FIIQHFADKVEYQCEGFLEK 591
Cdd:cd14893    481 KpFGIFDLLTENCKVRLPNDEDFVNKLFSgneavgglSRPNMGADTTNEYLAPSKdwrllFIVQHHCGKVTYNGKGLSSK 560

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  592 NKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISP-TSATSSGRTPLTRTPAKPTKGRPGQmAKEHKKTVGHQFRNSLHLL 670
Cdd:cd14893    561 NMLSISSTCAAIMQSSKNAVLHAVGAAQMAAASSeKAAKQTEERGSTSSKFRKSASSARE-SKNITDSAATDVYNQADAL 639

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  671 METLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYrvlmkqKDVLSDRKqT 750
Cdd:cd14893    640 LHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRY------KNVCGHRG-T 712

                          730       740
                   ....*....|....*....|....*...
gi 1836165656  751 CKNVLEKL----ILDKDKYQFGKTKIFF 774
Cdd:cd14893    713 LESLLRSLsaigVLEEEKFVVGKTKVYL 740
MYSc_Myo21 cd14882
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ...
 109-775 1.86e-65

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


Pssm-ID: 276848  Cd Length: 642  Bit Score: 235.79  E-value: 1.86e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  109 VLHNLRVRfIDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSGE 188
Cdd:cd14882      3 ILEELRHR-YLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  189 SGAGKTVSAKYAMRYFATVsGSASEaNVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYLL 268
Cdd:cd14882     82 SYSGKTTNARLLIKHLCYL-GDGNR-GATGRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFWMYQL 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  269 EKSRVVFQAEEERNYHIFY----QLCASAKLPEF--------KMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAhtrQAC 336
Cdd:cd14882    160 EKLRVSTTDGNQSNFHIFYyfydFIEAQNRLKEYnlkagrnyRYLRIPPEVPPSKLKYRRDDPEGNVERYKEFE---EIL 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  337 TLLGISESHQMGIFRILAGILHLGNVGFtsRDADSCTIPPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKPIS 416
Cdd:cd14882    237 KDLDFNEEQLETVRKVLAAILNLGEIRF--RQNGGYAELENTEIASRVAELLRLDEKKFMWALTNYCLIKGGSAERRKHT 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  417 KLQATNARDALAKHIYAKLFNWIVDNVNQALH--SAV--KQHSfIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMH 492
Cdd:cd14882    315 TEEARDARDVLASTLYSRLVDWIINRINMKMSfpRAVfgDKYS-ISIHDMFGFECFHRNRLEQLMVNTLNEQMQYHYNQR 393

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  493 VFKLEQEEYMKEQIPWTLIDFYDNQPCI-NLIESKLGILDLLDEECKMPKGtddtwAQKLYNTHLNKCALFEKPrLSNKA 571
Cdd:cd14882    394 IFISEMLEMEEEDIPTINLRFYDNKTAVdQLMTKPDGLFYIIDDASRSCQD-----QNYIMDRIKEKHSQFVKK-HSAHE 467

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  572 FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDdekaisptsatssgrtpltrtpakptkgrpgqm 651
Cdd:cd14882    468 FSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN--------------------------------- 514

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  652 AKEHK-KTVGHQFRNSLHLLMETL----NATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWT 726
Cdd:cd14882    515 SQVRNmRTLAATFRATSLELLKMLsigaNSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIP 594

                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|
gi 1836165656  727 YQEFFSRYRVLMKQKDVLSD-RKQTCKNVLEKLILdkDKYQFGKTKIFFR 775
Cdd:cd14882    595 FQEFLRRYQFLAFDFDETVEmTKDNCRLLLIRLKM--EGWAIGKTKVFLK 642
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
 130-253 5.99e-49

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: 172.14  E-value: 5.99e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  130 VLVAINPYEQLPIYGED-IINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSGESGAGKTVSAKYAMRYFATVS 208
Cdd:cd01363      1 VLVRVNPFKELPIYRDSkIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1836165656  209 GSASEAN--------------VEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFD 253
Cdd:cd01363     81 FNGINKGetegwvylteitvtLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLD 139
DIL pfam01843
DIL domain; The DIL domain has no known function.
 1711-1814 4.26e-42

DIL domain; The DIL domain has no known function.


Pssm-ID: 460359 [Multi-domain]  Cd Length: 103  Bit Score: 149.66  E-value: 4.26e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1711 QVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQIRYNVSQLEEWLRDKNLmNSGAKETLEPLIQAAQLLQVKKKTDDDAEA 1790
Cdd:pfam01843    1 QLFSQLFYFINAELFNRLLLRKKYCSWSKGMQIRYNLSRLEEWARSNGL-ESEARDHLAPLIQAAQLLQLRKSTLEDLDS 79

                           90       100
                   ....*....|....*....|....
gi 1836165656 1791 ICSMCNALTTAQIVKVLNLYTPVN 1814
Cdd:pfam01843   80 ILQVCPALNPLQLHRLLTLYQPDD 103
MYSc_Myo24B cd14938
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ...
 107-773 1.28e-40

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: 162.31  E-value: 1.28e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  107 PAVLHNLRVRFIDSKLiYTYCGIVLVAINPYEQLPIYGEDIINAYSGQN-MGDMDPHIFAVAEEAYKQMARDERNQSIIV 185
Cdd:cd14938      1 PSVLYHLKERFKNNKF-YTKMGPLLIFINPKINNNINNEETIEKYKCIDcIEDLSLNEYHVVHNALKNLNELKRNQSIII 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  186 SGESGAGKTVSAKYAMRYFA-TVSGSASEA---------------------NVEEKVLASNPIMESIGNAKTTRNDNSSR 243
Cdd:cd14938     80 SGESGSGKSEIAKNIINFIAyQVKGSRRLPtnlndqeednihneentdyqfNMSEMLKHVNVVMEAFGNAKTVKNNNSSR 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  244 FGKYIEIGFDKRyRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGV 323
Cdd:cd14938    160 FSKFCTIHIENE-EIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSD 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  324 DDAKEMAHTRQACTLLGISESHQMgIFRILAGILHLGNVGF--------TSRDADSCTIPPKHEpLCI----FCELMGVD 391
Cdd:cd14938    239 YSGKILELLKSLNYIFDDDKEIDF-IFSVLSALLLLGNTEIvkafrkksLLMGKNQCGQNINYE-TILseleNSEDIGLD 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  392 YEEMCHWLCHRKLATATETYIKPIS---------------KLQATNARDALAKHIYAKLFNWIVDNVNQ---ALHSAVKQ 453
Cdd:cd14938    317 ENVKNLLLACKLLSFDIETFVKYFTtnyifndsilikvhnETKIQKKLENFIKTCYEELFNWIIYKINEkctQLQNININ 396

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  454 HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTL-IDFYDNQPCIN-LIESKLGILD 531
Cdd:cd14938    397 TNYINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYnSENIDNEPLYNlLVGPTEGSLF 476

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  532 LLDEECKMPKGTDDTwaqKLYNTHLNKCA-----LFEKPRLSN-KAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLK 605
Cdd:cd14938    477 SLLENVSTKTIFDKS---NLHSSIIRKFSrnskyIKKDDITGNkKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVK 553

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  606 SSKFKMLPELFQ----DDEKAISPTSATSSGRTPLtrtpaKPTKGR---PGQMAKEhkktvghQFRNSLHLLMETLNATT 678
Cdd:cd14938    554 QSENEYMRQFCMfynyDNSGNIVEEKRRYSIQSAL-----KLFKRRydtKNQMAVS-------LLRNNLTELEKLQETTF 621

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  679 PHYVRCIKPNDFK-FPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMkqkdvlSDRKQTCKNVLEK 757
Cdd:cd14938    622 CHFIVCMKPNESKrELCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKN------EDLKEKVEALIKS 695

                          730
                   ....*....|....*.
gi 1836165656  758 LILDKDKYQFGKTKIF 773
Cdd:cd14938    696 YQISNYEWMIGNNMIF 711
Myo5p-like_CBD_DIL_ANK cd15473
cargo binding domain of myosin 5-like of dil and ankyrin domain containing protein; DIL and ...
 1532-1861 5.13e-32

cargo binding domain of myosin 5-like of dil and ankyrin domain containing protein; DIL and ankyrin domain-containing protein are a group of fungal proteins that contain a domain homologous to the cargo binding domain of class V myosins and ankyrin repeats. Their function is unknown.


Pssm-ID: 271257 [Multi-domain]  Cd Length: 316  Bit Score: 128.44  E-value: 5.13e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1532 LPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSNTCRFLHCLKQysgEEGFmkhntsrqne 1611
Cdd:cd15473     32 VPANLLFLCARYAHYHCSPELLEDLLLGALDRIEDVVEANPWDMTLLAFWLSNVTLLLHYLKK---DAGL---------- 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1612 hcltNFDLAEYRQVLSDLAIQIYQQLVRVLEnilqpmivsgmlehetiqgvsgvkptglrKRTSSIADEGTYTLDSIlrq 1691
Cdd:cd15473     99 ----VEATPEFQQELAELINEIFVLIIRDAE-----------------------------RRIDKLLDASPRNITSL--- 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1692 LNSFHSVMCQHGMDPELIKQVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQIRYNVSQLEEWLRDKNLM-------NSGA 1764
Cdd:cd15473    143 LSSTLYVLELYDVHPAIIIQALSQLFYWLGCELFNRILTNKKYLCRSKAMQIRMNLSALEDWARSNNLQpekgespPRIA 222

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1765 KETLEPLIQAAQLLQVKKKTDDDAEAICSM--CNALTTAQIVKVLNLYTP-VNefEERVSVSFIRTIQMRLRDRKDSpql 1841
Cdd:cd15473    223 RSHLAPVIQLLQWLQCLSSLDDFESLIATIqqLDALNPLQLLRAVKDYRYeVN--EGRMPEECVKYLAQLQKDWLDS--- 297

                          330       340
                   ....*....|....*....|
gi 1836165656 1842 lmdaKHIFPVTFPFNPSSLA 1861
Cdd:cd15473    298 ----RYMLPFSLPTDTEMLV 313
Myo5p-like_CBD_fungal cd15474
cargo binding domain of fungal myosin V -like proteins; Yeast myosin V travels along actin ...
 1511-1855 1.30e-29

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: 122.53  E-value: 1.30e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1511 LVKNLILELKPRGVAVN----LIPGLPAYILFMCVRHADYLNDDQKVRSL--LTSTINSIKKVLKKRgDDFETVSFWLSN 1584
Cdd:cd15474     11 LKSVEVLELKDISDEVSgdnlLFLGHVNFLIYSQMWKSLLELLTQSERFLshVLSYIASIVDSLPKK-ETIPDGAFWLAN 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1585 TCRFLHCL--KQYSGEEGFMKHNTSRQNEHCLTNFDlaEYRQVLSdlaiQIYQQLVRVLENILQPMIVSGMLEHETIQGV 1662
Cdd:cd15474     90 LHELRSFVvyLLSLIEHSSSDEFSKESEEYWNTLFD--KTLKHLS----NIYSTWIDKLNKHLSPKIEGAVLVLLTSLDL 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1663 SGvkptgLRKRTSSIADEGTYTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQ 1742
Cdd:cd15474    164 SE-----LIDLNKEFFNKPKKKMADLITFLNEVYDLLQSFSVQPELLNAIVSSTLQYINVEAFNSLITKRSALSWKRGSQ 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1743 IRYNVSQLEEWLRDKNLmnSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNeFEERVSV 1822
Cdd:cd15474    239 ISYNVSRLKEWCHQHGL--SDANLQLEPLIQASKLLQLRKDDENDFKIILSVCYALNPAQIQKLLDKYQPAN-YEAPVPK 315

                          330       340       350
                   ....*....|....*....|....*....|....
gi 1836165656 1823 SFIRTI-QMRLRDRKDSPQLLMDAKHIFPVTFPF 1855
Cdd:cd15474    316 EFLNALeKLIKKENLSLPGRKNNSKMEIPESSNF 349
MYSc_Myo33 cd14894
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ...
 220-758 1.52e-29

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: 128.32  E-value: 1.52e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  220 VLASNPIMESIGNAKTTRNDNSSRFGKY--IEIGFDK---RYRIIGANMRTYLLEKSRVVFQA------EEERNYHIFYQ 288
Cdd:cd14894    249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLhpwEFQICGCHISPFLLEKSRVTSERgresgdQNELNFHILYA 328

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  289 LCASAKLPEF-----KMLRLGNADNFNYTKQGGSP-----VIEGVD----DAKEMAHTRQACTLLGISESHQMGIFRILA 354
Cdd:cd14894    329 MVAGVNAFPFmrllaKELHLDGIDCSALTYLGRSDhklagFVSKEDtwkkDVERWQQVIDGLDELNVSPDEQKTIFKVLS 408

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  355 GILHLGNVGFTSRDADSCTIPPKH------EPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNARDALA 428
Cdd:cd14894    409 AVLWLGNIELDYREVSGKLVMSSTgalnapQKVVELLELGSVEKLERMLMTKSVSLQSTSETFEVTLEKGQVNHVRDTLA 488

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  429 KHIYAKLFNWIVDNVNQALH-----------------SAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQqfnm 491
Cdd:cd14894    489 RLLYQLAFNYVVFVMNEATKmsalstdgnkhqmdsnaSAPEAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKLYA---- 564

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  492 hvfKLEQEEYMKEQIPWTLIDFYDNQPCINLIESKLGILDLLdEECKMPKGTDDTWAQ------KLYNTHL---NKCALF 562
Cdd:cd14894    565 ---REEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASL-EELTILHQSENMNAQqeekrnKLFVRNIydrNSSRLP 640

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  563 EKPRLSNKA------------FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLK---SSKF-KMLPELFQDDEKAISPT 626
Cdd:cd14894    641 EPPRVLSNAkrhtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKtsnSSHFcRMLNESSQLGWSPNTNR 720

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  627 SATSSGRTPLTRTpakptkgrpgqmakehKKTVGhQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLR 706
Cdd:cd14894    721 SMLGSAESRLSGT----------------KSFVG-QFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCR 783

                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1836165656  707 ACGV---LETIRISAAGFPS-RWTYQEFFSRYRVLMKQKDVLSDRKQTCKNVLEKL 758
Cdd:cd14894    784 SQRLirqMEICRNSSSSYSAiDISKSTLLTRYGSLLREPYILDDVAGDNSNLMNWL 839
fMyo2p_CBD cd15480
cargo binding domain of fungal myosin 2; Yeast myosin V travels along actin cables, actin ...
 1684-1879 4.34e-29

cargo binding domain of fungal myosin 2; 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. 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: 271264  Cd Length: 363  Bit Score: 121.15  E-value: 4.34e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1684 TLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQIRYNVSQLEEWLRDKNlMNSG 1763
Cdd:cd15480    167 TMDDILNFFNKVYKSMKSYYIEESVIRQVVTELLKLIGVTAFNDLLMRRNFLSWKRGLQINYNITRLEEWCKSHD-IPEG 245

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1764 AkETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTpVNEFEERVSVSFIRTIQMRLR--DRKDSPQL 1841
Cdd:cd15480    246 T-LQLEHLMQATKLLQLKKATLEDIEIIYDVCWILTPAQIQKLISQYY-VADYENPISPEILKAVAARVKpeDKSDHLLL 323

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1836165656 1842 LMDAKHIFPVTFPFNPSSLALETIqIPASLGLGFISRV 1879
Cdd:cd15480    324 IPLVEEVGPFEDPFPREIAGLEAY-IPAWLNLPHIRRL 360
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 926-1468 5.01e-18

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: 91.27  E-value: 5.01e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  926 KRELKKLKIEARSVERYKKLHigmeNKIMQLQRKVdeQNKDYKCLVEKLTNLEGIYNSETEKLRSDLERLQLSEEEAKVA 1005
Cdd:TIGR02168  199 ERQLKSLERQAEKAERYKELK----AELRELELAL--LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEEL 272

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1006 TGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQekealnhriVQQAKEMTETMEKKLV 1085
Cdd:TIGR02168  273 RLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE---------LESKLDELAEELAELE 343

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1086 EETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTlmvhvpkpghKRTDSTHSSNESEYIFSSEI----AEMEDIP 1161
Cdd:TIGR02168  344 EKLEELKEELESLEAELEELEAELEELESRLEELEEQLE----------TLRSKVAQLELQIASLNNEIerleARLERLE 413

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1162 SRTEEPSEKKVPLDMSL----FLKLQKRVTELEQEKQVMQDELDRKEEQvlrskaKEEERPQIRGAELEYESLKRQELES 1237
Cdd:TIGR02168  414 DRRERLQQEIEELLKKLeeaeLKELQAELEELEEELEELQEELERLEEA------LEELREELEEAEQALDAAERELAQL 487

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1238 ENKK--LKNELNELRKALSEKSAPEVTAPGAPAYRVLMEQLTSVSEELDVRKEEVLILRSQLV------SQKEAIQ---- 1305
Cdd:TIGR02168  488 QARLdsLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVvvenlnAAKKAIAflkq 567

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1306 -------------PKDDKNTMTDSTIL---------LEDVQKMKDKGEIAQAYI--------GLKE-TNRSSALDYHELN 1354
Cdd:TIGR02168  568 nelgrvtflpldsIKGTEIQGNDREILkniegflgvAKDLVKFDPKLRKALSYLlggvlvvdDLDNaLELAKKLRPGYRI 647

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1355 --EDGELW-----LVYEGLKQANRLLE-----SQLQSQKRSHENEAEALRGEIQSLKEENNRQQQLLAQNLQLPPEARIE 1422
Cdd:TIGR02168  648 vtLDGDLVrpggvITGGSAKTNSSILErrreiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQ 727

                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*..
gi 1836165656 1423 -ASLQHEITRLTNENLDLMEQLEKQDKTVRKLKKQLKVFAKKIGELE 1468
Cdd:TIGR02168  728 iSALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAE 774
Myo5p-like_CBD_afadin cd15471
cargo binding domain of myosin 5-like of afadin; Afadin is an actin filament (F-actin) and ...
 1533-1812 8.04e-16

cargo binding domain of myosin 5-like of afadin; Afadin is an actin filament (F-actin) and Rap1 small G protein-binding protein, found in cadherin-based adherens junctions in epithelial cells, endothelial cells, and fibroblasts. It interacts with cell adhesion molecules and signaling molecules and plays a role in the formation of cell junctions, cell polarization, migration, survival, proliferation, and differentiation. Afadin is a multi domain protein, that contains beside a myosin5-like CBD, two Ras-associated domains, a forkhead-associated domain, a PDZ domain, three proline-rich domains, and an F-actin-binding domain.


Pssm-ID: 271255  Cd Length: 322  Bit Score: 80.82  E-value: 8.04e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1533 PAYILFMCVRH---ADYLNDD------QKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSNTCRFLHCLKQysgeegfmk 1603
Cdd:cd15471     25 PAYTLYLAARYrlsTHYRPELtpteraHKLTAFLNKIASLIQQVIQEQRNIAGALAFWMANASELLNFLKQ--------- 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1604 hntsrqnEHCLTNFDLaEYRQVLSDLAIQIYQQLVRVLENILQPMIVSGMLEHETIQGVSGVKPTglrkrtssiadegTY 1683
Cdd:cd15471     96 -------DRDLSAFSV-QAQDVLAEAVQSAFSYLVRCLQEELERSLPAFLDSLVSLDDEPAIGDV-------------LH 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1684 TLDSILRQLNsfhsvmcQHGMDPELIKQVVKQMFYIIGAITLNNLLLRKD--MCSWSKGMQIRYNVSQLEEWLrDKNLMN 1761
Cdd:cd15471    155 TLSSAMRLLR-------RCRVNAALTIQLFSQLFHFINAWLFNSLVSNPDsgLCTRYWGKRLRQRLAHVEAWA-ERQGLE 226

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1836165656 1762 SGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTP 1812
Cdd:cd15471    227 LAADCHLDRIVQAANLLTAPKYSAEDVANLSSTCFKLNSLQLRALLSHYQP 277
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 951-1458 1.41e-13

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: 76.30  E-value: 1.41e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  951 NKIMQLQRKVDEQNKDYKCLVEKLTNLegiyNSETEKLRSDLER----LQLSEEEAKVATGRVLSLQEEIAKLRKDLEQT 1026
Cdd:pfam05483  268 DKANQLEEKTKLQDENLKELIEKKDHL----TKELEDIKMSLQRsmstQKALEEDLQIATKTICQLTEEKEAQMEELNKA 343

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1027 RSEKKCIeehADRYKQETEQLVSNLKEENTLLKQEKEALNHRIVQQAKEMTETMEKKLVEETKQLELD------LNDERL 1100
Cdd:pfam05483  344 KAAHSFV---VTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEelkkilAEDEKL 420

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1101 RYQNllNEFSRLEERYDDLKEEMTLMVHV-PKPGHKRTDSTHSSNESEYIFSSEIAEMedipsRTEEPSEKKVPLDMSLF 1179
Cdd:pfam05483  421 LDEK--KQFEKIAEELKGKEQELIFLLQArEKEIHDLEIQLTAIKTSEEHYLKEVEDL-----KTELEKEKLKNIELTAH 493

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1180 L-KLQKRVTELEQEKQVMQDELDRKEEQVLRSKaKEEER--PQIRGAElEYESLKRQELESENKKLKNELNELRKAL--S 1254
Cdd:pfam05483  494 CdKLLLENKELTQEASDMTLELKKHQEDIINCK-KQEERmlKQIENLE-EKEMNLRDELESVREEFIQKGDEVKCKLdkS 571

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1255 EKSAPEV---TAPGAPAYRVLMEQLTSVSEELDVRKEEVlilrSQLVSQKEAIQPKDDKNTMTDSTILLEdVQKMKDKGE 1331
Cdd:pfam05483  572 EENARSIeyeVLKKEKQMKILENKCNNLKKQIENKNKNI----EELHQENKALKKKGSAENKQLNAYEIK-VNKLELELA 646

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1332 IAQAYIGLKETNRSSALDYHELNEDGELWLVYEGLKQANRLLESQLQSQKRSHENEAEAL----RGEIQSLKEENNRQQQ 1407
Cdd:pfam05483  647 SAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMValmeKHKHQYDKIIEERDSE 726

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1836165656 1408 LLAQNLQLPPEARIEASLQHEITRLTNENLDLMEQLEKQDKTVRKLKKQLK 1458
Cdd:pfam05483  727 LGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAK 777
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 981-1255 4.50e-13

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: 75.09  E-value: 4.50e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  981 YNSETEKLRSDLERLQLSEEEakvatgrvlsLQEEIAKLRKDLEQTRSEkkciEEHADRYKQETEQLVSNLKEENTLLKQ 1060
Cdd:TIGR02168  675 RRREIEELEEKIEELEEKIAE----------LEKALAELRKELEELEEE----LEQLRKELEELSRQISALRKDLARLEA 740

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1061 EKEALNHRIVQQAKEMTETMEK---------KLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMvhvpk 1131
Cdd:TIGR02168  741 EVEQLEERIAQLSKELTELEAEieeleerleEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL----- 815

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1132 pGHKRTDSTHSSNESEYIFSSEIAEMEDIPSRTEEPSEKkvpldmslFLKLQKRVTELEQEKQVMQDELDRKEEQvlrsK 1211
Cdd:TIGR02168  816 -NEEAANLRERLESLERRIAATERRLEDLEEQIEELSED--------IESLAAEIEELEELIEELESELEALLNE----R 882

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1836165656 1212 AKEEERPQIRGAELEYESLKRQELESENKKLKNELNELRKALSE 1255
Cdd:TIGR02168  883 ASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ 926
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 926-1305 1.13e-12

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: 73.56  E-value: 1.13e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  926 KRELKKLKIEARSVERYKKLHI---------------GMENKIMQLQRKVDEQNKDykclVEKLTNLEGIYNSETEKLRS 990
Cdd:TIGR02169  197 RQQLERLRREREKAERYQALLKekreyegyellkekeALERQKEAIERQLASLEEE----LEKLTEEISELEKRLEEIEQ 272

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  991 DLErlQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEkkcIEEHADRYKQETEQLVsNLKEENTLLKQEKEALNHRIV 1070
Cdd:TIGR02169  273 LLE--ELNKKIKDLGEEEQLRVKEKIGELEAEIASLERS---IAEKERELEDAEERLA-KLEAEIDKLLAEIEELEREIE 346

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1071 QQAKEMTETME--KKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMtlmvhvpkpghkrtdsthssNESEY 1148
Cdd:TIGR02169  347 EERKRRDKLTEeyAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREI--------------------NELKR 406

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1149 IFSSEIAEMEDIPSRTEEpsekkvpLDMSLFLKLQKrVTELEQEKQVMQDELDRKEEQVLRSKA-KEEERPQIRGAELEY 1227
Cdd:TIGR02169  407 ELDRLQEELQRLSEELAD-------LNAAIAGIEAK-INELEEEKEDKALEIKKQEWKLEQLAAdLSKYEQELYDLKEEY 478

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1836165656 1228 eslkrQELESENKKLKNELNELRKalsEKSAPEVTAPGAPAyrvlmeqltsVSEELDVRKEEVLILRSQLVSQKEAIQ 1305
Cdd:TIGR02169  479 -----DRVEKELSKLQRELAEAEA---QARASEERVRGGRA----------VEEVLKASIQGVHGTVAQLGSVGERYA 538
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 926-1310 1.28e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 73.43  E-value: 1.28e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  926 KRELKKLKIEARSVERYKKLHIGMEnkimqlQRKVDEQNKDYKCLVEKLTNLEGIYNSETEKLRSDLERLQLSEEEAKVA 1005
Cdd:COG1196    199 ERQLEPLERQAEKAERYRELKEELK------ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEEL 272

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1006 TGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEentlLKQEKEALNHRIVQQAKEMTETMEKKLV 1085
Cdd:COG1196    273 RLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE----LEEELAELEEELEELEEELEELEEELEE 348

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1086 EETK--QLELDLNDERLRYQNLLNEFSRLEERYDDLKEEmtlmvhvpkpghkrtdsthssneseyiFSSEIAEMEDIPSR 1163
Cdd:COG1196    349 AEEEleEAEAELAEAEEALLEAEAELAEAEEELEELAEE---------------------------LLEALRAAAELAAQ 401

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1164 TEEPSEKKvpldmslfLKLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEErpqiRGAELEYESLKRQELESENKKLK 1243
Cdd:COG1196    402 LEELEEAE--------EALLERLERLEEELEELEEALAELEEEEEEEEEALEE----AAEEEAELEEEEEALLELLAELL 469

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1836165656 1244 NELNELRKALSEKSAPEVTApgAPAYRVLMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQPKDDK 1310
Cdd:COG1196    470 EEAALLEAALAELLEELAEA--AARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEA 534
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
966-1468 1.59e-12

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 72.79  E-value: 1.59e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  966 DYKCLVEKLTNLEGIYNSETEKLRSDLERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKqETE 1045
Cdd:PRK03918   159 DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE-ELK 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1046 QLVSNLKEENTLLKQEKEALNHRIVQqakemTETMEKKLVEETKQLEldlndERLRYqnlLNEFSRLEERYDDLKEEMTL 1125
Cdd:PRK03918   238 EEIEELEKELESLEGSKRKLEEKIRE-----LEERIEELKKEIEELE-----EKVKE---LKELKEKAEEYIKLSEFYEE 304

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1126 MVHVPKPGHKRTDSTHSSNESeyiFSSEIAEMEDIPSRTEEPSEKKVpldmslflKLQKRVTELEQEKQVMQDELDRKEE 1205
Cdd:PRK03918   305 YLDELREIEKRLSRLEEEING---IEERIKELEEKEERLEELKKKLK--------ELEKRLEELEERHELYEEAKAKKEE 373

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1206 -QVLRSKAKEEERPQIRgAELEYESLKRQELESENKK-------LKNELNELRKALSEKSAPEVTAPgapayrVLMEQLT 1277
Cdd:PRK03918   374 lERLKKRLTGLTPEKLE-KELEELEKAKEEIEEEISKitarigeLKKEIKELKKAIEELKKAKGKCP------VCGRELT 446

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1278 SvSEELDVRKEEVLILRSQLVSQKEAI-QPKDDKNTMTDSTILLEDVQKMKDKGEIAQAYIGLKEtnRSSALDYHELNED 1356
Cdd:PRK03918   447 E-EHRKELLEEYTAELKRIEKELKEIEeKERKLRKELRELEKVLKKESELIKLKELAEQLKELEE--KLKKYNLEELEKK 523

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1357 GELwlvYEGLKQANRLLESQLQSQKRS------HENEAEALRGEIQSLKEEN---NRQQQLLAQNLQLPPEARIEA--SL 1425
Cdd:PRK03918   524 AEE---YEKLKEKLIKLKGEIKSLKKElekleeLKKKLAELEKKLDELEEELaelLKELEELGFESVEELEERLKElePF 600

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|...
gi 1836165656 1426 QHEITRLTNENLDLMEQLEKQDKTVRKLKKQLKVFAKKIGELE 1468
Cdd:PRK03918   601 YNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLE 643
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
922-1469 4.13e-12

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 71.63  E-value: 4.13e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  922 RMMAKRELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLVEKLTNLEGIYnSETEKLRSDLERLQLSEEE 1001
Cdd:PRK03918   171 IKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV-KELEELKEEIEELEKELES 249

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1002 AKvatGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQ-----ETEQLVSNLKEENTLLKQEKEALNHRIVQQAKEM 1076
Cdd:PRK03918   250 LE---GSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkekaEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGI 326

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1077 tetmeKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMVHVPKpghkrtdstHSSNESEYIFSSEIAE 1156
Cdd:PRK03918   327 -----EERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELER---------LKKRLTGLTPEKLEKE 392

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1157 MEDIPSRTEEPSEKkvpldmslFLKLQKRVTELEQEKQVMQDELDRKEEQ-----VLRSKAKEEERPQIRG---AELEYE 1228
Cdd:PRK03918   393 LEELEKAKEEIEEE--------ISKITARIGELKKEIKELKKAIEELKKAkgkcpVCGRELTEEHRKELLEeytAELKRI 464

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1229 SLKRQELESENKKLKNELNELRKALSEKsaPEVTApgapaYRVLMEQLTSVSEELDVR---------------KEEVLIL 1293
Cdd:PRK03918   465 EKELKEIEEKERKLRKELRELEKVLKKE--SELIK-----LKELAEQLKELEEKLKKYnleelekkaeeyeklKEKLIKL 537

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1294 RSQLVSQKEAIQPKDDKNTMtdstilLEDVQKMKDKGEIAQAYIgLKETNRSSALDYHELNED-GELWLVYE---GLKQA 1369
Cdd:PRK03918   538 KGEIKSLKKELEKLEELKKK------LAELEKKLDELEEELAEL-LKELEELGFESVEELEERlKELEPFYNeylELKDA 610

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1370 NRLLESQLQSQKRShENEAEALRGEIQSLKEENNRQQQLLAQNLQLPPEARIEaSLQHEITRLTNENLDLMEQLEKQD-- 1447
Cdd:PRK03918   611 EKELEREEKELKKL-EEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYE-ELREEYLELSRELAGLRAELEELEkr 688

                          570       580
                   ....*....|....*....|....*..
gi 1836165656 1448 -----KTVRKLKKQLKVFAKKIGELEV 1469
Cdd:PRK03918   689 reeikKTLEKLKEELEEREKAKKELEK 715
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 920-1466 1.67e-10

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: 65.92  E-value: 1.67e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  920 FRRMMAKRELKKLKIEarsverYKKLHIGMENKIMQLQRKVDEQNKDYKCLVEKLTNLEGIYNSETEKLRSDLERLQL-- 997
Cdd:pfam05557    9 ARLSQLQNEKKQMELE------HKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLkk 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  998 ----------SEEEAKVATGR--VLSLQEEIAKLRK-------DLEQTRSEKKCIEEHADRYK---QETEQLVSNLKEEN 1055
Cdd:pfam05557   83 kylealnkklNEKESQLADARevISCLKNELSELRRqiqraelELQSTNSELEELQERLDLLKakaSEAEQLRQNLEKQQ 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1056 TLLK---QEKEALNHRIVQQA--KEMTETMEKKLVEETkqlELDLNDERLRYQN-LLNEFSR----LEERYDDLKEEMtl 1125
Cdd:pfam05557  163 SSLAeaeQRIKELEFEIQSQEqdSEIVKNSKSELARIP---ELEKELERLREHNkHLNENIEnkllLKEEVEDLKRKL-- 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1126 mvhvpkpghkrtdsthssnESEYIFSSEIAEMEDIPSRTEEPSEKKVPLDMSLFLKLQKRVTELEQEKQVMQDELDRKEE 1205
Cdd:pfam05557  238 -------------------EREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQLQQREIVLKEE 298

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1206 Q-VLRSKAKEEERPQirgAELEYE-SLKRQELESENKKLKNELNELR----------------KALSEKSAPEVTAPGA- 1266
Cdd:pfam05557  299 NsSLTSSARQLEKAR---RELEQElAQYLKKIEDLNKKLKRHKALVRrlqrrvllltkerdgyRAILESYDKELTMSNYs 375

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1267 PAYRVLMEQLTSVSEELDVRKEEVLILRSQLvsQKEAIQPKDDKNTMTDSTILLEDVQKMKDKGEIAQAYIGLKETNRSS 1346
Cdd:pfam05557  376 PQLLERIEEAEDMTQKMQAHNEEMEAQLSVA--EEELGGYKQQAQTLERELQALRQQESLADPSYSKEEVDSLRRKLETL 453

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1347 ALDYHEL---NEDGELWLVYEGLKQANRLLES---QLQSQ-----KRSHENEAEALRGEIQSLKEENNRQQQLLAQNLQL 1415
Cdd:pfam05557  454 ELERQRLreqKNELEMELERRCLQGDYDPKKTkvlHLSMNpaaeaYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRL 533

                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1836165656 1416 PPEARIEASlqheitrltNENLDLMEQLEKQDKTVRKLKkqlKVFAKKIGE 1466
Cdd:pfam05557  534 PETTSTMNF---------KEVLDLRKELESAELKNQRLK---EVFQAKIQE 572
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 941-1515 2.51e-10

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: 65.81  E-value: 2.51e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  941 RYKKLHIGMENKIMQLQRKVDEQNKDYKCLVEKLTNLEGIYNSETEKLRSDLERLQLSEEEAKVATGRVLSLQEEIAKLR 1020
Cdd:TIGR04523   23 GYKNIANKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLN 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1021 KDLEQTRSEKKcieehadrykqETEQLVSNLKEENTLLKQEKEALNHRIvqqakemtetmeKKLVEETKQLELDLNDERL 1100
Cdd:TIGR04523  103 SDLSKINSEIK-----------NDKEQKNKLEVELNKLEKQKKENKKNI------------DKFLTEIKKKEKELEKLNN 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1101 RYQNLLNEFSRLEERYDDLKEEMTlmvhvpKPGHKRTDSTHSSNESEYIFSSEIAEMEDIPSRTEEPSEKKvpldmSLFL 1180
Cdd:TIGR04523  160 KYNDLKKQKEELENELNLLEKEKL------NIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELK-----KQNN 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1181 KLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEE---RPQIRGAELEYESLKRQELESENKKLKNELNELRKalsEKS 1257
Cdd:TIGR04523  229 QLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKikkQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNN---QKE 305

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1258 ApevtapgapayrvlmEQLTSVSEELDVRKEEVLILRSQLVSQKEAI-----QPKDDKNTMTDSTilLEDVQKMKDKGEI 1332
Cdd:TIGR04523  306 Q---------------DWNKELKSELKNQEKKLEEIQNQISQNNKIIsqlneQISQLKKELTNSE--SENSEKQRELEEK 368

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1333 AQAYIGLKETNRSSALDYHEL-NEDGELWLVYEGLKQANRLLESQLQSQkrshENEAEALRGEIQSLKEENNrqqqllaq 1411
Cdd:TIGR04523  369 QNEIEKLKKENQSYKQEIKNLeSQINDLESKIQNQEKLNQQKDEQIKKL----QQEKELLEKEIERLKETII-------- 436

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1412 nlqlppearieaSLQHEITRLTNENLDLMEQLEKQDKTVRKLKKQLKVFAKKIGELEVGQMENISpgqiidepirpvNIP 1491
Cdd:TIGR04523  437 ------------KNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQK------------ELK 492

                          570       580
                   ....*....|....*....|....
gi 1836165656 1492 RKEKDFQGMLEYKKEDEQKlVKNL 1515
Cdd:TIGR04523  493 SKEKELKKLNEEKKELEEK-VKDL 515
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 926-1233 2.97e-10

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: 65.47  E-value: 2.97e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  926 KRELKKLKIEARS-VERYKKLHIGMENKIMQLQRKVDEQNKDYKCLVEKLTNLE-GIYNSETE--KLRSDLERLQ----- 996
Cdd:TIGR02169  697 LRRIENRLDELSQeLSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEqEIENVKSElkELEARIEELEedlhk 776

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  997 ----LSEEEAKVATGRVLSLQEEIAKLRK----------DLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQEK 1062
Cdd:TIGR02169  777 leeaLNDLEARLSHSRIPEIQAELSKLEEevsriearlrEIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI 856

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1063 EALNHRivqqaKEMTETMEKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMVHVPKpghkrtdsthS 1142
Cdd:TIGR02169  857 ENLNGK-----KEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLS----------E 921

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1143 SNESEYIFSSEIAEMEDIPSRTEEPSEKKVPLDmslflKLQKRVTELEQEKQVMQ-------DELDRKEEQVLRSKAK-- 1213
Cdd:TIGR02169  922 LKAKLEALEEELSEIEDPKGEDEEIPEEELSLE-----DVQAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDELKEKra 996

                          330       340
                   ....*....|....*....|..
gi 1836165656 1214 --EEERPQIRGAELEYESLKRQ 1233
Cdd:TIGR02169  997 klEEERKAILERIEEYEKKKRE 1018
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 880-1458 6.51e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.57  E-value: 6.51e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  880 RYRKILREHKAVIIQKRVRGWLARTHYKRSMHAIIylqccfrrmmAKRELKKLKIEARSVERYKKLHIgMENKIMQLQRK 959
Cdd:COG1196    214 RYRELKEELKELEAELLLLKLRELEAELEELEAEL----------EELEAELEELEAELAELEAELEE-LRLELEELELE 282

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  960 VDEQNKDYKCLVEKLTNLEGIYNSETEKLRSDLERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADR 1039
Cdd:COG1196    283 LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1040 YKQETEQLVSNLKEENTLLKQEKEAlnhrivQQAKEMTETMEKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDL 1119
Cdd:COG1196    363 AEEALLEAEAELAEAEEELEELAEE------LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1120 KEEmtlmvhvpkpghkrtdsthsSNESEYIFSSEIAEMEdipsrteepsekkvpldmSLFLKLQKRVTELEQEKQVMQDE 1199
Cdd:COG1196    437 EEE--------------------EEEALEEAAEEEAELE------------------EEEEALLELLAELLEEAALLEAA 478

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1200 LDRKEEQVLRSKAKEE-ERPQIRGAELEYESLKRQELESENKKLKNELNELRKALSEKSAPEVTAPGAPAYRVLMEQLTS 1278
Cdd:COG1196    479 LAELLEELAEAAARLLlLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEV 558

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1279 VSEELDVRKEEVL----ILRSQLVSQKEAIQPKDDKNTMTDSTILLEDVQKMKDKGEIAQAYIGLKET----------NR 1344
Cdd:COG1196    559 AAAAIEYLKAAKAgratFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTlvaarleaalRR 638

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1345 SSALDYHELNEDGELWLVYEG--------------LKQANRLLESQLQSQKRSHENEAEALRGEIQSLKEENNRQQQLLA 1410
Cdd:COG1196    639 AVTLAGRLREVTLEGEGGSAGgsltggsrrellaaLLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLE 718

                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1836165656 1411 QNLQLPPEARIEASLQHEITRLTNEN-----------LDLMEQLEKQDKTVRKLKKQLK 1458
Cdd:COG1196    719 EELEEEALEEQLEAEREELLEELLEEeelleeealeeLPEPPDLEELERELERLEREIE 777
PTZ00121 PTZ00121
MAEBL; Provisional
 928-1347 7.15e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 64.78  E-value: 7.15e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  928 ELKKLKIEARSVERYKKlHIGMENKIMQLQRKVDEQNK--DYKCLVEKLTNLEGIYNSETEKLRSDleRLQLSEEEAKVA 1005
Cdd:PTZ00121  1409 ELKKAAAAKKKADEAKK-KAEEKKKADEAKKKAEEAKKadEAKKKAEEAKKAEEAKKKAEEAKKAD--EAKKKAEEAKKA 1485

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1006 TgRVLSLQEEIAKLRKDLEQTRSEKKCIEE--HADRYKQETEQLVSNLKEENTLLKQEKEALNHRIVQQAKEMTETMEKK 1083
Cdd:PTZ00121  1486 D-EAKKKAEEAKKKADEAKKAAEAKKKADEakKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKK 1564

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1084 LVEETKQLELDLNDERLRYQNLLN-EFSRLEERYDDLKEEMTLMVHVPKpghkrtdsthsSNESEYIFSSEIAEMEDIPS 1162
Cdd:PTZ00121  1565 KAEEAKKAEEDKNMALRKAEEAKKaEEARIEEVMKLYEEEKKMKAEEAK-----------KAEEAKIKAEELKKAEEEKK 1633

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1163 RTEEPSEKKVPLdmslfLKLQKRVTELEQEKQVMQDELDRKEEQVLRS-----KAKEEERPQIRGAELEYESLKRQEles 1237
Cdd:PTZ00121  1634 KVEQLKKKEAEE-----KKKAEELKKAEEENKIKAAEEAKKAEEDKKKaeeakKAEEDEKKAAEALKKEAEEAKKAE--- 1705

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1238 ENKKLKNElnELRKALSEKSAPEVTAPGAPAYRVLMEQLTSVSEELDVRKEEvlilrSQLVSQKEAIQPKDDKNTMTDST 1317
Cdd:PTZ00121  1706 ELKKKEAE--EKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE-----KKKIAHLKKEEEKKAEEIRKEKE 1778

                          410       420       430
                   ....*....|....*....|....*....|
gi 1836165656 1318 ILLEDVQKMKDKGEIAQAYIGLKETNRSSA 1347
Cdd:PTZ00121  1779 AVIEEELDEEDEKRRMEVDKKIKDIFDNFA 1808
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 924-1256 2.44e-09

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: 62.68  E-value: 2.44e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  924 MAKRELKKLKIEARSVERYKKLHIGMEN-KIMQLQRKVDEQNKDYKCLVEKLTNLEGIYNSETEKLRSDLERLQLSEEEA 1002
Cdd:pfam02463  694 ILRRQLEIKKKEQREKEELKKLKLEAEElLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKE 773

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1003 KvatgrvlSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQEKEalnhrivqQAKEMTETMEK 1082
Cdd:pfam02463  774 K-------ELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQE--------EKIKEEELEEL 838

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1083 KLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMVHVPKPGHKRTDSTHSSNESEYIFSSEIAEMEDIPS 1162
Cdd:pfam02463  839 ALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENE 918

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1163 RTEEPSEKKVPLDMSLFLKLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEERPQIRGAELEYESLK--RQELESENK 1240
Cdd:pfam02463  919 IEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEerYNKDELEKE 998

                          330
                   ....*....|....*.
gi 1836165656 1241 KLKNELNELRKALSEK 1256
Cdd:pfam02463  999 RLEEEKKKLIRAIIEE 1014
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 935-1469 3.99e-09

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: 62.06  E-value: 3.99e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  935 EARSVERYKKLHIGMENKIMQLQRKvdEQNKDYKClveKLTNLEgiynSETEKLRSDLErlqlseEEAKVATGRVLSLQE 1014
Cdd:pfam15921  285 EKASSARSQANSIQSQLEIIQEQAR--NQNSMYMR---QLSDLE----STVSQLRSELR------EAKRMYEDKIEELEK 349

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1015 EIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQEKEAlNHRIVQQAKEMTETMEkklveetkQLELD 1094
Cdd:pfam15921  350 QLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQ-NKRLWDRDTGNSITID--------HLRRE 420

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1095 LNDERLRYQnllnefsRLEERYDDLKEEMTLMVhvpkpgHKRTDSTHSSNESEYIFSSEIAEMEDIPSR----TEEPSEK 1170
Cdd:pfam15921  421 LDDRNMEVQ-------RLEALLKAMKSECQGQM------ERQMAAIQGKNESLEKVSSLTAQLESTKEMlrkvVEELTAK 487

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1171 KVPLDMS------LFLKLQKRVTELE---QEKQVMQDELDRKEEQVLRSKAKEEerpQIRGAELEYESLKRQELEsenkk 1241
Cdd:pfam15921  488 KMTLESSertvsdLTASLQEKERAIEatnAEITKLRSRVDLKLQELQHLKNEGD---HLRNVQTECEALKLQMAE----- 559

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1242 lKNELNELRKALSEKSAPEVTAPGAPAYRVLMEQlTSVSEELDVRK---EEVLILRSQLVSQKEAIQPKDDKNTMTDSTI 1318
Cdd:pfam15921  560 -KDKVIEILRQQIENMTQLVGQHGRTAGAMQVEK-AQLEKEINDRRlelQEFKILKDKKDAKIRELEARVSDLELEKVKL 637

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1319 LLEDVQKMKDKGEIAQAYIGLKETNRSSALDYHELNEDgelwlvYEGLKQANR-------LLESQLQSQKRSHENEAEAL 1391
Cdd:pfam15921  638 VNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSED------YEVLKRNFRnkseemeTTTNKLKMQLKSAQSELEQT 711

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1392 RGEIQSLKEENNRQQQLLAQNLQLPPEAR--IEAsLQHEITRL----TNENLDlmEQLEKQDKTvrKLKKQLKVFA---- 1461
Cdd:pfam15921  712 RNTLKSMEGSDGHAMKVAMGMQKQITAKRgqIDA-LQSKIQFLeeamTNANKE--KHFLKEEKN--KLSQELSTVAtekn 786


                   ....*...
gi 1836165656 1462 KKIGELEV 1469
Cdd:pfam15921  787 KMAGELEV 794
PTZ00121 PTZ00121
MAEBL; Provisional
 921-1510 8.62e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 60.93  E-value: 8.62e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  921 RRMMAKRELKklkiEARSVERYKKLHigmENKIMQLQRKVDEQNKDYKCL--VEKLTNLEGIYNSETEKLRSDLERLQLS 998
Cdd:PTZ00121  1200 RKAEAARKAE----EERKAEEARKAE---DAKKAEAVKKAEEAKKDAEEAkkAEEERNNEEIRKFEEARMAHFARRQAAI 1272

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  999 EEEAKVATGRVLSLQE--EIAKLRKDLEQTRSE--KKCIEE--HADRYKQETEQL---VSNLKEENTLLKQEKEALNHRI 1069
Cdd:PTZ00121  1273 KAEEARKADELKKAEEkkKADEAKKAEEKKKADeaKKKAEEakKADEAKKKAEEAkkkADAAKKKAEEAKKAAEAAKAEA 1352

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1070 VQQAKEMTETMEKKLVEETKQLELDLNDERLRYQnlLNEFSRLEERYDDLKEEMTLMVHVPKPGHKRTDSTHSSNESEYI 1149
Cdd:PTZ00121  1353 EAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK--AEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEK 1430

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1150 FSSEIAEMEDIPSRTEEPSEKKVPlDMSLFLKLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEERPQIRGAELEYES 1229
Cdd:PTZ00121  1431 KKADEAKKKAEEAKKADEAKKKAE-EAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAK 1509

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1230 LKRQELESENKKLKNElnELRKALSEKSAPEvtapgapayrvlMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQPKDD 1309
Cdd:PTZ00121  1510 KKADEAKKAEEAKKAD--EAKKAEEAKKADE------------AKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEED 1575

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1310 KNTMTDSTILLEDVQKmKDKGEIAQAYIGLKETNRSSALDYHELNEDGELWLVYEGLKQANRLLESQLQSQKRSHEN--- 1386
Cdd:PTZ00121  1576 KNMALRKAEEAKKAEE-ARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEElkk 1654

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1387 --EAEALRGEIQSLKEENNRQQQLLAQNLQLPPEARIEASLQ--------HEITRLTNENLDLMEQLEKQDKT----VRK 1452
Cdd:PTZ00121  1655 aeEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKeaeeakkaEELKKKEAEEKKKAEELKKAEEEnkikAEE 1734

                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1836165656 1453 LKKQLKVFAKKIGELEVGQMENISPGQIIDEPIRPVNIPRKEKDFQGMLEYKKEDEQK 1510
Cdd:PTZ00121  1735 AKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKR 1792
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 981-1397 4.22e-08

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: 58.54  E-value: 4.22e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  981 YNSETEKLRSDLERLQLSEEEakvatgrvlsLQEEIAKLRKDLEQTRSEKkcieEHADRYKQeteqLVSNLKE-ENTLLK 1059
Cdd:TIGR02169  168 FDRKKEKALEELEEVEENIER----------LDLIIDEKRQQLERLRRER----EKAERYQA----LLKEKREyEGYELL 229

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1060 QEKEALNHRIVQQAKEMTEtmekkLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMVHvpkpghKRTDS 1139
Cdd:TIGR02169  230 KEKEALERQKEAIERQLAS-----LEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVK------EKIGE 298

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1140 THSsneseyifssEIAEMEDIPSRTEEPSEKkvpldmslfLKLQKRVTELEQEKQVMQ-DELDRKEEQVLRSKAKEEERP 1218
Cdd:TIGR02169  299 LEA----------EIASLERSIAEKERELED---------AEERLAKLEAEIDKLLAEiEELEREIEEERKRRDKLTEEY 359

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1219 QIRGAELEYESLKRQELESENKKLKNELNELRKALSEksapevtapgapayrvLMEQLTSVSEELDVRKEEVLILRSQLV 1298
Cdd:TIGR02169  360 AELKEELEDLRAELEEVDKEFAETRDELKDYREKLEK----------------LKREINELKRELDRLQEELQRLSEELA 423

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1299 SQKEAIqpkddkntmtdsTILLEDVQKMKDKGEIAQAYIGLKETNRSSALDYHELNEDGelwlvYEGLKQANRLLESQLq 1378
Cdd:TIGR02169  424 DLNAAI------------AGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQE-----LYDLKEEYDRVEKEL- 485

                          410
                   ....*....|....*....
gi 1836165656 1379 SQKRSHENEAEALRGEIQS 1397
Cdd:TIGR02169  486 SKLQRELAEAEAQARASEE 504
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
924-1297 6.70e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 57.47  E-value: 6.70e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  924 MAKRELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLVEKLTNLEGIYN-----SETEKLRSDLERLQLS 998
Cdd:COG4717     68 LNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllplyQELEALEAELAELPER 147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  999 EEEAKVATGRVLSLQEEIAKLRKDLEQTRSEkkcIEEHADRYKQETEQLVSNLKEENTLLKQEKEALNHRIVQQAKEMTE 1078
Cdd:COG4717    148 LEELEERLEELRELEEELEELEAELAELQEE---LEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEE 224

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1079 TMEKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMVHVP---------------------KPGHKRT 1137
Cdd:COG4717    225 LEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAgvlflvlgllallflllarekASLGKEA 304

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1138 DSTHSSNESEYIFSSEIAEMEDIPSRTEEPSEKKVPLDMSLFLKLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEER 1217
Cdd:COG4717    305 EELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDE 384

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1218 PQIRGAELEYEslKRQELESENKKLKNELNELRKALSEKSAPEVTAPGAPAYRVLMEQLTSVSEELDVRKEEVLILRSQL 1297
Cdd:COG4717    385 EELRAALEQAE--EYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAEL 462
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 1016-1302 8.74e-08

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: 57.44  E-value: 8.74e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1016 IAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQEKE---ALNHRIVQQAKEMTETMEK-KLVEETKQL 1091
Cdd:pfam17380  277 IVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKArqaEMDRQAAIYAEQERMAMEReRELERIRQE 356

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1092 ELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMVHVPKPGHKRTDSTHSSNESEYIFSSEIAEMEDIPSRTEEPSEKK 1171
Cdd:pfam17380  357 ERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQRE 436

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1172 VPLDMSLFLKLQKRVTELEQEKQ-----VMQDELDRKEEQVLRSKAK------EEERPQIrgAELEYESLKRQELESENK 1240
Cdd:pfam17380  437 VRRLEEERAREMERVRLEEQERQqqverLRQQEEERKRKKLELEKEKrdrkraEEQRRKI--LEKELEERKQAMIEEERK 514

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1836165656 1241 K--LKNELNELRKALSEKSAPEV------TAPGAPAYRVLMEQLTSVSEE---LDVRKEEVLILRSQLVSQKE 1302
Cdd:pfam17380  515 RklLEKEMEERQKAIYEEERRREaeeerrKQQEMEERRRIQEQMRKATEErsrLEAMEREREMMRQIVESEKA 587
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 927-1458 9.27e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.25  E-value: 9.27e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  927 RELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLVEKLTNLEGIYNSETEKLRSDLERLQLSEEEAKVAT 1006
Cdd:COG1196    292 ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1007 GRVLSLQEEIAKLRKDLEQTRSEkkcIEEHADRYKQETEQLVSNLKEENTLLKQEKEALNHRI-VQQAKEMTETMEKKLV 1085
Cdd:COG1196    372 AELAEAEEELEELAEELLEALRA---AAELAAQLEELEEAEEALLERLERLEEELEELEEALAeLEEEEEEEEEALEEAA 448

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1086 EETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMtlmvhvpkpghkrtdstHSSNESEYIFSSEIAEME----DIP 1161
Cdd:COG1196    449 EEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL-----------------AEAAARLLLLLEAEADYEgfleGVK 511

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1162 SRTEEPSEKKVPLDMSLFLKLQKRVTELEQEK--QVMQDELDRKEEQVLRSKAKEEERPQIRGAELEYESLKRQELeSEN 1239
Cdd:COG1196    512 AALLLAGLRGLAGAVAVLIGVEAAYEAALEAAlaAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAA-LAA 590

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1240 KKLKNELNELRKALSEKSAPEvtapgAPAYRVLMEQLtsVSEELDVRKEEVLILRSQLVSQKEAIQPKDdkntMTDSTIL 1319
Cdd:COG1196    591 ALARGAIGAAVDLVASDLREA-----DARYYVLGDTL--LGRTLVAARLEAALRRAVTLAGRLREVTLE----GEGGSAG 659

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1320 LEDVQKMKDKGEIAQAYIGLKETNRSSALDYHELNEDGELWLVYEGLKQANRLLESQLQSQKRSHENEAEALRGEIQSLK 1399
Cdd:COG1196    660 GSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1836165656 1400 EENNRQQQLLAQNLQLPPEARIEASLQHEITRLTNE-------NLDLMEQLEKQDKTVRKLKKQLK 1458
Cdd:COG1196    740 ELLEEEELLEEEALEELPEPPDLEELERELERLEREiealgpvNLLAIEEYEELEERYDFLSEQRE 805
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
948-1401 1.07e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 56.97  E-value: 1.07e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  948 GMENKIMQLQRKVDEqnKDYKCLVEKLTNLEgiynSETEKLRSDLERLQLSEEEAKVATG--------------RVLSLQ 1013
Cdd:PRK02224   184 DQRGSLDQLKAQIEE--KEEKDLHERLNGLE----SELAELDEEIERYEEQREQARETRDeadevleeheerreELETLE 257

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1014 EEIAKLRKDLEQTRSEKkciEEHADRYKQETEQLvSNLKEENT--LLKQEKEALNHRIVQQAKemtETMEKKLVEetkqL 1091
Cdd:PRK02224   258 AEIEDLRETIAETERER---EELAEEVRDLRERL-EELEEERDdlLAEAGLDDADAEAVEARR---EELEDRDEE----L 326

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1092 ELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTlmvhvpkpgHKRTDSTHSSNESEyifsseiAEMEDIPSRTEEPSEkk 1171
Cdd:PRK02224   327 RDRLEECRVAAQAHNEEAESLREDADDLEERAE---------ELREEAAELESELE-------EAREAVEDRREEIEE-- 388

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1172 vpldmslflkLQKRVTELEQEKQVMQDELDRKEEqvlRSKAKEEERPQIRGaeleyeslKRQELESENKKLKNELNELRK 1251
Cdd:PRK02224   389 ----------LEEEIEELRERFGDAPVDLGNAED---FLEELREERDELRE--------REAELEATLRTARERVEEAEA 447

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1252 ALSEKSAPEVTAPGAPAYRVlmeqltsvsEELDVRKEEVLILRSQLVSQKEAIQPKDDKNTMTDSTILLED-VQKMKDKG 1330
Cdd:PRK02224   448 LLEAGKCPECGQPVEGSPHV---------ETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDrIERLEERR 518

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1836165656 1331 EIAQAYIGLKETnrssaldyhELNEDGElwlvyeglkQANRLLE--SQLQSQKRSHENEAEALRGEIQSLKEE 1401
Cdd:PRK02224   519 EDLEELIAERRE---------TIEEKRE---------RAEELREraAELEAEAEEKREAAAEAEEEAEEAREE 573
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 928-1512 1.35e-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: 56.65  E-value: 1.35e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  928 ELKKLKIEARSVERYKKLHIGMENKIMQLQR---------------KVDEQNKDYKCLVEKLTNLEGIYNSETEKLRSDL 992
Cdd:pfam05483   89 KIKKWKVSIEAELKQKENKLQENRKIIEAQRkaiqelqfenekvslKLEEEIQENKDLIKENNATRHLCNLLKETCARSA 168

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  993 ERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTR--SEKKCIEEHAdRYKQETEQlVSNLKEENTLLKQEKEALNHRIV 1070
Cdd:pfam05483  169 EKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRvqAENARLEMHF-KLKEDHEK-IQHLEEEYKKEINDKEKQVSLLL 246

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1071 QQAKEMTETMEKK--LVEETKQLELDLNDE-RLRYQNLlnefSRLEERYDDLKEEMTLMvhvpKPGHKRTDSTHSSNESE 1147
Cdd:pfam05483  247 IQITEKENKMKDLtfLLEESRDKANQLEEKtKLQDENL----KELIEKKDHLTKELEDI----KMSLQRSMSTQKALEED 318

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1148 Y-IFSSEIAEM-EDIPSRTEEPSEKKVPLDMSlflklqkrVTELEQEKQVMQdELDRKEEQVLRskaKEEERPQIRGAEL 1225
Cdd:pfam05483  319 LqIATKTICQLtEEKEAQMEELNKAKAAHSFV--------VTEFEATTCSLE-ELLRTEQQRLE---KNEDQLKIITMEL 386

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1226 EYESLKRQELESENKKLKNELNELRKALSEKsapEVTAPGAPAYRVLMEQLTSVSEE----LDVRKEEVLILRSQLVSQK 1301
Cdd:pfam05483  387 QKKSSELEEMTKFKNNKEVELEELKKILAED---EKLLDEKKQFEKIAEELKGKEQEliflLQAREKEIHDLEIQLTAIK 463

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1302 EA-----IQPKDDKNTMTDSTilLEDVQKMKDKGEIAQAYIGLKETNRSSALDYHELNEDgelwlVYEGLKQANRLLES- 1375
Cdd:pfam05483  464 TSeehylKEVEDLKTELEKEK--LKNIELTAHCDKLLLENKELTQEASDMTLELKKHQED-----IINCKKQEERMLKQi 536

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1376 -QLQSQKRSHENEAEALRGEIQSL---------KEENNRQQQLLAQNLQLPPEARIEASLQHEITRLTNENLDLmEQLEK 1445
Cdd:pfam05483  537 eNLEEKEMNLRDELESVREEFIQKgdevkckldKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNI-EELHQ 615

                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1836165656 1446 QDKTVRKL----KKQLKVFAKKIGELEvgqMENISPGQIIDEPIrpvniprkeKDFQGMLEYKKEDEQKLV 1512
Cdd:pfam05483  616 ENKALKKKgsaeNKQLNAYEIKVNKLE---LELASAKQKFEEII---------DNYQKEIEDKKISEEKLL 674
Myo5p-like_CBD_Rasip1 cd15472
cargo binding domain of myosin 5-like of Ras-interacting protein 1; Ras-interacting protein 1 ...
 1533-1812 1.77e-07

cargo binding domain of myosin 5-like of Ras-interacting protein 1; Ras-interacting protein 1 (Rasip1 or RAIN) is an effector of the small G protein Rap1 and plays an important role in endothelial junction stabilization. Rasip1, like afadin, is a multi domain protein, that contains beside a myosin5-like CBD, a Ras-associated domain and a PDZ domain.


Pssm-ID: 271256  Cd Length: 366  Bit Score: 55.36  E-value: 1.77e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1533 PAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVL----KKRGD---------------------DFETVSFWLSNTCR 1587
Cdd:cd15472     25 PAFLLCLCIQHSATHFEPGHFGKLLLKIAKRIQEIVwektKELAEkqpehqdpaslsllsiaelapDLQPLLFWMSNSIE 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1588 FLHCLKQ----YSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPmIVSGMLE-----HET 1658
Cdd:cd15472    105 LLYFIQQkvplYEQSMEEELDVGSKESLLSSTLTASEEAMTVLEEVIMYTFQQCVYYLTKTLYV-ALPALLDsnpftAEE 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1659 IQGVSG--VKPTGLRkRTSSIADEgtyTLDsILRQLnsfhsvmCQHgmdPELIKQVVKQMFYIIGAITLNNLLLRKDMCS 1736
Cdd:cd15472    184 RESWSGgsRLPEGVR-RVLEIYQA---TLD-LLRQY-------QVH---PEIASQMFAYLFFFSNASLFNQLMEKGSGGG 248

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1737 ---WSKGMQIRYNVSQLEEWLRDKNLmNSGAKETLEPLIQAAQLLQVKKKTDDDAE--AICSMCNALTTAQIVKVLNLYT 1811
Cdd:cd15472    249 ffqWSRGVQIRANLDLLLDWLQGAGL-GDLAEEFFRKLSSTVNLLATPKEQLLQMSwsSLRAEFPALNPAQLHHLLRQYQ 327


                   .
gi 1836165656 1812 P 1812
Cdd:cd15472    328 L 328
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 927-1468 1.87e-07

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: 56.18  E-value: 1.87e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  927 RELKKLKieaRSVERYKKLhigMENKIMQLQRKVDEQNKDYKCLVEKLTNLEGiYNSETEKLRSDLERLqlsEEEAKVAT 1006
Cdd:TIGR04523  162 NDLKKQK---EELENELNL---LEKEKLNIQKNIDKIKNKLLKLELLLSNLKK-KIQKNKSLESQISEL---KKQNNQLK 231

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1007 GRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQEKEALNhrivqQAKEMTETMEKKLVE 1086
Cdd:TIGR04523  232 DNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLN-----QLKSEISDLNNQKEQ 306

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1087 E-TKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMvhvpkpghkRTDSTHSSNESEYIfSSEIAEMED-IPSRT 1164
Cdd:TIGR04523  307 DwNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQL---------KKELTNSESENSEK-QRELEEKQNeIEKLK 376

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1165 EEPSEKKvpldmslflklqKRVTELEQEKQVMQDELDRKEEQvlrSKAKEEerpQIRGAELEYESLKR--QELESENKKL 1242
Cdd:TIGR04523  377 KENQSYK------------QEIKNLESQINDLESKIQNQEKL---NQQKDE---QIKKLQQEKELLEKeiERLKETIIKN 438

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1243 KNELNELRKALSEKSApevtapgapAYRVLMEQLTSVSEELDVRKEEVLILRSQL-VSQKEAIQPKDDKNTMTDSTILLE 1321
Cdd:TIGR04523  439 NSEIKDLTNQDSVKEL---------IIKNLDNTRESLETQLKVLSRSINKIKQNLeQKQKELKSKEKELKKLNEEKKELE 509

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1322 DVQK--------MKDKGEIAQAYIGLKETNRSSALDyhELNEDGElwlvyeglkqanRLLESQLQSQKRSHENEAEALRG 1393
Cdd:TIGR04523  510 EKVKdltkkissLKEKIEKLESEKKEKESKISDLED--ELNKDDF------------ELKKENLEKEIDEKNKEIEELKQ 575

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1836165656 1394 EIQSLKEENNRqqqllaqnlqlppearieasLQHEITRLTNENLDLMEQLEKQDKTVRKLKKQLKVFAKKIGELE 1468
Cdd:TIGR04523  576 TQKSLKKKQEE--------------------KQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLS 630
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 952-1283 2.36e-07

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: 56.23  E-value: 2.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  952 KIMQLQRKVDEQNKDYKCLVEKLTNLEGIYNSETEKLrSDLERlQLSEEEAkvatgRVLSLQEEIAKLRKDLEQTRSEKK 1031
Cdd:TIGR02169  675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQEL-SDASR-KIGEIEK-----EIEQLEQEEEKLKERLEELEEDLS 747

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1032 CIEEHADRYKQETEQLVSNLKEENTLLKQEKEALNH----------RIVQQAKEMTETMEKKLVEETKQLELDLNDERLR 1101
Cdd:TIGR02169  748 SLEQEIENVKSELKELEARIEELEEDLHKLEEALNDlearlshsriPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLE 827

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1102 YQNLLNEFSRLEERYDDLKEEMtlmvhvpkpghkrtdsthssneseyifSSEIAEMEDIPSRTEEPSEKkvpldmslFLK 1181
Cdd:TIGR02169  828 KEYLEKEIQELQEQRIDLKEQI---------------------------KSIEKEIENLNGKKEELEEE--------LEE 872

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1182 LQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEErpqirgAELEYEsLKRQELESENKKLKNELNELRKALSEKSAPEV 1261
Cdd:TIGR02169  873 LEAALRDLESRLGDLKKERDELEAQLRELERKIEE------LEAQIE-KKRKRLSELKAKLEALEEELSEIEDPKGEDEE 945

                          330       340
                   ....*....|....*....|..
gi 1836165656 1262 TAPGAPAYRVLMEQLTSVSEEL 1283
Cdd:TIGR02169  946 IPEEELSLEDVQAELQRVEEEI 967
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 905-1520 2.87e-07

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: 55.75  E-value: 2.87e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  905 HYKRSMHAIIYLQCCFRRMmaKRELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLVEKLTNLEGIYNSE 984
Cdd:pfam02463  221 LEEEYLLYLDYLKLNEERI--DLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEEL 298

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  985 TEKLRSDLERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQEKEA 1064
Cdd:pfam02463  299 KSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAK 378

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1065 LNHRIVQQAKEMTETMEKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLmvhvpkpghkRTDSTHSSN 1144
Cdd:pfam02463  379 KKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESI----------ELKQGKLTE 448

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1145 ESEYIFSSEIAEMEDIPSRTEEPSEKKVPLDMSLFLKLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEERPQIRGAE 1224
Cdd:pfam02463  449 EKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAH 528

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1225 LEYESLKRQELESENKKLKNELNELRKA-----LSEKSAPEVTAPGAPAYRVLMEQLTSVSEELDVRKEEVLILRsQLVS 1299
Cdd:pfam02463  529 GRLGDLGVAVENYKVAISTAVIVEVSATadeveERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPIL-NLAQ 607

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1300 QKEAIQPKDDKNTMTDSTILLEDVQKMKDKGEIAQAYIGLKETNRSSALDYHELNEDGelwlvYEGLKQANRLLESQLQS 1379
Cdd:pfam02463  608 LDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVK-----ASLSELTKELLEIQELQ 682

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1380 QKRSHENEAEALRGEIQSLKEENNRQQQLLAQNLQLppEARIEASLQHEITRLTNENLDLMEQLEKQDKTVrKLKKQLKV 1459
Cdd:pfam02463  683 EKAESELAKEEILRRQLEIKKKEQREKEELKKLKLE--AEELLADRVQEAQDKINEELKLLKQKIDEEEEE-EEKSRLKK 759

                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1836165656 1460 FAKKIGELEVGQMENISPGQIIDEPIRPVNIpRKEKDFQGMLEYKKEDEQKLVKNLILELK 1520
Cdd:pfam02463  760 EEKEEEKSELSLKEKELAEEREKTEKLKVEE-EKEEKLKAQEEELRALEEELKEEAELLEE 819
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 1008-1493 3.29e-07

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: 55.75  E-value: 3.29e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1008 RVLSLQ--EEIAKLRKDLEQTRSE--------KKCIEEHADRYKQETEQLVSNLKEENTLLKQEKEALNHRivQQAKEMT 1077
Cdd:pfam02463  136 NFLVQGgkIEIIAMMKPERRLEIEeeaagsrlKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQA--KKALEYY 213

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1078 ETMEKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLmvhvpkpghKRTDSTHSSNESEYIFSSEIAEM 1157
Cdd:pfam02463  214 QLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIE---------KEEEKLAQVLKENKEEEKEKKLQ 284

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1158 EDIPSRTEEPSEKKVP---LDMSLFLKLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEERPQIRGAELEYESLKRQE 1234
Cdd:pfam02463  285 EEELKLLAKEEEELKSellKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKL 364

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1235 LESENKKLKNELNELRKALSEKSAPEvtapgapayRVLMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQPKDDKNTMT 1314
Cdd:pfam02463  365 QEKLEQLEEELLAKKKLESERLSSAA---------KLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEE 435

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1315 DSTILLEDVQKMKDKGEIAQAYIGLKETNRSSALDYHELNEDGELWLVYEGLKQANRLLESQLQSQKRSHENEAEALRGE 1394
Cdd:pfam02463  436 EESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLAL 515

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1395 IQSLKEennrQQQLLAQNLQLPPEARIEASLQHEITRLTNENLDLMEQLEKQDKTVRKLKKQLKVFAKKIGELEVGQMEN 1474
Cdd:pfam02463  516 IKDGVG----GRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPL 591

                          490
                   ....*....|....*....
gi 1836165656 1475 ISPGQIIDEPIRPVNIPRK 1493
Cdd:pfam02463  592 KSIAVLEIDPILNLAQLDK 610
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 920-1282 5.48e-07

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: 54.74  E-value: 5.48e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  920 FRRMMAKRELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLVEKLTNLEGIYNS----ETEKLRS----- 990
Cdd:pfam17380  293 FEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEerkrELERIRQeeiam 372

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  991 ------DLERLQLSEeeakvatgrvlslQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQEKEA 1064
Cdd:pfam17380  373 eisrmrELERLQMER-------------QQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRR 439

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1065 LNHrivQQAKEMTETMEKKLvEETKQLELDLNDERLRYQNLLnEFSRlEERYDDLKEEMTLMVhVPKPGHKRTDSTHSSN 1144
Cdd:pfam17380  440 LEE---ERAREMERVRLEEQ-ERQQQVERLRQQEEERKRKKL-ELEK-EKRDRKRAEEQRRKI-LEKELEERKQAMIEEE 512

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1145 ESEYIFSSEIAEMEDipsrteepsekkvpldmSLFLKLQKRVTELEQEKQVMQDELDRKEEQVLRSKakeEERPQIRGAE 1224
Cdd:pfam17380  513 RKRKLLEKEMEERQK-----------------AIYEEERRREAEEERRKQQEMEERRRIQEQMRKAT---EERSRLEAME 572

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1836165656 1225 LEYEsLKRQELESENKKLKNELNELRKALSEKSAPEVTAPGAPAYRVLMEQLTSVSEE 1282
Cdd:pfam17380  573 RERE-MMRQIVESEKARAEYEATTPITTIKPIYRPRISEYQPPDVESHMIRFTTQSPE 629
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 925-1468 7.97e-07

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: 54.30  E-value: 7.97e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  925 AKRELKKL-KIEARSVERYKKLhigmENKIMQLQRKVDEQNKDYKCLVEKLTNLEgiynSETEKLRSDLERLqlsEEEAK 1003
Cdd:TIGR02169  313 KERELEDAeERLAKLEAEIDKL----LAEIEELEREIEEERKRRDKLTEEYAELK----EELEDLRAELEEV---DKEFA 381

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1004 VATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQL---VSNLKEENTLLKQEKEALNHRIvqqakemtetm 1080
Cdd:TIGR02169  382 ETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLnaaIAGIEAKINELEEEKEDKALEI----------- 450

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1081 eKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEM-----TLMVHVPK-PGHKRTDSTHSSN---------- 1144
Cdd:TIGR02169  451 -KKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELaeaeaQARASEERvRGGRAVEEVLKASiqgvhgtvaq 529

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1145 ----ESEYIFSSEIA---EMEDIPSRTEEPSE------KKVPLDMSLFLKLQK---------------------RVTELE 1190
Cdd:TIGR02169  530 lgsvGERYATAIEVAagnRLNNVVVEDDAVAKeaiellKRRKAGRATFLPLNKmrderrdlsilsedgvigfavDLVEFD 609

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1191 QE-----KQVMQDEL-----------------------------------DRKEEQVLRSKAKEEERPQIRGaelEYESL 1230
Cdd:TIGR02169  610 PKyepafKYVFGDTLvvedieaarrlmgkyrmvtlegelfeksgamtggsRAPRGGILFSRSEPAELQRLRE---RLEGL 686

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1231 KRQE--LESENKKLKNELNELRKALSEKSApevtapgapAYRVLMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQPKD 1308
Cdd:TIGR02169  687 KRELssLQSELRRIENRLDELSQELSDASR---------KIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK 757

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1309 DKntmtdstilLEDVQKMKDKGEIAQAYIGLKETNRSSALDYHELNEDGELwlvYEGLKQANRLLESQLQSQKR---SHE 1385
Cdd:TIGR02169  758 SE---------LKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAE---LSKLEEEVSRIEARLREIEQklnRLT 825

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1386 NEAEALRGEIQSLKEENNRQQQLLAQNlqlppEARIE------ASLQHEITRLTNENLDLMEQLEKQDKTVRKLKKQLKV 1459
Cdd:TIGR02169  826 LEKEYLEKEIQELQEQRIDLKEQIKSI-----EKEIEnlngkkEELEEELEELEAALRDLESRLGDLKKERDELEAQLRE 900


                   ....*....
gi 1836165656 1460 FAKKIGELE 1468
Cdd:TIGR02169  901 LERKIEELE 909
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 925-1123 7.99e-07

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: 54.29  E-value: 7.99e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  925 AKRELKKLKIEARSVErykklhigmeNKIMQLQRKVDEQNKDYKCLVEKLTNLEG---IYNSETEKLRSDLERLqlsEEE 1001
Cdd:TIGR02168  808 LRAELTLLNEEAANLR----------ERLESLERRIAATERRLEDLEEQIEELSEdieSLAAEIEELEELIEEL---ESE 874

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1002 AKVATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLvsnlKEENTLLKQEKEALNHRIVQQAK------- 1074
Cdd:TIGR02168  875 LEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEEL----REKLAQLELRLEGLEVRIDNLQErlseeys 950

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1836165656 1075 ---EMTETMEKKLVEETKQLELDLNDERLRYQNL-------LNEFSRLEERYDDLKEEM 1123
Cdd:TIGR02168  951 ltlEEAEALENKIEDDEEEARRRLKRLENKIKELgpvnlaaIEEYEELKERYDFLTAQK 1009
PRK12704 PRK12704
phosphodiesterase; Provisional
 924-1090 1.42e-06

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 53.24  E-value: 1.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  924 MAKRELKKLKIEARSVERYKKLHIgmENKIMQLQRKVDEQNKDYKclvEKLTNLEGIYNSETEKLRSDLERLQLSEEEAK 1003
Cdd:PRK12704    39 EAKRILEEAKKEAEAIKKEALLEA--KEEIHKLRNEFEKELRERR---NELQKLEKRLLQKEENLDRKLELLEKREEELE 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1004 VATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQE--TEQLVSNLKEEntlLKQEKEALNHRIVQQAKEMTETME 1081
Cdd:PRK12704   114 KKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEeaKEILLEKVEEE---ARHEAAVLIKEIEEEAKEEADKKA 190


                   ....*....
gi 1836165656 1082 KKLVEETKQ 1090
Cdd:PRK12704   191 KEILAQAIQ 199
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1004-1268 1.57e-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: 52.46  E-value: 1.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1004 VATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEentlLKQEKEALNHRIVQQAKEMTETMEK- 1082
Cdd:COG4942     10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA----LERRIAALARRIRALEQELAALEAEl 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1083 -KLVEETKQLELDLNDERLRYQNLLNEFSRLEERyddlkEEMTLMVHVPKPghkrTDSTHSSNESEYIFSSEIAEMEDIP 1161
Cdd:COG4942     86 aELEKEIAELRAELEAQKEELAELLRALYRLGRQ-----PPLALLLSPEDF----LDAVRRLQYLKYLAPARREQAEELR 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1162 SRTEEpsekkvpldmslflkLQKRVTELEQEKQVMQDELDRKEEQVLR-SKAKEEERPQIRGAELEYESLKRQ--ELESE 1238
Cdd:COG4942    157 ADLAE---------------LAALRAELEAERAELEALLAELEEERAAlEALKAERQKLLARLEKELAELAAElaELQQE 221

                          250       260       270
                   ....*....|....*....|....*....|
gi 1836165656 1239 NKKLKNELNELRKALSEKSAPEVTAPGAPA 1268
Cdd:COG4942    222 AEELEALIARLEAEAAAAAERTPAAGFAAL 251
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 950-1401 1.64e-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: 53.26  E-value: 1.64e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  950 ENKIMQLQRKVDEQNKDYKCLVEKLTNLEGiYNSEtekLRSDLERLQLSEEEAkvaTGRVLSLQEEIAKLRKDLEQT--- 1026
Cdd:pfam01576  242 EEELQAALARLEEETAQKNNALKKIRELEA-QISE---LQEDLESERAARNKA---EKQRRDLGEELEALKTELEDTldt 314

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1027 -------RSE--------KKCIEEHADRYKQE---------------TEQLvSNLKEENTLLKQEKEALNH--------- 1067
Cdd:pfam01576  315 taaqqelRSKreqevtelKKALEEETRSHEAQlqemrqkhtqaleelTEQL-EQAKRNKANLEKAKQALESenaelqael 393

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1068 RIVQQAKEMTETMEKKLVEETKQLELDLND-ERLRyQNLLNEFSRLEERYDDLKeemTLMVHVPKPGHKRTDSThSSNES 1146
Cdd:pfam01576  394 RTLQQAKQDSEHKRKKLEGQLQELQARLSEsERQR-AELAEKLSKLQSELESVS---SLLNEAEGKNIKLSKDV-SSLES 468

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1147 eyifsseiaEMEDIPSRTEEPSEKKvpldmslfLKLQKRVTELEQEKQVMQDELDrKEEQVLRSKAKEEERPQIRGAE-- 1224
Cdd:pfam01576  469 ---------QLQDTQELLQEETRQK--------LNLSTRLRQLEDERNSLQEQLE-EEEEAKRNVERQLSTLQAQLSDmk 530

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1225 --LEYESLKRQELESENKKLKNELNELRKALSEKSApevtapgapAYRVLMEQLTSVSEELDVRKEEVLILRsQLVSQKE 1302
Cdd:pfam01576  531 kkLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAA---------AYDKLEKTKNRLQQELDDLLVDLDHQR-QLVSNLE 600

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1303 AIQPKDDKNTMTDSTIlledVQKMKDKGEIAQAYIGLKETnRSSALDyHELNEDGELwlvYEGLKQANRLLES------- 1375
Cdd:pfam01576  601 KKQKKFDQMLAEEKAI----SARYAEERDRAEAEAREKET-RALSLA-RALEEALEA---KEELERTNKQLRAemedlvs 671

                          490       500       510
                   ....*....|....*....|....*....|....*.
gi 1836165656 1376 ----------QLQSQKRSHENEAEALRGEIQSLKEE 1401
Cdd:pfam01576  672 skddvgknvhELERSKRALEQQVEEMKTQLEELEDE 707
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 837-859 1.65e-06

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 45.78  E-value: 1.65e-06
                            10        20
                    ....*....|....*....|...
gi 1836165656   837 RRTKAATIIQKYWRMYVVRRRYK 859
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRYK 23
fMyo4p_CBD cd15479
cargo binding domain of fungal myosin 4; Yeast myosin V travels along actin cables, actin ...
 1692-1820 3.00e-06

cargo binding domain of fungal myosin 4; 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).


Pssm-ID: 271263  Cd Length: 329  Bit Score: 51.51  E-value: 3.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1692 LNSFHSVMCQHGMDPELIKQVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQIRYNVSQLEEWLRDKnlmNSGAKETLEPL 1771
Cdd:cd15479    168 LNEFDAVLCKFQVVDSMHTKIFNDTLKYLNVMLFNDLITKCPALNWKYGYEVDRNIERLVSWFEPR---IEDVRPNLIQI 244

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1836165656 1772 IQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERV 1820
Cdd:cd15479    245 IQAVKILQLKISNLNEFKLLFDFWYALNPAQIQAILLKYKPANKGEAGV 293
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
 663-687 3.09e-06

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: 49.27  E-value: 3.09e-06
                           10        20
                   ....*....|....*....|....*
gi 1836165656  663 FRNSLHLLMETLNATTPHYVRCIKP 687
Cdd:cd01363    146 INESLNTLMNVLRATRPHFVRCISP 170
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 924-1249 3.56e-06

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 52.28  E-value: 3.56e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  924 MAKRELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLVEKLTNLegIYNSETEKLRSDLERLQLSEEEAK 1003
Cdd:TIGR00618  602 KLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTL--TQERVREHALSIRVLPKELLASRQ 679

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1004 VATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQEKEALNHRIVQ-------QAKEM 1076
Cdd:TIGR00618  680 LALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKElmhqartVLKAR 759

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1077 TETMEKKLVEETKQLELDLNDERLRyQNLLNEFSRLEERYDDLKE-EMTLMVHVPKPGHKRTDSTHSSNESEYIFSSEIA 1155
Cdd:TIGR00618  760 TEAHFNNNEEVTAALQTGAELSHLA-AEIQFFNRLREEDTHLLKTlEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLE 838

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1156 E----MEDIPSRTEEPSEKKVPLDMSlfLKLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKE--EERPQIRGAELEYES 1229
Cdd:TIGR00618  839 EksatLGEITHQLLKYEECSKQLAQL--TQEQAKIIQLSDKLNGINQIKIQFDGDALIKFLHEitLYANVRLANQSEGRF 916

                          330       340
                   ....*....|....*....|
gi 1836165656 1230 LKRQELESENKKLKNELNEL 1249
Cdd:TIGR00618  917 HGRYADSHVNARKYQGLALL 936
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
1153-1294 6.57e-06

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 51.01  E-value: 6.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1153 EIAEMEDIPSRTEEPSEKKVPLDMSLFLKLQKRVTELEQEKQVMQDELDRKEEQVLR-----SKAKEEERPQIRgAELEY 1227
Cdd:COG2433    389 ELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERlerelSEARSEERREIR-KDREI 467

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1836165656 1228 ESLKR--QELESENKKLKNELNELR------KALSEKSAPEVTAPGAPAYRVLMEQLTSVSEELDVRKEEVLILR 1294
Cdd:COG2433    468 SRLDReiERLERELEEERERIEELKrklerlKELWKLEHSGELVPVKVVEKFTKEAIRRLEEEYGLKEGDVVYLR 542
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
949-1401 7.78e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 51.19  E-value: 7.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  949 MENKIMQLQRKVDEQNKDYKCLVEKLTNLEGIYNSETEKLRSDLERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRS 1028
Cdd:PRK02224   256 LEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRV 335

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1029 EKKCIEEHADRYKQETEQlvsnLKEENTLLKQEKEALNHRIvQQAKEMTETMEKKLVEetkqLELDLNDERLRYQNLLNE 1108
Cdd:PRK02224   336 AAQAHNEEAESLREDADD----LEERAEELREEAAELESEL-EEAREAVEDRREEIEE----LEEEIEELRERFGDAPVD 406

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1109 FSRLEERYDDLKEEmtlmvhvpkpghkRTDSTHSSNESEYIFSSE---IAE----------------MEDIP--SRTEEP 1167
Cdd:PRK02224   407 LGNAEDFLEELREE-------------RDELREREAELEATLRTArerVEEaealleagkcpecgqpVEGSPhvETIEED 473

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1168 SEKKVPLDMSL------FLKLQKRVTELEQEKQVmQDELDRKEEQVLRSkakeEERPQIRGAELEYESLKRQELESENKK 1241
Cdd:PRK02224   474 RERVEELEAELedleeeVEEVEERLERAEDLVEA-EDRIERLEERREDL----EELIAERRETIEEKRERAEELRERAAE 548

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1242 LKNELNELRKALSEksAPEVTAPGAPAYRVLMEQLTSVSEELDV--RKEEVLILRSQLVSQKEAIQPK-DDKNTMTDsti 1318
Cdd:PRK02224   549 LEAEAEEKREAAAE--AEEEAEEAREEVAELNSKLAELKERIESleRIRTLLAAIADAEDEIERLREKrEALAELND--- 623

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1319 llEDVQKMKDK--------GEIAQAYIGLKETNRSSALDYHElNEDGELwlvyeglkQANRLLESQLQSQKRSHENEAEA 1390
Cdd:PRK02224   624 --ERRERLAEKrerkreleAEFDEARIEEAREDKERAEEYLE-QVEEKL--------DELREERDDLQAEIGAVENELEE 692

                          490
                   ....*....|.
gi 1836165656 1391 LRgeiqSLKEE 1401
Cdd:PRK02224   693 LE----ELRER 699
MyosinXI_CBD cd15475
cargo binding domain of myosin XI; Class XI myosins are a plant specific group, homologous to ...
 1557-1810 1.44e-05

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: 49.11  E-value: 1.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1557 LTSTINSIKKVlkkrGDDFETVSFWLSNTCRFLhCLKQysgeegfmkhntsrqneHCLTnfdlaeyrqvlsdlAIQIYQQ 1636
Cdd:cd15475     52 IIQTIGSAIED----QDNNDHLAYWLSNTSTLL-FLLQ-----------------RSLP--------------ALLFKQQ 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1637 LVRVLENILqPMI-------VSGMLEhETIQGVSGVKPTGLRKRTSSIADEGTYTL---DSILRQLNSFHSVMCQHGMDP 1706
Cdd:cd15475     96 LTAYVEKIY-GIIrdnlkkeLSPLLS-LCIQAPRTSRGSSSKSSSSANSLGQQSPSshwQSIIKSLNSLLSTLKENHVPP 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1707 ELIKQVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQIRYNVSQLEEWLRDknlmnsgAKET--------LEPLIQAAQLL 1778
Cdd:cd15475    174 FLVQKIFTQVFSFINVQLFNSLLLRRECCSFSNGEYVKAGLAELELWCSQ-------ATEEyagsswdeLKHIRQAVGFL 246

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1836165656 1779 QVKKKTDDDAEAICS-MCNALTTAQIVKVLNLY 1810
Cdd:cd15475    247 VIHQKSRKSYDEITNdLCPVLSVQQLYRICTMY 279
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 984-1391 2.50e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 2.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  984 ETE-KLRS---DLERLQLSEEEakvatgrvlsLQEEIAKLRKDLEQtrsekkcieehADRYKQeteqlvsnLKEENTLLK 1059
Cdd:COG1196    176 EAErKLEAteeNLERLEDILGE----------LERQLEPLERQAEK-----------AERYRE--------LKEELKELE 226

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1060 QEKEALNHRIVQQAKEMTETMEKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEmtlmvhvpkpghkrtds 1139
Cdd:COG1196    227 AELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE----------------- 289

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1140 thssnesEYIFSSEIAEMEdipsrteepSEKKVpldmslflkLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEE--- 1216
Cdd:COG1196    290 -------EYELLAELARLE---------QDIAR---------LEERRRELEERLEELEEELAELEEELEELEEELEElee 344

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1217 -----RPQIRGAELEYESLKRQELESENKKLKNELNELRKALSEKSAPEVTAPGAPAYRVLMEQLTSVSEELDVRKEEVL 1291
Cdd:COG1196    345 eleeaEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE 424

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1292 ILRSQLVSQKEAIQPKDDKNTMTDSTILLEDVQKMKDKGEIAQAyigLKETNRSSALDYHELNEDGELWLVYEGLKQANR 1371
Cdd:COG1196    425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL---LEEAALLEAALAELLEELAEAAARLLLLLEAEA 501

                          410       420
                   ....*....|....*....|
gi 1836165656 1372 LLESQLQSQKRSHENEAEAL 1391
Cdd:COG1196    502 DYEGFLEGVKAALLLAGLRG 521
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
926-1255 2.75e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 49.29  E-value: 2.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  926 KRELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLVEKLTNLEGIYNSETEKLRSDLERLQLSEEEAKva 1005
Cdd:PRK03918   451 KELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYE-- 528

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1006 tgrvlSLQEEIAKLRKDLEQTRSEKKCIEEhadrYKQETEQLVSNLKEentlLKQEKEALNHRIVQQAKEMTETMEKKLv 1085
Cdd:PRK03918   529 -----KLKEKLIKLKGEIKSLKKELEKLEE----LKKKLAELEKKLDE----LEEELAELLKELEELGFESVEELEERL- 594

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1086 eetKQLElDLNDERLRYQNLLNEFSRLEERYDDLKEEMTlmvhvpkpgHKRTDSTHSSNESEYIfSSEIAEMEDI--PSR 1163
Cdd:PRK03918   595 ---KELE-PFYNEYLELKDAEKELEREEKELKKLEEELD---------KAFEELAETEKRLEEL-RKELEELEKKysEEE 660

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1164 TEEPSEKKVPLDMSLFlKLQKRVTELEQEKQVMQDELDRKEEQvlrskaKEEerpqIRGAELEYESLKR-----QELESE 1238
Cdd:PRK03918   661 YEELREEYLELSRELA-GLRAELEELEKRREEIKKTLEKLKEE------LEE----REKAKKELEKLEKalervEELREK 729

                          330
                   ....*....|....*..
gi 1836165656 1239 NKKLKNELNElrKALSE 1255
Cdd:PRK03918   730 VKKYKALLKE--RALSK 744
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
996-1293 2.85e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 48.36  E-value: 2.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  996 QLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQEKEALNHRI--VQQA 1073
Cdd:COG4372     27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQeeLESL 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1074 KEMTETMEKKLVE---ETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLM---VHVPKPGHKRTDSTHSSNESE 1147
Cdd:COG4372    107 QEEAEELQEELEElqkERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLqeeLAALEQELQALSEAEAEQALD 186

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1148 YIFSSEIAEMEDIPSRTEEPSEKKVPLDMSLFLKLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEERPQIRGAELEY 1227
Cdd:COG4372    187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1836165656 1228 ESLKRQELESENKKLKNELNELRKALSEKSAPEVTAPGAPAYRVLMEQLTSVSEELDVRKEEVLIL 1293
Cdd:COG4372    267 ILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELAL 332
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 921-1258 3.00e-05

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: 49.27  E-value: 3.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  921 RRMMAKRELKKLKIEARSVERYKKlhiGMENKIMQLQRKVD---EQNKDYKCLVE------KLTNLEGIYNSETEKLRSD 991
Cdd:TIGR00606  320 ELVDCQRELEKLNKERRLLNQEKT---ELLVEQGRLQLQADrhqEHIRARDSLIQslatrlELDGFERGPFSERQIKNFH 396

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  992 LERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLLkQEKEALNHRIVQ 1071
Cdd:TIGR00606  397 TLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKEL-QQLEGSSDRILE 475

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1072 QAKEMTETM-------EKKLVEETKQLELDLNDERLryqNLLNEFSRLEERYDDLKEEMTLMVHVPKPGHKRTDSTHSSN 1144
Cdd:TIGR00606  476 LDQELRKAErelskaeKNSLTETLKKEVKSLQNEKA---DLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIR 552

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1145 ESEYIFSSE-IAEMEDIP-----SRTEEPSEKKVPLDMSLFLKLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKeeerp 1218
Cdd:TIGR00606  553 KIKSRHSDElTSLLGYFPnkkqlEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDK----- 627

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 1836165656 1219 qirgaelEYESLKRQELESENKKLKNELNELRKALSEKSA 1258
Cdd:TIGR00606  628 -------LFDVCGSQDEESDLERLKEEIEKSSKQRAMLAG 660
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 928-1223 4.11e-05

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: 48.96  E-value: 4.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  928 ELKKLKI------EARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLVEKLTN----LEGIYN----------SETEK 987
Cdd:pfam15921  631 ELEKVKLvnagseRLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNkseeMETTTNklkmqlksaqSELEQ 710

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  988 LRSDLERLQLSEEEA-KVATGrvlsLQEEIAKLRKDLEQTRSEKKCIEEhadrykqeteqLVSNLKEENTLLKQEKEALN 1066
Cdd:pfam15921  711 TRNTLKSMEGSDGHAmKVAMG----MQKQITAKRGQIDALQSKIQFLEE-----------AMTNANKEKHFLKEEKNKLS 775

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1067 HRIVQQAK---------EMTETMEKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMV-HVPKPGHkr 1136
Cdd:pfam15921  776 QELSTVATeknkmagelEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQHTLDVkELQGPGY-- 853

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1137 tdSTHSSNESEYIFSSEIAEME-DIPSRTEEPSekkvpldmslFLKLQKRVTELEQE------KQVMQD--ELDRKEEQV 1207
Cdd:pfam15921  854 --TSNSSMKPRLLQPASFTRTHsNVPSSQSTAS----------FLSHHSRKTNALKEdptrdlKQLLQElrSVINEEPTV 921

                          330
                   ....*....|....*.
gi 1836165656 1208 LRSKAKEEERPQIRGA 1223
Cdd:pfam15921  922 QLSKAEDKGRAPSLGA 937
Caldesmon pfam02029
Caldesmon;
983-1256 4.50e-05

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 48.33  E-value: 4.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  983 SETEKLRSDLERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADR------------YKQETEQLVSN 1050
Cdd:pfam02029   50 LKPSGQGGLDEEEAFLDRTAKREERRQKRLQEALERQKEFDPTIADEKESVAERKENneeeensswekeEKRDSRLGRYK 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1051 LKEENTLLKQEKEALNHRIVQQAKEMTETMEKKLVEETKQLELDLNDERLRYQNLLNEfsrLEERYDDLK---------- 1120
Cdd:pfam02029  130 EEETEIREKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKE---KKVKYESKVfldqkrghpe 206

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1121 ---EEMTLMVHVPKPGHKRTDSTHSSNESEYIFSSEIAE----MEDIP-SRTEEPSEKKVPLDMslflKLQKRVTELEqe 1192
Cdd:pfam02029  207 vksQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEaeqkLEELRrRRQEKESEEFEKLRQ----KQQEAELELE-- 280

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1836165656 1193 kqvmqdELDRKEEQvlRSKAKEEERPQiRGAEleyESLKRQELESENKKLKNELNELRKALSEK 1256
Cdd:pfam02029  281 ------ELKKKREE--RRKLLEEEEQR-RKQE---EAERKLREEEEKRRMKEEIERRRAEAAEK 332
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
 839-859 5.76e-05

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 459869  Cd Length: 21  Bit Score: 41.53  E-value: 5.76e-05
                           10        20
                   ....*....|....*....|.
gi 1836165656  839 TKAATIIQKYWRMYVVRRRYK 859
Cdd:pfam00612    1 RKAAIKIQAAWRGYLARKRYK 21
FPP pfam05911
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ...
 947-1123 6.88e-05

Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.


Pssm-ID: 461778 [Multi-domain]  Cd Length: 859  Bit Score: 48.13  E-value: 6.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  947 IGMENKIMqlqrKVDEQNKdYKCLVEKLTNLEGIYnSETEKLRSDLERLQlseeEAKVATGRVLSLQEEIAKLRKDLEQT 1026
Cdd:pfam05911  624 SSMEDEIK----KHDCIDK-VTLSENKVAQVDNGC-SEIDNLSSDPEIPS----DGPLVSGSNDLKTEENKRLKEEFEQL 693

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1027 RSEKKCIEEHADRYK----------QETEQLVSNLKEENTLLKQEKEALNHRIVQQAkEMTETMEKKLVEetkqLELDLN 1096
Cdd:pfam05911  694 KSEKENLEVELASCTenlestksqlQESEQLIAELRSELASLKESNSLAETQLKCMA-ESYEDLETRLTE----LEAELN 768

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1836165656 1097 DERLRYQNLLNEFS-------RLEERYDDLKEEM 1123
Cdd:pfam05911  769 ELRQKFEALEVELEeekncheELEAKCLELQEQL 802
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 949-1297 8.02e-05

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: 47.86  E-value: 8.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  949 MENKIMQLQRKVDEQNKDYKCLVEKLTNLEGiynsETEKLRSDLERLQLSEEE----AKVATGRVLSLQEEIAKLRKDLE 1024
Cdd:pfam01576  775 LELDLKELEAQIDAANKGREEAVKQLKKLQA----QMKDLQRELEEARASRDEilaqSKESEKKLKNLEAELLQLQEDLA 850

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1025 QTRSEKKCIEEHADRYKQEteqlVSNLKEENTLLKQEKEALNHRIVQQAKEMTE---TME------KKLVEETKQLELDL 1095
Cdd:pfam01576  851 ASERARRQAQQERDELADE----IASGASGKSALQDEKRRLEARIAQLEEELEEeqsNTEllndrlRKSTLQVEQLTTEL 926

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1096 NDERLRYQNLLNEFSRLEERYDDLKEEMTLMVHVPKPGHKRTDSThssneseyiFSSEIAEME---DIPSRTEEPSEKKV 1172
Cdd:pfam01576  927 AAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKSKFKSSIAA---------LEAKIAQLEeqlEQESRERQAANKLV 997

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1173 pldmslflklqkRVTELEQEKQVMQDELDRKEeqvlrskaKEEERPQIRGAELEYESLKRQELESENkklknelnelrka 1252
Cdd:pfam01576  998 ------------RRTEKKLKEVLLQVEDERRH--------ADQYKDQAEKGNSRMKQLKRQLEEAEE------------- 1044

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 1836165656 1253 lseksapEVTAPGApAYRVLMEQLTSVSEELDVRKEEVLILRSQL 1297
Cdd:pfam01576 1045 -------EASRANA-ARRKLQRELDDATESNESMNREVSTLKSKL 1081
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 983-1467 8.76e-05

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 47.66  E-value: 8.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  983 SETEKLRSDLERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKcIEEHADRYKQETEQLVSNLKEENTllKQEK 1062
Cdd:TIGR00618  338 SSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQ-QKTTLTQKLQSLCKELDILQREQA--TIDT 414

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1063 EALNHRIVQQAKEMTETMEKKLVEETKQLEL----DLNDERLRYQNLLNEFSRLEERYDDLKEEMTLmvhvpkpgHKRTD 1138
Cdd:TIGR00618  415 RTSAFRDLQGQLAHAKKQQELQQRYAELCAAaitcTAQCEKLEKIHLQESAQSLKEREQQLQTKEQI--------HLQET 486

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1139 STHSSNESeyiFSSEIAEME-DIPSRTEEPSEKKV-----PLDMSLFLKLQKRVTELEQEKQVMQDELDRKEEQVLRSKA 1212
Cdd:TIGR00618  487 RKKAVVLA---RLLELQEEPcPLCGSCIHPNPARQdidnpGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKE 563

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1213 KEEERPQirgaELEYESLKRQELESENKKLKNELNELRKALSEKSAPEVTAPGApaYRVLMEQLTSVSEELDVRKEEVLI 1292
Cdd:TIGR00618  564 QMQEIQQ----SFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACE--QHALLRKLQPEQDLQDVRLHLQQC 637

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1293 LRSQ--LVSQKEAIQ---PKDDKN-----TMTDSTILLEDVQKMKDK--GEIAQAYIGLKETNRSSALDYHELNEDGELW 1360
Cdd:TIGR00618  638 SQELalKLTALHALQltlTQERVRehalsIRVLPKELLASRQLALQKmqSEKEQLTYWKEMLAQCQTLLRELETHIEEYD 717

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1361 ----------------------LVYEGLKQANRLLESQLQSQKRSHENEAEALRGEIQSLKEENNRQQQLLAQNLQLPPE 1418
Cdd:TIGR00618  718 refneienassslgsdlaaredALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREED 797

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1419 ARIEASLQHEITRLTNENLDLME-QLEKQDKTVRKLKKQLKVFAKKIGEL 1467
Cdd:TIGR00618  798 THLLKTLEAEIGQEIPSDEDILNlQCETLVQEEEQFLSRLEEKSATLGEI 847
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 926-1506 8.82e-05

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: 47.73  E-value: 8.82e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  926 KRELKKLKIEARSVERykklhigMENKIMQLQRKVDEQNKDYKclvEKLTNLEGiynseTEKLRSDLERLQlseEEAKVA 1005
Cdd:TIGR00606  590 RDRLAKLNKELASLEQ-------NKNHINNELESKEEQLSSYE---DKLFDVCG-----SQDEESDLERLK---EEIEKS 651

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1006 TGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADR---YKQETEQLVSNLKEENTLLKQEKEALNHRIVQQAKEMTETMEK 1082
Cdd:TIGR00606  652 SKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRvfqTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGL 731

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1083 KLVE--ETKQLELDLNDERLRYQNLLNEFSRLEeryDDLKEEMTLMvhvpkpghkrtDSTHSSNESEYIFSSEIAEMEDI 1160
Cdd:TIGR00606  732 APGRqsIIDLKEKEIPELRNKLQKVNRDIQRLK---NDIEEQETLL-----------GTIMPEEESAKVCLTDVTIMERF 797

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1161 PSRTEEpSEKKVPLDMSLF--LKLQKRVTELEQEKQVMQDELDRKEEQV-LRSKAKEEERPQIrgaeleyeslkrQELES 1237
Cdd:TIGR00606  798 QMELKD-VERKIAQQAAKLqgSDLDRTVQQVNQEKQEKQHELDTVVSKIeLNRKLIQDQQEQI------------QHLKS 864

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1238 ENKKLKNELNELRKALSEKSAPEvtapgapayrvlmEQLTSVSEELDVRKEEVlilrsqlvsqkeaiqpKDDKNTMTDST 1317
Cdd:TIGR00606  865 KTNELKSEKLQIGTNLQRRQQFE-------------EQLVELSTEVQSLIREI----------------KDAKEQDSPLE 915

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1318 ILLEDVQKMKDKgeiaqaYIGLKETNRSSALDyhELNE-DGELWLVYEGLKQANRLLESQLQSQKRSHENEaeaLRGEIQ 1396
Cdd:TIGR00606  916 TFLEKDQQEKEE------LISSKETSNKKAQD--KVNDiKEKVKNIHGYMKDIENKIQDGKDDYLKQKETE---LNTVNA 984

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1397 SLKEENNRQQQLLAQNLQLppeaRIEASLQHEITRLTNENLDLMeqleKQDKTVRKLKKQLKVFAKKIGELEVGQMENis 1476
Cdd:TIGR00606  985 QLEECEKHQEKINEDMRLM----RQDIDTQKIQERWLQDNLTLR----KRENELKEVEEELKQHLKEMGQMQVLQMKQ-- 1054

                          570       580       590
                   ....*....|....*....|....*....|.
gi 1836165656 1477 PGQIIDEPIRpvNIPRKE-KDFQGMLEYKKE 1506
Cdd:TIGR00606 1055 EHQKLEENID--LIKRNHvLALGRQKGYEKE 1083
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
981-1123 9.71e-05

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 47.32  E-value: 9.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  981 YNSETEKLRSDLERLQL-------------SEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQL 1047
Cdd:COG3206    180 LEEQLPELRKELEEAEAaleefrqknglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL 259

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1048 -----VSNLKEENTLLKQEKEAL------NHRIVQQAKEMTETMEKKLVEETKQLELDLNDERLRYQNLLNEfsrLEERY 1116
Cdd:COG3206    260 lqspvIQQLRAQLAELEAELAELsarytpNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREAS---LQAQL 336


                   ....*..
gi 1836165656 1117 DDLKEEM 1123
Cdd:COG3206    337 AQLEARL 343
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 950-1122 1.42e-04

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: 46.30  E-value: 1.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  950 ENKIMQLQRKVDEQNKDYKCLVEKLTNLEGIYNSETEKLRSDLERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSE 1029
Cdd:COG4942     26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1030 kkcIEEH------------------------ADRYKQETEQLVSNLKEENTLLKQEKEALNHRIVQQAKEMT--ETMEKK 1083
Cdd:COG4942    106 ---LAELlralyrlgrqpplalllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAelEALLAE 182

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1836165656 1084 LVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEE 1122
Cdd:COG4942    183 LEEERAALEALKAERQKLLARLEKELAELAAELAELQQE 221
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 953-1227 1.51e-04

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: 46.96  E-value: 1.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  953 IMQLQRKVDEQNKDYKCLVEKLTNLEGI--YNSETEKLRSDLERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEK 1030
Cdd:TIGR00606  794 MERFQMELKDVERKIAQQAAKLQGSDLDrtVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEK 873

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1031 KCIEEHADRYKQETEQLVSNLKEENTLLKQEKEALNHRI-VQQAKEMTETMEKKLV----EETKQLELDLNDERLRYQNL 1105
Cdd:TIGR00606  874 LQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSpLETFLEKDQQEKEELIsskeTSNKKAQDKVNDIKEKVKNI 953

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1106 LNEFSRLEERYDDLKEEM---------TLMVHVPK-PGHKRTDSTHSSNESEYIFSSEIAE---MEDIPSRTEEPSEKKV 1172
Cdd:TIGR00606  954 HGYMKDIENKIQDGKDDYlkqketelnTVNAQLEEcEKHQEKINEDMRLMRQDIDTQKIQErwlQDNLTLRKRENELKEV 1033

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1836165656 1173 PLDMSLFLKL--QKRVTELEQEKQVMQDELD--------------RKEEQVLRSKAKEEErPQIRGAELEY 1227
Cdd:TIGR00606 1034 EEELKQHLKEmgQMQVLQMKQEHQKLEENIDlikrnhvlalgrqkGYEKEIKHFKKELRE-PQFRDAEEKY 1103
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
 833-863 2.14e-04

IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory complex protein 10 (DRC10), belongs to the IQ motif-containing protein family which contains a C-terminal conserved IQ motif domain and two coiled-coil domains. The IQ motif ([ILV]QxxxRxxxx[RK]), where x stands for any amino-acid residue, interacts with calmodulin (CaM) in a calcium-independent manner and is present in proteins with a wide diversity of biological functions. The IQCD protein was found to primarily accumulate in the acrosome area of round and elongating spermatids of the testis during late stage of spermiogenesis and was then localized to the acrosome and tail regions of mature spermatozoa. The expression of IQCD follows the trajectory of acrosome development during spermatogenesis. IQCD is associated with neuroblastoma and neurodegenerative diseases, and is reported to interact with the nuclear retinoid X receptor in the presence of 9-cis-retinoic acid, thereby activating the transcriptional activity of the receptor.


Pssm-ID: 467745 [Multi-domain]  Cd Length: 37  Bit Score: 40.22  E-value: 2.14e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1836165656  833 AKFLRRTKAATIIQKYWRMYVVRRRYKIRRA 863
Cdd:cd23767      3 EELQRMNRAATLIQALWRGYKVRKELKKKKK 33
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
1232-1487 2.90e-04

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.78  E-value: 2.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1232 RQELESENKKLKNELNELRKALSE-KSAPEVTAPGAPAyRVLMEQLTSVSEELdvrkEEVLILRSQLVSQKEAIQPKDDK 1310
Cdd:COG3206    177 LEFLEEQLPELRKELEEAEAALEEfRQKNGLVDLSEEA-KLLLQQLSELESQL----AEARAELAEAEARLAALRAQLGS 251

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1311 NTMTDSTiLLEDVQKMKDKGEIAQA---YIGLKETNRSSALDYHELNEDgelwlvyegLKQANRLLESQLQSQKRSHENE 1387
Cdd:COG3206    252 GPDALPE-LLQSPVIQQLRAQLAELeaeLAELSARYTPNHPDVIALRAQ---------IAALRAQLQQEAQRILASLEAE 321

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1388 AEALRGEIQSLKEENNRQQQllaqnlqlppEARIEASLQHEITRLTNEnldlmeqlekqdktVRKLKKQLKVFAKKIGEL 1467
Cdd:COG3206    322 LEALQAREASLQAQLAQLEA----------RLAELPELEAELRRLERE--------------VEVARELYESLLQRLEEA 377

                          250       260
                   ....*....|....*....|
gi 1836165656 1468 EVGQMENISPGQIIDEPIRP 1487
Cdd:COG3206    378 RLAEALTVGNVRVIDPAVVP 397
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 984-1458 4.34e-04

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: 45.55  E-value: 4.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  984 ETEKLRSDLERLQLSEEEAKVATGR-VLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLkEENTLLKQEK 1062
Cdd:pfam01576  493 QLEDERNSLQEQLEEEEEAKRNVERqLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQL-EEKAAAYDKL 571

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1063 EALNHRIVQQAKEMTETM--EKKLVE--ETKQLELD--LNDERLRYQNLLNEFSRLEErydDLKEEMTLMVHVpkpGHKR 1136
Cdd:pfam01576  572 EKTKNRLQQELDDLLVDLdhQRQLVSnlEKKQKKFDqmLAEEKAISARYAEERDRAEA---EAREKETRALSL---ARAL 645

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1137 TDSTHSSNESEYIFSSEIAEMEDIPSRTE---------EPSEKKVPLDMSlflKLQKRVTELEQEKQVMQDELDRKEEQV 1207
Cdd:pfam01576  646 EEALEAKEELERTNKQLRAEMEDLVSSKDdvgknvhelERSKRALEQQVE---EMKTQLEELEDELQATEDAKLRLEVNM 722

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1208 LRSKAK------------EEERPQIRG------AELEYESLKRQELESENKKLKNELNELRKALSE---------KSAPE 1260
Cdd:pfam01576  723 QALKAQferdlqardeqgEEKRRQLVKqvreleAELEDERKQRAQAVAAKKKLELDLKELEAQIDAankgreeavKQLKK 802

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1261 VTAPGAPAYRVLMEQLTSVSEELDVRKE----------EVLILRSQLVS----QKEAIQPKDD-----KNTMTDSTILLE 1321
Cdd:pfam01576  803 LQAQMKDLQRELEEARASRDEILAQSKEsekklknleaELLQLQEDLAAseraRRQAQQERDEladeiASGASGKSALQD 882

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1322 DVQKMKDKgeIAQayigLKETNRSSALDYHELNEDgelwlvYEGLKQANRLLESQLQSQkRSHENEAEALRgeiQSLKEE 1401
Cdd:pfam01576  883 EKRRLEAR--IAQ----LEEELEEEQSNTELLNDR------LRKSTLQVEQLTTELAAE-RSTSQKSESAR---QQLERQ 946

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1836165656 1402 NNRQQQLLAQNlqlppEARIEASLQHEITRLTNENLDLMEQLEKQ-------DKTVRKLKKQLK 1458
Cdd:pfam01576  947 NKELKAKLQEM-----EGTVKSKFKSSIAALEAKIAQLEEQLEQEsrerqaaNKLVRRTEKKLK 1005
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1186-1468 4.47e-04

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: 45.44  E-value: 4.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1186 VTELEQEKQVMQDELDRKEEQVLRSKAKEEE-RPQI------RGAELEYESLKRQELESENKKLKNELNELRKALSEksa 1258
Cdd:TIGR02169  165 VAEFDRKKEKALEELEEVEENIERLDLIIDEkRQQLerlrreREKAERYQALLKEKREYEGYELLKEKEALERQKEA--- 241

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1259 peVTAPGAPAYRVLmEQLTSVSEELDVRKEEVLILRSQL------VSQKEAIQPKDDKNTMTDSTILLEDVQKMKdKGEI 1332
Cdd:TIGR02169  242 --IERQLASLEEEL-EKLTEEISELEKRLEEIEQLLEELnkkikdLGEEEQLRVKEKIGELEAEIASLERSIAEK-EREL 317

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1333 AQAyiglKETNRSSALDYHELNEDGElwlVYEGLKQANRLLESQLQSQKRSHENEAEALRGEIQSLKEENNRQQQLLAQN 1412
Cdd:TIGR02169  318 EDA----EERLAKLEAEIDKLLAEIE---ELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDY 390

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1836165656 1413 lqlppEARIEAsLQHEITRLTNENLDLMEQLEKQDKTVRKLKKQLKVFAKKIGELE 1468
Cdd:TIGR02169  391 -----REKLEK-LKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELE 440
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 950-1468 5.12e-04

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 45.34  E-value: 5.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  950 ENKIMQLQRKVD---EQNKDYKCLVEKLTNLEGiyNSETEKLRSDLERLQLSeeeakVATGRVLSLQEEIAKLRKDLEQT 1026
Cdd:TIGR00618  378 TQHIHTLQQQKTtltQKLQSLCKELDILQREQA--TIDTRTSAFRDLQGQLA-----HAKKQQELQQRYAELCAAAITCT 450

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1027 RSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQEKEalNHRIVQQAKEMTETMEKKLVEETKQLELDLNDERL------ 1100
Cdd:TIGR00618  451 AQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETR--KKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNpgpltr 528

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1101 RYQNLLNEFSRLEERYDDLKEEMTlmvHVPKPGHKRTDSTHSSNESEYIFSSEIAEM-EDIPSRTEEPSEKKVPLDMSLF 1179
Cdd:TIGR00618  529 RMQRGEQTYAQLETSEEDVYHQLT---SERKQRASLKEQMQEIQQSFSILTQCDNRSkEDIPNLQNITVRLQDLTEKLSE 605

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1180 LKLQKRVT--ELEQEKQVMQDELDRKEEQvlRSKAKEEERPQIRGAELEYESLKRQELES-------ENKKLKNELNELR 1250
Cdd:TIGR00618  606 AEDMLACEqhALLRKLQPEQDLQDVRLHL--QQCSQELALKLTALHALQLTLTQERVREHalsirvlPKELLASRQLALQ 683

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1251 KALSEKSAPEVTAPGAPAYRVLMEQLTSVSEELDVRKEEvliLRSQLVSQKEAIQPKDDknTMTDSTILLEDVQKMKDKG 1330
Cdd:TIGR00618  684 KMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNE---IENASSSLGSDLAARED--ALNQSLKELMHQARTVLKA 758

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1331 -EIAQAYIGLKETNRSSALD-YHELNEDGELWL-VYEGLKQANRLLESQLQSQKRSHENEAEAlrGEIQSLKEENNRQQQ 1407
Cdd:TIGR00618  759 rTEAHFNNNEEVTAALQTGAeLSHLAAEIQFFNrLREEDTHLLKTLEAEIGQEIPSDEDILNL--QCETLVQEEEQFLSR 836

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1836165656 1408 LlaqnlqlppeaRIEASLQHEITRLT---NENLDLMEQLEKQDKTVRKLKKQLKVFAKKIGELE 1468
Cdd:TIGR00618  837 L-----------EEKSATLGEITHQLlkyEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFD 889
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 984-1122 6.05e-04

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: 42.61  E-value: 6.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  984 ETEKLRSDLERL-----QLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRsekkcieehadRYKQETEQLVSNLKEENTLL 1058
Cdd:pfam08614   22 ENAKLQSEPESVlpstsSSKLSKASPQSASIQSLEQLLAQLREELAELY-----------RSRGELAQRLVDLNEELQEL 90

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1059 KQEKEALNHRI------VQQAKEMTETMEKKLVEETKQLElDLNDErlrYQNLLNEFSRLEERYDDLKEE 1122
Cdd:pfam08614   91 EKKLREDERRLaaleaeRAQLEEKLKDREEELREKRKLNQ-DLQDE---LVALQLQLNMAEEKLRKLEKE 156
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 934-1322 6.13e-04

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: 45.04  E-value: 6.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  934 IEARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLV-EKLTNLEGIYNSETEKLRS---DLERLQLSEEEAKVATGRV 1009
Cdd:TIGR00606  185 IKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIrDQITSKEAQLESSREIVKSyenELDPLKNRLKEIEHNLSKI 264

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1010 LSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQEKEA----LNHRIVQQAKEMTETMEKKLV 1085
Cdd:TIGR00606  265 MKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERelvdCQRELEKLNKERRLLNQEKTE 344

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1086 EETKQLELDLNDERLRYQNLlnefsrleeRYDDLKEEMTLmvhvpkpgHKRTDSTHSSNESEyifsSEIAEMEDIPSRTE 1165
Cdd:TIGR00606  345 LLVEQGRLQLQADRHQEHIR---------ARDSLIQSLAT--------RLELDGFERGPFSE----RQIKNFHTLVIERQ 403

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1166 EPSEKKVPLDMSLFlklqkrvTELEQEKQVMQDELDRKEEQVLRSKAKEEERPQIRGAELEYESLKRQELESENKKLKNE 1245
Cdd:TIGR00606  404 EDEAKTAAQLCADL-------QSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILEL 476

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1836165656 1246 LNELRKALSEKSAPEVTApgapayrvLMEqlTSVSEELDVRKEEVLILRSQLVSQKEAIQPKDDKNTMTDSTILLED 1322
Cdd:TIGR00606  477 DQELRKAERELSKAEKNS--------LTE--TLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKD 543
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 1011-1520 6.25e-04

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: 44.63  E-value: 6.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1011 SLQEEIAKLRKDLEQTRSEKKCIeehaDRYKQETEQLVSNLKEENTLLKQEKEALNHRIVQQAKEMTetmekKLVEETKQ 1090
Cdd:TIGR04523   37 QLEKKLKTIKNELKNKEKELKNL----DKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKIN-----KLNSDLSK 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1091 LELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLmvhvpkpghkrtdsthssneseyiFSSEIAEMEDIpsrTEEPSEK 1170
Cdd:TIGR04523  108 INSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDK------------------------FLTEIKKKEKE---LEKLNNK 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1171 kvpldmslFLKLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEeerpqirgAELEYESLKRQELESENKKLKNELNELR 1250
Cdd:TIGR04523  161 --------YNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKL--------LKLELLLSNLKKKIQKNKSLESQISELK 224

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1251 KALSEksapevtapgapayrvLMEQLTSVSEELDVRKEEVLILRSQLVSQKEaiQPKDDKNTmtdstilLEDVQKmkdkg 1330
Cdd:TIGR04523  225 KQNNQ----------------LKDNIEKKQQEINEKTTEISNTQTQLNQLKD--EQNKIKKQ-------LSEKQK----- 274

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1331 EIAQAYIGLKETNRssaldyhELNEDGELWLVYEGLKQAN--RLLESQLQSQKRSHENEAEALRGEIQSLKEENNRQqql 1408
Cdd:TIGR04523  275 ELEQNNKKIKELEK-------QLNQLKSEISDLNNQKEQDwnKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQI--- 344

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1409 laqnlqlppearieASLQHEITRLTNENLDLMEQLEKQDKTVRKLKKQ-------LKVFAKKIGELEVGQMENISPGQII 1481
Cdd:TIGR04523  345 --------------SQLKKELTNSESENSEKQRELEEKQNEIEKLKKEnqsykqeIKNLESQINDLESKIQNQEKLNQQK 410

                          490       500       510
                   ....*....|....*....|....*....|....*....
gi 1836165656 1482 DEpirpvNIPRKEKDFQgmleyKKEDEQKLVKNLILELK 1520
Cdd:TIGR04523  411 DE-----QIKKLQQEKE-----LLEKEIERLKETIIKNN 439
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 983-1453 8.08e-04

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 44.57  E-value: 8.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  983 SETEKLRSDLERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEqtrSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQEK 1062
Cdd:TIGR00618  163 KEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQ---LLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQ 239

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1063 EALNHRivqqakemteTMEKKLVEETKQLELDLNDERLRYQNLLNEFSRLEEryddLKEEMTLMVHVPKPGHKRTDSTHS 1142
Cdd:TIGR00618  240 QSHAYL----------TQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEE----TQERINRARKAAPLAAHIKAVTQI 305

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1143 SNESEYIFsSEIAEMEDipSRTEEPSEKKVPLDMSLFLKLQKRvteLEQEKQVMQDELDRKEEQVL-----RSKAKEEER 1217
Cdd:TIGR00618  306 EQQAQRIH-TELQSKMR--SRAKLLMKRAAHVKQQSSIEEQRR---LLQTLHSQEIHIRDAHEVATsireiSCQQHTLTQ 379

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1218 PqIRGAELEYESLKrQELESENKKLKNELNELRKALSEKSapevtapgapAYRVLMEQLTSVSEELDVRKEEVLILRSQL 1297
Cdd:TIGR00618  380 H-IHTLQQQKTTLT-QKLQSLCKELDILQREQATIDTRTS----------AFRDLQGQLAHAKKQQELQQRYAELCAAAI 447

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1298 VSQ-KEAIQPKDDKNTMTDStiLLEDVQKMKDKGEIAQAYiglketNRSSALDYHELNEDGELWLVYEG----------- 1365
Cdd:TIGR00618  448 TCTaQCEKLEKIHLQESAQS--LKEREQQLQTKEQIHLQE------TRKKAVVLARLLELQEEPCPLCGscihpnparqd 519

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1366 --LKQANRLLESQLQSQKRSHENEAEALRGEIQSLKEENNRQQQLLAQNL-QLPPEARIEASLQHEITRLTNENLDLMEQ 1442
Cdd:TIGR00618  520 idNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQqSFSILTQCDNRSKEDIPNLQNITVRLQDL 599

                          490
                   ....*....|.
gi 1836165656 1443 LEKQDKTVRKL 1453
Cdd:TIGR00618  600 TEKLSEAEDML 610
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 935-1308 8.31e-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: 44.43  E-value: 8.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  935 EARSVERYKKLHIGMENKIMQL----QRKVDE-------------QNKDYK----CLVEKLTNLE---GIYNSETEKLRS 990
Cdd:pfam10174  273 EIKQMEVYKSHSKFMKNKIDQLkqelSKKESEllalqtkletltnQNSDCKqhieVLKESLTAKEqraAILQTEVDALRL 352

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  991 DLER-----------LQLSEEEAKVATG--------------RVLSLQEEIAKLrkdLEQTRSEKKCIEEHADRYKqETE 1045
Cdd:pfam10174  353 RLEEkesflnkktkqLQDLTEEKSTLAGeirdlkdmldvkerKINVLQKKIENL---QEQLRDKDKQLAGLKERVK-SLQ 428

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1046 QLVSNlkeENTLLKQEKEAL--NHRIVQQAKEMTETMEKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEM 1123
Cdd:pfam10174  429 TDSSN---TDTALTTLEEALseKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHA 505

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1124 TLMVHVPkpghKRTDSTHSSNEseyifsSEIAEMEDIPSRTEEPSEKKVPLDMSLFLK--LQKRVTELEQEKQVMQDELD 1201
Cdd:pfam10174  506 SSLASSG----LKKDSKLKSLE------IAVEQKKEECSKLENQLKKAHNAEEAVRTNpeINDRIRLLEQEVARYKEESG 575

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1202 RKEEQV------LRSKAKEEERPQIRGAELeyESLKRQELESENKK---LKNELNELRK---ALSEKSAPEVTAPGAPAY 1269
Cdd:pfam10174  576 KAQAEVerllgiLREVENEKNDKDKKIAEL--ESLTLRQMKEQNKKvanIKHGQQEMKKkgaQLLEEARRREDNLADNSQ 653

                          410       420       430
                   ....*....|....*....|....*....|....*....
gi 1836165656 1270 RVLMEQLTsvsEELDVRKEEVLILRSQLVSQKEAIQPKD 1308
Cdd:pfam10174  654 QLQLEELM---GALEKTRQELDATKARLSSTQQSLAEKD 689
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 926-1401 9.94e-04

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: 44.06  E-value: 9.94e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  926 KRELKKLKIEARSVerYKKLHIGMENKIMQLQRKVDEQNKDYKclvEKLTNLEG-----IYNSET-EKLRSDLERLQLSE 999
Cdd:pfam12128  403 REARDRQLAVAEDD--LQALESELREQLEAGKLEFNEEEYRLK---SRLGELKLrlnqaTATPELlLQLENFDERIERAR 477

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1000 EEAKVATGRVLSLQEEIAKLRKDLEQTrsekkciEEHADRYKQETEQLVSNLKEENTLLKQEKEALNHRIVQQAKEMTET 1079
Cdd:pfam12128  478 EEQEAANAEVERLQSELRQARKRRDQA-------SEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEAPDWEQS 550

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1080 MEK--------------KLVEETKQLELDLNDERLRYQNL-LNEFSRLEErydDLKEemtlmvhvpkpghkRTDSTHSSN 1144
Cdd:pfam12128  551 IGKvispellhrtdldpEVWDGSVGGELNLYGVKLDLKRIdVPEWAASEE---ELRE--------------RLDKAEEAL 613

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1145 ESEyifSSEIAEMEdipsrtEEPSEKKVPLD-MSLFLKLQKRVTELEQEKQ-----VMQDELDRKEEQVLRSKAKEEERp 1218
Cdd:pfam12128  614 QSA---REKQAAAE------EQLVQANGELEkASREETFARTALKNARLDLrrlfdEKQSEKDKKNKALAERKDSANER- 683

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1219 qirgaeleyeslkRQELESENKKLKNELNELRKALSEKSApEVTAPGAPAYRVLMEQLtsvSEELDVRKEEVLILRSQLV 1298
Cdd:pfam12128  684 -------------LNSLEAQLKQLDKKHQAWLEEQKEQKR-EARTEKQAYWQVVEGAL---DAQLALLKAAIAARRSGAK 746

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1299 SQKEAIQpKDDKNTMTDSTILLEDVQKMKDKGEIAQAYIGLKETNRSSALDYHElnedgelWLVYEGLKQANRllesqLQ 1378
Cdd:pfam12128  747 AELKALE-TWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFD-------WYQETWLQRRPR-----LA 813

                          490       500
                   ....*....|....*....|...
gi 1836165656 1379 SQKRSHENEAEALRGEIQSLKEE 1401
Cdd:pfam12128  814 TQLSNIERAISELQQQLARLIAD 836
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 949-1119 1.00e-03

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: 42.99  E-value: 1.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  949 MENKIMQLQRKVDEQNKDYKCLVEKLTNLEgiynSETEKLRSDLERLQlsEEEAKVATGRVL-SLQEEIAKLRKDLEQTR 1027
Cdd:COG1579     36 LEDELAALEARLEAAKTELEDLEKEIKRLE----LEIEEVEARIKKYE--EQLGNVRNNKEYeALQKEIESLKRRISDLE 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1028 SEKKCIEEHADRYKQETEQLVSNLKEENTLLKQEKEALNHRIVQQAKEmtetmEKKLVEETKQLELDLNDErlryqnLLN 1107
Cdd:COG1579    110 DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE-----LEELEAEREELAAKIPPE------LLA 178

                          170
                   ....*....|..
gi 1836165656 1108 EFSRLEERYDDL 1119
Cdd:COG1579    179 LYERIRKRKNGL 190
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 950-1122 1.02e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 43.67  E-value: 1.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  950 ENKIMQLQRKVDEQNKDYKCLVEKLTNLegiyNSETEKLRSDLERLQlseeeAKVATgrvlsLQEEIAKLRKDLEQTRSE 1029
Cdd:COG3883     15 DPQIQAKQKELSELQAELEAAQAELDAL----QAELEELNEEYNELQ-----AELEA-----LQAEIDKLQAEIAEAEAE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1030 kkcIEEHADRYKQ----------------------ETEQLVSNLKEENTLLKQEKEALNHriVQQAKEMTETMEKKLVEE 1087
Cdd:COG3883     81 ---IEERREELGEraralyrsggsvsyldvllgseSFSDFLDRLSALSKIADADADLLEE--LKADKAELEAKKAELEAK 155

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1836165656 1088 TKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEE 1122
Cdd:COG3883    156 LAELEALKAELEAAKAELEAQQAEQEALLAQLSAE 190
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 1011-1128 1.19e-03

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 42.20  E-value: 1.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1011 SLQEEIAKLRKDleqtrsekkciEEHADRYKQETEQLVSNLKEENTLLKQEKEALNHRIVQQAKEMTETMEKKlvEETKQ 1090
Cdd:pfam13851   30 SLKEEIAELKKK-----------EERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENYEKDKQSLKNLK--ARLKV 96

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1836165656 1091 LELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMVH 1128
Cdd:pfam13851   97 LEKELKDLKWEHEVLEQRFEKVERERDELYDKFEAAIQ 134
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
982-1236 1.28e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.35  E-value: 1.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  982 NSETEKLRSDLER----LQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQlvsnLKEENTL 1057
Cdd:COG4372     51 REELEQAREELEQleeeLEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE----LQKERQD 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1058 LKQEKEALNHRIVQQAKEMTETMEKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMVHVPKPGHKRT 1137
Cdd:COG4372    127 LEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAE 206

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1138 DSTHSSNESEYIFSSEIAEM-EDIPSRTEEPSEKKVPLDMSLFLKLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEE 1216
Cdd:COG4372    207 KLIESLPRELAEELLEAKDSlEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELE 286

                          250       260
                   ....*....|....*....|
gi 1836165656 1217 RPQIRGAELEYESLKRQELE 1236
Cdd:COG4372    287 ALEEAALELKLLALLLNLAA 306
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
984-1262 1.35e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.88  E-value: 1.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  984 ETEKLRSDLERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSnLKEENTLLkqEKE 1063
Cdd:PRK02224   476 RVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEE-LRERAAEL--EAE 552

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1064 ALNHRivQQAKEMTETMEKKLvEETKQLELDL--NDERL----RYQNLLNEFSRLEERYDDLKEemtlmvhvpkpghKRt 1137
Cdd:PRK02224   553 AEEKR--EAAAEAEEEAEEAR-EEVAELNSKLaeLKERIesleRIRTLLAAIADAEDEIERLRE-------------KR- 615

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1138 dsthssneseyifsSEIAEMEDIP-SRTEEPSEKKVPLDMSLflkLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEE 1216
Cdd:PRK02224   616 --------------EALAELNDERrERLAEKRERKRELEAEF---DEARIEEAREDKERAEEYLEQVEEKLDELREERDD 678

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1836165656 1217 -RPQIRGAELEYESLKrqELESENKKLKNELNELRKALSEKSAPEVT 1262
Cdd:PRK02224   679 lQAEIGAVENELEELE--ELRERREALENRVEALEALYDEAEELESM 723
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 986-1122 1.50e-03

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 43.45  E-value: 1.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  986 EKLRSDLER--------LQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQlvsnlkeentL 1057
Cdd:pfam05262  184 EALREDNEKgvnfrrdmTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQ----------K 253

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1836165656 1058 LKQEKEALNHRIVQQAKEMTETMEKKLVE-ETKQLELDLNDERLRYQNllnefsrlEERYDDLKEE 1122
Cdd:pfam05262  254 QQEAKNLPKPADTSSPKEDKQVAENQKREiEKAQIEIKKNDEEALKAK--------DHKAFDLKQE 311
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 993-1133 1.51e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 43.66  E-value: 1.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  993 ERLQLSE---EEAK-VATGRVLSLQEEIAKL---RKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKE--ENTLLKQEKE 1063
Cdd:PRK00409   495 KRLGLPEniiEEAKkLIGEDKEKLNELIASLeelERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEeeDKLLEEAEKE 574

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1836165656 1064 AlnHRIVQQAKEMTETMEKKLVEETKQLELDLNDerlryQNLLNEFSRLEERYDDLKE---EMTLMVHVPKPG 1133
Cdd:PRK00409   575 A--QQAIKEAKKEADEIIKELRQLQKGGYASVKA-----HELIEARKRLNKANEKKEKkkkKQKEKQEELKVG 640
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 812-834 1.85e-03

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 37.31  E-value: 1.85e-03
                            10        20
                    ....*....|....*....|...
gi 1836165656   812 RMRKAAITMQRYVRGYQARCYAK 834
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRYK 23
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
956-1115 1.90e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 1.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  956 LQRKVDEQNKDYKCLVEKLTNLEgiynSETEKLRSDLERLQlsEEEAKVATGRVLSLQEEIAKLRKDLEQtrsekkcIEE 1035
Cdd:COG4913    293 LEAELEELRAELARLEAELERLE----ARLDALREELDELE--AQIRGNGGDRLEQLEREIERLERELEE-------RER 359

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1036 HADRYkqetEQLVSNLKEENTLLKQEKEALnHRIVQQAKEMTETMEKKLVEETKQLELDLNDERLRYQNLLNEFSRLEER 1115
Cdd:COG4913    360 RRARL----EALLAALGLPLPASAEEFAAL-RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
Paralemmin pfam03285
Paralemmin;
1184-1306 1.97e-03

Paralemmin;


Pssm-ID: 460875  Cd Length: 301  Bit Score: 42.42  E-value: 1.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1184 KRVTELEQEKQvmQDELDRKEEQVLRSKAKEE----ERPQIRGAElEYESLKRQELESENKK---------LKNELNELR 1250
Cdd:pfam03285    5 KRQTEIENKRR--QLEDDRRQLQHLKSKALRErwllEGPPSSASE-EDEARRRQEEEDEQKKklleeiirrLEEEIELLE 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1836165656 1251 KALSEKSAPEvtapgapayrVLMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQP 1306
Cdd:pfam03285   82 EESSISAKKE----------NLAEKLLEITVEKDKVTGETRVLSSTTLLPDDVQPQ 127
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 789-810 2.06e-03

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 37.31  E-value: 2.06e-03
                            10        20
                    ....*....|....*....|..
gi 1836165656   789 KLRAACIRIQKTIRGWLLRKKY 810
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRY 22
PRK12704 PRK12704
phosphodiesterase; Provisional
 995-1128 2.37e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.84  E-value: 2.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  995 LQLSEEEAKVATG-RVLSLQEEIAKLRKDLEQTRSEKkciEEHADRYKQETEQLVSNLKEENTLLKQEKEALNHRIVQQA 1073
Cdd:PRK12704    44 LEEAKKEAEAIKKeALLEAKEEIHKLRNEFEKELRER---RNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELE 120

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1836165656 1074 KEMTETMEKKlvEETKQLELDLNDERLRYQNLLNEFSR---LEERYDDLKEEMTLMVH 1128
Cdd:PRK12704   121 QKQQELEKKE--EELEELIEEQLQELERISGLTAEEAKeilLEKVEEEARHEAAVLIK 176
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 924-1266 3.00e-03

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: 42.25  E-value: 3.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  924 MAKRELKKLKIEArSVERYKKLHIGMENKIMQLQRKVDEqnkdYKCLVEKLTNLEgiynseTEKLRSDLERLQLSEEEAK 1003
Cdd:COG5185    217 SESTLLEKAKEII-NIEEALKGFQDPESELEDLAQTSDK----LEKLVEQNTDLR------LEKLGENAESSKRLNENAN 285

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1004 VATGRVLSLQEEIAKLRKDLEQTRS-EKKCIEEHADRYKQETEQLVSNLKEENTLLKQEkealnhrIVQQAKEMTETMEk 1082
Cdd:COG5185    286 NLIKQFENTKEKIAEYTKSIDIKKAtESLEEQLAAAEAEQELEESKRETETGIQNLTAE-------IEQGQESLTENLE- 357

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1083 KLVEETKQLELDLNDERLRyQNLLNEFSRLEERYDDLKEEMTLMVHVPKPGHKRTDSTHSSNEseyifsSEIAEM----E 1158
Cdd:COG5185    358 AIKEEIENIVGEVELSKSS-EELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAAD------RQIEELqrqiE 430

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1159 DIPSRTEEPSEKKVPLDMSlflkLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKE--EERPQIRGAELEYeslkRQELE 1236
Cdd:COG5185    431 QATSSNEEVSKLLNELISE----LNKVMREADEESQSRLEEAYDEINRSVRSKKEDlnEELTQIESRVSTL----KATLE 502

                          330       340       350
                   ....*....|....*....|....*....|
gi 1836165656 1237 SENKKLKNELNELRKALSEKSAPEVTAPGA 1266
Cdd:COG5185    503 KLRAKLERQLEGVRSKLDQVAESLKDFMRA 532
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 984-1076 3.16e-03

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: 42.06  E-value: 3.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  984 ETEKLRSDLERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQEKE 1063
Cdd:COG4942    151 QAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230

                           90
                   ....*....|...
gi 1836165656 1064 ALNHRIVQQAKEM 1076
Cdd:COG4942    231 RLEAEAAAAAERT 243
CBD_MYO6-like cd21759
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, ...
 791-818 3.36e-03

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


Pssm-ID: 409646 [Multi-domain]  Cd Length: 149  Bit Score: 39.80  E-value: 3.36e-03
                           10        20
                   ....*....|....*....|....*...
gi 1836165656  791 RAACIRIQKTIRGWLLRKKYlRMRKAAI 818
Cdd:cd21759     45 REALIKIQKTVRGYLARKKH-RPRIKGL 71
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
992-1468 3.55e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 3.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  992 LERLQLSEEEAKVATGRVLSLQ-EEIAKLRKDLEQTRSEKKCIEEHADRyKQETEQLVSNLKEENTLLKQEKEALnhRIV 1070
Cdd:COG4717     48 LERLEKEADELFKPQGRKPELNlKELKELEEELKEAEEKEEEYAELQEE-LEELEEELEELEAELEELREELEKL--EKL 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1071 QQAKEMTETMEK---KLVEETKQLElDLNDERLRYQNLLNEFSRLEERYDDLKEEMTlmvhvpkpghkrtdsthssnese 1147
Cdd:COG4717    125 LQLLPLYQELEAleaELAELPERLE-ELEERLEELRELEEELEELEAELAELQEELE----------------------- 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1148 yifsseiAEMEDIPSRTEEPsekkvpldmslFLKLQKRVTELEQEKQVMQDELDRKEEQVlrskakEEERPQIRGAELEY 1227
Cdd:COG4717    181 -------ELLEQLSLATEEE-----------LQDLAEELEELQQRLAELEEELEEAQEEL------EELEEELEQLENEL 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1228 ESLKRQELESENKKLKNELNELRKALSEKSAPEVTAPGAPAYRVLMEQLTSVSEELDVRKEEVL---ILRSQLVSQKEAI 1304
Cdd:COG4717    237 EAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLgkeAEELQALPALEEL 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1305 QPKDDKNTMTDSTILLED-----VQKMKDKGEIAQAYIGLKETNRSSALDYHELNEDgelwlvyEGLKQANRLLESQLQs 1379
Cdd:COG4717    317 EEEELEELLAALGLPPDLspeelLELLDRIEELQELLREAEELEEELQLEELEQEIA-------ALLAEAGVEDEEELR- 388

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1380 QKRSHENEAEALRGEIQSLKEENNRQQQLLAQNLQLPPEARIEASLQheitrltnenlDLMEQLEKQDKTVRKLKKQLKV 1459
Cdd:COG4717    389 AALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELE-----------ELEEELEELEEELEELREELAE 457


                   ....*....
gi 1836165656 1460 FAKKIGELE 1468
Cdd:COG4717    458 LEAELEQLE 466
CBD_MYO6-like cd21759
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, ...
 853-886 3.66e-03

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


Pssm-ID: 409646 [Multi-domain]  Cd Length: 149  Bit Score: 39.80  E-value: 3.66e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1836165656  853 VVRRRYKI--RRAATIVLQSYLRGFLARNRYRKILR 886
Cdd:cd21759     34 VIKLKNKIlyRREALIKIQKTVRGYLARKKHRPRIK 69
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
949-1248 3.90e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 41.43  E-value: 3.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  949 MENKIMQLQRKVDEQNKDYKCLVEKLTNLegiyNSETEKLRsdlERLQLSEEEAKvatgrvlSLQEEIAKLRKDLEQTRS 1028
Cdd:COG1340     20 LREEIEELKEKRDELNEELKELAEKRDEL----NAQVKELR---EEAQELREKRD-------ELNEKVKELKEERDELNE 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1029 EKKCIEEHADRYKQETEQLVSNLKEENTlLKQEKEALNHRivQQAKEMTETMEKKLVEETKQLELDLnDERLRYQNLLNE 1108
Cdd:COG1340     86 KLNELREELDELRKELAELNKAGGSIDK-LRKEIERLEWR--QQTEVLSPEEEKELVEKIKELEKEL-EKAKKALEKNEK 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1109 FSRLEERYDDLKEEMtlmvhvpkpghkrtdSTHSSNESEYifsseiaeMEDIPSRTEEPSEKKVPLDmslflKLQKRVTE 1188
Cdd:COG1340    162 LKELRAELKELRKEA---------------EEIHKKIKEL--------AEEAQELHEEMIELYKEAD-----ELRKEADE 213

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1836165656 1189 LEQEKQVMQDELDRKEEQVLRSKAKEEE-RPQIRGAELEYESLKRQELESENKKLKNELNE 1248
Cdd:COG1340    214 LHKEIVEAQEKADELHEEIIELQKELRElRKELKKLRKKQRALKREKEKEELEEKAEEIFE 274
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1206-1463 3.92e-03

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: 41.67  E-value: 3.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1206 QVLRSKAKEEERPQIRgAELEYESLKRQELESENKKLKNELNELRKALSEKSApevtapgapAYRVLMEQLTSVSEELDV 1285
Cdd:COG4942     18 QADAAAEAEAELEQLQ-QEIAELEKELAALKKEEKALLKQLAALERRIAALAR---------RIRALEQELAALEAELAE 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1286 RKEEVLILRSQLVSQKEAIQPKDDKNTMTDSTILLEDVQKMKDKGEIAQAYIGLKETNRSSALDYHELNEDgelwlvyeg 1365
Cdd:COG4942     88 LEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD--------- 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1366 lKQANRLLESQLQSQKRSHENEAEALRGEIQSLKEENNRQQqllaqnlqlppeaRIEASLQHEITRLTNENLDLMEQLEK 1445
Cdd:COG4942    159 -LAELAALRAELEAERAELEALLAELEEERAALEALKAERQ-------------KLLARLEKELAELAAELAELQQEAEE 224

                          250
                   ....*....|....*...
gi 1836165656 1446 QDKTVRKLKKQLKVFAKK 1463
Cdd:COG4942    225 LEALIARLEAEAAAAAER 242
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
924-1122 4.11e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.81  E-value: 4.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  924 MAKRELKKLKIEARSVERYKKlhiGMENKIMQLQRKVDEQNKDYKCLVEKLTNLEGIYNSETEKLRSDLERLQLSEEEAK 1003
Cdd:COG4372     35 KALFELDKLQEELEQLREELE---QAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAE 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1004 VATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQEKEALNHRIVQQAKEMTETMEKK 1083
Cdd:COG4372    112 ELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKE 191

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1836165656 1084 LVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEE 1122
Cdd:COG4372    192 ANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAK 230
CBD_MYO6-like cd21759
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, ...
 834-861 4.26e-03

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


Pssm-ID: 409646 [Multi-domain]  Cd Length: 149  Bit Score: 39.80  E-value: 4.26e-03
                           10        20
                   ....*....|....*....|....*...
gi 1836165656  834 KFLRRTKAATIIQKYWRMYVVRRRYKIR 861
Cdd:cd21759     40 KILYRREALIKIQKTVRGYLARKKHRPR 67
BMS1 COG5192
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ...
 961-1236 4.44e-03

GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and biogenesis];


Pssm-ID: 227519 [Multi-domain]  Cd Length: 1077  Bit Score: 42.03  E-value: 4.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  961 DEQNKDYKCLVEKLTNLEGIYNSETEKLRSDLErLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQ------TRSEKKCIE 1034
Cdd:COG5192    439 DENEDVDFTGKKGAINNEDESDNEEVAFDSDSQ-FDESEGNLRWKEGLASKLAYSQSGKRGRNIQkifydeSLSPEECIE 517

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1035 EHADRYKQETEQLVSNLKEENTLLKQEKEALNHRIVQQAKEMTETMEkKLVEETKQleLDLNDERLRYQNLLNEFSRLEE 1114
Cdd:COG5192    518 EYKGESAKSSESDLVVQDEPEDFFDVSKVANESISSNHEKLMESEFE-ELKKKWSS--LAQLKSRFQKDATLDSIEGEEE 594

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1115 RYDDLkEEMTLMVHVPKPGHKRTDSTHSSNESEYIFSSEIAEMEDIPSRTEEPSEKKVPLDMSLflklqkrvtELEQEKQ 1194
Cdd:COG5192    595 LIQDD-EKGNFEDLEDEENSSDNEMEESRGSSVTAENEESADEVDYETEREENARKKEELRGNF---------ELEERGD 664

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1836165656 1195 VMQDELDRKEEQvlrsKAKEEErpQIRGAELEYESL---KRQELE 1236
Cdd:COG5192    665 PEKKDVDWYTEE----KRKIEE--QLKINRSEFETMvpeSRVVIE 703
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
1012-1255 4.73e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 41.05  E-value: 4.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1012 LQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEentllkqekealnhrIVQQAKEMTETMeKKLVEETKQl 1091
Cdd:COG1340     13 LEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKE---------------LREEAQELREKR-DELNEKVKE- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1092 eldLNDERlryQNLLNEFSRLEERYDDLKEEMtlmvhvpkpghkrtDSTHSSNESEYIFSSEIAEMEDipsrteepsekk 1171
Cdd:COG1340     76 ---LKEER---DELNEKLNELREELDELRKEL--------------AELNKAGGSIDKLRKEIERLEW------------ 123

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1172 vpldmslflKLQKRVTELEQEKQVMqDELDRKEEQVLRSKAKEEERPQIRGAELEYESLKRQ--ELESENKKLKNELNEL 1249
Cdd:COG1340    124 ---------RQQTEVLSPEEEKELV-EKIKELEKELEKAKKALEKNEKLKELRAELKELRKEaeEIHKKIKELAEEAQEL 193


                   ....*.
gi 1836165656 1250 RKALSE 1255
Cdd:COG1340    194 HEEMIE 199
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 967-1109 5.57e-03

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


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 41.02  E-value: 5.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  967 YKCLVEKLTNLEGIYNSETEKLRSDLERLQL------SEEEAKVATGRVLSLQE-EIAKLRKDLEQTRSEKKCIEEHADR 1039
Cdd:cd16269    144 YQLYLEDREKLVEKYRQVPRKGVKAEEVLQEflqskeAEAEAILQADQALTEKEkEIEAERAKAEAAEQERKLLEEQQRE 223

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1040 YKQETEQLVSNLKEENTLLKQEKEAlnhRIVQQAKEMTETMEKKLVEETKQLELDLNDERLRYQNLLNEF 1109
Cdd:cd16269    224 LEQKLEDQERSYEEHLRQLKEKMEE---ERENLLKEQERALESKLKEQEALLEEGFKEQAELLQEEIRSL 290
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 886-907 6.69e-03

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 35.76  E-value: 6.69e-03
                            10        20
                    ....*....|....*....|..
gi 1836165656   886 REHKAVIIQKRVRGWLARTHYK 907
Cdd:smart00015    2 LTRAAIIIQAAWRGYLARKRYK 23
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 912-1258 6.76e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 41.36  E-value: 6.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  912 AIIYLQCCFRRMMAKRELKKLKIEARSV----ERYKKLH-IGmenkimQLQRKVDEQNKDYKCLV-EKLTNLEG-IYNSE 984
Cdd:PRK04778    19 AGLILRKRNYKRIDELEERKQELENLPVndelEKVKKLNlTG------QSEEKFEEWRQKWDEIVtNSLPDIEEqLFEAE 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  985 --TEKLRSDLERLQLSEEEAKVAT--GRVLSLQEEIAKLRKDLEQTRSE-----------KKCIEEHADRYKQETEQLVS 1049
Cdd:PRK04778    93 elNDKFRFRKAKHEINEIESLLDLieEDIEQILEELQELLESEEKNREEveqlkdlyrelRKSLLANRFSFGPALDELEK 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1050 NLKEENTLLKQ---EKEALNH----RIVQQAKEMTETMEKKlVEETKQLELDLNDE--------------------RLRY 1102
Cdd:PRK04778   173 QLENLEEEFSQfveLTESGDYvearEILDQLEEELAALEQI-MEEIPELLKELQTElpdqlqelkagyrelveegyHLDH 251

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1103 QNLLNEFSRLEERYDDLKEEMtlmvhvpkpghKRTDSTHSSNESEYIfSSEIAEMEDIpSRTEEPSEKKVpldMSLFLKL 1182
Cdd:PRK04778   252 LDIEKEIQDLKEQIDENLALL-----------EELDLDEAEEKNEEI-QERIDQLYDI-LEREVKARKYV---EKNSDTL 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1183 QKRVTELEQEKQVMQDELDR-------KEEQVLRSKAKEEERPQIRG--------------------AELEYESLKRQEL 1235
Cdd:PRK04778   316 PDFLEHAKEQNKELKEEIDRvkqsytlNESELESVRQLEKQLESLEKqydeiteriaeqeiayselqEELEEILKQLEEI 395

                          410       420
                   ....*....|....*....|...
gi 1836165656 1236 ESENKKLKNELNELRKalSEKSA 1258
Cdd:PRK04778   396 EKEQEKLSEMLQGLRK--DELEA 416
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 928-1126 6.82e-03

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: 40.95  E-value: 6.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  928 ELKKL--KIEARSVERYKKlHIGMENKIMQLQRKVDEQNKDYKCLVEKLTNLEGIYN---SETEKLRSDLERLQlseeea 1002
Cdd:pfam15905  160 ELMKLrnKLEAKMKEVMAK-QEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIeekSETEKLLEYITELS------ 232

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1003 kvatgrvlSLQEEIAKLRKDLEQtrsekkcIEEHADRYKQETEQLVSNLKEENTLLKqekealnhrivQQAKEMTETMek 1082
Cdd:pfam15905  233 --------CVSEQVEKYKLDIAQ-------LEELLKEKNDEIESLKQSLEEKEQELS-----------KQIKDLNEKC-- 284

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1836165656 1083 KLVEetKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLM 1126
Cdd:pfam15905  285 KLLE--SEKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKL 326
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
949-1042 6.84e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 41.38  E-value: 6.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  949 MENKIMQLQRKVDE---QNKDYKCLVEKLtnlegiyNSETEKLRSDLERLQlSEEEAKVATGRVLS-LQEEIAKLRKDLE 1024
Cdd:COG2433    411 EEEEIRRLEEQVERleaEVEELEAELEEK-------DERIERLERELSEAR-SEERREIRKDREISrLDREIERLERELE 482

                           90
                   ....*....|....*...
gi 1836165656 1025 QTRSEKKCIEEHADRYKQ 1042
Cdd:COG2433    483 EERERIEELKRKLERLKE 500
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
923-1257 7.07e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.18  E-value: 7.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  923 MMAKRELKKLKIEARSVERYKklhigMENKIMQLQRKVDEQ-------NKDYKCLVEKLTNLEgiynSETEKLRSDLERL 995
Cdd:PRK02224   298 LLAEAGLDDADAEAVEARREE-----LEDRDEELRDRLEECrvaaqahNEEAESLREDADDLE----ERAEELREEAAEL 368

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656  996 QLSEEEAKVAT----GRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQEKEAL--NHRI 1069
Cdd:PRK02224   369 ESELEEAREAVedrrEEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVeeAEAL 448

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1070 VQQAK-----------EMTETMEKKLvEETKQLELDLNDERLryqnllnEFSRLEERYDDLKEEMTLMVHVPKPGHKRTD 1138
Cdd:PRK02224   449 LEAGKcpecgqpvegsPHVETIEEDR-ERVEELEAELEDLEE-------EVEEVEERLERAEDLVEAEDRIERLEERRED 520

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836165656 1139 SthssneseyifSSEIAEMEDipsRTEEPSEKKVpldmslflKLQKRVTELEQEKQVMQDELDRKEEQV--LRSKAKEEE 1216
Cdd:PRK02224   521 L-----------EELIAERRE---TIEEKRERAE--------ELRERAAELEAEAEEKREAAAEAEEEAeeAREEVAELN 578

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1836165656 1217 RpqiRGAEL--EYESLKR------------QELESENKKLKN--ELNELRK-ALSEKS 1257
Cdd:PRK02224   579 S---KLAELkeRIESLERirtllaaiadaeDEIERLREKREAlaELNDERReRLAEKR 633
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH