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Conserved domains on  [gi|1677538261|ref|NP_001135967|]
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unconventional myosin-Va isoform 2 [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

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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 ...
 83-751 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: 1319.08  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   83 PAVLHNLRVRFIDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd01380      1 PAVLHNLKVRFCQRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  163 GESGAGKTVSAKYAMRYFATVSGSAS-EANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRT 241
Cdd:cd01380     81 GESGAGKTVSAKYAMRYFATVGGSSSgETQVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANMRT 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  242 YLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQACTLLGISESH 321
Cdd:cd01380    161 YLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPVIDGVDDAAEFEETRKALTLLGISEEE 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  322 QMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNARD 401
Cdd:cd01380    241 QMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQAIVARD 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  402 ALAKHIYAKLFNWIVDNVNQALHSAV--KQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMK 479
Cdd:cd01380    321 ALAKHIYAQLFDWIVDRINKALASPVkeKQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQEEYVK 400

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  480 EQIPWTLIDFYDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNK-CALFEKPRLSNKAFIIQHFADKVE 558
Cdd:cd01380    401 EEIEWSFIDFYDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKpNKHFKKPRFSNTAFIVKHFADDVE 480

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  559 YQCEGFLEKNKDTVFEEQIKVLKSSKFkmlpelfqddekaisptsatssgrtpltrtpakptkgrpgqmakeHKKTVGHQ 638
Cdd:cd01380    481 YQVEGFLEKNRDTVSEEHLNVLKASKN---------------------------------------------RKKTVGSQ 515

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  639 FRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMKQKD 718
Cdd:cd01380    516 FRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSKE 595

                          650       660       670
                   ....*....|....*....|....*....|....
gi 1677538261  719 VL-SDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd01380    596 WLrDDKKKTCENILENLILDPDKYQFGKTKIFFR 629
Myo5a_CBD cd15478
Cargo binding domain of myosin 5a; Class V myosins are well studied unconventional myosins, ...
 1454-1828 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: 721.82  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1454 KEDEQKLVKNLILELKPRGVAVNLIPGLPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSN 1533
Cdd:cd15478      1 KEDEQKLVKNLILELKPRGVAVNLIPGLPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1534 TCRFLHCLKQYSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPMIVSGMLEHETIQGVSG 1613
Cdd:cd15478     81 TCRFLHCLKQYSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPMIVSGMLEHETIQGVSG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1614 VKPTGLRKRTSSIADEGTYTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQIR 1693
Cdd:cd15478    161 VKPTGLRKRTSSIADEGTYTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQIR 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1694 YNVSQLEEWLRDKNLMNSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERVSVSF 1773
Cdd:cd15478    241 YNVSQLEEWLRDKNLMNSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERVSVSF 320

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1677538261 1774 IRTIQMRLRDRKDSPQLLMDAKHIFPVTFPFNPSSLALETIQIPASLGLGFISRV 1828
Cdd:cd15478    321 IRTIQMRLRDRKDSPQLLMDAKHIFPVTFPFNPSSLALETIQIPASLGLGFISRV 375
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 902-1281 6.06e-16

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: 84.34  E-value: 6.06e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  902 KRELKKLKIEARSVERYKKLHigmeNKIMQLQRKVdeQNKDYKCLVEKLTNLEGIYNSETEKLRSDLERLQLSEEEAKVA 981
Cdd:TIGR02168  199 ERQLKSLERQAEKAERYKELK----AELRELELAL--LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEEL 272

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  982 TGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQekealnhriVQQAKEMTETMEKKLV 1061
Cdd:TIGR02168  273 RLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE---------LESKLDELAEELAELE 343

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1062 EETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTlmvhvpkpghKRTDSTHSSNESEYIFSSEI----AEMEDIP 1137
Cdd:TIGR02168  344 EKLEELKEELESLEAELEELEAELEELESRLEELEEQLE----------TLRSKVAQLELQIASLNNEIerleARLERLE 413

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1138 SRTEEPSEKKVPLDMSL----FLKLQKRVTELEQEKQVMQDELDRKEEQvlrskaKEEERPQIRGAELEYESLKRQELES 1213
Cdd:TIGR02168  414 DRRERLQQEIEELLKKLeeaeLKELQAELEELEEELEELQEELERLEEA------LEELREELEEAEQALDAAERELAQL 487

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1677538261 1214 ENKK--LKNELNELRKALSEKSAPEVTAPGAPAYRVLMEQLTSVSEELDVRKEEVLILRSQLV------SQKEAIQ 1281
Cdd:TIGR02168  488 QARLdsLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVvvenlnAAKKAIA 563
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 813-835 1.78e-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: 1.78e-06
                            10        20
                    ....*....|....*....|...
gi 1677538261   813 RRTKAATIIQKYWRMYVVRRRYK 835
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRYK 23
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 1158-1417 6.71e-06

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.


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 51.22  E-value: 6.71e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1158 LQKRVTELEQEK------QVMQDELdRKEEQVLRSKAKEEERPQIRGAELEYESLKRQ--ELESENKKLKNELNELRKAL 1229
Cdd:TIGR02169  196 KRQQLERLRRERekaeryQALLKEK-REYEGYELLKEKEALERQKEAIERQLASLEEEleKLTEEISELEKRLEEIEQLL 274

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1230 SEKSApEVTAPGAPAYRVLMEQLTSVSEEL-------DVRKEEVLILRSQLVSQKEAIQPKddKNTMTDSTILLEDVQKM 1302
Cdd:TIGR02169  275 EELNK-KIKDLGEEEQLRVKEKIGELEAEIaslersiAEKERELEDAEERLAKLEAEIDKL--LAEIEELEREIEEERKR 351

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1303 KDKgeIAQAYIGLKETNRLLESQLQSQkrshENEAEALRGEIQSLKEEnnrqqqllaqnlqlppearIEAsLQHEITRLT 1382
Cdd:TIGR02169  352 RDK--LTEEYAELKEELEDLRAELEEV----DKEFAETRDELKDYREK-------------------LEK-LKREINELK 405

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1677538261 1383 NENLDLMEQLEKQDKTVRKLKKQLKVFAKKIGELE 1417
Cdd:TIGR02169  406 RELDRLQEELQRLSEELADLNAAIAGIEAKINELE 440
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 788-810 1.91e-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: 1.91e-03
                            10        20
                    ....*....|....*....|...
gi 1677538261   788 RMRKAAITMQRYVRGYQARCYAK 810
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRYK 23
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 765-786 2.10e-03

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


:

Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 36.92  E-value: 2.10e-03
                            10        20
                    ....*....|....*....|..
gi 1677538261   765 KLRAACIRIQKTIRGWLLRKKY 786
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRY 22
CBD_MYO6-like super family cl41207
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, ...
 829-862 3.63e-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: 3.63e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1677538261  829 VVRRRYKI--RRAATIVLQSYLRGFLARNRYRKILR 862
Cdd:cd21759     34 VIKLKNKIlyRREALIKIQKTVRGYLARKKHRPRIK 69
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 862-883 6.90e-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: 6.90e-03
                            10        20
                    ....*....|....*....|..
gi 1677538261   862 REHKAVIIQKRVRGWLARTHYK 883
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 ...
 83-751 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: 1319.08  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   83 PAVLHNLRVRFIDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd01380      1 PAVLHNLKVRFCQRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  163 GESGAGKTVSAKYAMRYFATVSGSAS-EANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRT 241
Cdd:cd01380     81 GESGAGKTVSAKYAMRYFATVGGSSSgETQVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANMRT 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  242 YLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQACTLLGISESH 321
Cdd:cd01380    161 YLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPVIDGVDDAAEFEETRKALTLLGISEEE 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  322 QMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNARD 401
Cdd:cd01380    241 QMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQAIVARD 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  402 ALAKHIYAKLFNWIVDNVNQALHSAV--KQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMK 479
Cdd:cd01380    321 ALAKHIYAQLFDWIVDRINKALASPVkeKQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQEEYVK 400

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  480 EQIPWTLIDFYDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNK-CALFEKPRLSNKAFIIQHFADKVE 558
Cdd:cd01380    401 EEIEWSFIDFYDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKpNKHFKKPRFSNTAFIVKHFADDVE 480

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  559 YQCEGFLEKNKDTVFEEQIKVLKSSKFkmlpelfqddekaisptsatssgrtpltrtpakptkgrpgqmakeHKKTVGHQ 638
Cdd:cd01380    481 YQVEGFLEKNRDTVSEEHLNVLKASKN---------------------------------------------RKKTVGSQ 515

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  639 FRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMKQKD 718
Cdd:cd01380    516 FRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSKE 595

                          650       660       670
                   ....*....|....*....|....*....|....
gi 1677538261  719 VL-SDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd01380    596 WLrDDKKKTCENILENLILDPDKYQFGKTKIFFR 629
Myosin_head pfam00063
Myosin head (motor domain);
72-751 0e+00

Myosin head (motor domain);


Pssm-ID: 395017 [Multi-domain]  Cd Length: 674  Bit Score: 1078.45  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   72 NDLTALSYLHEPAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMA 151
Cdd:pfam00063    2 EDMVELSYLNEPSVLHNLKKRY-KSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  152 RDERNQSIIVSGESGAGKTVSAKYAMRYFATVSGSASEAN---VEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGF 228
Cdd:pfam00063   81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGNvgrLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQF 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  229 DKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHT 308
Cdd:pfam00063  161 DAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQSGCYTIDGIDDSEEFKIT 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  309 RQACTLLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATETYI 388
Cdd:pfam00063  241 DKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGRETVS 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  389 KPISKLQATNARDALAKHIYAKLFNWIVDNVNQALHS-AVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNM 467
Cdd:pfam00063  321 KPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVkTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQFFNH 400

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  468 HVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNTHlNKCALFEKPRL-SN 545
Cdd:pfam00063  401 HMFKLEQEEYVREGIEWTFIDFGDNQPCIDLIEKKpLGILSLLDEECLFPKATDQTFLDKLYSTF-SKHPHFQKPRLqGE 479

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  546 KAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGRTPltrtpaKPTKgrpg 625
Cdd:pfam00063  480 THFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGKSTP------KRTK---- 549

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  626 qmaKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQE 705
Cdd:pfam00063  550 ---KKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQE 626

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*...
gi 1677538261  706 FFSRYRVLMKQKDV--LSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:pfam00063  627 FVQRYRILAPKTWPkwKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
MYSc smart00242
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...
 64-762 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: 1018.24  E-value: 0e+00
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261    64 NPDILVGENDLTALSYLHEPAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVA 143
Cdd:smart00242    1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRY-LKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIA 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   144 EEAYKQMARDERNQSIIVSGESGAGKTVSAKYAMRYFATVSGSASEAN-VEEKVLASNPIMESIGNAKTTRNDNSSRFGK 222
Cdd:smart00242   80 DNAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEVGsVEDQILESNPILEAFGNAKTLRNNNSSRFGK 159

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   223 YIEIGFDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDA 302
Cdd:smart00242  160 FIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQGGCLTVDGIDDA 239

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   303 KEMAHTRQACTLLGISESHQMGIFRILAGILHLGNVGFTSRDAD-SCTIPPKHEPLCIFCELMGVDYEEMCHWLCHRKLA 381
Cdd:smart00242  240 EEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDnAASTVKDKEELSNAAELLGVDPEELEKALTKRKIK 319

                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   382 TATETYIKPISKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKL 461
Cdd:smart00242  320 TGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSFEQLCINYANEKL 399

                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   462 QQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEK 540
Cdd:smart00242  400 QQFFNQHVFKLEQEEYEREGIDWTFIDFFDNQDCIDLIEKKpPGILSLLDEECRFPKGTDQTFLEKLNQHHKKHPHFSKP 479

                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   541 PRLSNKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEkaispTSATSSGRtpltrtpakpt 620
Cdd:smart00242  480 KKKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGV-----SNAGSKKR----------- 543

                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   621 kgrpgqmakehKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSR 700
Cdd:smart00242  544 -----------FQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYR 612

                           650       660       670       680       690       700
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1677538261   701 WTYQEFFSRYRVLMKQK--DVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFRAGQVAYLEKLR 762
Cdd:smart00242  613 LPFDEFLQRYRVLLPDTwpPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELR 676
COG5022 COG5022
Myosin heavy chain [General function prediction only];
7-1233 0e+00

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 969.16  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261    7 YTKFARVWIPDPEEVWKSAELLK-DYKPGDKVLLLHLEEGK--DLEYHLDPKTKelphlRNPDILVGENDLTALSYLHEP 83
Cdd:COG5022      6 AEVGSGCWIPDEEKGWIWAEIIKeAFNKGKVTEEGKKEDGEsvSVKKKVLGNDR-----IKLPKFDGVDDLTELSYLNEP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   84 AVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:COG5022     81 AVLHNLEKRY-NNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISG 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  164 ESGAGKTVSAKYAMRYFATVSGSASE--ANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRT 241
Cdd:COG5022    160 ESGAGKTENAKRIMQYLASVTSSSTVeiSSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIET 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  242 YLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQACTLLGISESH 321
Cdd:COG5022    240 YLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDKIDGIDDAKEFKITLDALKTIGIDEEE 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  322 QMGIFRILAGILHLGNVGFTSrDADSCTIPPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNARD 401
Cdd:COG5022    320 QDQIFKILAAILHIGNIEFKE-DRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRD 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  402 ALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQ 481
Cdd:COG5022    399 SLAKALYSNLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEG 478

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  482 IPWTLIDFYDNQPCINLIESK--LGILDLLDEECKMPKGTDDTWAQKLYNT-HLNKCALFEKPRLSNKAFIIQHFADKVE 558
Cdd:COG5022    479 IEWSFIDYFDNQPCIDLIEKKnpLGILSLLDEECVMPHATDESFTSKLAQRlNKNSNPKFKKSRFRDNKFVVKHYAGDVE 558

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  559 YQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKaisptsatssgrtpltrtpaKPTKGRPgqmakehkKTVGHQ 638
Cdd:COG5022    559 YDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEEN--------------------IESKGRF--------PTLGSR 610

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  639 FRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMKQK- 717
Cdd:COG5022    611 FKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKs 690

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  718 -----DVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFRAGQVAYLEKLRADKLRAACIRIQKTIRGWLLRKKYLRMRKA 792
Cdd:COG5022    691 wtgeyTWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKR 770

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  793 AITMQRYVRGYQARCYAKFLRRTKAATIIQKYWRMYVVRRRYKIRRAATIVLQSYL-RGFLARNRYRKILREHKAVIIQK 871
Cdd:COG5022    771 IKKIQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIkREKKLRETEEVEFSLKAEVLIQK 850

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  872 RVRGWLARTHYKRSMHAIIYLQCCFRRMMAKRELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQ-NKDYKCLVEKL 950
Cdd:COG5022    851 FGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKKSLSSDlIENLEFKTELI 930

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  951 TNLEGIYNSETEKLRSDLERLQLSEeeakvatgrVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEE 1030
Cdd:COG5022    931 ARLKKLLNNIDLEEGPSIEYVKLPE---------LNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKEL 1001

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1031 NTLLKQ------EKEALNHRIVQQAKEMTETMEKKLVEETKQLELDLNDERlryQNLLNEFSRLEERYDDLKeemtlmvh 1104
Cdd:COG5022   1002 AELSKQygalqeSTKQLKELPVEVAELQSASKIISSESTELSILKPLQKLK---GLLLLENNQLQARYKALK-------- 1070

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1105 VPKPGHKRTDSTHSSNESEYIFSSEI----AEMEDIPSRTEEPSEKKVPLDMSLFLKLQKRVTELEQ-----EKQVMQDE 1175
Cdd:COG5022   1071 LRRENSLLDDKQLYQLESTENLLKTInvkdLEVTNRNLVKPANVLQFIVAQMIKLNLLQEISKFLSQlvntlEPVFQKLS 1150

                         1210      1220      1230      1240      1250      1260
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1176 LDRKEEQVLRSKAKEEERPQIRGAELEYESLKRQE--LESENKKLKNELNELRKALSEKS 1233
Cdd:COG5022   1151 VLQLELDGLFWEANLEALPSPPPFAALSEKRLYQSalYDEKSKLSSSEVNDLKNELIALF 1210
Myo5a_CBD cd15478
Cargo binding domain of myosin 5a; Class V myosins are well studied unconventional myosins, ...
 1454-1828 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: 721.82  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1454 KEDEQKLVKNLILELKPRGVAVNLIPGLPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSN 1533
Cdd:cd15478      1 KEDEQKLVKNLILELKPRGVAVNLIPGLPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1534 TCRFLHCLKQYSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPMIVSGMLEHETIQGVSG 1613
Cdd:cd15478     81 TCRFLHCLKQYSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPMIVSGMLEHETIQGVSG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1614 VKPTGLRKRTSSIADEGTYTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQIR 1693
Cdd:cd15478    161 VKPTGLRKRTSSIADEGTYTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQIR 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1694 YNVSQLEEWLRDKNLMNSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERVSVSF 1773
Cdd:cd15478    241 YNVSQLEEWLRDKNLMNSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERVSVSF 320

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1677538261 1774 IRTIQMRLRDRKDSPQLLMDAKHIFPVTFPFNPSSLALETIQIPASLGLGFISRV 1828
Cdd:cd15478    321 IRTIQMRLRDRKDSPQLLMDAKHIFPVTFPFNPSSLALETIQIPASLGLGFISRV 375
PTZ00014 PTZ00014
myosin-A; Provisional
 34-798 1.48e-141

myosin-A; Provisional


Pssm-ID: 240229 [Multi-domain]  Cd Length: 821  Bit Score: 460.27  E-value: 1.48e-141
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   34 GDKVLLLHLEEGKDLEYHLDPKtkelpHLRNPDILVGEN---DLTALSYLHEPAVLHNLRVRFIdSKLIYTYCGIVLVAI 110
Cdd:PTZ00014    63 GEKLTLKQIDPPTNSTFEVKPE-----HAFNANSQIDPMtygDIGLLPHTNIPCVLDFLKHRYL-KNQIYTTADPLLVAI 136

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  111 NPYEQLPIYGEDIINAY-SGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSGESGAGKTVSAKYAMRYFATVSGSASE 189
Cdd:PTZ00014   137 NPFKDLGNTTNDWIRRYrDAKDSDKLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFASSKSGNMD 216

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  190 ANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLC--A 267
Cdd:PTZ00014   217 LKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLkgA 296

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  268 SAKLPE-FKMLRLGNADNFNytkqGGSPVIEGVDDAKEMAHTRQACTLLGISESHQMGIFRILAGILHLGNVGFTSRDAD 346
Cdd:PTZ00014   297 NDEMKEkYKLKSLEEYKYIN----PKCLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEG 372

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  347 -----SCTIPPKHEPLCIFCELMGVDYEEMCHWLchrklaTATETYI------KPISKLQATNARDALAKHIYAKLFNWI 415
Cdd:PTZ00014   373 gltdaAAISDESLEVFNEACELLFLDYESLKKEL------TVKVTYAgnqkieGPWSKDESEMLKDSLSKAVYEKLFLWI 446

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  416 VDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPC 495
Cdd:PTZ00014   447 IRNLNATIEPPGGFKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGISTEELEYTSNESV 526

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  496 INLIESKL-GILDLLDEECKMPKGTDD----TWAQKLYNthlNKCALFEKpRLSNKAFIIQHFADKVEYQCEGFLEKNKD 570
Cdd:PTZ00014   527 IDLLCGKGkSVLSILEDQCLAPGGTDEkfvsSCNTNLKN---NPKYKPAK-VDSNKNFVIKHTIGDIQYCASGFLFKNKD 602

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  571 TVFEEQIKVLKSSKFKMLPELFQDDEkaisptsatssgrtpLTRtpakptkgrpGQMAKehKKTVGHQFRNSLHLLMETL 650
Cdd:PTZ00014   603 VLRPELVEVVKASPNPLVRDLFEGVE---------------VEK----------GKLAK--GQLIGSQFLNQLDSLMSLI 655

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  651 NATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRV--LMKQKDVLSDRKQTCK 728
Cdd:PTZ00014   656 NSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYldLAVSNDSSLDPKEKAE 735

                          730       740       750       760       770       780       790
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1677538261  729 NVLEKLILDKDKYQFGKTKIFFRAGQVAYLEKLRADKLRA--ACIRIqktIRGWLLRKKYLR-MRKAAITMQR 798
Cdd:PTZ00014   736 KLLERSGLPKDSYAIGKTMVFLKKDAAKELTQIQREKLAAwePLVSV---LEALILKIKKKRkVRKNIKSLVR 805
DIL pfam01843
DIL domain; The DIL domain has no known function.
 1660-1763 2.89e-42

DIL domain; The DIL domain has no known function.


Pssm-ID: 460359 [Multi-domain]  Cd Length: 103  Bit Score: 150.05  E-value: 2.89e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1660 QVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQIRYNVSQLEEWLRDKNLmNSGAKETLEPLIQAAQLLQVKKKTDDDAEA 1739
Cdd:pfam01843    1 QLFSQLFYFINAELFNRLLLRKKYCSWSKGMQIRYNLSRLEEWARSNGL-ESEARDHLAPLIQAAQLLQLRKSTLEDLDS 79

                           90       100
                   ....*....|....*....|....
gi 1677538261 1740 ICSMCNALTTAQIVKVLNLYTPVN 1763
Cdd:pfam01843   80 ILQVCPALNPLQLHRLLTLYQPDD 103
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 902-1281 6.06e-16

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: 84.34  E-value: 6.06e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  902 KRELKKLKIEARSVERYKKLHigmeNKIMQLQRKVdeQNKDYKCLVEKLTNLEGIYNSETEKLRSDLERLQLSEEEAKVA 981
Cdd:TIGR02168  199 ERQLKSLERQAEKAERYKELK----AELRELELAL--LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEEL 272

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  982 TGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQekealnhriVQQAKEMTETMEKKLV 1061
Cdd:TIGR02168  273 RLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE---------LESKLDELAEELAELE 343

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1062 EETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTlmvhvpkpghKRTDSTHSSNESEYIFSSEI----AEMEDIP 1137
Cdd:TIGR02168  344 EKLEELKEELESLEAELEELEAELEELESRLEELEEQLE----------TLRSKVAQLELQIASLNNEIerleARLERLE 413

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1138 SRTEEPSEKKVPLDMSL----FLKLQKRVTELEQEKQVMQDELDRKEEQvlrskaKEEERPQIRGAELEYESLKRQELES 1213
Cdd:TIGR02168  414 DRRERLQQEIEELLKKLeeaeLKELQAELEELEEELEELQEELERLEEA------LEELREELEEAEQALDAAERELAQL 487

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1677538261 1214 ENKK--LKNELNELRKALSEKSAPEVTAPGAPAYRVLMEQLTSVSEELDVRKEEVLILRSQLV------SQKEAIQ 1281
Cdd:TIGR02168  488 QARLdsLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVvvenlnAAKKAIA 563
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 927-1407 1.56e-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: 75.91  E-value: 1.56e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  927 NKIMQLQRKVDEQNKDYKCLVEKLTNLegiyNSETEKLRSDLER----LQLSEEEAKVATGRVLSLQEEIAKLRKDLEQT 1002
Cdd:pfam05483  268 DKANQLEEKTKLQDENLKELIEKKDHL----TKELEDIKMSLQRsmstQKALEEDLQIATKTICQLTEEKEAQMEELNKA 343

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1003 RSEKKCIeehADRYKQETEQLVSNLKEENTLLKQEKEALNHRIVQQAKEMTETMEKKLVEETKQLELD------LNDERL 1076
Cdd:pfam05483  344 KAAHSFV---VTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEelkkilAEDEKL 420

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1077 RYQNllNEFSRLEERYDDLKEEMTLMVHV-PKPGHKRTDSTHSSNESEYIFSSEIAEMedipsRTEEPSEKKVPLDMSLF 1155
Cdd:pfam05483  421 LDEK--KQFEKIAEELKGKEQELIFLLQArEKEIHDLEIQLTAIKTSEEHYLKEVEDL-----KTELEKEKLKNIELTAH 493

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1156 L-KLQKRVTELEQEKQVMQDELDRKEEQVLRSKaKEEER--PQIRGAElEYESLKRQELESENKKLKNELNELRKAL--S 1230
Cdd:pfam05483  494 CdKLLLENKELTQEASDMTLELKKHQEDIINCK-KQEERmlKQIENLE-EKEMNLRDELESVREEFIQKGDEVKCKLdkS 571

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1231 EKSAPEVTAPGAPAY-------------------------------RVLMEQLTSVSEELDVRKEEVLILRSQLVSQKEA 1279
Cdd:pfam05483  572 EENARSIEYEVLKKEkqmkilenkcnnlkkqienknknieelhqenKALKKKGSAENKQLNAYEIKVNKLELELASAKQK 651

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1280 IQPKDD--KNTMTDSTI----LLEDVQKMK---DKGEIAQAYIGLKETNRLLESQLQSQKRSHE-----NEAEALRGEIQ 1345
Cdd:pfam05483  652 FEEIIDnyQKEIEDKKIseekLLEEVEKAKaiaDEAVKLQKEIDKRCQHKIAEMVALMEKHKHQydkiiEERDSELGLYK 731

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1677538261 1346 SLKEEnnrqqqllaqnlqlppEARIEASLQHEITRLTNENLDLMEQLEKQDKTVRKLKKQLK 1407
Cdd:pfam05483  732 NKEQE----------------QSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAK 777
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 902-1286 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 1677538261  902 KRELKKLKIEARSVERYKKLHIGMEnkimqlQRKVDEQNKDYKCLVEKLTNLEGIYNSETEKLRSDLERLQLSEEEAKVA 981
Cdd:COG1196    199 ERQLEPLERQAEKAERYRELKEELK------ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEEL 272

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  982 TGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEentlLKQEKEALNHRIVQQAKEMTETMEKKLV 1061
Cdd:COG1196    273 RLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE----LEEELAELEEELEELEEELEELEEELEE 348

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1062 EETK--QLELDLNDERLRYQNLLNEFSRLEERYDDLKEEmtlmvhvpkpghkrtdsthssneseyiFSSEIAEMEDIPSR 1139
Cdd:COG1196    349 AEEEleEAEAELAEAEEALLEAEAELAEAEEELEELAEE---------------------------LLEALRAAAELAAQ 401

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1140 TEEPSEKKvpldmslfLKLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEErpqiRGAELEYESLKRQELESENKKLK 1219
Cdd:COG1196    402 LEELEEAE--------EALLERLERLEEELEELEEALAELEEEEEEEEEALEE----AAEEEAELEEEEEALLELLAELL 469

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1677538261 1220 NELNELRKALSEKSAPEVTApgAPAYRVLMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQPKDDK 1286
Cdd:COG1196    470 EEAALLEAALAELLEELAEA--AARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEA 534
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
942-1417 3.41e-12

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 71.63  E-value: 3.41e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  942 DYKCLVEKLTNLEGIYNSETEKLRSDLERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKqETE 1021
Cdd:PRK03918   159 DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE-ELK 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1022 QLVSNLKEENTLLKQEKEALNHRIVQqakemTETMEKKLVEETKQLEldlndERLRYqnlLNEFSRLEERYDDLKEEMTL 1101
Cdd:PRK03918   238 EEIEELEKELESLEGSKRKLEEKIRE-----LEERIEELKKEIEELE-----EKVKE---LKELKEKAEEYIKLSEFYEE 304

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1102 MVHVPKPGHKRTDSTHSSNESeyiFSSEIAEMEDIPSRTEEPSEKKVpldmslflKLQKRVTELEQEKQVMQDELDRKEE 1181
Cdd:PRK03918   305 YLDELREIEKRLSRLEEEING---IEERIKELEEKEERLEELKKKLK--------ELEKRLEELEERHELYEEAKAKKEE 373

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1182 -QVLRSKAKEEERPQIRgAELEYESLKRQELESENKK-------LKNELNELRKALSEKSAPEVTAP--GAP-------- 1243
Cdd:PRK03918   374 lERLKKRLTGLTPEKLE-KELEELEKAKEEIEEEISKitarigeLKKEIKELKKAIEELKKAKGKCPvcGRElteehrke 452

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1244 ---AYRVLMEQLTSVSEELDVRKEEVLI----LRSQLVSQKEAIQPKddknTMTDSTILLEDVQKMKDKGEIAQA---YI 1313
Cdd:PRK03918   453 lleEYTAELKRIEKELKEIEEKERKLRKelreLEKVLKKESELIKLK----ELAEQLKELEEKLKKYNLEELEKKaeeYE 528

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1314 GLKETNRLLESQLQSQKRS------HENEAEALRGEIQSLKEEN---NRQQQLLAQNLQLPPEARIEA--SLQHEITRLT 1382
Cdd:PRK03918   529 KLKEKLIKLKGEIKSLKKElekleeLKKKLAELEKKLDELEEELaelLKELEELGFESVEELEERLKElePFYNEYLELK 608

                          490       500       510
                   ....*....|....*....|....*....|....*
gi 1677538261 1383 NENLDLMEQLEKQDKTVRKLKKQLKVFAKKIGELE 1417
Cdd:PRK03918   609 DAEKELEREEKELKKLEEELDKAFEELAETEKRLE 643
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 813-835 1.78e-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: 1.78e-06
                            10        20
                    ....*....|....*....|...
gi 1677538261   813 RRTKAATIIQKYWRMYVVRRRYK 835
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRYK 23
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1158-1417 6.71e-06

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: 51.22  E-value: 6.71e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1158 LQKRVTELEQEK------QVMQDELdRKEEQVLRSKAKEEERPQIRGAELEYESLKRQ--ELESENKKLKNELNELRKAL 1229
Cdd:TIGR02169  196 KRQQLERLRRERekaeryQALLKEK-REYEGYELLKEKEALERQKEAIERQLASLEEEleKLTEEISELEKRLEEIEQLL 274

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1230 SEKSApEVTAPGAPAYRVLMEQLTSVSEEL-------DVRKEEVLILRSQLVSQKEAIQPKddKNTMTDSTILLEDVQKM 1302
Cdd:TIGR02169  275 EELNK-KIKDLGEEEQLRVKEKIGELEAEIaslersiAEKERELEDAEERLAKLEAEIDKL--LAEIEELEREIEEERKR 351

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1303 KDKgeIAQAYIGLKETNRLLESQLQSQkrshENEAEALRGEIQSLKEEnnrqqqllaqnlqlppearIEAsLQHEITRLT 1382
Cdd:TIGR02169  352 RDK--LTEEYAELKEELEDLRAELEEV----DKEFAETRDELKDYREK-------------------LEK-LKREINELK 405

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1677538261 1383 NENLDLMEQLEKQDKTVRKLKKQLKVFAKKIGELE 1417
Cdd:TIGR02169  406 RELDRLQEELQRLSEELADLNAAIAGIEAKINELE 440
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
1158-1436 1.16e-05

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 50.40  E-value: 1.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1158 LQKRVTELEQEKQVMQDELDRKEEQVLRSKAKE-----EERPQIRGAELEYESLKRQELESENKKLKNELNELRKALSEK 1232
Cdd:COG3206    173 ARKALEFLEEQLPELRKELEEAEAALEEFRQKNglvdlSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSG 252

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1233 SAPEVTAPGAPAYRVLMEQLTSvseeldvrkeevliLRSQLVSQKEAIQPKDdkntmtdstillEDVQKMKDKgeiaqay 1312
Cdd:COG3206    253 PDALPELLQSPVIQQLRAQLAE--------------LEAELAELSARYTPNH------------PDVIALRAQ------- 299

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1313 igLKETNRLLESQLQSQKRSHENEAEALRGEIQSLKEENNRQQQllaqnlqlppEARIEASLQHEITRLTNEnldlmeql 1392
Cdd:COG3206    300 --IAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEA----------RLAELPELEAELRRLERE-------- 359

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1677538261 1393 ekqdktVRKLKKQLKVFAKKIGELEVGQMENISPGQIIDEPIRP 1436
Cdd:COG3206    360 ------VEVARELYESLLQRLEEARLAEALTVGNVRVIDPAVVP 397
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
 815-835 5.89e-05

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 459869  Cd Length: 21  Bit Score: 41.53  E-value: 5.89e-05
                           10        20
                   ....*....|....*....|.
gi 1677538261  815 TKAATIIQKYWRMYVVRRRYK 835
Cdd:pfam00612    1 RKAAIKIQAAWRGYLARKRYK 21
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
 809-839 2.37e-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: 2.37e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1677538261  809 AKFLRRTKAATIIQKYWRMYVVRRRYKIRRA 839
Cdd:cd23767      3 EELQRMNRAATLIQALWRGYKVRKELKKKKK 33
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 788-810 1.91e-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: 1.91e-03
                            10        20
                    ....*....|....*....|...
gi 1677538261   788 RMRKAAITMQRYVRGYQARCYAK 810
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRYK 23
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 765-786 2.10e-03

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


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 36.92  E-value: 2.10e-03
                            10        20
                    ....*....|....*....|..
gi 1677538261   765 KLRAACIRIQKTIRGWLLRKKY 786
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRY 22
CBD_MYO6-like cd21759
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, ...
 767-794 3.27e-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: 3.27e-03
                           10        20
                   ....*....|....*....|....*...
gi 1677538261  767 RAACIRIQKTIRGWLLRKKYlRMRKAAI 794
Cdd:cd21759     45 REALIKIQKTVRGYLARKKH-RPRIKGL 71
CBD_MYO6-like cd21759
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, ...
 829-862 3.63e-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: 3.63e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1677538261  829 VVRRRYKI--RRAATIVLQSYLRGFLARNRYRKILR 862
Cdd:cd21759     34 VIKLKNKIlyRREALIKIQKTVRGYLARKKHRPRIK 69
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 943-1085 5.31e-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: 5.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  943 YKCLVEKLTNLEGIYNSETEKLRSDLERLQL------SEEEAKVATGRVLSLQE-EIAKLRKDLEQTRSEKKCIEEHADR 1015
Cdd:cd16269    144 YQLYLEDREKLVEKYRQVPRKGVKAEEVLQEflqskeAEAEAILQADQALTEKEkEIEAERAKAEAAEQERKLLEEQQRE 223

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1016 YKQETEQLVSNLKEENTLLKQEKEAlnhRIVQQAKEMTETMEKKLVEETKQLELDLNDERLRYQNLLNEF 1085
Cdd:cd16269    224 LEQKLEDQERSYEEHLRQLKEKMEE---ERENLLKEQERALESKLKEQEALLEEGFKEQAELLQEEIRSL 290
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 862-883 6.90e-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: 6.90e-03
                            10        20
                    ....*....|....*....|..
gi 1677538261   862 REHKAVIIQKRVRGWLARTHYK 883
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 ...
 83-751 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: 1319.08  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   83 PAVLHNLRVRFIDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd01380      1 PAVLHNLKVRFCQRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  163 GESGAGKTVSAKYAMRYFATVSGSAS-EANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRT 241
Cdd:cd01380     81 GESGAGKTVSAKYAMRYFATVGGSSSgETQVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANMRT 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  242 YLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQACTLLGISESH 321
Cdd:cd01380    161 YLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPVIDGVDDAAEFEETRKALTLLGISEEE 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  322 QMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNARD 401
Cdd:cd01380    241 QMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQAIVARD 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  402 ALAKHIYAKLFNWIVDNVNQALHSAV--KQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMK 479
Cdd:cd01380    321 ALAKHIYAQLFDWIVDRINKALASPVkeKQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQEEYVK 400

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  480 EQIPWTLIDFYDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNK-CALFEKPRLSNKAFIIQHFADKVE 558
Cdd:cd01380    401 EEIEWSFIDFYDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKpNKHFKKPRFSNTAFIVKHFADDVE 480

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  559 YQCEGFLEKNKDTVFEEQIKVLKSSKFkmlpelfqddekaisptsatssgrtpltrtpakptkgrpgqmakeHKKTVGHQ 638
Cdd:cd01380    481 YQVEGFLEKNRDTVSEEHLNVLKASKN---------------------------------------------RKKTVGSQ 515

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  639 FRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMKQKD 718
Cdd:cd01380    516 FRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSKE 595

                          650       660       670
                   ....*....|....*....|....*....|....
gi 1677538261  719 VL-SDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd01380    596 WLrDDKKKTCENILENLILDPDKYQFGKTKIFFR 629
Myosin_head pfam00063
Myosin head (motor domain);
72-751 0e+00

Myosin head (motor domain);


Pssm-ID: 395017 [Multi-domain]  Cd Length: 674  Bit Score: 1078.45  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   72 NDLTALSYLHEPAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMA 151
Cdd:pfam00063    2 EDMVELSYLNEPSVLHNLKKRY-KSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  152 RDERNQSIIVSGESGAGKTVSAKYAMRYFATVSGSASEAN---VEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGF 228
Cdd:pfam00063   81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGNvgrLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQF 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  229 DKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHT 308
Cdd:pfam00063  161 DAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQSGCYTIDGIDDSEEFKIT 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  309 RQACTLLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATETYI 388
Cdd:pfam00063  241 DKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGRETVS 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  389 KPISKLQATNARDALAKHIYAKLFNWIVDNVNQALHS-AVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNM 467
Cdd:pfam00063  321 KPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVkTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQFFNH 400

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  468 HVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNTHlNKCALFEKPRL-SN 545
Cdd:pfam00063  401 HMFKLEQEEYVREGIEWTFIDFGDNQPCIDLIEKKpLGILSLLDEECLFPKATDQTFLDKLYSTF-SKHPHFQKPRLqGE 479

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  546 KAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGRTPltrtpaKPTKgrpg 625
Cdd:pfam00063  480 THFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGKSTP------KRTK---- 549

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  626 qmaKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQE 705
Cdd:pfam00063  550 ---KKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQE 626

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*...
gi 1677538261  706 FFSRYRVLMKQKDV--LSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:pfam00063  627 FVQRYRILAPKTWPkwKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
MYSc smart00242
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...
 64-762 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: 1018.24  E-value: 0e+00
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261    64 NPDILVGENDLTALSYLHEPAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVA 143
Cdd:smart00242    1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRY-LKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIA 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   144 EEAYKQMARDERNQSIIVSGESGAGKTVSAKYAMRYFATVSGSASEAN-VEEKVLASNPIMESIGNAKTTRNDNSSRFGK 222
Cdd:smart00242   80 DNAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEVGsVEDQILESNPILEAFGNAKTLRNNNSSRFGK 159

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   223 YIEIGFDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDA 302
Cdd:smart00242  160 FIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQGGCLTVDGIDDA 239

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   303 KEMAHTRQACTLLGISESHQMGIFRILAGILHLGNVGFTSRDAD-SCTIPPKHEPLCIFCELMGVDYEEMCHWLCHRKLA 381
Cdd:smart00242  240 EEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDnAASTVKDKEELSNAAELLGVDPEELEKALTKRKIK 319

                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   382 TATETYIKPISKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKL 461
Cdd:smart00242  320 TGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSFEQLCINYANEKL 399

                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   462 QQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEK 540
Cdd:smart00242  400 QQFFNQHVFKLEQEEYEREGIDWTFIDFFDNQDCIDLIEKKpPGILSLLDEECRFPKGTDQTFLEKLNQHHKKHPHFSKP 479

                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   541 PRLSNKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEkaispTSATSSGRtpltrtpakpt 620
Cdd:smart00242  480 KKKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGV-----SNAGSKKR----------- 543

                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   621 kgrpgqmakehKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSR 700
Cdd:smart00242  544 -----------FQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYR 612

                           650       660       670       680       690       700
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1677538261   701 WTYQEFFSRYRVLMKQK--DVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFRAGQVAYLEKLR 762
Cdd:smart00242  613 LPFDEFLQRYRVLLPDTwpPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELR 676
COG5022 COG5022
Myosin heavy chain [General function prediction only];
7-1233 0e+00

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 969.16  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261    7 YTKFARVWIPDPEEVWKSAELLK-DYKPGDKVLLLHLEEGK--DLEYHLDPKTKelphlRNPDILVGENDLTALSYLHEP 83
Cdd:COG5022      6 AEVGSGCWIPDEEKGWIWAEIIKeAFNKGKVTEEGKKEDGEsvSVKKKVLGNDR-----IKLPKFDGVDDLTELSYLNEP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   84 AVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:COG5022     81 AVLHNLEKRY-NNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISG 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  164 ESGAGKTVSAKYAMRYFATVSGSASE--ANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRT 241
Cdd:COG5022    160 ESGAGKTENAKRIMQYLASVTSSSTVeiSSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIET 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  242 YLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQACTLLGISESH 321
Cdd:COG5022    240 YLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDKIDGIDDAKEFKITLDALKTIGIDEEE 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  322 QMGIFRILAGILHLGNVGFTSrDADSCTIPPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNARD 401
Cdd:COG5022    320 QDQIFKILAAILHIGNIEFKE-DRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRD 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  402 ALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQ 481
Cdd:COG5022    399 SLAKALYSNLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEG 478

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  482 IPWTLIDFYDNQPCINLIESK--LGILDLLDEECKMPKGTDDTWAQKLYNT-HLNKCALFEKPRLSNKAFIIQHFADKVE 558
Cdd:COG5022    479 IEWSFIDYFDNQPCIDLIEKKnpLGILSLLDEECVMPHATDESFTSKLAQRlNKNSNPKFKKSRFRDNKFVVKHYAGDVE 558

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  559 YQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKaisptsatssgrtpltrtpaKPTKGRPgqmakehkKTVGHQ 638
Cdd:COG5022    559 YDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEEN--------------------IESKGRF--------PTLGSR 610

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  639 FRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMKQK- 717
Cdd:COG5022    611 FKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKs 690

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  718 -----DVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFRAGQVAYLEKLRADKLRAACIRIQKTIRGWLLRKKYLRMRKA 792
Cdd:COG5022    691 wtgeyTWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKR 770

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  793 AITMQRYVRGYQARCYAKFLRRTKAATIIQKYWRMYVVRRRYKIRRAATIVLQSYL-RGFLARNRYRKILREHKAVIIQK 871
Cdd:COG5022    771 IKKIQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIkREKKLRETEEVEFSLKAEVLIQK 850

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  872 RVRGWLARTHYKRSMHAIIYLQCCFRRMMAKRELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQ-NKDYKCLVEKL 950
Cdd:COG5022    851 FGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKKSLSSDlIENLEFKTELI 930

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  951 TNLEGIYNSETEKLRSDLERLQLSEeeakvatgrVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEE 1030
Cdd:COG5022    931 ARLKKLLNNIDLEEGPSIEYVKLPE---------LNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKEL 1001

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1031 NTLLKQ------EKEALNHRIVQQAKEMTETMEKKLVEETKQLELDLNDERlryQNLLNEFSRLEERYDDLKeemtlmvh 1104
Cdd:COG5022   1002 AELSKQygalqeSTKQLKELPVEVAELQSASKIISSESTELSILKPLQKLK---GLLLLENNQLQARYKALK-------- 1070

                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1105 VPKPGHKRTDSTHSSNESEYIFSSEI----AEMEDIPSRTEEPSEKKVPLDMSLFLKLQKRVTELEQ-----EKQVMQDE 1175
Cdd:COG5022   1071 LRRENSLLDDKQLYQLESTENLLKTInvkdLEVTNRNLVKPANVLQFIVAQMIKLNLLQEISKFLSQlvntlEPVFQKLS 1150

                         1210      1220      1230      1240      1250      1260
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1176 LDRKEEQVLRSKAKEEERPQIRGAELEYESLKRQE--LESENKKLKNELNELRKALSEKS 1233
Cdd:COG5022   1151 VLQLELDGLFWEANLEALPSPPPFAALSEKRLYQSalYDEKSKLSSSEVNDLKNELIALF 1210
MYSc cd00124
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ...
 83-751 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: 880.00  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMG-DMDPHIFAVAEEAYKQMARDERNQSIIV 161
Cdd:cd00124      1 AAILHNLRERY-ARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  162 SGESGAGKTVSAKYAMRYFATVSGSAS------EANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRII 235
Cdd:cd00124     80 SGESGAGKTETTKLVLKYLAALSGSGSskssssASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLV 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  236 GANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADN----FNYTKQGGSPVIEGVDDAKEMAHTRQA 311
Cdd:cd00124    160 GASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSyyylNDYLNSSGCDRIDGVDDAEEFQELLDA 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  312 CTLLGISESHQMGIFRILAGILHLGNVGFTSR--DADSCTIPPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATETYIK 389
Cdd:cd00124    240 LDVLGFSDEEQDSIFRILAAILHLGNIEFEEDeeDEDSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETITK 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  390 PISKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQH--SFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNM 467
Cdd:cd00124    320 PLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAEstSFIGILDIFGFENFEVNSFEQLCINYANEKLQQFFNQ 399

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  468 HVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRLSNK 546
Cdd:cd00124    400 HVFKLEQEEYEEEGIDWSFIDFPDNQDCLDLIEGKpLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKRKAKL 479

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  547 AFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKfkmlpelfqddekaisptsatssgrtpltrtpakptkgrpgq 626
Cdd:cd00124    480 EFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGS------------------------------------------ 517

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  627 makehkktvghQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEF 706
Cdd:cd00124    518 -----------QFRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEF 586

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*..
gi 1677538261  707 FSRYRVLMKQKDVLSDR--KQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd00124    587 LKRYRILAPGATEKASDskKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
MYSc_class_II cd01377
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ...
 83-751 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: 798.21  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd01377      1 ASVLHNLRERY-YSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILIT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  163 GESGAGKTVSAKYAMRYFATVSGSA--------SEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRI 234
Cdd:cd01377     80 GESGAGKTENTKKVIQYLASVAASSkkkkesgkKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKI 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  235 IGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQACTL 314
Cdd:cd01377    160 AGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAFDI 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  315 LGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKPISKL 394
Cdd:cd01377    240 LGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKE 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  395 QATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQ 474
Cdd:cd01377    320 QVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQ 399

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  475 EEYMKEQIPWTLIDF-YDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPR--LSNKAFII 550
Cdd:cd01377    400 EEYKKEGIEWTFIDFgLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKPKpkKSEAHFIL 479

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  551 QHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGRTPLtrtpakptkgrpgqmake 630
Cdd:cd01377    480 KHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEESGGGGGKKKKKGGSF------------------ 541

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  631 hkKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRY 710
Cdd:cd01377    542 --RTVSQLHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRY 619

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|...
gi 1677538261  711 RVLMKQ--KDVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd01377    620 SILAPNaiPKGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
MYSc_Myo11 cd01384
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ...
 83-751 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: 762.60  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLP-IYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIV 161
Cdd:cd01384      1 PGVLHNLKVRY-ELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  162 SGESGAGKTVSAKYAMRYFATVSGSAS--EANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANM 239
Cdd:cd01384     80 SGESGAGKTETTKMLMQYLAYMGGRAVteGRSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAAI 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  240 RTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQACTLLGISE 319
Cdd:cd01384    160 RTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNQSKCFELDGVDDAEEYRATRRAMDVVGISE 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  320 SHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEP---LCIFCELMGVDYEEMCHWLCHRKLATATETYIKPISKLQA 396
Cdd:cd01384    240 EEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKSefhLKAAAELLMCDEKALEDALCKRVIVTPDGIITKPLDPDAA 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  397 TNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEE 476
Cdd:cd01384    320 TLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQHVFKMEQEE 399

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  477 YMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNThLNKCALFEKPRLSNKAFIIQHFAD 555
Cdd:cd01384    400 YTKEEIDWSYIEFVDNQDVLDLIEKKpGGIIALLDEACMFPRSTHETFAQKLYQT-LKDHKRFSKPKLSRTDFTIDHYAG 478

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  556 KVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELF--QDDEKAISPTSATSsgrtpltrtpakptkgrpgqmakehkk 633
Cdd:cd01384    479 DVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFppLPREGTSSSSKFSS--------------------------- 531

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  634 tVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVL 713
Cdd:cd01384    532 -IGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLL 610

                          650       660       670
                   ....*....|....*....|....*....|....*....
gi 1677538261  714 MKQKDVLS-DRKQTCKNVLEKLILdkDKYQFGKTKIFFR 751
Cdd:cd01384    611 APEVLKGSdDEKAACKKILEKAGL--KGYQIGKTKVFLR 647
MYSc_Myo7 cd01381
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ...
 84-751 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: 754.09  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   84 AVLHNLRVRFIDsKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd01381      2 GILRNLLIRYRE-KLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  164 ESGAGKTVSAKYAMRYFATVSGSASEanVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYL 243
Cdd:cd01381     81 ESGAGKTESTKLILQYLAAISGQHSW--IEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKIEQYL 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  244 LEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQACTLLGISESHQM 323
Cdd:cd01381    159 LEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGNCLTCEGRDDAAEFADIRSAMKVLMFTDEEIW 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  324 GIFRILAGILHLGNVGFTSRDA---DSCTIpPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNAR 400
Cdd:cd01381    239 DIFKLLAAILHLGNIKFEATVVdnlDASEV-RDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAEQALDVR 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  401 DALAKHIYAKLFNWIVDNVNQALHSAVKQHSF---IGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEY 477
Cdd:cd01381    318 DAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtsIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFKLEQEEY 397

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  478 MKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNTHLNKcALFEKPR-LSNKAFIIQHFAD 555
Cdd:cd01381    398 DKEGINWQHIEFVDNQDVLDLIALKpMNIMSLIDEESKFPKGTDQTMLEKLHSTHGNN-KNYLKPKsDLNTSFGINHFAG 476

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  556 KVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEkaisPTSATSSGRTPltrtpakptkgrpgqmakehkkTV 635
Cdd:cd01381    477 VVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDI----SMGSETRKKSP----------------------TL 530

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  636 GHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMK 715
Cdd:cd01381    531 SSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVP 610

                          650       660       670
                   ....*....|....*....|....*....|....*...
gi 1677538261  716 --QKDVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd01381    611 giPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
MYSc_Myo8 cd01383
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ...
 83-751 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: 732.20  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDmdPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd01383      1 PSVLHNLEYRY-SQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYRQKLLDS--PHVYAVADTAYREMMRDEINQSIIIS 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  163 GESGAGKTVSAKYAMRYFATVSGSASeaNVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTY 242
Cdd:cd01383     78 GESGAGKTETAKIAMQYLAALGGGSS--GIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQTY 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  243 LLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQACTLLGISESHQ 322
Cdd:cd01383    156 LLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNQSNCLTIDGVDDAKKFHELKEALDTVGISKEDQ 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  323 MGIFRILAGILHLGNVGFTSRDADSCTIPPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNARDA 402
Cdd:cd01383    236 EHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAIDARDA 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  403 LAKHIYAKLFNWIVDNVNQALHSAVKQHS-FIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQ 481
Cdd:cd01383    316 LAKAIYASLFDWLVEQINKSLEVGKRRTGrSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEEYELDG 395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  482 IPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLyNTHLNKCALFEKPRlsNKAFIIQHFADKVEYQ 560
Cdd:cd01383    396 IDWTKVDFEDNQECLDLIEKKpLGLISLLDEESNFPKATDLTFANKL-KQHLKSNSCFKGER--GGAFTIRHYAGEVTYD 472

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  561 CEGFLEKNKDTVFEEQIKVLKSSKFKmLPELFQddekaispTSATSSGRTPLTRTPAkptkGRPGQMakehKKTVGHQFR 640
Cdd:cd01383    473 TSGFLEKNRDLLHSDLIQLLSSCSCQ-LPQLFA--------SKMLDASRKALPLTKA----SGSDSQ----KQSVATKFK 535

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  641 NSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLM-KQKDV 719
Cdd:cd01383    536 GQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLpEDVSA 615

                          650       660       670
                   ....*....|....*....|....*....|..
gi 1677538261  720 LSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd01383    616 SQDPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
Myo5a_CBD cd15478
Cargo binding domain of myosin 5a; Class V myosins are well studied unconventional myosins, ...
 1454-1828 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: 721.82  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1454 KEDEQKLVKNLILELKPRGVAVNLIPGLPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSN 1533
Cdd:cd15478      1 KEDEQKLVKNLILELKPRGVAVNLIPGLPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1534 TCRFLHCLKQYSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPMIVSGMLEHETIQGVSG 1613
Cdd:cd15478     81 TCRFLHCLKQYSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPMIVSGMLEHETIQGVSG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1614 VKPTGLRKRTSSIADEGTYTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQIR 1693
Cdd:cd15478    161 VKPTGLRKRTSSIADEGTYTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQIR 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1694 YNVSQLEEWLRDKNLMNSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERVSVSF 1773
Cdd:cd15478    241 YNVSQLEEWLRDKNLMNSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERVSVSF 320

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1677538261 1774 IRTIQMRLRDRKDSPQLLMDAKHIFPVTFPFNPSSLALETIQIPASLGLGFISRV 1828
Cdd:cd15478    321 IRTIQMRLRDRKDSPQLLMDAKHIFPVTFPFNPSSLALETIQIPASLGLGFISRV 375
MYSc_Myo22 cd14883
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ...
 84-751 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: 718.34  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   84 AVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd14883      2 GINTNLKVRY-KKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  164 ESGAGKTVSAKYAMRYFATVSGSASEanVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYL 243
Cdd:cd14883     81 ESGAGKTETTKLILQYLCAVTNNHSW--VEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGAIIQDYL 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  244 LEKSRVVFQAEEERNYHIFYQLCASAKL-PEFK-MLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQACTLLGISESH 321
Cdd:cd14883    159 LEQSRITFQAPGERNYHVFYQLLAGAKHsKELKeKLKLGEPEDYHYLNQSGCIRIDNINDKKDFDHLRLAMNVLGIPEEM 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  322 QMGIFRILAGILHLGNVGFTSRDADSCTIPPKH-EPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNAR 400
Cdd:cd14883    239 QEGIFSVLSAILHLGNLTFEDIDGETGALTVEDkEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQEARDNR 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  401 DALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKE 480
Cdd:cd14883    319 DAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKLEQEEYEKE 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  481 QIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNTHlNKCALFEKP--RLSNKAFIIQHFADKV 557
Cdd:cd14883    399 GINWSHIVFTDNQECLDLIEKPpLGILKLLDEECRFPKGTDLTYLEKLHAAH-EKHPYYEKPdrRRWKTEFGVKHYAGEV 477

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  558 EYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQ-DDEKAISPTSATSSGRTPLTRTpakpTKGRPgqmakehkkTVG 636
Cdd:cd14883    478 TYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTyPDLLALTGLSISLGGDTTSRGT----SKGKP---------TVG 544

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  637 HQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMKQ 716
Cdd:cd14883    545 DTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPR 624

                          650       660       670
                   ....*....|....*....|....*....|....*..
gi 1677538261  717 KDVLSDRKQ--TCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14883    625 ARSADHKETcgAVRALMGLGGLPEDEWQVGKTKVFLR 661
MYSc_Myo1 cd01378
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ...
 84-751 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: 716.63  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   84 AVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd01378      2 AINENLKKRF-ENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  164 ESGAGKTVSAKYAMRYFATVSGSaSEANVE---EKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMR 240
Cdd:cd01378     81 ESGAGKTEASKRIMQYIAAVSGG-SESEVErvkDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGHIT 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  241 TYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQACTLLGISES 320
Cdd:cd01378    160 NYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVIGFTEE 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  321 HQMGIFRILAGILHLGNVGFTSRDADSCTIPPKhEPLCIFCELMGVDYEEMCHWLCHRKLATATE---TYIKPISKLQAT 397
Cdd:cd01378    240 EQDSIFRILAAILHLGNIQFAEDEEGNAAISDT-SVLDFVAYLLGVDPDQLEKALTHRTIETGGGgrsVYEVPLNVEQAA 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  398 NARDALAKHIYAKLFNWIVDNVNQALHSAVKQHS-FIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEE 476
Cdd:cd01378    319 YARDALAKAIYSRLFDWIVERINKSLAAKSGGKKkVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELTLKAEQEE 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  477 YMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECK-MPKGTDDTWAQKLyNTHLNKCALFEKP----RLSNKAFII 550
Cdd:cd01378    399 YVREGIEWTPIKYFNNKIICDLIEEKpPGIFAILDDACLtAGDATDQTFLQKL-NQLFSNHPHFECPsghfELRRGEFRI 477

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  551 QHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDekaisptsatssgrtpltrtPAKPTKGRPgqmake 630
Cdd:cd01378    478 KHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEG--------------------VDLDSKKRP------ 531

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  631 hkKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRY 710
Cdd:cd01378    532 --PTAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERY 609

                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1677538261  711 RVLMK----------QKDVLSDRKQTCknvlekliLDKDKYQFGKTKIFFR 751
Cdd:cd01378    610 KLLSPktwpawdgtwQGGVESILKDLN--------IPPEEYQMGKTKIFIR 652
Myo5b_CBD cd15477
Cargo binding domain of myosin 5b; Class V myosins are well studied unconventional myosins, ...
 1454-1825 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: 647.30  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1454 KEDEQKLVKNLILELKPRGVAVNlIPGLPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSN 1533
Cdd:cd15477      1 KEDEALLIRNLVTDLKPQAVSAT-VPCLPAYILYMCIRHADYINDDQKVHSLLTSTINGIKKVLKKHNDDFEMTSFWLAN 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1534 TCRFLHCLKQYSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPMIVSGMLEHETIQGVSG 1613
Cdd:cd15477     80 TCRLLHCLKQYSGDEGFMTQNTAKQNEHCLKNFDLTEYRQVLSDLSIQIYQQLIKIAEGILQPMIVSAMLENESIQGLSG 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1614 VKPTGLRKRTSSIAD-EGTYTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQI 1692
Cdd:cd15477    160 VKPMGYRKRSSSMADgDNSYTLEALIRQLNTFHSIMCDQGLDPEIIQQVFKQLFYMINAVTLNNLLLRKDVCSWSTGMQL 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1693 RYNVSQLEEWLRDKNLMNSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERVSVS 1772
Cdd:cd15477    240 RYNISQLEEWLRGRNLHQSGAAQTMEPLIQAAQLLQLKKKTSEDAEAICSLCTALSTQQIVKILNLYTPLNEFEERVTVS 319

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1677538261 1773 FIRTIQMRLRDRKDSPQLLMDAKHIFPVTFPFNPSSLALETIQIPASLGLGFI 1825
Cdd:cd15477    320 FIRTIQAQLQERNDPPQLLLDTKHMFPVLFPFNPSALTLDSIHIPASLNLDFL 372
MYSc_Myo42 cd14903
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ...
 83-751 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 1677538261   83 PAVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLP-IYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIV 161
Cdd:cd14903      1 AAILYNVKKRFL-RKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  162 SGESGAGKTVSAKYAMRYFATVSGSASEANVEeKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRT 241
Cdd:cd14903     80 SGESGAGKTETTKILMNHLATIAGGLNDSTIK-KIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLVGAKCRT 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  242 YLLEKSRVVFQAEEERNYHIFYQLCASAKLPEfkMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQACTLLGISESH 321
Cdd:cd14903    159 YLLEKTRVISHERPERNYHIFYQLLASPDVEE--RLFLDSANECAYTGANKTIKIEGMSDRKHFARTKEALSLIGVSEEK 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  322 QMGIFRILAGILHLGNVGFTSRDAD--SCTIPPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNA 399
Cdd:cd14903    237 QEVLFEVLAGILHLGQLQIQSKPNDdeKSAIAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKKDQAEDC 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  400 RDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMK 479
Cdd:cd14903    317 RDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFKTVQIEYEE 396

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  480 EQIPWTLIDFYDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRLSNKAFIIQHFADKVEY 559
Cdd:cd14903    397 EGIRWAHIDFADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFPRTSRTQFTIKHYAGPVTY 476

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  560 QCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFqdDEKAISPTSATSSGRTPltrtpakptkGRPGQMAKEHKKTVGHQF 639
Cdd:cd14903    477 ESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLF--KEKVESPAAASTSLARG----------ARRRRGGALTTTTVGTQF 544

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  640 RNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMKQK-D 718
Cdd:cd14903    545 KDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFLPEGrN 624

                          650       660       670
                   ....*....|....*....|....*....|....
gi 1677538261  719 VLSDRKQTCKNVLEKLILDK-DKYQFGKTKIFFR 751
Cdd:cd14903    625 TDVPVAERCEALMKKLKLESpEQYQMGLTRIYFQ 658
MYSc_Myo6 cd01382
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ...
 86-751 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: 629.66  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   86 LHNLRVRFIDSKlIYTYCGIVLVAINPYEQLP-IYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSGE 164
Cdd:cd01382      4 LNNIRVRYSKDK-IYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVSGE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  165 SGAGKTVSAKYAMRYFATVSGSASeANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYLL 244
Cdd:cd01382     83 SGAGKTESTKYILRYLTESWGSGA-GPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYLL 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  245 EKSRVVFQAEEERNYHIFYQLCASAklPE---FKMLRLGNadnfnytkqggspviegVDDAKEMAHTRQACTLLGISESH 321
Cdd:cd01382    162 EKSRICVQSKEERNYHIFYRLCAGA--PEdlrEKLLKDPL-----------------LDDVGDFIRMDKAMKKIGLSDEE 222

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  322 QMGIFRILAGILHLGNVGFTSRDADS---CTIPPKHEPLCIFC-ELMGVDYEEMCHWLCHRKLATATE----TYIK-PIS 392
Cdd:cd01382    223 KLDIFRVVAAVLHLGNIEFEENGSDSgggCNVKPKSEQSLEYAaELLGLDQDELRVSLTTRVMQTTRGgakgTVIKvPLK 302

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  393 KLQATNARDALAKHIYAKLFNWIVDNVNQAL---HSAvkqhSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHV 469
Cdd:cd01382    303 VEEANNARDALAKAIYSKLFDHIVNRINQCIpfeTSS----YFIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQFFNERI 378

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  470 FKLEQEEYMKEQIPWTLIDFYDNQPCINLIESKL-GILDLLDEECKMPKGTDDTWAQKLYNTHLNKcALFEKPRLS---- 544
Cdd:cd01382    379 LKEEQELYEKEGLGVKEVEYVDNQDCIDLIEAKLvGILDLLDEESKLPKPSDQHFTSAVHQKHKNH-FRLSIPRKSklki 457

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  545 ------NKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAiSPTSATSSGRTPLtrtpak 618
Cdd:cd01382    458 hrnlrdDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNN-NKDSKQKAGKLSF------ 530

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  619 ptkgrpgqmakehkKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFP 698
Cdd:cd01382    531 --------------ISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFP 596

                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1677538261  699 SRWTYQEFFSRYRVLMKQKDVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd01382    597 SRTSFHDLYNMYKKYLPPKLARLDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
MYSc_Myo4 cd14872
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ...
 83-751 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: 623.34  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   83 PAVLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14872      1 AMIVHNLRKRFKNDQ-IYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILIS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  163 GESGAGKTVSAKYAMRYFATVSGSASeaNVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTY 242
Cdd:cd14872     80 GESGAGKTEATKQCLSFFAEVAGSTN--GVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGASTENY 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  243 LLEKSRVVFQAEEERNYHIFYQLCASAklPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQACTLLGISESHQ 322
Cdd:cd14872    158 LLEKSRVVYQIKGERNFHIFYQLLASP--DPASRGGWGSSAAYGYLSLSGCIEVEGVDDVADFEEVVLAMEQLGFDDADI 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  323 MGIFRILAGILHLGNVGFTS----RDADSCTIPPKHEpLCIFCELMGVDYEEMCHWLCHRKLAT-ATETYIKPISKLQAT 397
Cdd:cd14872    236 NNVMSLIAAILKLGNIEFASgggkSLVSGSTVANRDV-LKEVATLLGVDAATLEEALTSRLMEIkGCDPTRIPLTPAQAT 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  398 NARDALAKHIYAKLFNWIVDNVNQALHSA-VKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEE 476
Cdd:cd14872    315 DACDALAKAAYSRLFDWLVKKINESMRPQkGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTFKLEEAL 394

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  477 YMKEQIPWTLIDFYDNQPCINLIESKL-GILDLLDEECKMPKGTDDTWAQKLYNTH-LNKCALFEKPRLSNKAFIIQHFA 554
Cdd:cd14872    395 YQSEGVKFEHIDFIDNQPVLDLIEKKQpGLMLALDDQVKIPKGSDATFMIAANQTHaAKSTFVYAEVRTSRTEFIVKHYA 474

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  555 DKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEkaisptsatssgrtpltrtPAKPTKgrpgqmakehKKT 634
Cdd:cd14872    475 GDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPPSE-------------------GDQKTS----------KVT 525

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  635 VGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLM 714
Cdd:cd14872    526 LGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFLV 605

                          650       660       670
                   ....*....|....*....|....*....|....*....
gi 1677538261  715 K--QKDVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14872    606 KtiAKRVGPDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
MYSc_Myo9 cd01385
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ...
 86-751 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: 621.32  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   86 LHNLRVRFIDSKlIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSGES 165
Cdd:cd01385      4 LENLRARFKHGK-IYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISGES 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  166 GAGKTVSAKYAMRYFATVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYLLE 245
Cdd:cd01385     83 GSGKTESTNFLLHHLTALSQKGYGSGVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVEKYLLE 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  246 KSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQACTLLGISESHQMGI 325
Cdd:cd01385    163 KSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNQSDCYTLEGEDEKYEFERLKQAMEMVGFLPETQRQI 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  326 FRILAGILHLGNVGFTSRDA---DSCTIPPKhEPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNARDA 402
Cdd:cd01385    243 FSVLSAVLHLGNIEYKKKAYhrdESVTVGNP-EVLDIISELLRVKEETLLEALTTKKTVTVGETLILPYKLPEAIATRDA 321

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  403 LAKHIYAKLFNWIVDNVNQAL----HSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYM 478
Cdd:cd01385    322 MAKCLYSALFDWIVLRINHALlnkkDLEEAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIFKLEQEEYK 401

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  479 KEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKlYNTHLNKCALFEKPRLSNKAFIIQHFADKV 557
Cdd:cd01385    402 KEGISWHNIEYTDNTGCLQLISKKpTGLLCLLDEESNFPGATNQTLLAK-FKQQHKDNKYYEKPQVMEPAFIIAHYAGKV 480

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  558 EYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAI-----------------SPTSATSSGRT-PLTRTPAKP 619
Cdd:cd01385    481 KYQIKDFREKNLDLMRPDIVAVLRSSSSAFVRELIGIDPVAVfrwavlrafframaafrEAGRRRAQRTAgHSLTLHDRT 560

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  620 TKGRPGQMAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPS 699
Cdd:cd01385    561 TKSLLHLHKKKKPPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTGMLETVRIRRSGYSV 640

                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1677538261  700 RWTYQEFFSRYRVLMKqKDVLSdRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd01385    641 RYTFQEFITQFQVLLP-KGLIS-SKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
Myo5_CBD cd15470
Cargo binding domain of myosin 5; Class V myosins are well studied unconventional myosins, ...
 1455-1821 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: 615.76  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1455 EDEQKLVKNLILELKPRGvAVNLIPGLPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSNT 1534
Cdd:cd15470      1 EDESRLIKNLITDLKPRG-AVGLLPGLPAYILFMCIRHADYVNDEAKVRSLLTATINAIKKVLKKHSEDFEMLSFWLVNT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1535 CRFLHCLKQYSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPmivsgmlehetiqgvsgv 1614
Cdd:cd15470     80 CRLLNCLKQYSGEEEFMKHNTPKQNEHCLKNFDLSEYRQVLSDLAIQIYQQLIKRAEEILQP------------------ 141

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1615 kptglrkrtssiadegtyTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQIRY 1694
Cdd:cd15470    142 ------------------TLDSLLQQLNSFHTTLTQHGLDPELIKQVFRQLFYLICASTLNNLLLRKDLCSWSKGMQIRY 203

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1695 NVSQLEEWLRDKNLMNSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERVSVSFI 1774
Cdd:cd15470    204 NVSQLEEWLRDKGLQDSGARETLEPLIQAAQLLQVKKTTEEDAQSICEMCTKLTTAQIVKILNLYTPVDDFEERVTPSFI 283

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1677538261 1775 RTIQMRLRDRKDSP--QLLMDAKHIFPVTFPFNPSSLALETIQIPASLG 1821
Cdd:cd15470    284 RKVQARLNERADSNqlQLLMDTKYIFPVTFPFNPSPVALEELQIPPSLH 332
MYSc_Myo15 cd01387
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ...
 84-751 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 1677538261   84 AVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd01387      2 TVLWNLKTRY-ERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  164 ESGAGKTVSAKYAMRYFATVSGSAsEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFdKRYRIIGANMRTYL 243
Cdd:cd01387     81 ESGSGKTEATKLIMQYLAAVNQRR-NNLVTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-EGGVIVGAITSQYL 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  244 LEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQACTLLGISESHQM 323
Cdd:cd01387    159 LEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGGNCEIAGKSDADDFRRLLAAMQVLGFSSEEQD 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  324 GIFRILAGILHLGNVGFTSRDA----DSCTIPPKHEPLCIfCELMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNA 399
Cdd:cd01387    239 SIFRILASVLHLGNVYFHKRQLrhgqEGVSVGSDAEIQWV-AHLLQISPEGLQKALTFKVTETRRERIFTPLTIDQALDA 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  400 RDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMK 479
Cdd:cd01387    318 RDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVFKLEQEEYIR 397

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  480 EQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKL-YNTHLNKcaLFEKPRLSNKAFIIQHFADKV 557
Cdd:cd01387    398 EQIDWTEIAFADNQPVINLISKKpVGILHILDDECNFPQATDHSFLEKChYHHALNE--LYSKPRMPLPEFTIKHYAGQV 475

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  558 EYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDekaisptsatssgRTPLTRTPAKPTKGRPGQMaKEHKKTVGH 637
Cdd:cd01387    476 WYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSH-------------RAQTDKAPPRLGKGRFVTM-KPRTPTVAA 541

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  638 QFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMKQK 717
Cdd:cd01387    542 RFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVALK 621

                          650       660       670
                   ....*....|....*....|....*....|....*.
gi 1677538261  718 DVLSDRKQTCKNVLEKL--ILDKDKYQFGKTKIFFR 751
Cdd:cd01387    622 LPRPAPGDMCVSLLSRLctVTPKDMYRLGATKVFLR 657
MYSc_Myo29 cd14890
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ...
 84-751 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 1677538261   84 AVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLP-IYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMAR----DERNQS 158
Cdd:cd14890      2 SLLHTLRLRY-ERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  159 IIVSGESGAGKTVSAKYAMRYFATVS-----------------GSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFG 221
Cdd:cd14890     81 IIISGESGAGKTEATKIIMQYLARITsgfaqgasgegeaaseaIEQTLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  222 KYIEIGFDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNA-DNFNYTKQGGSpvIEGVD 300
Cdd:cd14890    161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPvEYFYLRGECSS--IPSCD 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  301 DAKEMAHTRQACTLLGISESHQMGIFRILAGILHLGNVGFTS-RDADSCTIPPKHEPLCIFCELMGVDYEEMCHWLCHRK 379
Cdd:cd14890    239 DAKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESeNDTTVLEDATTLQSLKLAAELLGVNEDALEKALLTRQ 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  380 LATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANE 459
Cdd:cd14890    319 LFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYANE 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  460 KLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESKL----GILDLLDeECKMPKGTDdtwAQKLYNTHLNkc 535
Cdd:cd14890    399 KLQRHFNQHMFEVEQVEYSNEGIDWQYITFNDNQACLELIEGKVngkpGIFITLD-DCWRFKGEE---ANKKFVSQLH-- 472

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  536 ALFEKPRLSNKA--------------------FIIQHFADKVEYQCEGFLEKNKDTVFEEqikvlksskfkmLPELFQDD 595
Cdd:cd14890    473 ASFGRKSGSGGTrrgssqhphfvhpkfdadkqFGIKHYAGDVIYDASGFNEKNNETLNAE------------MKELIKQS 540

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  596 EKAISPTSatssgrtpltrtpakptkgrpgqmakehkktVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEK 675
Cdd:cd14890    541 RRSIREVS-------------------------------VGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGL 589

                          650       660       670       680       690       700       710
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1677538261  676 RAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMKQKDVLsdrKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
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 ...
 84-751 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 1677538261   84 AVLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLP-IYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14873      2 SIMYNLFQRYKRNQ-IYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  163 GESGAGKTVSAKYAMRYFATVS-------GSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRII 235
Cdd:cd14873     81 GESGAGKTESTKLILKFLSVISqqslelsLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQ 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  236 GANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQACTLL 315
Cdd:cd14873    161 GGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNQSGCVEDKTISDQESFREVITAMEVM 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  316 GISESHQMGIFRILAGILHLGNVGFTSrdADSCTIPPKhEPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKPISKLQ 395
Cdd:cd14873    241 QFSKEEVREVSRLLAGILHLGNIEFIT--AGGAQVSFK-TALGRSAELLGLDPTQLTDALTQRSMFLRGEEILTPLNVQQ 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  396 ATNARDALAKHIYAKLFNWIVDNVNQALHSAvKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQE 475
Cdd:cd14873    318 AVDSRDSLAMALYARCFEWVIKKINSRIKGK-EDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLEQL 396

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  476 EYMKEQIPWTLIDFYDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKcALFEKPRLSNKAFIIQHFAD 555
Cdd:cd14873    397 EYSREGLVWEDIDWIDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQHANN-HFYVKPRVAVNNFGVKHYAG 475

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  556 KVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDekaisptSATSSGRTPltrtpakptkgrpgQMAKEHKK-T 634
Cdd:cd14873    476 EVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHV-------SSRNNQDTL--------------KCGSKHRRpT 534

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  635 VGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLM 714
Cdd:cd14873    535 VSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLM 614

                          650       660       670
                   ....*....|....*....|....*....|....*..
gi 1677538261  715 KQKDVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14873    615 RNLALPEDVRGKCTSLLQLYDASNSEWQLGKTKVFLR 651
MYSc_Myo40 cd14901
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ...
 83-749 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: 585.98  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAY---SGQNMGD---MDPHIFAVAEEAYKQMARDER- 155
Cdd:cd14901      1 PSILHVLRRRF-AHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehGERRAAGerkLPPHVYAVADKAFRAMLFASRg 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  156 ---NQSIIVSGESGAGKTVSAKYAMRYFATVS-------GSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIE 225
Cdd:cd14901     80 qkcDQSILVSGESGAGKTETTKIIMNYLASVSsatthgqNATERENVRDRVLESNPILEAFGNARTNRNNNSSRFGKFIR 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  226 IGFDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPV-IEGVDDAKE 304
Cdd:cd14901    160 LGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLNSSQCYDrRDGVDDSVQ 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  305 MAHTRQACTLLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEP-LCIFCELMGVDYEEMCHWLCHRKLATA 383
Cdd:cd14901    240 YAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGGTFSMSSLAnVRAACDLLGLDMDVLEKTLCTREIRAG 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  384 TETYIKPISKLQATNARDALAKHIYAKLFNWIVDNVNQAL--HSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKL 461
Cdd:cd14901    320 GEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIaySESTGASRFIGIVDIFGFEIFATNSLEQLCINFANEKL 399

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  462 QQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNThLNKCALFEK 540
Cdd:cd14901    400 QQLFGKFVFEMEQDEYVAEAIPWTFVEYPNNDACVAMFEARpTGLFSLLDEQCLLPRGNDEKLANKYYDL-LAKHASFSV 478

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  541 PRLSN--KAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPelfqddekaisptsatssgrtpltrtpak 618
Cdd:cd14901    479 SKLQQgkRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLS----------------------------- 529

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  619 ptkgrpgqmakehkKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFP 698
Cdd:cd14901    530 --------------STVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYP 595

                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1677538261  699 SRWTYQEFFSRYRVLMKQK-------DVLSDRKQTCKNVLEKLILDKDKYQFGKTKIF 749
Cdd:cd14901    596 VRFPHDAFVHTYSCLAPDGasdtwkvNELAERLMSQLQHSELNIEHLPPFQVGKTKVF 653
MYSc_Myo27 cd14888
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ...
 83-751 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: 568.17  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLP-IYGEDIINAYSgQNMGDMDPHIFAVAEEAYKQMARDERNQSIIV 161
Cdd:cd14888      1 ASILHSLNLRF-DIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILI 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  162 SGESGAGKTVSAKYAMRYFATVsGSASE---ANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDK-------- 230
Cdd:cd14888     79 SGESGAGKTESTKYVMKFLACA-GSEDIkkrSLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSKlkskrmsg 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  231 -RYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCA-----------------------SAKLPEFKMLRLGNADNFN 286
Cdd:cd14888    158 dRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAaareakntglsyeendeklakgaDAKPISIDMSSFEPHLKFR 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  287 YTKQGGSPVIEGVDDAKEMAHTRQACTLLGISESHQMGIFRILAGILHLGNVGF-TSRDADSCTI--PPKHEPLCIFCEL 363
Cdd:cd14888    238 YLTKSSCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFeNNEACSEGAVvsASCTDDLEKVASL 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  364 MGVDYEEMCHWLCHRKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDNVNQAL-HSAVKQHSFIGVLDIYGFE 442
Cdd:cd14888    318 LGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIgYSKDNSLLFCGVLDIFGFE 397

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  443 TFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDD 521
Cdd:cd14888    398 CFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFPDNQDCVDLLQEKpLGIFCMLDEECFVPGGKDQ 477

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  522 TWAQKLYNTHLNKcALFEKPRLSNKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQddekaisp 601
Cdd:cd14888    478 GLCNKLCQKHKGH-KRFDVVKTDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNLFS-------- 548

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  602 tsatssgrtpltrtpAKPTKGRPGQMAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQL 681
Cdd:cd14888    549 ---------------AYLRRGTDGNTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQL 613

                          650       660       670       680       690       700       710
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  682 RACGVLETIRISAAGFPSRWTYQEFFSRYRVLMkqkdvlsdRKQTCKNVLEklildkdkYQFGKTKIFFR 751
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 ...
 83-751 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: 563.82  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   83 PAVLHNLRVRFIDSkLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd01379      1 DTIVSQLQKRYSRD-QIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVIS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  163 GESGAGKTVSAKYAMRYFaTVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTY 242
Cdd:cd01379     80 GESGAGKTESANLLVQQL-TVLGKANNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEY 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  243 LLEKSRVVFQAEEERNYHIFYQLCA----SAKLPEFKmlrLGNADNFNYTKQGGspviEGVDDAKEMAHTR------QAC 312
Cdd:cd01379    159 LLEKSRVVHQAIGERNFHIFYYIYAglaeDKKLAKYK---LPENKPPRYLQNDG----LTVQDIVNNSGNRekfeeiEQC 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  313 -TLLGISESHQMGIFRILAGILHLGNVGFTS-----RDADSCTIpPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATET 386
Cdd:cd01379    232 fKVIGFTKEEVDSVYSILAAILHIGDIEFTEvesnhQTDKSSRI-SNPEALNNVAKLLGIEADELQEALTSHSVVTRGET 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  387 YIKPISKLQATNARDALAKHIYAKLFNWIVDNVNQAL----HSAVKQHSfIGVLDIYGFETFEINSFEQFCINYANEKLQ 462
Cdd:cd01379    311 IIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpdrSASDEPLS-IGILDIFGFENFQKNSFEQLCINIANEQIQ 389

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  463 QQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNthlN-KCALFEK 540
Cdd:cd01379    390 YYFNQHIFAWEQQEYLNEGIDVDLIEYEDNRPLLDMFLQKpMGLLALLDEESRFPKATDQTLVEKFHN---NiKSKYYWR 466

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  541 PRLSNKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLpelfqddekaisptsatssgrtpltrtpakpt 620
Cdd:cd01379    467 PKSNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLV-------------------------------- 514

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  621 kgrpgqmakehKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSR 700
Cdd:cd01379    515 -----------RQTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHR 583

                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1677538261  701 WTYQEFFSRYRVL---MKQKDVLSdrKQTCKNVLEKLILdkDKYQFGKTKIFFR 751
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 ...
 83-751 1.04e-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: 558.05  E-value: 1.04e-179
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14929      1 ASVLHTLRRRY-DHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  163 GESGAGKTVSAKYAMRYFATVSGSASE----ANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGAN 238
Cdd:cd14929     80 GESGAGKTVNTKHIIQYFATIAAMIESkkklGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSAD 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  239 MRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPViEGVDDAKEMAHTRQACTLLGIS 318
Cdd:cd14929    160 IDIYLLEKSRVIFQQPGERNYHIFYQILSGKKELRDLLLVSANPSDFHFCSCGAVAV-ESLDDAEELLATEQAMDILGFL 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  319 ESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKPISKLQATN 398
Cdd:cd14929    239 PDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIEQVTY 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  399 ARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYM 478
Cdd:cd14929    319 AVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLEQEEYR 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  479 KEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRLSNKAFIIQ----HF 553
Cdd:cd14929    399 KEGIDWVSIDFgLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKPDKKKFEAHfelvHY 478

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  554 ADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDekaISPTSATSSGRtpltrtpakptkgrpgqmaKEHKK 633
Cdd:cd14929    479 AGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENY---ISTDSAIQFGE-------------------KKRKK 536

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  634 TVGHQFRNSLH-----LLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFS 708
Cdd:cd14929    537 GASFQTVASLHkenlnKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQ 616

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*...
gi 1677538261  709 RY-----RVLMKQKDVlSDRKQTcKNVLEKLILDKDKYQFGKTKIFFR 751
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 ...
 89-751 1.40e-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: 557.45  E-value: 1.40e-179
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   89 LRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGE--DIINAYSGQNMGDMD-PHIFAVAEEAYKQMARD----ERNQSIIV 161
Cdd:cd14892      7 LRRRY-ERDAIYTFTADILISINPYKSIPLLYDvpGFDSQRKEEATASSPpPHVFSIAERAYRAMKGVgkgqGTPQSIVV 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  162 SGESGAGKTVSAKYAMRYFATVSGSASEA-----------NVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDK 230
Cdd:cd14892     86 SGESGAGKTEASKYIMKYLATASKLAKGAstskgaanaheSIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQIHYNS 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  231 RYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQ 310
Cdd:cd14892    166 DGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGNCVEVDGVDDATEFKQLRD 245

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  311 ACTLLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEP--LCIFCELMGVDYEEMCHWLCHRKLATATETYI 388
Cdd:cd14892    246 AMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDVFAQSADGvnVAKAAGLLGVDAAELMFKLVTQTTSTARGSVL 325

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  389 K-PISKLQATNARDALAKHIYAKLFNWIVDNVNqALHSAV-----------KQHSFIGVLDIYGFETFEINSFEQFCINY 456
Cdd:cd14892    326 EiKLTAREAKNALDALCKYLYGELFDWLISRIN-ACHKQQtsgvtggaaspTFSPFIGILDIFGFEIMPTNSFEQLCINF 404

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  457 ANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMP-KGTDDTWAQKLYNTHLNK 534
Cdd:cd14892    405 TNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQDNQDCLDLIQKKpLGLLPLLEEQMLLKrKTTDKQLLTIYHQTHLDK 484

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  535 CALFEKPRLSNKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKfkmlpelfqddekaisptsatssgrtpltr 614
Cdd:cd14892    485 HPHYAKPRFECDEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSS------------------------------ 534

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  615 tpakptkgrpgqmakehkktvghQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISA 694
Cdd:cd14892    535 -----------------------KFRTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRR 591

                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1677538261  695 AGFPSRWTYQEFFSRYRVLMKQKDVLSDRKQTCKNVLE--------KLILDKDKYQFGKTKIFFR 751
Cdd:cd14892    592 EGFPIRRQFEEFYEKFWPLARNKAGVAASPDACDATTArkkceeivARALERENFQLGRTKVFLR 656
MYSc_Myh3 cd14913
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ...
 83-751 7.60e-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: 556.20  E-value: 7.60e-179
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14913      1 PAVLYNLKDRY-TSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  163 GESGAGKTVSAKYAMRYFATVSG---------SASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYR 233
Cdd:cd14913     80 GESGAGKTVNTKRVIQYFATIAAtgdlakkkdSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  234 IIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLG-NADNFNYTKQGgSPVIEGVDDAKEMAHTRQAC 312
Cdd:cd14913    160 LASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITtNPYDYPFISQG-EILVASIDDAEELLATDSAI 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  313 TLLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKPIS 392
Cdd:cd14913    239 DILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQT 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  393 KLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKL 472
Cdd:cd14913    319 VDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVL 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  473 EQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPR-LSNKA--- 547
Cdd:cd14913    399 EQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKvVKGRAeah 478

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  548 FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFqddekaisPTSATSSGrtPLTRTPAKPTKGRPGQm 627
Cdd:cd14913    479 FSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLY--------ATFATADA--DSGKKKVAKKKGSSFQ- 547

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  628 akehkkTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFF 707
Cdd:cd14913    548 ------TVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFK 621

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*..
gi 1677538261  708 SRYRVLMKQ---KDVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14913    622 QRYRVLNASaipEGQFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
MYSc_Myo43 cd14904
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ...
 83-751 1.12e-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: 549.54  E-value: 1.12e-176
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   83 PAVLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLP-IYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIV 161
Cdd:cd14904      1 PSILFNLKKRFAASK-PYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  162 SGESGAGKTVSAKYAMRYFATVSGSASEANVEeKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRT 241
Cdd:cd14904     80 SGESGAGKTETTKIVMNHLASVAGGRKDKTIA-KVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAKCET 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  242 YLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQG-GSPVIEGVDDAKEMAHTRQACTLLGISES 320
Cdd:cd14904    159 YLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLGDSlAQMQIPGLDDAKLFASTQKSLSLIGLDND 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  321 HQMGIFRILAGILHLGNVGFTSRDADSCTIPpKHEPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNAR 400
Cdd:cd14904    239 AQRTLFKILSGVLHLGEVMFDKSDENGSRIS-NGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLAPVEAEENR 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  401 DALAKHIYAKLFNWIVDNVNQAL---HSAVKQHsfIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEY 477
Cdd:cd14904    318 DALAKAIYSKLFDWMVVKINAAIstdDDRIKGQ--IGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKTVEEEY 395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  478 MKEQIPWTLIDFYDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHL----NKCALFekPRLSNKAFIIQHF 553
Cdd:cd14904    396 IREGLQWDHIEYQDNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHQtkkdNESIDF--PKVKRTQFIINHY 473

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  554 ADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEkAISPTSATSSGRtpltrtpakptkgrpgqmAKEHKK 633
Cdd:cd14904    474 AGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSE-APSETKEGKSGK------------------GTKAPK 534

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  634 TVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVL 713
Cdd:cd14904    535 SLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIM 614

                          650       660       670
                   ....*....|....*....|....*....|....*....
gi 1677538261  714 MKQKDVLSDRKQTCKNVLEKLILDKD-KYQFGKTKIFFR 751
Cdd:cd14904    615 FPPSMHSKDVRRTCSVFMTAIGRKSPlEYQIGKSLIYFK 653
MYSc_Myh7b cd14927
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ...
 84-751 6.50e-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: 548.40  E-value: 6.50e-176
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   84 AVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd14927      2 SVLHNLRRRY-SRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  164 ESGAGKTVSAKYAMRYFATVS-------------GSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDK 230
Cdd:cd14927     81 ESGAGKTVNTKRVIQYFAIVAalgdgpgkkaqflATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  231 RYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKlPEFK--MLRLGNADNFNYTKQGGSPViEGVDDAKEMAHT 308
Cdd:cd14927    161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKK-PELQdmLLVSMNPYDYHFCSQGVTTV-DNMDDGEELMAT 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  309 RQACTLLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATETYI 388
Cdd:cd14927    239 DHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVT 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  389 KPISKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMH 468
Cdd:cd14927    319 KGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHH 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  469 VFKLEQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRLSNKA 547
Cdd:cd14927    399 MFILEQEEYKREGIEWVFIDFgLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPDKKR 478

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  548 -----FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFqddEKAISPTSATSsgrtPLTRTPAKPTKG 622
Cdd:cd14927    479 kyeahFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLY---ENYVGSDSTED----PKSGVKEKRKKA 551

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  623 RPGQmakehkkTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWT 702
Cdd:cd14927    552 ASFQ-------TVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRIL 624

                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1677538261  703 YQEFFSRYRVLMKQ---KDVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14927    625 YADFKQRYRILNPSaipDDKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
MYSc_Myh10 cd14920
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ...
 84-751 1.25e-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: 542.29  E-value: 1.25e-173
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   84 AVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd14920      2 SVLHNLKDRYY-SGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  164 ESGAGKTVSAKYAMRYFATVSGS-------ASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIG 236
Cdd:cd14920     81 ESGAGKTENTKKVIQYLAHVASShkgrkdhNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  237 ANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPvIEGVDDAKEMAHTRQACTLLG 316
Cdd:cd14920    161 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIP-IPGQQDKDNFQETMEAMHIMG 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  317 ISESHQMGIFRILAGILHLGNVGF-TSRDADSCTIpPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKPISKLQ 395
Cdd:cd14920    240 FSHEEILSMLKVVSSVLQFGNISFkKERNTDQASM-PENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQ 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  396 ATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQ-HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQ 474
Cdd:cd14920    319 ADFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQ 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  475 EEYMKEQIPWTLIDF-YDNQPCINLIESKL---GILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRLSNKA-FI 549
Cdd:cd14920    399 EEYQREGIEWNFIDFgLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKAdFC 478

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  550 IQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKaISPTSATSSGRTPLTRTPAKPTKGRpgqmak 629
Cdd:cd14920    479 IIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDR-IVGLDQVTGMTETAFGSAYKTKKGM------ 551

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  630 ehKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSR 709
Cdd:cd14920    552 --FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQR 629

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....
gi 1677538261  710 YRVLMKQK--DVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
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 ...
 83-751 8.15e-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: 534.42  E-value: 8.15e-171
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   83 PAVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14909      1 ASVLHNLRQRYY-AKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLIT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  163 GESGAGKTVSAKYAMRYFATVSGS-------ASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRII 235
Cdd:cd14909     80 GESGAGKTENTKKVIAYFATVGASkktdeaaKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLA 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  236 GANMRTYLLEKSRVVFQAEEERNYHIFYQLcASAKLPEFKMLRL--GNADNFNYTKQGGSpVIEGVDDAKEMAHTRQACT 313
Cdd:cd14909    160 GADIETYLLEKARVISQQSLERSYHIFYQI-MSGSVPGVKEMCLlsDNIYDYYIVSQGKV-TVPNVDDGEEFSLTDQAFD 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  314 LLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKPISK 393
Cdd:cd14909    238 ILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNV 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  394 LQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLE 473
Cdd:cd14909    318 QQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLE 397

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  474 QEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRLSNKA----- 547
Cdd:cd14909    398 QEEYKREGIDWAFIDFgMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKPGqqaah 477

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  548 FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGRTpltrtpakpTKGrpGQM 627
Cdd:cd14909    478 FAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGEQAKGGRG---------KKG--GGF 546

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  628 AkehkkTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFF 707
Cdd:cd14909    547 A-----TVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFK 621

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*
gi 1677538261  708 SRYRVLM-KQKDVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14909    622 MRYKILNpAGIQGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
MYSc_Myo46 cd14907
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ...
 85-751 3.53e-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: 532.68  E-value: 3.53e-170
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   85 VLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLP---------IYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDER 155
Cdd:cd14907      3 LLINLKKRYQQDK-IFTYVGPTLIVMNPYKQIDnlfseevmqMYKEQIIQNGEYFDIKKEPPHIYAIAALAFKQLFENNK 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  156 NQSIIVSGESGAGKTVSAKYAMRYFATVSG------------------SASEANVEEKVLASNPIMESIGNAKTTRNDNS 217
Cdd:cd14907     82 KQAIVISGESGAGKTENAKYAMKFLTQLSQqeqnseevltltssiratSKSTKSIEQKILSCNPILEAFGNAKTVRNDNS 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  218 SRFGKYIEIGFDKRYR-IIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAK---LPEFKMLRLGNADNFNYTKQGGS 293
Cdd:cd14907    162 SRFGKYVSILVDKKKRkILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADqqlLQQLGLKNQLSGDRYDYLKKSNC 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  294 PVIEGVDDAKEMAHTRQACTLLGISESHQMGIFRILAGILHLGNVGFTSR--DADSCTIPPKHEPLCIFCELMGVDYEEM 371
Cdd:cd14907    242 YEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDStlDDNSPCCVKNKETLQIIAKLLGIDEEEL 321

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  372 CHWLCHRKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDNVNQAL--HSAVKQHSF------IGVLDIYGFET 443
Cdd:cd14907    322 KEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpKDEKDQQLFqnkylsIGLLDIFGFEV 401

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  444 FEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTL--IDFYDNQPCINLIES-KLGILDLLDEECKMPKGTD 520
Cdd:cd14907    402 FQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSYTDNQDVIDLLDKpPIGIFNLLDDSCKLATGTD 481

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  521 DTWAQKLYNTHLNKCALFEKPRLSNKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAis 600
Cdd:cd14907    482 EKLLNKIKKQHKNNSKLIFPNKINKDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFSGEDGS-- 559

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  601 ptsaTSSGRTPLTRTPAKptkgrpgqmakehKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQ 680
Cdd:cd14907    560 ----QQQNQSKQKKSQKK-------------DKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQ 622

                          650       660       670       680       690       700       710
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1677538261  681 LRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMkqkdvlsdrkqtcKNVLeklildkdkyqFGKTKIFFR 751
Cdd:cd14907    623 IRYLGVLESIRVRKQGYPYRKSYEDFYKQYSLLK-------------KNVL-----------FGKTKIFMK 669
Myo5c_CBD cd15476
Cargo binding domain of myosin 5C; Class V myosins are well studied unconventional myosins, ...
 1455-1822 2.42e-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: 517.03  E-value: 2.42e-169
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1455 EDEQKLVKNLILELKPRGVAVNLIPGLPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSNT 1534
Cdd:cd15476      1 EDEAKLIQNLILDLKPRGVVVNMIPGLPAHILFMCVRHADYLNDANKLKSLMNAIITGVKQVIKEHQEDFEMLSFWLSNT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1535 CRFLHCLKQYSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPmivsgmlehetiqgvsgv 1614
Cdd:cd15476     81 YHFLNCLKQYSGEEEFMKHNTPRQNKNCLKNFDLSEHRQILSDLAIRIYHQFISVMENNLQP------------------ 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1615 kptglrkrtssiadegtyTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQIRY 1694
Cdd:cd15476    143 ------------------TISSILQQLSYFYSTMCQHGMDPELIKQAVKQLFFLIGAVTLNSIFLRKDMCSCRKGMQIRC 204

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1695 NVSQLEEWLRDKNLMNSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERVSVSFI 1774
Cdd:cd15476    205 NISYLEEWLKEKNLQNSNAKETLEPLSQAAWLLQVNKTTDDDAKEICERCTELSAVQIVKILNSYTPIDDFEKRVTPSFV 284

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 1677538261 1775 RTIQMRLRDRKDSPQLLMDAKHIFPVTFPFNPSSLALETIQIPASLGL 1822
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 ...
 84-751 3.52e-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: 524.93  E-value: 3.52e-167
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   84 AVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd14911      2 SVLHNIKDRYY-SGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  164 ESGAGKTVSAKYAMRYFATVSGSASEAN----------------VEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIG 227
Cdd:cd14911     81 ESGAGKTENTKKVIQFLAYVAASKPKGSgavphpavnpavligeLEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  228 FDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPViEGVDDAKEMAH 307
Cdd:cd14911    161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPV-PGVDDYAEFQA 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  308 TRQACTLLGISESHQMGIFRILAGILHLGNVGF-TSRDADSCTIPPKHEPLCIfCELMGVDYEEMCHWLCHRKLATATET 386
Cdd:cd14911    240 TVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFrQERNNDQATLPDNTVAQKI-AHLLGLSVTDMTRAFLTPRIKVGRDF 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  387 YIKPISKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQ-HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQF 465
Cdd:cd14911    319 VTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQgASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLF 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  466 NMHVFKLEQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHlNKCALFEKPRLS 544
Cdd:cd14911    399 NHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAH-SMHPKFMKTDFR 477

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  545 NKA-FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSgrtplTRTPAKPTKGR 623
Cdd:cd14911    478 GVAdFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIVGMAQQALTD-----TQFGARTRKGM 552

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  624 pgqmakehKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTY 703
Cdd:cd14911    553 --------FRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPF 624

                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|
gi 1677538261  704 QEFFSRYRVLMKQ--KDVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14911    625 QEFRQRYELLTPNviPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
MYSc_Myo47 cd14908
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ...
 83-751 9.92e-167

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: 524.09  E-value: 9.92e-167
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAY------SGQNM---GDMDPHIFAVAEEAYKQMARD 153
Cdd:cd14908      1 PAILHSLSRRF-FRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYrqegllRSQGIespQALGPHVFAIADRSYRQMMSE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  154 ER-NQSIIVSGESGAGKTVSAKYAMRYFATV----------SGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGK 222
Cdd:cd14908     80 IRaSQSILISGESGAGKTESTKIVMLYLTTLgngeegapneGEELGKLSIMDRVLQSNPILEAFGNARTLRNDNSSRFGK 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  223 YIEIGFDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASA--------KLPEFKMLRLGNADNFNYTKQGGSP 294
Cdd:cd14908    160 FIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGdeeehekyEFHDGITGGLQLPNEFHYTGQGGAP 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  295 VIEGVDDAKEMAHTRQACTLLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPK---HEPLCIFCELMGVDYEEM 371
Cdd:cd14908    240 DLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEegnEKCLARVAKLLGVDVDKL 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  372 CHWLCHRKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQ--HSFIGVLDIYGFETFEINSF 449
Cdd:cd14908    320 LRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKdiRSSVGVLDIFGFECFAHNSF 399

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  450 EQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIES-KLGILDLLDEECKMP-KGTDDTWAQKL 527
Cdd:cd14908    400 EQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFPDNQDCLDTIQAkKKGILTMLDDECRLGiRGSDANYASRL 479

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  528 YNTHLNKC--ALFEKPRLSNKA-------FIIQHFADKVEYQCE-GFLEKNKDtvfeeqiKVLKSSKfkmlpELFQDdek 597
Cdd:cd14908    480 YETYLPEKnqTHSENTRFEATSiqktkliFAVRHFAGQVQYTVEtTFCEKNKD-------EIPLTAD-----SLFES--- 544

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  598 aisptsatssgrtpltrtpakptkgrpgqmakehkktvGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRA 677
Cdd:cd14908    545 --------------------------------------GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRV 586

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  678 VQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMK--QKDVLS------DRKQTCKNVLEKLI-------------- 735
Cdd:cd14908    587 TEQLRYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLLPliPEVVLSwsmerlDPQKLCVKKMCKDLvkgvlspamvsmkn 666

                          730
                   ....*....|....*.
gi 1677538261  736 LDKDKYQFGKTKIFFR 751
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 ...
 83-751 1.02e-164

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: 518.12  E-value: 1.02e-164
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14917      1 PAVLYNLKERY-ASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  163 GESGAGKTVSAKYAMRYFATVSG---------SASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYR 233
Cdd:cd14917     80 GESGAGKTVNTKRVIQYFAVIAAigdrskkdqTPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  234 IIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRL-GNADNFNYTKQGGSPViEGVDDAKEMAHTRQAC 312
Cdd:cd14917    160 LASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLItNNPYDYAFISQGETTV-ASIDDAEELMATDNAF 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  313 TLLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKPIS 392
Cdd:cd14917    239 DVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQN 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  393 KLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKL 472
Cdd:cd14917    319 VQQVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  473 EQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPR-LSNKA--- 547
Cdd:cd14917    399 EQEEYKKEGIEWTFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPRnIKGKPeah 478

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  548 FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDdekaisptsaTSSGRTPLTRTPAKPTKGRPGQm 627
Cdd:cd14917    479 FSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFAN----------YAGADAPIEKGKGKAKKGSSFQ- 547

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  628 akehkkTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFF 707
Cdd:cd14917    548 ------TVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFR 621

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*..
gi 1677538261  708 SRYRVLMKQ---KDVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14917    622 QRYRILNPAaipEGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
MYSc_Myh6 cd14916
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ...
 83-751 3.00e-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: 511.53  E-value: 3.00e-162
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   83 PAVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14916      1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  163 GESGAGKTVSAKYAMRYFATVSG----------SASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRY 232
Cdd:cd14916     80 GESGAGKTVNTKRVIQYFASIAAigdrskkenpNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  233 RIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRL-GNADNFNYTKQGgSPVIEGVDDAKEMAHTRQA 311
Cdd:cd14916    160 KLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVtNNPYDYAFVSQG-EVSVASIDDSEELLATDSA 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  312 CTLLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKPI 391
Cdd:cd14916    239 FDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  392 SKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFK 471
Cdd:cd14916    319 SVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  472 LEQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPR----LSNK 546
Cdd:cd14916    399 LEQEEYKKEGIEWEFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRnvkgKQEA 478

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  547 AFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAisptSATSSGrtpltrtpakptKGRPGQ 626
Cdd:cd14916    479 HFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASA----DTGDSG------------KGKGGK 542

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  627 MAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEF 706
Cdd:cd14916    543 KKGSSFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDF 622

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*....
gi 1677538261  707 FSRYRVL----MKQKDVLSDRKQTCKnVLEKLILDKDKYQFGKTKIFFR 751
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 ...
 84-751 1.89e-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: 508.80  E-value: 1.89e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   84 AVLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd14934      2 SVLDNLRQRYTNMR-IYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  164 ESGAGKTVSAKYAMRYFATVSGSASEA-----NVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGAN 238
Cdd:cd14934     81 ESGAGKTENTKKVIQYFANIGGTGKQSsdgkgSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGAD 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  239 MRTYLLEKSRVVFQAEEERNYHIFYQLCASAKlPEF--KMLRLGNADNFNYTKQGGSpVIEGVDDAKEMAHTRQACTLLG 316
Cdd:cd14934    161 IESYLLEKSRVISQQAAERGYHIFYQILSNKK-PELieSLLLVPNPKEYHWVSQGVT-VVDNMDDGEELQITDVAFDVLG 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  317 ISESHQMGIFRILAGILHLGNVGFTSR------DADSCTIPPKheplciFCELMGVDYEEMCHWLCHRKLATATETYIKP 390
Cdd:cd14934    239 FSAEEKIGVYKLTGGIMHFGNMKFKQKpreeqaEVDTTEVADK------VAHLMGLNSGELQKGITRPRVKVGNEFVQKG 312

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  391 ISKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVF 470
Cdd:cd14934    313 QNMEQCNNSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMF 392

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  471 KLEQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKP-----RLS 544
Cdd:cd14934    393 VLEQEEYKREGIEWVFIDFgLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKPkggkgKGP 472

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  545 NKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFkMLPELFQDDEKAISPTSATSSGRTPLtrtpakptkgrp 624
Cdd:cd14934    473 EAHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSL-GLLALLFKEEEAPAGSKKQKRGSSFM------------ 539

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  625 gqmakehkkTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQ 704
Cdd:cd14934    540 ---------TVSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYP 610

                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1677538261  705 EFFSRYRVLmkQKDVLS----DRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
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 ...
 83-751 6.69e-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: 505.42  E-value: 6.69e-160
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   83 PAVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14912      1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  163 GESGAGKTVSAKYAMRYFATVSGSAS-----------EANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKR 231
Cdd:cd14912     80 GESGAGKTVNTKRVIQYFATIAVTGEkkkeeitsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  232 YRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLG-NADNFNYTKQGGSPViEGVDDAKEMAHTRQ 310
Cdd:cd14912    160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITtNPYDYPFVSQGEISV-ASIDDQEELMATDS 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  311 ACTLLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKP 390
Cdd:cd14912    239 AIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKG 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  391 ISKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVF 470
Cdd:cd14912    319 QTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  471 KLEQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRL----SN 545
Cdd:cd14912    399 VLEQEEYKKEGIEWTFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVvkgkAE 478

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  546 KAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSgrtpltrtpakpTKGrpG 625
Cdd:cd14912    479 AHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEGASAGGGA------------KKG--G 544

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  626 QMAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQE 705
Cdd:cd14912    545 KKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYAD 624

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*....
gi 1677538261  706 FFSRYRVLMKQ---KDVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14912    625 FKQRYKVLNASaipEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
MYSc_Myo28 cd14889
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ...
 85-751 2.08e-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: 503.28  E-value: 2.08e-159
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   85 VLHNLRVRFIDSkLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQM----ARDERNQSII 160
Cdd:cd14889      3 LLEVLKVRFMQS-NIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMlgrlARGPKNQCIV 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  161 VSGESGAGKTVSAKYAMRYFATVSGSASEanVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFdKRYRIIGANMR 240
Cdd:cd14889     82 ISGESGAGKTESTKLLLRQIMELCRGNSQ--LEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RNGHVKGAKIN 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  241 TYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQACTLLGISES 320
Cdd:cd14889    159 EYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLLDPGKYRYLNNGAGCKREVQYWKKKYDEVCNAMDMVGFTEQ 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  321 HQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHE-PLCIFCELMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNA 399
Cdd:cd14889    239 EEVDMFTILAGILSLGNITFEMDDDEALKVENDSNgWLKAAAGQFGVSEEDLLKTLTCTVTFTRGEQIQRHHTKQQAEDA 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  400 RDALAKHIYAKLFNWIVDNVNQALHSAVK---QHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEE 476
Cdd:cd14889    319 RDSIAKVAYGRVFGWIVSKINQLLAPKDDssvELREIGILDIFGFENFAVNRFEQACINLANEQLQYFFNHHIFLMEQKE 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  477 YMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLyNTHLNKCALFEKPRLSNKAFIIQHFAD 555
Cdd:cd14889    399 YKKEGIDWKEITYKDNKPILDLFLNKpIGILSLLDEQSHFPQATDESFVDKL-NIHFKGNSYYGKSRSKSPKFTVNHYAG 477

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  556 KVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFqddekaisptsATSSGRTPLTRTPAKPTKGRPGQMAKEHKKTV 635
Cdd:cd14889    478 KVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLF-----------TATRSRTGTLMPRAKLPQAGSDNFNSTRKQSV 546

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  636 GHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMK 715
Cdd:cd14889    547 GAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAERYKILLC 626

                          650       660       670
                   ....*....|....*....|....*....|....*.
gi 1677538261  716 QKDvLSDRKQTCKNVLEKliLDKDKYQFGKTKIFFR 751
Cdd:cd14889    627 EPA-LPGTKQSCLRILKA--TKLVGWKCGKTRLFFK 659
MYSc_Myh13 cd14923
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ...
 83-751 2.45e-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: 503.45  E-value: 2.45e-159
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   83 PAVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14923      1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILIT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  163 GESGAGKTVSAKYAMRYFATVS----------GSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRY 232
Cdd:cd14923     80 GESGAGKTVNTKRVIQYFATIAvtgdkkkeqqPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  233 RIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKlPEFKMLRL--GNADNFNYTKQGgSPVIEGVDDAKEMAHTRQ 310
Cdd:cd14923    160 KLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKK-PELIDLLLisTNPFDFPFVSQG-EVTVASIDDSEELLATDN 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  311 ACTLLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKP 390
Cdd:cd14923    238 AIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKG 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  391 ISKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVF 470
Cdd:cd14923    318 QNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 397

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  471 KLEQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPR-LSNKA- 547
Cdd:cd14923    398 VLEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKpAKGKAe 477

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  548 --FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFqddekaiSPTSATSSGRTPLTRTPAKpTKGRPG 625
Cdd:cd14923    478 ahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLF-------SNYAGAEAGDSGGSKKGGK-KKGSSF 549

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  626 QmakehkkTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQE 705
Cdd:cd14923    550 Q-------TVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYAD 622

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*....
gi 1677538261  706 FFSRYRVLMKQ---KDVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14923    623 FKQRYRILNASaipEGQFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
MYSc_Myh8 cd14918
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ...
 83-751 6.05e-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: 502.34  E-value: 6.05e-159
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   83 PAVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14918      1 PGVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  163 GESGAGKTVSAKYAMRYFATVSGSAS---------EANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYR 233
Cdd:cd14918     80 GESGAGKTVNTKRVIQYFATIAVTGEkkkeesgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  234 IIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLG-NADNFNYTKQGgSPVIEGVDDAKEMAHTRQAC 312
Cdd:cd14918    160 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITtNPYDYAFVSQG-EITVPSIDDQEELMATDSAI 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  313 TLLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKPIS 392
Cdd:cd14918    239 DILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  393 KLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKL 472
Cdd:cd14918    319 VQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  473 EQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRL----SNKA 547
Cdd:cd14918    399 EQEEYKKEGIEWTFIDFgMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVvkgkAEAH 478

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  548 FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGRtpltrtpakpTKGRPGQm 627
Cdd:cd14918    479 FSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSGAKKGAK----------KKGSSFQ- 547

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  628 akehkkTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFF 707
Cdd:cd14918    548 ------TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFK 621

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*..
gi 1677538261  708 SRYRVLMKQ---KDVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14918    622 QRYKVLNASaipEGQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
MYSc_Myo36 cd14897
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ...
 85-751 4.36e-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: 498.83  E-value: 4.36e-158
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   85 VLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDM-DPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd14897      3 IVQTLKSRYNKDK-FYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSVRSQrPPHLFWIADQAYRRLLETGRNQCILVSG 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  164 ESGAGKTVSAKYAMRYFATVSGSASEaNVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYL 243
Cdd:cd14897     82 ESGAGKTESTKYMIKHLMKLSPSDDS-DLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAKIDDYL 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  244 LEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNyTKQGGSPVIEGVDDAKEMAHTRQACT-------LLG 316
Cdd:cd14897    161 LEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHR-ILRDDNRNRPVFNDSEELEYYRQMFHdltnimkLIG 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  317 ISESHQMGIFRILAGILHLGNVGF-TSRDADSCTIPPKHePLCIFCELMGVDYEEMCHWLCHRKLATATETYIKPISKLQ 395
Cdd:cd14897    240 FSEEDISVIFTILAAILHLTNIVFiPDEDTDGVTVADEY-PLHAVAKLLGIDEVELTEALISNVNTIRGERIQSWKSLRQ 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  396 ATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQH-----SFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVF 470
Cdd:cd14897    319 ANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDFQimtrgPSIGILDMSGFENFKINSFDQLCINLSNERLQQYFNDYVF 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  471 KLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLyNTHLNKCALFEKPRLSNKAFI 549
Cdd:cd14897    399 PRERSEYEIEGIEWRDIEYHDNDDVLELFFKKpLGILPLLDEESTFPQSTDSSLVQKL-NKYCGESPRYVASPGNRVAFG 477

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  550 IQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFqddekaispTSatssgrtpltrtpakptkgrpgqmak 629
Cdd:cd14897    478 IRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLF---------TS-------------------------- 522

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  630 ehkktvghQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSR 709
Cdd:cd14897    523 --------YFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKR 594

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|...
gi 1677538261  710 YRVLM-KQKDVLSDRKQTCKNVLEklILDKDKYQFGKTKIFFR 751
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 ...
 83-751 3.65e-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: 497.72  E-value: 3.65e-157
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   83 PAVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14910      1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  163 GESGAGKTVSAKYAMRYFATVSGSAS-----------EANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKR 231
Cdd:cd14910     80 GESGAGKTVNTKRVIQYFATIAVTGEkkkeeatsgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  232 YRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLG-NADNFNYTKQGgSPVIEGVDDAKEMAHTRQ 310
Cdd:cd14910    160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITtNPYDYAFVSQG-EITVPSIDDQEELMATDS 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  311 ACTLLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKP 390
Cdd:cd14910    239 AIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKG 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  391 ISKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVF 470
Cdd:cd14910    319 QTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  471 KLEQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRLSNKA-- 547
Cdd:cd14910    399 VLEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKve 478

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  548 --FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFqddekaisptsatsSGRTPLTRTPAKPTKGrpG 625
Cdd:cd14910    479 ahFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLF--------------SGAAAAEAEEGGGKKG--G 542

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  626 QMAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQE 705
Cdd:cd14910    543 KKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYAD 622

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*....
gi 1677538261  706 FFSRYRVLMKQ---KDVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14910    623 FKQRYKVLNASaipEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
MYSc_Myh18 cd14932
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ...
 84-751 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: 496.47  E-value: 1.10e-156
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   84 AVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd14932      2 SVLHNLKERYY-SGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  164 ESGAGKTVSAKYAMRYFATVSGSA-----------SEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRY 232
Cdd:cd14932     81 ESGAGKTENTKKVIQYLAYVASSFktkkdqssialSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  233 RIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQgGSPVIEGVDDAKEMAHTRQAC 312
Cdd:cd14932    161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSN-GNVTIPGQQDKELFAETMEAF 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  313 TLLGISESHQMGIFRILAGILHLGNVGF-TSRDADSCTIPPKHEPLCIfCELMGVDYEEMCHWLCHRKLATATETYIKPI 391
Cdd:cd14932    240 RIMSIPEEEQTGLLKVVSAVLQLGNMSFkKERNSDQASMPDDTAAQKV-CHLLGMNVTDFTRAILSPRIKVGRDYVQKAQ 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  392 SKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQ-HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVF 470
Cdd:cd14932    319 TQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  471 KLEQEEYMKEQIPWTLIDF-YDNQPCINLIESKL---GILDLLDEECKMPKGTDDTWAQKLYNTHLNKcALFEKP-RLSN 545
Cdd:cd14932    399 ILEQEEYQREGIEWSFIDFgLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVVQEQGNN-PKFQKPkKLKD 477

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  546 KA-FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSsgrtpLTRTPAKPTKGRP 624
Cdd:cd14932    478 DAdFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRIVGLDKVAG-----MGESLHGAFKTRK 552

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  625 GQMakehkKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQ 704
Cdd:cd14932    553 GMF-----RTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 627

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*....
gi 1677538261  705 EFFSRYRVLMKQK--DVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14932    628 EFRQRYEILTPNAipKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
MYSc_Myh4 cd14915
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ...
 83-751 1.35e-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: 496.17  E-value: 1.35e-156
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   83 PAVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14915      1 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  163 GESGAGKTVSAKYAMRYFATVSGSAS-----------EANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKR 231
Cdd:cd14915     80 GESGAGKTVNTKRVIQYFATIAVTGEkkkeeaasgkmQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  232 YRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLG-NADNFNYTKQGgSPVIEGVDDAKEMAHTRQ 310
Cdd:cd14915    160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITtNPYDFAFVSQG-EITVPSIDDQEELMATDS 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  311 ACTLLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKP 390
Cdd:cd14915    239 AVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKG 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  391 ISKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVF 470
Cdd:cd14915    319 QTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  471 KLEQEEYMKEQIPWTLIDF-YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRLSN-KA- 547
Cdd:cd14915    399 VLEQEEYKKEGIEWEFIDFgMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKgKAe 478

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  548 --FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGrtpltrtpakptkgrpG 625
Cdd:cd14915    479 ahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQTAEAEGGGGKKG----------------G 542

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  626 QMAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQE 705
Cdd:cd14915    543 KKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYAD 622

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*....
gi 1677538261  706 FFSRYRVLMKQ---KDVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14915    623 FKQRYKVLNASaipEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
MYSc_Myh11 cd14921
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ...
 84-751 2.36e-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: 2.36e-156
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   84 AVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd14921      2 SVLHNLRERYF-SGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  164 ESGAGKTVSAKYAMRYFATVSGS-------ASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIG 236
Cdd:cd14921     81 ESGAGKTENTKKVIQYLAVVASShkgkkdtSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  237 ANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPvIEGVDDAKEMAHTRQACTLLG 316
Cdd:cd14921    161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVP-IPAAQDDEMFQETLEAMSIMG 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  317 ISESHQMGIFRILAGILHLGNVGF-TSRDADSCTIPPKHEPLCIfCELMGVDYEEMCHWLCHRKLATATETYIKPISKLQ 395
Cdd:cd14921    240 FSEEEQLSILKVVSSVLQLGNIVFkKERNTDQASMPDNTAAQKV-CHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQ 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  396 ATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQ-HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQ 474
Cdd:cd14921    319 ADFAIEALAKATYERLFRWILTRVNKALDKTHRQgASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQ 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  475 EEYMKEQIPWTLIDF-YDNQPCINLIE---SKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKcALFEKPR-LSNKA-F 548
Cdd:cd14921    399 EEYQREGIEWNFIDFgLDLQPCIELIErpnNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNH-PKFQKPKqLKDKTeF 477

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  549 IIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGRTPLTrTPAKPTKGRpgqma 628
Cdd:cd14921    478 SIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSLP-SASKTKKGM----- 551

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  629 kehKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFS 708
Cdd:cd14921    552 ---FRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 628

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*
gi 1677538261  709 RYRVLMKQK--DVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14921    629 RYEILAANAipKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
MYSc_Myo30 cd14891
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ...
 83-751 2.15e-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: 491.87  E-value: 2.15e-155
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   83 PAVLHNLRVRF-IDSKLIYTYCGIVLVAINPYEQLPiygEDIINAYSGQNMGDMDPHIFAVAEEAYKQM---ARDERNQS 158
Cdd:cd14891      1 AGILHNLEERSkLDNQRPYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMclgSGRMQNQS 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  159 IIVSGESGAGKTVSAKYAMRYFATVS-----------------GSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFG 221
Cdd:cd14891     78 IVISGESGAGKTETSKIILRFLTTRAvggkkasgqdieqsskkRKLSVTSLDERLMDTNPILESFGNAKTLRNHNSSRFG 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  222 KYIEIGFDKR-YRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVD 300
Cdd:cd14891    158 KFMKLQFTKDkFKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNQSGCVSDDNID 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  301 DAKEMAHTRQACTLLGISESHQMGIFRILAGILHLGNVGFTSRD-----ADSCTIPPKhEPLCIFCELMGVDYEEMCHWL 375
Cdd:cd14891    238 DAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDtsegeAEIASESDK-EALATAAELLGVDEEALEKVI 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  376 CHRKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEI-NSFEQFCI 454
Cdd:cd14891    317 TQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFETkNDFEQLLI 396

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  455 NYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESKL-GILDLLDEECKMPKGTDDTWAQKLYNTHL- 532
Cdd:cd14891    397 NYANEALQATFNQQVFIAEQELYKSEGIDVGVITWPDNRECLDLIASKPnGILPLLDNEARNPNPSDAKLNETLHKTHKr 476

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  533 NKCALFEKPRLSNKAFIIQHFADKVEYQCEGFLEKNKDTVfeeqikvlksskfkmlPELFQDdekaisptsatssgrtpL 612
Cdd:cd14891    477 HPCFPRPHPKDMREMFIVKHYAGTVSYTIGSFIDKNNDII----------------PEDFED-----------------L 523

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  613 TRTPAKptkgrpgqmakehkktvghqFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRI 692
Cdd:cd14891    524 LASSAK--------------------FSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEV 583

                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1677538261  693 SAAGFPSRWTYQEFFSRYRVLM----KQKDVLSDRKQTcKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14891    584 LKVGLPTRVTYAELVDVYKPVLppsvTRLFAENDRTLT-QAILWAFRVPSDAYRLGRTRVFFR 645
MYSc_Myo19 cd14880
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ...
 85-749 5.55e-154

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: 5.55e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   85 VLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLP-IYGEDIINAY-SGQNMGDMDPHIFAVAEEAYK--QMARDERNQSII 160
Cdd:cd14880      3 VLRCLQARYT-ADTFYTNAGCTLVALNPFKPVPqLYSPELMREYhAAPQPQKLKPHIFTVGEQTYRnvKSLIEPVNQSIV 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  161 VSGESGAGKTVSAKYAMRYFATVSGSAS--EAN-----VEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYR 233
Cdd:cd14880     82 VSGESGAGKTWTSRCLMKFYAVVAASPTswESHkiaerIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQQ 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  234 IIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTkqggsPVIEGVDDAKEMAHTRQACT 313
Cdd:cd14880    162 MTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWL-----PNPERNLEEDCFEVTREAML 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  314 LLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEPLC---IFCELMGVDYEEMCHWLCHRKLATATE--TYI 388
Cdd:cd14880    237 HLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTKEsvrTSALLLKLPEDHLLETLQIRTIRAGKQqqVFK 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  389 KPISKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQ-HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNM 467
Cdd:cd14880    317 KPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSwTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQHFVA 396

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  468 HVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIE-SKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRLSNK 546
Cdd:cd14880    397 HYLRAQQEEYAVEGLEWSFINYQDNQTCLDLIEgSPISICSLINEECRLNRPSSAAQLQTRIESALAGNPCLGHNKLSRE 476

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  547 -AFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGRTPLTrtpakptkgrpg 625
Cdd:cd14880    477 pSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEKTQEEPSGQSRAPVL------------ 544

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  626 qmakehkkTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQE 705
Cdd:cd14880    545 --------TVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQN 616

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....
gi 1677538261  706 FFSRYRVLMKqkdvLSDRKQTCKNVLEKLILDKDKYQFGKTKIF 749
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 ...
 84-751 1.93e-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: 1.93e-151
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   84 AVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd14919      2 SVLHNLKERYY-SGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  164 ESGAGKTVSAKYAMRYFATVSGS----ASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANM 239
Cdd:cd14919     81 ESGAGKTENTKKVIQYLAHVASShkskKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  240 RTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQgGSPVIEGVDDAKEMAHTRQACTLLGISE 319
Cdd:cd14919    161 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSN-GHVTIPGQQDKDMFQETMEAMRIMGIPE 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  320 SHQMGIFRILAGILHLGNVGF-TSRDADSCTIPPKHEPLCIfCELMGVDYEEMCHWLCHRKLATATETYIKPISKLQATN 398
Cdd:cd14919    240 EEQMGLLRVISGVLQLGNIVFkKERNTDQASMPDNTAAQKV-SHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQADF 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  399 ARDALAKHIYAKLFNWIVDNVNQALHSAVKQ-HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEY 477
Cdd:cd14919    319 AIEALAKATYERMFRWLVLRINKALDKTKRQgASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEEY 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  478 MKEQIPWTLIDF-YDNQPCINLIESKL---GILDLLDEECKMPKGTDDTWAQKLYN---THLNkcalFEKPR-LSNKA-F 548
Cdd:cd14919    399 QREGIEWNFIDFgLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQeqgTHPK----FQKPKqLKDKAdF 474

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  549 IIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGRTPLtrtpAKPTKGRPGQMa 628
Cdd:cd14919    475 CIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETAL----PGAFKTRKGMF- 549

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  629 kehkKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFS 708
Cdd:cd14919    550 ----RTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQ 625

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*
gi 1677538261  709 RYRVLMKQK--DVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14919    626 RYEILTPNSipKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
MYSc_Myo41 cd14902
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ...
 83-751 6.44e-151

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: 6.44e-151
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLP-IYGEDIINAY--------SGQNMGDMDPHIFAVAEEAYKQMARD 153
Cdd:cd14902      1 AALLQALSERF-EHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYkasmtstsPVSQLSELPPHVFAIGGKAFGGLLKP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  154 ER-NQSIIVSGESGAGKTVSAKYAMRYFATVSGSASEANVE--------EKVLASNPIMESIGNAKTTRNDNSSRFGKYI 224
Cdd:cd14902     80 ERrNQSILVSGESGSGKTESTKFLMQFLTSVGRDQSSTEQEgsdaveigKRILQTNPILESFGNAQTIRNDNSSRFGKFI 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  225 EIGFDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGS----PVIEGVD 300
Cdd:cd14902    160 KIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELLNSYGPsfarKRAVADK 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  301 DAKEMAHTRQACTLLGISESHQMGIFRILAGILHLGNVGFT---SRDADSCTIPPKHEPLCIFCELMGVDYEEMCHWLCH 377
Cdd:cd14902    240 YAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTaenGQEDATAVTAASRFHLAKCAELMGVDVDKLETLLSS 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  378 RKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSF---------IGVLDIYGFETFEINS 448
Cdd:cd14902    320 REIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINYFDSAVSIsdedeelatIGILDIFGFESLNRNG 399

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  449 FEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESKL-GILDLLDEECKMPKGTDDTWAQKL 527
Cdd:cd14902    400 FEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYPSNAACLALFDDKSnGLFSLLDQECLMPKGSNQALSTKF 479

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  528 YNTHLNKcalfekprlsnKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEK--AISPTSAT 605
Cdd:cd14902    480 YRYHGGL-----------GQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGADENRdsPGADNGAA 548

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  606 SSGRTPLTRTPakptkgrpgqmakehkkTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACG 685
Cdd:cd14902    549 GRRRYSMLRAP-----------------SVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVG 611

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  686 VLETIRISAAGFPSRWTYQEF---FSRYRVLMKQKD----------------------VLSDRKQTCKNVLEKLILDKDK 740
Cdd:cd14902    612 VLEAVRIARHGYSVRLAHASFielFSGFKCFLSTRDraakmnnhdlaqalvtvlmdrvLLEDGVEREEKNPGALTAVTGD 691

                          730       740
                   ....*....|....*....|....*
gi 1677538261  741 Y--------------QFGKTKIFFR 751
Cdd:cd14902    692 GsgtafendcrrkdvQVGRTLVFCK 716
MYSc_Myo34 cd14895
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ...
 83-751 1.54e-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: 1.54e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   83 PAVLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLP-IYGediINAYSGQNMGDMD--PHIFAVAEEAYKQMAR------- 152
Cdd:cd14895      1 PAFVDYLAQRYGVDQ-VYCRSGAVLIAVNPFKHIPgLYD---LHKYREEMPGWTAlpPHVFSIAEGAYRSLRRrlhepga 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  153 DERNQSIIVSGESGAGKTVSAKYAMRYFA--------TVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYI 224
Cdd:cd14895     77 SKKNQTILVSGESGAGKTETTKFIMNYLAesskhttaTSSSKRRRAISGSELLSANPILESFGNARTLRNDNSSRFGKFV 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  225 EIGF-----DKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLG--NADNFNYTKQGGSPVI- 296
Cdd:cd14895    157 RMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLEllSAQEFQYISGGQCYQRn 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  297 EGVDDAKEMAHTRQACTLLGISESHQMGIFRILAGILHLGNVGFTS-------RDADSCTIPPK-----------HEPLC 358
Cdd:cd14895    237 DGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVAssedegeEDNGAASAPCRlasaspssltvQQHLD 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  359 IFCELMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDNVNQAlhSAVKQHS------- 431
Cdd:cd14895    317 IVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSA--SPQRQFAlnpnkaa 394

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  432 ------FIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LG 504
Cdd:cd14895    395 nkdttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDNSVCLEMLEQRpSG 474

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  505 ILDLLDEECKMPKGTDDTWAQKLYNThLNKCALFEKPRL--SNKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKS 582
Cdd:cd14895    475 IFSLLDEECVVPKGSDAGFARKLYQR-LQEHSNFSASRTdqADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAELFSVLGK 553

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  583 SKFKMLPELFqdDEKAISPTSATSSGRTPLTRtpakptkgRPGQMAkehKKTVGHQFRNSLHLLMETLNATTPHYVRCIK 662
Cdd:cd14895    554 TSDAHLRELF--EFFKASESAELSLGQPKLRR--------RSSVLS---SVGIGSQFKQQLASLLDVVQQTQTHYIRCIK 620

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  663 PNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMKQKDVLSdrkQTCKNVLEKliLDKDKYQ 742
Cdd:cd14895    621 PNDESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKNASD---ATASALIET--LKVDHAE 695


                   ....*....
gi 1677538261  743 FGKTKIFFR 751
Cdd:cd14895    696 LGKTRVFLR 704
MYSc_Myo39 cd14900
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ...
 85-725 2.18e-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: 474.79  E-value: 2.18e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   85 VLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLP-IYGEDIINAY---------SGQNMGD--MDPHIFAVAEEAYKQMAR 152
Cdd:cd14900      3 ILSALETRFYAQK-IYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssSTRNKGSdpMPPHIYQVAGEAYKAMML 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  153 ----DERNQSIIVSGESGAGKTVSAKYAMRYFA---------TVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSR 219
Cdd:cd14900     82 glngVMSDQSILVSGESGSGKTESTKFLMEYLAqagdnnlaaSVSMGKSTSGIAAKVLQTNILLESFGNARTLRNDNSSR 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  220 FGKYIEIGFDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKmlrlgnADNFNYtkqggspviegV 299
Cdd:cd14900    162 FGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARK------RDMYRR-----------V 224

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  300 DDAKEMahtrqactlLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHE--PLCIF-----CELMGVDYEEMC 372
Cdd:cd14900    225 MDAMDI---------IGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSDlaPSSIWsrdaaATLLSVDATKLE 295

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  373 HWLCHRKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDNVNQALH--SAVKQHS---FIGVLDIYGFETFEIN 447
Cdd:cd14900    296 KALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLKmdDSSKSHGglhFIGILDIFGFEVFPKN 375

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  448 SFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQK 526
Cdd:cd14900    376 SFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFCDNQDCVNLISQRpTGILSLIDEECVMPKGSDTTLASK 455

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  527 LYnTHLNKCALFEKPRL--SNKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIkvlksskfkmlpELFQDdekaisptsa 604
Cdd:cd14900    456 LY-RACGSHPRFSASRIqrARGLFTIVHYAGHVEYSTDGFLEKNKDVLHQEAV------------DLFVY---------- 512

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  605 tssgrtpltrtpakptkgrpgqmakehkktvGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRAC 684
Cdd:cd14900    513 -------------------------------GLQFKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCN 561

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|.
gi 1677538261  685 GVLETIRISAAGFPSRWTYQEFFSRYRVLMKQKDVLSDRKQ 725
Cdd:cd14900    562 GVMEAVRVARAGFPIRLLHDEFVARYFSLARAKNRLLAKKQ 602
MYSc_Myh19 cd15896
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ...
 84-751 3.21e-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: 476.10  E-value: 3.21e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   84 AVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd15896      2 SVLHNLKERYY-SGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  164 ESGAGKTVSAKYAMRYFATVSGS-----------ASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRY 232
Cdd:cd15896     81 ESGAGKTENTKKVIQYLAHVASShktkkdqnslaLSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  233 RIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQgGSPVIEGVDDAKEMAHTRQAC 312
Cdd:cd15896    161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSN-GNVTIPGQQDKDLFTETMEAF 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  313 TLLGISESHQMGIFRILAGILHLGNVGF-TSRDADSCTIPPKHEPLCIfCELMGVDYEEMCHWLCHRKLATATETYIKPI 391
Cdd:cd15896    240 RIMGIPEDEQIGMLKVVASVLQLGNMSFkKERHTDQASMPDNTAAQKV-CHLMGMNVTDFTRAILSPRIKVGRDYVQKAQ 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  392 SKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQ-HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVF 470
Cdd:cd15896    319 TQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  471 KLEQEEYMKEQIPWTLIDF-YDNQPCINLIE---SKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPRLSNK 546
Cdd:cd15896    399 ILEQEEYQREGIEWSFIDFgLDLQPCIDLIEkpaSPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKKLKDE 478

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  547 A-FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGRTPltrtpaKPTKGRPG 625
Cdd:cd15896    479 AdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVGLDKVSGMSEMP------GAFKTRKG 552

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  626 QMakehkKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQE 705
Cdd:cd15896    553 MF-----RTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 627

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*...
gi 1677538261  706 FFSRYRVLMKQK--DVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
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 ...
 84-751 3.73e-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: 3.73e-147
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   84 AVLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSG 163
Cdd:cd14930      2 SVLHNLRERYY-SGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  164 ESGAGKTVSAKYAMRYFATVSGSAS-------EANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIG 236
Cdd:cd14930     81 ESGAGKTENTKKVIQYLAHVASSPKgrkepgvPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  237 ANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGgsPVIEGVDDAKEMAHTRQACTLLG 316
Cdd:cd14930    161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNG--PSSSPGQERELFQETLESLRVLG 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  317 ISESHQMGIFRILAGILHLGNVGF-TSRDADSCTIpPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKPISKLQ 395
Cdd:cd14930    239 FSHEEITSMLRMVSAVLQFGNIVLkRERNTDQATM-PDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQ 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  396 ATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQ-HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQ 474
Cdd:cd14930    318 ADFALEALAKATYERLFRWLVLRLNRALDRSPRQgASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQ 397

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  475 EEYMKEQIPWTLIDF-YDNQPCINLIESKL---GILDLLDEECKMPKGTDDTWAQKLYNTHlNKCALFEKPR-LSNKA-F 548
Cdd:cd14930    398 EEYQREGIPWTFLDFgLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRPRhLRDQAdF 476

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  549 IIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGRtpltrtpaKPTKGRPgqmA 628
Cdd:cd14930    477 SVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGD--------GPPGGRP---R 545

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  629 KEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFS 708
Cdd:cd14930    546 RGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQ 625

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*
gi 1677538261  709 RYRVLMKQK--DVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14930    626 RYEILTPNAipKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
PTZ00014 PTZ00014
myosin-A; Provisional
 34-798 1.48e-141

myosin-A; Provisional


Pssm-ID: 240229 [Multi-domain]  Cd Length: 821  Bit Score: 460.27  E-value: 1.48e-141
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   34 GDKVLLLHLEEGKDLEYHLDPKtkelpHLRNPDILVGEN---DLTALSYLHEPAVLHNLRVRFIdSKLIYTYCGIVLVAI 110
Cdd:PTZ00014    63 GEKLTLKQIDPPTNSTFEVKPE-----HAFNANSQIDPMtygDIGLLPHTNIPCVLDFLKHRYL-KNQIYTTADPLLVAI 136

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  111 NPYEQLPIYGEDIINAY-SGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSGESGAGKTVSAKYAMRYFATVSGSASE 189
Cdd:PTZ00014   137 NPFKDLGNTTNDWIRRYrDAKDSDKLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFASSKSGNMD 216

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  190 ANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLC--A 267
Cdd:PTZ00014   217 LKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLkgA 296

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  268 SAKLPE-FKMLRLGNADNFNytkqGGSPVIEGVDDAKEMAHTRQACTLLGISESHQMGIFRILAGILHLGNVGFTSRDAD 346
Cdd:PTZ00014   297 NDEMKEkYKLKSLEEYKYIN----PKCLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEG 372

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  347 -----SCTIPPKHEPLCIFCELMGVDYEEMCHWLchrklaTATETYI------KPISKLQATNARDALAKHIYAKLFNWI 415
Cdd:PTZ00014   373 gltdaAAISDESLEVFNEACELLFLDYESLKKEL------TVKVTYAgnqkieGPWSKDESEMLKDSLSKAVYEKLFLWI 446

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  416 VDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPC 495
Cdd:PTZ00014   447 IRNLNATIEPPGGFKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGISTEELEYTSNESV 526

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  496 INLIESKL-GILDLLDEECKMPKGTDD----TWAQKLYNthlNKCALFEKpRLSNKAFIIQHFADKVEYQCEGFLEKNKD 570
Cdd:PTZ00014   527 IDLLCGKGkSVLSILEDQCLAPGGTDEkfvsSCNTNLKN---NPKYKPAK-VDSNKNFVIKHTIGDIQYCASGFLFKNKD 602

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  571 TVFEEQIKVLKSSKFKMLPELFQDDEkaisptsatssgrtpLTRtpakptkgrpGQMAKehKKTVGHQFRNSLHLLMETL 650
Cdd:PTZ00014   603 VLRPELVEVVKASPNPLVRDLFEGVE---------------VEK----------GKLAK--GQLIGSQFLNQLDSLMSLI 655

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  651 NATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRV--LMKQKDVLSDRKQTCK 728
Cdd:PTZ00014   656 NSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYldLAVSNDSSLDPKEKAE 735

                          730       740       750       760       770       780       790
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1677538261  729 NVLEKLILDKDKYQFGKTKIFFRAGQVAYLEKLRADKLRA--ACIRIqktIRGWLLRKKYLR-MRKAAITMQR 798
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 ...
 83-751 1.87e-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: 448.07  E-value: 1.87e-139
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   83 PAVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14896      1 SSVLLCLKKRF-HLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  163 GESGAGKTVSAKYAMRYFATVSGSASEANVE--EKVLasnPIMESIGNAKTTRNDNSSRFGKYIEIGFdKRYRIIGANMR 240
Cdd:cd14896     80 GHSGSGKTEAAKKIVQFLSSLYQDQTEDRLRqpEDVL---PILESFGHAKTILNANASRFGQVLRLHL-QHGVIVGASVS 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  241 TYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQACTLLGISES 320
Cdd:cd14896    156 HYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGACRLQGKEDAQDFEGLLKALQGLGLCAE 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  321 HQMGIFRILAGILHLGNVGFTSRDADSctippkHEPLCIFCE--------LMGVDYEEMCHWLCHRKLATATETYIKPIS 392
Cdd:cd14896    236 ELTAIWAVLAAILQLGNICFSSSERES------QEVAAVSSWaeihtaarLLQVPPERLEGAVTHRVTETPYGRVSRPLP 309

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  393 KLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSF--IGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVF 470
Cdd:cd14896    310 VEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESDatIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLL 389

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  471 KLEQEEYMKEQIPWTLIDFYDNQPCINLIESKL-GILDLLDEECKMPKGTDDTWAQKLYNTHLNKcALFEKPRLSNKAFI 549
Cdd:cd14896    390 AQEEEECQRELLPWVPIPQPPRESCLDLLVDQPhSLLSILDDQTWLSQATDHTFLQKCHYHHGDH-PSYAKPQLPLPVFT 468

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  550 IQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDdekaisptsatssgrtpltrtpAKPTKGRpgqmaK 629
Cdd:cd14896    469 VRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQE----------------------AEPQYGL-----G 521

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  630 EHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSR 709
Cdd:cd14896    522 QGKPTLASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLAR 601

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....
gi 1677538261  710 YRVLMKQK-DVLSDRKQtCKNVLEKLI-LDKDKYQFGKTKIFFR 751
Cdd:cd14896    602 FGALGSERqEALSDRER-CGAILSQVLgAESPLYHLGATKVLLK 644
MYSc_Myo45 cd14906
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ...
 85-749 1.80e-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: 445.19  E-value: 1.80e-137
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   85 VLHNLRVRFIdSKLIYTYCGIVLVAINPYEQLP-IYGEDIINAYSGQN-MGDMDPHIFAVAEEAYKQMARDERNQSIIVS 162
Cdd:cd14906      3 ILNNLGKRYK-SDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINqNKSPIPHIYAVALRAYQSMVSEKKNQSIIIS 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  163 GESGAGKTVSAKYAMRYFATVSGSASEAN---------VEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKR-Y 232
Cdd:cd14906     82 GESGSGKTEASKTILQYLINTSSSNQQQNnnnnnnnnsIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSdG 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  233 RIIGANMRTYLLEKSRVVFQAEEER-NYHIFYQLCASAKLPEFKMLRLGN--------------ADNFNYTKQGGSPVIE 297
Cdd:cd14906    162 KIDGASIETYLLEKSRISHRPDNINlSYHIFYYLVYGASKDERSKWGLNNdpskyryldarddvISSFKSQSSNKNSNHN 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  298 GVDDAKE-MAHTRQACTLLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTI---PPKHEPLCIFCELMGVDYEEMCH 373
Cdd:cd14906    242 NKTESIEsFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAyqkDKVTASLESVSKLLGYIESVFKQ 321

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  374 WLCHRKLATATE--TYIKPISKLQATNARDALAKHIYAKLFNWIVDNVNQ-----------ALHSAVKQHSFIGVLDIYG 440
Cdd:cd14906    322 ALLNRNLKAGGRgsVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRkfnqntqsndlAGGSNKKNNLFIGVLDIFG 401

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  441 FETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGT 519
Cdd:cd14906    402 FENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNFIDNKECIELIEKKsDGILSLLDDECIMPKGS 481

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  520 DDTWAQKlYNTHLNKCALFEKPRLSNKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEKAI 599
Cdd:cd14906    482 EQSLLEK-YNKQYHNTNQYYQRTLAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLFQQQITST 560

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  600 SPTSATSSGRTpltrtpakptkgrpgqmakehkkTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQ 679
Cdd:cd14906    561 TNTTKKQTQSN-----------------------TVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLS 617

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  680 QLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMKQKDVLSDRKQTCKNVLEKLIL----------------------- 736
Cdd:cd14906    618 QLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDMYNRKNNNNPKLASQLILQNIqsklktmgisnnkkknnsnsnsn 697

                          730
                   ....*....|....*.
gi 1677538261  737 ---DKDKYQFGKTKIF 749
Cdd:cd14906    698 ttnDKPLFQIGKTKIF 713
MYSc_Myo14 cd14876
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ...
 83-749 8.45e-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: 440.96  E-value: 8.45e-137
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   83 PAVLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLPIYGEDIINAYSG-QNMGDMDPHIFAVAEEAYKQMARDERNQSIIV 161
Cdd:cd14876      1 PCVLDFLKHRYLKNQ-IYTTADPLLVAINPFKDLGNATDEWIRKYRDaPDLTKLPPHVFYTARRALENLHGVNKSQTIIV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  162 SGESGAGKTVSAKYAMRYFATVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRT 241
Cdd:cd14876     80 SGESGAGKTEATKQIMRYFASAKSGNMDLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIRYGSVVA 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  242 YLLEKSRVVFQAEEERNYHIFYQLC--ASAKLPE-FKMLRLGNADNFNytkqGGSPVIEGVDDAKEMAHTRQACTLLGIS 318
Cdd:cd14876    160 FLLEKSRIVTQDDNERSYHIFYQLLkgADSEMKSkYHLLGLKEYKFLN----PKCLDVPGIDDVADFEEVLESLKSMGLT 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  319 ESHQMGIFRILAGILHLGNVGFTSRDA----DSCTIPPkhEPLCIF---CELMGVDYEEMCHWLChRKLATATETYIK-P 390
Cdd:cd14876    236 EEQIDTVFSIVSGVLLLGNVKITGKTEqgvdDAAAISN--ESLEVFkeaCSLLFLDPEALKRELT-VKVTKAGGQEIEgR 312

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  391 ISKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVF 470
Cdd:cd14876    313 WTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFIDIVF 392

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  471 KLEQEEYMKEQIPWTLIDFYDNQPCIN-LIESKLGILDLLDEECKMPKGTDD----TWAQKLYNthlNKCALFEKpRLSN 545
Cdd:cd14876    393 ERESKLYKDEGIPTAELEYTSNAEVIDvLCGKGKSVLSILEDQCLAPGGSDEkfvsACVSKLKS---NGKFKPAK-VDSN 468

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  546 KAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDdekaisptsatssgrTPLTRtpakptkgrpG 625
Cdd:cd14876    469 INFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEG---------------VVVEK----------G 523

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  626 QMAKehKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQE 705
Cdd:cd14876    524 KIAK--GSLIGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEE 601

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*.
gi 1677538261  706 FFSRYRVL-MKQKDVLSDRKQT-CKNVLEKLILDKDKYQFGKTKIF 749
Cdd:cd14876    602 FLYQFKFLdLGIANDKSLDPKVaALKLLESSGLSEDEYAIGKTMVF 647
MYSc_Myo38 cd14899
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ...
 84-736 7.73e-129

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: 7.73e-129
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   84 AVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLP-IYGEDIINAYS---GQNMGDM-------DPHIFAVAEEAYKQMAR 152
Cdd:cd14899      2 SILNALRLRY-ERHAIYTHIGDILISINPFQDLPqLYGDEILRGYAydhNSQFGDRvtstdprEPHLFAVARAAYIDIVQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  153 DERNQSIIVSGESGAGKTVSAKYAMRYFATVSG----------------SASEANVEEKVLASNPIMESIGNAKTTRNDN 216
Cdd:cd14899     81 NGRSQSILISGESGAGKTEATKIIMTYFAVHCGtgnnnltnsesisppaSPSRTTIEEQVLQSNPILEAFGNARTVRNDN 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  217 SSRFGKYIEIGF-DKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQL------CASAKLPEFKMLRlGNADNFNYTK 289
Cdd:cd14899    161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELlsadnnCVSKEQKQVLALS-GGPQSFRLLN 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  290 QG-GSPVIEGVDDAKEMAHTRQACTLLGISESHQMGIFRILAGILHLGNVGFT--------------SRDADSCTIPPKH 354
Cdd:cd14899    240 QSlCSKRRDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEqiphkgddtvfadeARVMSSTTGAFDH 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  355 epLCIFCELMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVK------ 428
Cdd:cd14899    320 --FTKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQASapwgad 397

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  429 ---------QHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLI 499
Cdd:cd14899    398 esdvddeedATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNNRACLELF 477

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  500 ESK-LGILDLLDEECKMPKGTDDTWAQKLY--------NTHLNKCALFEKprlsNKAFIIQHFADKVEYQCEGFLEKNKD 570
Cdd:cd14899    478 EHRpIGIFSLTDQECVFPQGTDRALVAKYYlefekknsHPHFRSAPLIQR----TTQFVVAHYAGCVTYTIDGFLAKNKD 553

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  571 TVFEEQIKVLKSSKFKMLPELFQDDEKAISPTSATSSGRTPLTRTPAKPTKGrpgqmakehKKTVGHQFRNSLHLLMETL 650
Cdd:cd14899    554 SFCESAAQLLAGSSNPLIQALAAGSNDEDANGDSELDGFGGRTRRRAKSAIA---------AVSVGTQFKIQLNELLSTV 624

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  651 NATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYR----VLMKQKDVLSDRKQT 726
Cdd:cd14899    625 RATTPRYVRCIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRYRrvllSLYKWGDNDFERQMR 704

                          730
                   ....*....|
gi 1677538261  727 CKNVLEKLIL 736
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 ...
 85-751 2.09e-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: 406.58  E-value: 2.09e-124
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   85 VLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLP-IYGEDIINAYSGQNMG-----DMDPHIFAVAEEAYKQMARDERNQS 158
Cdd:cd14886      3 VIDILRDRFAKDK-IYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQS 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  159 IIVSGESGAGKTVSAKYAMRYFAtVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGAN 238
Cdd:cd14886     82 CIVSGESGAGKTETAKQLMNFFA-YGHSTSSTDVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGLKGGK 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  239 MRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQACTLLgIS 318
Cdd:cd14886    161 ITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCYDAPGIDDQKEFAPVRSQLEKL-FS 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  319 ESHQMGIFRILAGILHLGNVGF---TSRDADSCTIPPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKPISKLQ 395
Cdd:cd14886    240 KNEIDSFYKCISGILLAGNIEFseeGDMGVINAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNETIISPVTQAQ 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  396 ATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQE 475
Cdd:cd14886    320 AEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFINQVFKSEIQ 399

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  476 EYMKEQIPWTLIDFYDNQPCINLIES-KLGILDLLDEECKMPKGTDDTWAQKLyNTHLNKcALFEKPRLSNKAFIIQHFA 554
Cdd:cd14886    400 EYEIEGIDHSMITFTDNSNVLAVFDKpNLSIFSFLEEQCLIQTGSSEKFTSSC-KSKIKN-NSFIPGKGSQCNFTIVHTA 477

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  555 DKVEYQCEGFLEKNKDTVFEEQIKVLKSSKfkmlpelfqddekaisptsatssgrTPLTRTPAKPTKGRPGQMAKehkKT 634
Cdd:cd14886    478 ATVTYNTEEFVDKNKHKLSVDILELLMGST-------------------------NPIVNKAFSDIPNEDGNMKG---KF 529

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  635 VGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLM 714
Cdd:cd14886    530 LGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILI 609

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|.
gi 1677538261  715 KQKDVL----SDRKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
Cdd:cd14886    610 SHNSSSqnagEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
MYSc_Myo13 cd14875
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ...
 85-751 2.48e-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: 401.11  E-value: 2.48e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   85 VLHNLRVRFIDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAY-SGQNMGDMDPHIFAVAEEAYKQM-ARDERNQSIIVS 162
Cdd:cd14875      3 LLHCIKERFEKLHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYlALPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVVIS 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  163 GESGAGKTVSAKYAMRYFATVS----GSASEANVEEKVLA----SNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRI 234
Cdd:cd14875     83 GESGSGKTENAKMLIAYLGQLSymhsSNTSQRSIADKIDEnlkwSNPVMESFGNARTVRNDNSSRFGKYIKLYFDPTSGV 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  235 -IGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKML-RLGNADNFNYTKQGGSPVIEGVD-----DAKEMAH 307
Cdd:cd14875    163 mVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKCLNGGNTFVRRGVDgktldDAHEFQN 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  308 TRQACTLLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPpKHEPLCIFCELMGVDYEEM--CHWLchrKLATATE 385
Cdd:cd14875    243 VRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQNDKAQIA-DETPFLTACRLLQLDPAKLreCFLV---KSKTSLV 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  386 TYIKpiSKLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHS--FIGVLDIYGFETFEINSFEQFCINYANEKLQQ 463
Cdd:cd14875    319 TILA--NKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITPQGDCSGckYIGLLDIFGFENFTRNSFEQLCINYANESLQN 396

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  464 QFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEKPR 542
Cdd:cd14875    397 HYNKYTFINDEEECRREGIQIPKIEFPDNSECVNMFDQKrTGIFSMLDEECNFKGGTTERFTTNLWDQWANKSPYFVLPK 476

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  543 --LSNKaFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDekaisptsatssgrtpltrtpakpt 620
Cdd:cd14875    477 stIPNQ-FGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTE------------------------- 530

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  621 kgrpgQMAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSR 700
Cdd:cd14875    531 -----KGLARRKQTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVR 605

                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  701 WTYQEFFSRYRVLM--------KQKDvLSDRKQTCKNVLEKLI-LDKDKYQFGKTKIFFR 751
Cdd:cd14875    606 RPIEQFCRYFYLIMprstaslfKQEK-YSEAAKDFLAYYQRLYgWAKPNYAVGKTKVFLR 664
MYSc_Myo37 cd14898
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ...
 84-713 5.88e-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: 5.88e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   84 AVLHNLRVRFIDSKlIYTYCGIVLVAINPYEQlpIYGEDIINAYSgQNMGDMDPHIFAVAEEAYKQMARdERNQSIIVSG 163
Cdd:cd14898      2 ATLEILEKRYASGK-IYTKSGLVFLALNPYET--IYGAGAMKAYL-KNYSHVEPHVYDVAEASVQDLLV-HGNQTIVISG 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  164 ESGAGKTVSAKYAMRYFatVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRyrIIGANMRTYL 243
Cdd:cd14898     77 ESGSGKTENAKLVIKYL--VERTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFDGK--ITGAKFETYL 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  244 LEKSRVVFQAEEERNYHIFYQLCASaklpefKMLRLGNaDNFNYTKQGGSPViEGVDDAKEMAHTRQACTLLGISESHQm 323
Cdd:cd14898    153 LEKSRVTHHEKGERNFHIFYQFCAS------KRLNIKN-DFIDTSSTAGNKE-SIVQLSEKYKMTCSAMKSLGIANFKS- 223

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  324 gIFRILAGILHLGNVGFTSrdaDSCTIPPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATEtYIKPISKL-QATNARDA 402
Cdd:cd14898    224 -IEDCLLGILYLGSIQFVN---DGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGE-TIEVFNTLkQARTIRNS 298

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  403 LAKHIYAKLFNWIVDNVNQALhSAVKQHSfIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQI 482
Cdd:cd14898    299 MARLLYSNVFNYITASINNCL-EGSGERS-ISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGMYKEEGI 376

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  483 PWTLIDFYDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKL--YNTHlnkcalFEKPRLSNKaFIIQHFADKVEYQ 560
Cdd:cd14898    377 EWPDVEFFDNNQCIRDFEKPCGLMDLISEESFNAWGNVKNLLVKIkkYLNG------FINTKARDK-IKVSHYAGDVEYD 449

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  561 CEGFLEKNKDtvfEEQIKVLKSskfkmlpelfqddekaisptsatssgrtpltrtpakptkgrPGQMAKEHKKTVGHQFR 640
Cdd:cd14898    450 LRDFLDKNRE---KGQLLIFKN-----------------------------------------LLINDEGSKEDLVKYFK 485

                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1677538261  641 NSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVL 713
Cdd:cd14898    486 DSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRIL 558
MYSc_Myo17 cd14879
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ...
 84-750 1.26e-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: 1.26e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   84 AVLHNLRVRFIdSKLIYTYCGI-VLVAINPYEQLPI--------YGEDIINAYSGQNMGDMdPHIFAVAEEAYKQMARDE 154
Cdd:cd14879      5 AITSHLASRFR-SDLPYTRLGSsALVAVNPYKYLSSnsdaslgeYGSEYYDTTSGSKEPLP-PHAYDLAARAYLRMRRRS 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  155 RNQSIIVSGESGAGKTVSAKYAMRYFATVSGSAS-EANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYR 233
Cdd:cd14879     83 EDQAVVFLGETGSGKSESRRLLLRQLLRLSSHSKkGTKLSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQFNERGR 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  234 IIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGG---SPVIEGVDDAKEMAHTRQ 310
Cdd:cd14879    163 LIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLASYGchpLPLGPGSDDAEGFQELKT 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  311 ACTLLGISESHQMGIFRILAGILHLGNVGFT---SRDADSCTIPPKHEpLCIFCELMGVDYEEmchwlchrkLATATeTY 387
Cdd:cd14879    243 ALKTLGFKRKHVAQICQLLAAILHLGNLEFTydhEGGEESAVVKNTDV-LDIVAAFLGVSPED---------LETSL-TY 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  388 iKpiSKL-------------QATNARDALAKHIYAKLFNWIVDNVNQALhSAVKQ--HSFIGVLDIYGFETF---EINSF 449
Cdd:cd14879    312 -K--TKLvrkelctvfldpeGAAAQRDELARTLYSLLFAWVVETINQKL-CAPEDdfATFISLLDFPGFQNRsstGGNSL 387

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  450 EQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESK-LGILDLLDEECK-MPKGTDDTWAQKL 527
Cdd:cd14879    388 DQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSYFDNSDCVRLLRGKpGGLLGILDDQTRrMPKKTDEQMLEAL 467

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  528 YNTHLNKCALFEKPRLSNK----AFIIQHFADKVEYQCEGFLEKNKDTVfeeqikvlkSSKFKMLpelfqddekaISPTs 603
Cdd:cd14879    468 RKRFGNHSSFIAVGNFATRsgsaSFTVNHYAGEVTYSVEGFLERNGDVL---------SPDFVNL----------LRGA- 527

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  604 atssgrtpltrtpakptkgrpgqmakehkktvgHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRA 683
Cdd:cd14879    528 ---------------------------------TQLNAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRS 574

                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1677538261  684 CGVLETIRISAAGFPSRWTYQEFFSRYrvlmKQKDVLSDRKQTCKNVLEKLILDKDKYQFGKTKIFF 750
Cdd:cd14879    575 LGLPELAARLRVEYVVSLEHAEFCERY----KSTLRGSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
MYSc_Myo16 cd14878
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ...
 84-751 4.32e-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: 331.78  E-value: 4.32e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   84 AVLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLPIYGEDIINAY---SGQNMGDMDPHIFAVAEEAYKQMARDERNQSII 160
Cdd:cd14878      2 SLLYEIQKRFGNNQ-IYTFIGDILLLVNPYKELPIYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  161 VSGESGAGKTVSAKYAMRYFATVSGSaSEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGF-DKRYRIIGANM 239
Cdd:cd14878     81 LSGERGSGKTEASKQIMKHLTCRASS-SRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKKHLTGARI 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  240 RTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQG---GSPVIEGVDDAKEMAHTRQACTLLG 316
Cdd:cd14878    160 YTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTmreDVSTAERSLNREKLAVLKQALNVVG 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  317 ISESHQMGIFRILAGILHLGNVGFTS-RDADSCTIppkhEPLCIFCELMG---VDYEEMCHWLCHRKLATATETYIKPIS 392
Cdd:cd14878    240 FSSLEVENLFVILSAILHLGDIRFTAlTEADSAFV----SDLQLLEQVAGmlqVSTDELASALTTDIQYFKGDMIIRRHT 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  393 KLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSF----IGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMH 468
Cdd:cd14878    316 IQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLQSQDEQKSMqtldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEV 395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  469 VFKLEQEEYMKEQIPW----------TLIDFYDNQPcinlieskLGILDLLDEECKMPKGTDDTWAQKLY----NTHLNK 534
Cdd:cd14878    396 LFLQEQTECVQEGVTMetayspgnqtGVLDFFFQKP--------SGFLSLLDEESQMIWSVEPNLPKKLQslleSSNTNA 467

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  535 CALFEK-------PRLSNKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQddekaisptsatss 607
Cdd:cd14878    468 VYSPMKdgngnvaLKDQGTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQ-------------- 533

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  608 grTPLTrtpakptkgrpgqmakehkkTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVL 687
Cdd:cd14878    534 --SKLV--------------------TIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVL 591

                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1677538261  688 ETIRISAAGFPSRWTYQEFFSRYRVLMKQkdVLSDRKQT-----CKNVLEKLILdkDKYQFGKTKIFFR 751
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 ...
 85-751 9.99e-97

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: 328.89  E-value: 9.99e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   85 VLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSGE 164
Cdd:cd01386      3 VLHTLRQRY-GANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLGR 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  165 SGAGKTVSAKYAMRYFATVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYLL 244
Cdd:cd01386     82 SGSGKTTNCRHILEYLVTAAGSVGGVLSVEKLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASIQTLLL 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  245 EKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGN-ADNFNYtkqGGSPVIEGVD---DAKEMAHTRQACTLLGISES 320
Cdd:cd01386    162 ERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQlAESNSF---GIVPLQKPEDkqkAAAAFSKLQAAMKTLGISEE 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  321 HQMGIFRILAGILHLGNVGftsrdadSCTIPP-------KHEPLCIFCELMGVDYEEMCHWLCHRKL------ATATETY 387
Cdd:cd01386    239 EQRAIWSILAAIYHLGAAG-------ATKAASagrkqfaRPEWAQRAAYLLGCTLEELSSAIFKHHLsggpqqSTTSSGQ 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  388 IKPIS------KLQATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFE------INSFEQFCIN 455
Cdd:cd01386    312 ESPARsssggpKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPAhsgsqrGATFEDLCHN 391

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  456 YANEKLQQQFNMHVFKLEQEEYMKEQIPwtlIDFYDNQPC----INLI---------------ESKLGILDLLDEECKMP 516
Cdd:cd01386    392 YAQERLQLLFHERTFVAPLERYKQENVE---VDFDLPELSpgalVALIdqapqqalvrsdlrdEDRRGLLWLLDEEALYP 468

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  517 KGTDDTWAQKLYnTHLNKCALFEKPRLSNKA-----FIIQHF--ADKVEYQCEGFLEKNKDTVFEEQikvlksskfkmLP 589
Cdd:cd01386    469 GSSDDTFLERLF-SHYGDKEGGKGHSLLRRSegplqFVLGHLlgTNPVEYDVSGWLKAAKENPSAQN-----------AT 536

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  590 ELFQDDEKaisptsatssgrtpltrtpakptkgrpgQMAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPN----- 664
Cdd:cd01386    537 QLLQESQK----------------------------ETAAVKRKSPCLQIKFQVDALIDTLRRTGLHFVHCLLPQhnagk 588

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  665 -DFKFPFTFDEKRAVQ------QLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMK-------QKDVLSDRKQTCKNV 730
Cdd:cd01386    589 dERSTSSPAAGDELLDvpllrsQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPpltkklgLNSEVADERKAVEEL 668

                          730       740
                   ....*....|....*....|.
gi 1677538261  731 LEKLILDKDKYQFGKTKIFFR 751
Cdd:cd01386    669 LEELDLEKSSYRIGLSQVFFR 689
MYSc_Myo26 cd14887
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ...
 83-751 4.11e-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: 325.06  E-value: 4.11e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   83 PAVLHNLRVRFI-------DSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDER 155
Cdd:cd14887      1 PNLLENLYQRYNkayinkeNRNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  156 NQSIIVSGESGAGKTVSAKYAMRYFATVS---GSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRY 232
Cdd:cd14887     81 SQSILISGESGAGKTETSKHVLTYLAAVSdrrHGADSQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGRG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  233 RIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYtkqggspviegvddakEMAHTRQAC 312
Cdd:cd14887    161 KLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSSAGEGDPEST----------------DLRRITAAM 224

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  313 TLLGISESHQMGIFRILAGILHLGNVGFTSRDADSCTIPPKHEPLCIFCELMGVDYEEMCHWLCHR---KLATATETYIK 389
Cdd:cd14887    225 KTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKLTSVSVGCEETAADRSHSSEVKCLSsglKVTEASRKHLK 304

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  390 PISKL--------------------------------QATNARDALAKHIYAKLFNWIVDNVNQALHSAVK--------- 428
Cdd:cd14887    305 TVARLlglppgvegeemlrlalvsrsvretrsffdldGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKpsesdsded 384

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  429 -----QHSFIGVLDIYGFETFE---INSFEQFCINYANEKLqqqfnmHVFKLEQ-----------EEYMKEQI------- 482
Cdd:cd14887    385 tpsttGTQTIGILDLFGFEDLRnhsKNRLEQLCINYANERL------HCFLLEQlilnehmlytqEGVFQNQDcsafpfs 458

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  483 ----------PWTLIDF-----------YDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCAL-FEK 540
Cdd:cd14887    459 fplastltssPSSTSPFsptpsfrsssaFATSPSLPSSLSSLSSSLSSSPPVWEGRDNSDLFYEKLNKNIINSAKYkNIT 538

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  541 PRLS--NKAFIIQHFADKVEYQCEGFLEKNKDTVFEEqikvlksskfkmLPELFqddekaisptsatSSGRTPLTRTPAK 618
Cdd:cd14887    539 PALSreNLEFTVSHFACDVTYDARDFCRANREATSDE------------LERLF-------------LACSTYTRLVGSK 593

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  619 PTKGRpgQMAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFP 698
Cdd:cd14887    594 KNSGV--RAISSRRSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFP 671

                          730       740       750       760       770
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1677538261  699 SRWTYQEFFSRY--RVLMKQKDVLSDrKQTCKNVLEKLILDKDKYQFGKTKIFFR 751
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 ...
 85-751 1.06e-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: 1.06e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   85 VLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYgediINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSGE 164
Cdd:cd14937      3 VLNMLALRY-KKNYIYTIAEPMLISINPYQVIDVD----INEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  165 SGAGKTVSAKYAMRYFatVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYLL 244
Cdd:cd14937     78 SGSGKTEASKLVIKYY--LSGVKEDNEISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSIEIFLL 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  245 EKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGgSPVIEGVDDAKEMAHTRQACTLLGISESHQmG 324
Cdd:cd14937    156 ENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNK-NVVIPEIDDAKDFGNLMISFDKMNMHDMKD-D 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  325 IFRILAGILHLGNVGFTSRDA---DSCTIPPKH--EPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNA 399
Cdd:cd14937    234 LFLTLSGLLLLGNVEYQEIEKggkTNCSELDKNnlELVNEISNLLGINYENLKDCLVFTEKTIANQKIEIPLSVEESVSI 313

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  400 RDALAKHIYAKLFNWIVDNVNQALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMK 479
Cdd:cd14937    314 CKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYEKETELYKA 393

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  480 EQIPWTLIDFYDNQPCINLIESKLGILDLLDEECKMPKGTDDTwaqkLYNTHLNKCALFEK----PRLSNKAFIIQHFAD 555
Cdd:cd14937    394 EDILIESVKYTTNESIIDLLRGKTSIISILEDSCLGPVKNDES----IVSVYTNKFSKHEKyastKKDINKNFVIKHTVS 469

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  556 KVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDDEkaisptSATSSGRtpltrtpakptkgrpgqmakehKKTV 635
Cdd:cd14937    470 DVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVE------VSESLGR----------------------KNLI 521

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  636 GHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAgFPSRWTYQEFFSRYRVL-- 713
Cdd:cd14937    522 TFKYLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNISFF-FQYKYTFDVFLSYFEYLdy 600

                          650       660       670
                   ....*....|....*....|....*....|....*...
gi 1677538261  714 MKQKDVLSDRKQTCKNVLEKLIlDKDKYQFGKTKIFFR 751
Cdd:cd14937    601 STSKDSSLTDKEKVSMILQNTV-DPDLYKVGKTMVFLK 637
MYSc_Myo20 cd14881
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ...
 84-750 2.77e-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: 2.77e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   84 AVLHNLRVRFIDSKLiYTYCGIVLVAINPYEqlpiygeDIINAY---SGQNMGDMdPHIFAVAEEAYKQMARDERNQSII 160
Cdd:cd14881      2 AVMKCLQARFYAKEF-FTNVGPILLSVNPYR-------DVGNPLtltSTRSSPLA-PQLLKVVQEAVRQQSETGYPQAII 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  161 VSGESGAGKTVSAKYAMRYFATVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKryriiGANMR 240
Cdd:cd14881     73 LSGTSGSGKTYASMLLLRQLFDVAGGGPETDAFKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQVTD-----GALYR 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  241 T----YLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLG--NADNFNYTkQGGSPVIEGVDDAKEMAHTRQACTL 314
Cdd:cd14881    148 TkihcYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDgySPANLRYL-SHGDTRQNEAEDAARFQAWKACLGI 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  315 LGISESHQMgifRILAGILHLGNVGFTsrDADSCTIPPKHE-PLCIFCELMGVDYEEMchwlcHRKLATATET----YIK 389
Cdd:cd14881    227 LGIPFLDVV---RVLAAVLLLGNVQFI--DGGGLEVDVKGEtELKSVAALLGVSGAAL-----FRGLTTRTHNargqLVK 296

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  390 PISKLQATNA-RDALAKHIYAKLFNWIVDNVN--QALHSAVKQHS---FIGVLDIYGFETFEINSFEQFCINYANEKLQQ 463
Cdd:cd14881    297 SVCDANMSNMtRDALAKALYCRTVATIVRRANslKRLGSTLGTHAtdgFIGILDMFGFEDPKPSQLEHLCINLCAETMQH 376

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  464 QFNMHVFKLEQEEYMKEQIPWTL-IDFYDNQPCINLIES-KLGILDLLDEECKmPKGTDDTWAQKLYNTHLNKCALFEKP 541
Cdd:cd14881    377 FYNTHIFKSSIESCRDEGIQCEVeVDYVDNVPCIDLISSlRTGLLSMLDVECS-PRGTAESYVAKIKVQHRQNPRLFEAK 455

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  542 RLSNKAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVL--KSSKFKMLPELfQDdekaisptsatssgrtpltrtpakp 619
Cdd:cd14881    456 PQDDRMFGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFykQNCNFGFATHT-QD------------------------- 509

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  620 tkgrpgqmakehkktvghqFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPS 699
Cdd:cd14881    510 -------------------FHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPH 570

                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1677538261  700 RWTYQEFFSRYRVL--MKQKDVLSDRKQTCKNVLEKLILDKDK---------YQFGKTKIFF 750
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 ...
 83-750 7.58e-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: 7.58e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   83 PAVLHNLRVRFIDSKlIYTYCGIVLVAINPYEQLP-IYGEDIINAYS-------GQNMGDMDPHIFAVAEEAYKQMARDE 154
Cdd:cd14884      1 PNVLQNLKNRYLKNK-IYTFHASLLLALNPYKPLKeLYDQDVMNVYLhkksnsaASAAPFPKAHIYDIANMAYKNMRGKL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  155 RNQSIIVSGESGAGKTVSAKYAMRYFATVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKR--- 231
Cdd:cd14884     80 KRQTIVVSGHSGSGKTENCKFLFKYFHYIQTDSQMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFEEVent 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  232 ------YRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQL---CASAKLPEFKMLR------LGNADNFNYTKQGGSPVI 296
Cdd:cd14884    160 qknmfnGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVlrgLSDEDLARRNLVRncgvygLLNPDESHQKRSVKGTLR 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  297 EGVD-----------DAKEMAHTRQACTLLGISESHQMGIFRILAGILHLGNvgftsrDADSCTippkheplcifCELMG 365
Cdd:cd14884    240 LGSDsldpseeekakDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGN------RAYKAA-----------AECLQ 302

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  366 VDYEEMCHWLCHRKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDNVNQAL------------HSAVKQHSFI 433
Cdd:cd14884    303 IEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVlkckekdesdneDIYSINEAII 382

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  434 GVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTLIDFYDNQPCINLIESklgILDLLDEEC 513
Cdd:cd14884    383 SILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAPSYSDTLIFIAK---IFRRLDDIT 459

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  514 KMP----KGTDDTWAQKLYNTHlNKCALFEK-------PRL---SNKA-------FIIQHFADKVEYQCEGFLEKNKDTV 572
Cdd:cd14884    460 KLKnqgqKKTDDHFFRYLLNNE-RQQQLEGKvsygfvlNHDadgTAKKqnikkniFFIRHYAGLVTYRINNWIDKNSDKI 538

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  573 feeqikvlksskfkmlpelfqddEKAISPTSATSSGRTpLTRTPAKPTKGrpgqmakeHKKTVGHQFRNSLHLLMETLNA 652
Cdd:cd14884    539 -----------------------ETSIETLISCSSNRF-LREANNGGNKG--------NFLSVSKKYIKELDNLFTQLQS 586

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  653 TTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMkQKDVLSDRKQTCKNVLE 732
Cdd:cd14884    587 TDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKETAAALKEQI-AKELEKCNSNTDIEYQR 665

                          730
                   ....*....|....*...
gi 1677538261  733 KLILDKDKYQFGKTKIFF 750
Cdd:cd14884    666 RLAALDVQFIPDGRLYAF 683
Myo5-like_CBD cd14945
Cargo binding domain of myosin 5 and similar proteins; Class V myosins are well studied ...
 1455-1778 4.04e-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: 283.52  E-value: 4.04e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1455 EDEQKLVKNLILELKPRGVAVNLipgLPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSNT 1534
Cdd:cd14945      1 SEEDSLLRGIVTDFEPSSGDHKL---TPAYILYLCIRHAASNGLTGQSTSLLNKVLKTIQQVVQQHNDDMQLLAFWLSNA 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1535 CRFLHCLKQYSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPmivsgmlehetiqgvsgv 1614
Cdd:cd14945     78 SELLYFLKQDSKLYGAAGEAPQKEEEQKLTVSDLNELKQDLEAVSIKIYQQALKYLNKNLQP------------------ 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1615 kptglrkrtssiadegtyTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQIRY 1694
Cdd:cd14945    140 ------------------KIRDIVKFLNSFLDLLKSFHVHPEIRSQVFTQLFSFINARLFNQLITKKDALSWSRGMQIRA 201

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1695 NVSQLEEWLRDKNLmNSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERVSVSFI 1774
Cdd:cd14945    202 NISRLEEWCEGRGL-EHLAVDFLSKLIQAVQLLQLKKYTQEDIEILCELCPSLNPAQLQAILTQYQPANYGESPVPKEIL 280


                   ....
gi 1677538261 1775 RTIQ 1778
Cdd:cd14945    281 RTLA 284
MYSc_Myo44 cd14905
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ...
 97-751 9.13e-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: 9.13e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   97 KLIYTYCGIVLVAINPYEQLP-IYGEDIINAYSgQNMGdMDPHIFAVAEEAYKQMARDERNQSIIVSGESGAGKTVSAKY 175
Cdd:cd14905     14 EIIYTYIGPILVSVNPLRYLPfLHSQELVRNYN-QRRG-LPPHLFALAAKAISDMQDFRRDQLIFIGGESGSGKSENTKI 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  176 AMRYFATVSGSASEAnVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYLLEKSRVVFQAEE 255
Cdd:cd14905     92 IIQYLLTTDLSRSKY-LRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKLYSYFLDENRVTYQNKG 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  256 ERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAHTRQACTLLGISESHQMGIFRILAGILHL 335
Cdd:cd14905    171 ERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQGGSISVESIDDNRVFDRLKMSFVFFDFPSEKIDLIFKTLSFIIIL 250

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  336 GNVGFTSRDADSctippkheplcifcelmGVDYEEMCHWLCHRKLATATETYIKPISKL-----QATNARDALAKHIYAK 410
Cdd:cd14905    251 GNVTFFQKNGKT-----------------EVKDRTLIESLSHNITFDSTKLENILISDRsmpvnEAVENRDSLARSLYSA 313

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  411 LFNWIVDNVNQALHSAVKQHSfIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPW-TLIDF 489
Cdd:cd14905    314 LFHWIIDFLNSKLKPTQYSHT-LGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQREYQTERIPWmTPISF 392

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  490 YDNQPCINLIESklgILDLLDEECKMPKGTDDTWAQKLYNtHLNKCALF-EKPrlsNKaFIIQHFADKVEYQCEGFLEKN 568
Cdd:cd14905    393 KDNEESVEMMEK---IINLLDQESKNINSSDQIFLEKLQN-FLSRHHLFgKKP---NK-FGIEHYFGQFYYDVRGFIIKN 464

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  569 KDTVFEEQIKVLKSSKFKMLpeLFQDDEKAISPTSA---------TSSGRTPLT----------------RTPAKPTKGR 623
Cdd:cd14905    465 RDEILQRTNVLHKNSITKYL--FSRDGVFNINATVAelnqmfdakNTAKKSPLSivkvllscgsnnpnnvNNPNNNSGGG 542

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  624 PGQMAKEHKKTVGHQFRNSLHLLMETLNATTP--HYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRW 701
Cdd:cd14905    543 GGGGNSGGGSGSGGSTYTTYSSTNKAINNSNCdfHFIRCIKPNSKKTHLTFDVKSVNEQIKSLCLLETTRIQRFGYTIHY 622

                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1677538261  702 TYQEFFSRYRVLMKQkdvlsdrKQTCKNVLEKLI---LDKDK-----YQFGKTKIFFR 751
Cdd:cd14905    623 NNKIFFDRFSFFFQN-------QRNFQNLFEKLKendINIDSilpppIQVGNTKIFLR 673
MYSc_Myo12 cd14874
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ...
 84-751 9.06e-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: 9.06e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   84 AVLHNLRVRFiDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYsgqnmgdmdpHIFAVAEEAYKQMARDERN-QSIIVS 162
Cdd:cd14874      2 GIAQNLHERF-KKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  163 GESGAGKTVSAKYAMRYFATVSGSASEAnveEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFdKRYRIIGANMR-T 241
Cdd:cd14874     71 GESGSGKSYNAFQVFKYLTSQPKSKVTT---KHSSAIESVFKSFGCAKTLKNDEATRFGCSIDLLY-KRNVLTGLNLKyT 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  242 YLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSpvIEGV-DDAKEMAHTRQACTLLGISES 320
Cdd:cd14874    147 VPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNS--TENIqSDVNHFKHLEDALHVLGFSDD 224

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  321 HQMGIFRILAGILHLGNVGFTSR-----DADSCTIPPKHEPLCIfCELMGVDYEEMCHWLchrklaTATETYIKPISKLQ 395
Cdd:cd14874    225 HCISIYKIISTILHIGNIYFRTKrnpnvEQDVVEIGNMSEVKWV-AFLLEVDFDQLVNFL------LPKSEDGTTIDLNA 297

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  396 ATNARDALAKHIYAKLFNWIVDNVNQALHSAVKQHSfIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQE 475
Cdd:cd14874    298 ALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGV-ISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHSFHDQLV 376

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  476 EYMKEQIPwtlIDF-----YDNQPCINLIESK-LGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCAlFEKPRLSNK-AF 548
Cdd:cd14874    377 DYAKDGIS---VDYkvpnsIENGKTVELLFKKpYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSS-YGKARNKERlEF 452

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  549 IIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQddekaiSPTSATSsgrtpltrtpakptkgrpgqma 628
Cdd:cd14874    453 GVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFE------SYSSNTS---------------------- 504

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  629 kEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFS 708
Cdd:cd14874    505 -DMIVSQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFAR 583

                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1677538261  709 RYRVLM--------KQKDVLSDRKQTCKNVLEklildkDKYQFGKTKIFFR 751
Cdd:cd14874    584 QYRCLLpgdiamcqNEKEIIQDILQGQGVKYE------NDFKIGTEYVFLR 628
MYSc_Myo32 cd14893
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ...
 86-750 1.25e-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: 1.25e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   86 LHNLRVRF-IDSklIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQN----------MGDMDPHIFAVAEEAYKQMARDE 154
Cdd:cd14893      4 LYTLRARYrMEQ--VYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSReqtplyekdtVNDAPPHVFALAQNALRCMQDAG 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  155 RNQSIIVSGESGAGKTVSAKYAMRYFATVSGSASEAN-----------VEEKVLASNPIMESIGNAKTTRNDNSSRFGKY 223
Cdd:cd14893     82 EDQAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPdsegasgvlhpIGQQILHAFTILEAFGNAATRQNRNSSRFAKM 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  224 IEIGFDKRYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKL-PEFK-MLRLGN-ADNFNYTKQGGSPVIEGVD 300
Cdd:cd14893    162 ISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHdPTLRdSLEMNKcVNEFVMLKQADPLATNFAL 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  301 DAKEMAHTRQACTLLGISESHQMGIFRILAGILHLGNVGF----------------TSRDADSCTIPPKHEPLcIFCELM 364
Cdd:cd14893    242 DARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpeggksvgganstTVSDAQSCALKDPAQIL-LAAKLL 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  365 GVDYEEMCHWLCHRKL----ATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDNVNQAL---------HSAVKQHS 431
Cdd:cd14893    321 EVEPVVLDNYFRTRQFfskdGNKTVSSLKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifdryekSNIVINSQ 400

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  432 FIGVLDIYGFETFE--INSFEQFCINYANEKLQQQF-------NMHVFKLEQEEYMKEQIPWTLIDF-YDNQPCINLIES 501
Cdd:cd14893    401 GVHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYvqntlaiNFSFLEDESQQVENRLTVNSNVDItSEQEKCLQLFED 480

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  502 K-LGILDLLDEECKMPKGTDDTWAQKLYN--------THLNKCALFEKPRLSNKA-----FIIQHFADKVEYQCEGFLEK 567
Cdd:cd14893    481 KpFGIFDLLTENCKVRLPNDEDFVNKLFSgneavgglSRPNMGADTTNEYLAPSKdwrllFIVQHHCGKVTYNGKGLSSK 560

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  568 NKDTVFEEQIKVLKSSKFKMLPELFQDDEKAISP-TSATSSGRTPLTRTPAKPTKGRPGQmAKEHKKTVGHQFRNSLHLL 646
Cdd:cd14893    561 NMLSISSTCAAIMQSSKNAVLHAVGAAQMAAASSeKAAKQTEERGSTSSKFRKSASSARE-SKNITDSAATDVYNQADAL 639

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  647 METLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYrvlmkqKDVLSDRKqT 726
Cdd:cd14893    640 LHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRY------KNVCGHRG-T 712

                          730       740
                   ....*....|....*....|....*...
gi 1677538261  727 CKNVLEKL----ILDKDKYQFGKTKIFF 750
Cdd:cd14893    713 LESLLRSLsaigVLEEEKFVVGKTKVYL 740
MYSc_Myo21 cd14882
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ...
 85-751 2.18e-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: 235.41  E-value: 2.18e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   85 VLHNLRVRfIDSKLIYTYCGIVLVAINPYEQLPIYGEDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSGE 164
Cdd:cd14882      3 ILEELRHR-YLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  165 SGAGKTVSAKYAMRYFATVSGSASeaNVEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFDKRYRIIGANMRTYLL 244
Cdd:cd14882     82 SYSGKTTNARLLIKHLCYLGDGNR--GATGRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFWMYQL 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  245 EKSRVVFQAEEERNYHIFY----QLCASAKLPEF--------KMLRLGNADNFNYTKQGGSPVIEGVDDAKEMAhtrQAC 312
Cdd:cd14882    160 EKLRVSTTDGNQSNFHIFYyfydFIEAQNRLKEYnlkagrnyRYLRIPPEVPPSKLKYRRDDPEGNVERYKEFE---EIL 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  313 TLLGISESHQMGIFRILAGILHLGNVGFtsRDADSCTIPPKHEPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKPIS 392
Cdd:cd14882    237 KDLDFNEEQLETVRKVLAAILNLGEIRF--RQNGGYAELENTEIASRVAELLRLDEKKFMWALTNYCLIKGGSAERRKHT 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  393 KLQATNARDALAKHIYAKLFNWIVDNVNQALH--SAV--KQHSfIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMH 468
Cdd:cd14882    315 TEEARDARDVLASTLYSRLVDWIINRINMKMSfpRAVfgDKYS-ISIHDMFGFECFHRNRLEQLMVNTLNEQMQYHYNQR 393

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  469 VFKLEQEEYMKEQIPWTLIDFYDNQPCI-NLIESKLGILDLLDEECKMPKGtddtwAQKLYNTHLNKCALFEKPrLSNKA 547
Cdd:cd14882    394 IFISEMLEMEEEDIPTINLRFYDNKTAVdQLMTKPDGLFYIIDDASRSCQD-----QNYIMDRIKEKHSQFVKK-HSAHE 467

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  548 FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQDdekaisptsatssgrtpltrtpakptkgrpgqm 627
Cdd:cd14882    468 FSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN--------------------------------- 514

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  628 AKEHK-KTVGHQFRNSLHLLMETL----NATTPHYVRCIKPNDFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWT 702
Cdd:cd14882    515 SQVRNmRTLAATFRATSLELLKMLsigaNSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIP 594

                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|
gi 1677538261  703 YQEFFSRYRVLMKQKDVLSD-RKQTCKNVLEKLILdkDKYQFGKTKIFFR 751
Cdd:cd14882    595 FQEFLRRYQFLAFDFDETVEmTKDNCRLLLIRLKM--EGWAIGKTKVFLK 642
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
 106-229 7.07e-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: 171.76  E-value: 7.07e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  106 VLVAINPYEQLPIYGED-IINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSGESGAGKTVSAKYAMRYFATVS 184
Cdd:cd01363      1 VLVRVNPFKELPIYRDSkIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1677538261  185 GSASEAN--------------VEEKVLASNPIMESIGNAKTTRNDNSSRFGKYIEIGFD 229
Cdd:cd01363     81 FNGINKGetegwvylteitvtLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLD 139
DIL pfam01843
DIL domain; The DIL domain has no known function.
 1660-1763 2.89e-42

DIL domain; The DIL domain has no known function.


Pssm-ID: 460359 [Multi-domain]  Cd Length: 103  Bit Score: 150.05  E-value: 2.89e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1660 QVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQIRYNVSQLEEWLRDKNLmNSGAKETLEPLIQAAQLLQVKKKTDDDAEA 1739
Cdd:pfam01843    1 QLFSQLFYFINAELFNRLLLRKKYCSWSKGMQIRYNLSRLEEWARSNGL-ESEARDHLAPLIQAAQLLQLRKSTLEDLDS 79

                           90       100
                   ....*....|....*....|....
gi 1677538261 1740 ICSMCNALTTAQIVKVLNLYTPVN 1763
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 ...
 83-749 1.52e-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: 161.93  E-value: 1.52e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261   83 PAVLHNLRVRFIDSKLiYTYCGIVLVAINPYEQLPIYGEDIINAYSGQN-MGDMDPHIFAVAEEAYKQMARDERNQSIIV 161
Cdd:cd14938      1 PSVLYHLKERFKNNKF-YTKMGPLLIFINPKINNNINNEETIEKYKCIDcIEDLSLNEYHVVHNALKNLNELKRNQSIII 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  162 SGESGAGKTVSAKYAMRYFA-TVSGSASEA---------------------NVEEKVLASNPIMESIGNAKTTRNDNSSR 219
Cdd:cd14938     80 SGESGSGKSEIAKNIINFIAyQVKGSRRLPtnlndqeednihneentdyqfNMSEMLKHVNVVMEAFGNAKTVKNNNSSR 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  220 FGKYIEIGFDKRyRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADNFNYTKQGGSPVIEGV 299
Cdd:cd14938    160 FSKFCTIHIENE-EIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSD 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  300 DDAKEMAHTRQACTLLGISESHQMgIFRILAGILHLGNVGF--------TSRDADSCTIPPKHEpLCI----FCELMGVD 367
Cdd:cd14938    239 YSGKILELLKSLNYIFDDDKEIDF-IFSVLSALLLLGNTEIvkafrkksLLMGKNQCGQNINYE-TILseleNSEDIGLD 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  368 YEEMCHWLCHRKLATATETYIKPIS---------------KLQATNARDALAKHIYAKLFNWIVDNVNQ---ALHSAVKQ 429
Cdd:cd14938    317 ENVKNLLLACKLLSFDIETFVKYFTtnyifndsilikvhnETKIQKKLENFIKTCYEELFNWIIYKINEkctQLQNININ 396

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  430 HSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKEQIPWTL-IDFYDNQPCIN-LIESKLGILD 507
Cdd:cd14938    397 TNYINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYnSENIDNEPLYNlLVGPTEGSLF 476

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  508 LLDEECKMPKGTDDTwaqKLYNTHLNKCA-----LFEKPRLSN-KAFIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLK 581
Cdd:cd14938    477 SLLENVSTKTIFDKS---NLHSSIIRKFSrnskyIKKDDITGNkKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVK 553

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  582 SSKFKMLPELFQ----DDEKAISPTSATSSGRTPLtrtpaKPTKGR---PGQMAKEhkktvghQFRNSLHLLMETLNATT 654
Cdd:cd14938    554 QSENEYMRQFCMfynyDNSGNIVEEKRRYSIQSAL-----KLFKRRydtKNQMAVS-------LLRNNLTELEKLQETTF 621

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  655 PHYVRCIKPNDFK-FPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMkqkdvlSDRKQTCKNVLEK 733
Cdd:cd14938    622 CHFIVCMKPNESKrELCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKN------EDLKEKVEALIKS 695

                          730
                   ....*....|....*.
gi 1677538261  734 LILDKDKYQFGKTKIF 749
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 ...
 1481-1810 4.11e-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: 4.11e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1481 LPAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSNTCRFLHCLKQysgEEGFmkhntsrqne 1560
Cdd:cd15473     32 VPANLLFLCARYAHYHCSPELLEDLLLGALDRIEDVVEANPWDMTLLAFWLSNVTLLLHYLKK---DAGL---------- 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1561 hcltNFDLAEYRQVLSDLAIQIYQQLVRVLEnilqpmivsgmlehetiqgvsgvkptglrKRTSSIADEGTYTLDSIlrq 1640
Cdd:cd15473     99 ----VEATPEFQQELAELINEIFVLIIRDAE-----------------------------RRIDKLLDASPRNITSL--- 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1641 LNSFHSVMCQHGMDPELIKQVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQIRYNVSQLEEWLRDKNLM-------NSGA 1713
Cdd:cd15473    143 LSSTLYVLELYDVHPAIIIQALSQLFYWLGCELFNRILTNKKYLCRSKAMQIRMNLSALEDWARSNNLQpekgespPRIA 222

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1714 KETLEPLIQAAQLLQVKKKTDDDAEAICSM--CNALTTAQIVKVLNLYTP-VNefEERVSVSFIRTIQMRLRDRKDSpql 1790
Cdd:cd15473    223 RSHLAPVIQLLQWLQCLSSLDDFESLIATIqqLDALNPLQLLRAVKDYRYeVN--EGRMPEECVKYLAQLQKDWLDS--- 297

                          330       340
                   ....*....|....*....|
gi 1677538261 1791 lmdaKHIFPVTFPFNPSSLA 1810
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 ...
 1460-1804 1.24e-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: 1.24e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1460 LVKNLILELKPRGVAVN----LIPGLPAYILFMCVRHADYLNDDQKVRSL--LTSTINSIKKVLKKRgDDFETVSFWLSN 1533
Cdd:cd15474     11 LKSVEVLELKDISDEVSgdnlLFLGHVNFLIYSQMWKSLLELLTQSERFLshVLSYIASIVDSLPKK-ETIPDGAFWLAN 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1534 TCRFLHCL--KQYSGEEGFMKHNTSRQNEHCLTNFDlaEYRQVLSdlaiQIYQQLVRVLENILQPMIVSGMLEHETIQGV 1611
Cdd:cd15474     90 LHELRSFVvyLLSLIEHSSSDEFSKESEEYWNTLFD--KTLKHLS----NIYSTWIDKLNKHLSPKIEGAVLVLLTSLDL 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1612 SGvkptgLRKRTSSIADEGTYTLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQ 1691
Cdd:cd15474    164 SE-----LIDLNKEFFNKPKKKMADLITFLNEVYDLLQSFSVQPELLNAIVSSTLQYINVEAFNSLITKRSALSWKRGSQ 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1692 IRYNVSQLEEWLRDKNLmnSGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNeFEERVSV 1771
Cdd:cd15474    239 ISYNVSRLKEWCHQHGL--SDANLQLEPLIQASKLLQLRKDDENDFKIILSVCYALNPAQIQKLLDKYQPAN-YEAPVPK 315

                          330       340       350
                   ....*....|....*....|....*....|....
gi 1677538261 1772 SFIRTI-QMRLRDRKDSPQLLMDAKHIFPVTFPF 1804
Cdd:cd15474    316 EFLNALeKLIKKENLSLPGRKNNSKMEIPESSNF 349
MYSc_Myo33 cd14894
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ...
 196-734 1.46e-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: 1.46e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  196 VLASNPIMESIGNAKTTRNDNSSRFGKY--IEIGFDK---RYRIIGANMRTYLLEKSRVVFQA------EEERNYHIFYQ 264
Cdd:cd14894    249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLhpwEFQICGCHISPFLLEKSRVTSERgresgdQNELNFHILYA 328

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  265 LCASAKLPEF-----KMLRLGNADNFNYTKQGGSP-----VIEGVD----DAKEMAHTRQACTLLGISESHQMGIFRILA 330
Cdd:cd14894    329 MVAGVNAFPFmrllaKELHLDGIDCSALTYLGRSDhklagFVSKEDtwkkDVERWQQVIDGLDELNVSPDEQKTIFKVLS 408

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  331 GILHLGNVGFTSRDADSCTIPPKH------EPLCIFCELMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNARDALA 404
Cdd:cd14894    409 AVLWLGNIELDYREVSGKLVMSSTgalnapQKVVELLELGSVEKLERMLMTKSVSLQSTSETFEVTLEKGQVNHVRDTLA 488

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  405 KHIYAKLFNWIVDNVNQALH-----------------SAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQqfnm 467
Cdd:cd14894    489 RLLYQLAFNYVVFVMNEATKmsalstdgnkhqmdsnaSAPEAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKLYA---- 564

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  468 hvfKLEQEEYMKEQIPWTLIDFYDNQPCINLIESKLGILDLLdEECKMPKGTDDTWAQ------KLYNTHL---NKCALF 538
Cdd:cd14894    565 ---REEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASL-EELTILHQSENMNAQqeekrnKLFVRNIydrNSSRLP 640

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  539 EKPRLSNKA------------FIIQHFADKVEYQCEGFLEKNKDTVFEEQIKVLK---SSKF-KMLPELFQDDEKAISPT 602
Cdd:cd14894    641 EPPRVLSNAkrhtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKtsnSSHFcRMLNESSQLGWSPNTNR 720

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  603 SATSSGRTPLTRTpakptkgrpgqmakehKKTVGhQFRNSLHLLMETLNATTPHYVRCIKPNDFKFPFTFDEKRAVQQLR 682
Cdd:cd14894    721 SMLGSAESRLSGT----------------KSFVG-QFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCR 783

                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1677538261  683 ACGV---LETIRISAAGFPS-RWTYQEFFSRYRVLMKQKDVLSDRKQTCKNVLEKL 734
Cdd:cd14894    784 SQRLirqMEICRNSSSSYSAiDISKSTLLTRYGSLLREPYILDDVAGDNSNLMNWL 839
fMyo2p_CBD cd15480
cargo binding domain of fungal myosin 2; Yeast myosin V travels along actin cables, actin ...
 1633-1828 4.12e-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: 4.12e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1633 TLDSILRQLNSFHSVMCQHGMDPELIKQVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQIRYNVSQLEEWLRDKNlMNSG 1712
Cdd:cd15480    167 TMDDILNFFNKVYKSMKSYYIEESVIRQVVTELLKLIGVTAFNDLLMRRNFLSWKRGLQINYNITRLEEWCKSHD-IPEG 245

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1713 AkETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTpVNEFEERVSVSFIRTIQMRLR--DRKDSPQL 1790
Cdd:cd15480    246 T-LQLEHLMQATKLLQLKKATLEDIEIIYDVCWILTPAQIQKLISQYY-VADYENPISPEILKAVAARVKpeDKSDHLLL 323

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1677538261 1791 LMDAKHIFPVTFPFNPSSLALETIqIPASLGLGFISRV 1828
Cdd:cd15480    324 IPLVEEVGPFEDPFPREIAGLEAY-IPAWLNLPHIRRL 360
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 902-1281 6.06e-16

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: 84.34  E-value: 6.06e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  902 KRELKKLKIEARSVERYKKLHigmeNKIMQLQRKVdeQNKDYKCLVEKLTNLEGIYNSETEKLRSDLERLQLSEEEAKVA 981
Cdd:TIGR02168  199 ERQLKSLERQAEKAERYKELK----AELRELELAL--LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEEL 272

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  982 TGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQekealnhriVQQAKEMTETMEKKLV 1061
Cdd:TIGR02168  273 RLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE---------LESKLDELAEELAELE 343

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1062 EETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTlmvhvpkpghKRTDSTHSSNESEYIFSSEI----AEMEDIP 1137
Cdd:TIGR02168  344 EKLEELKEELESLEAELEELEAELEELESRLEELEEQLE----------TLRSKVAQLELQIASLNNEIerleARLERLE 413

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1138 SRTEEPSEKKVPLDMSL----FLKLQKRVTELEQEKQVMQDELDRKEEQvlrskaKEEERPQIRGAELEYESLKRQELES 1213
Cdd:TIGR02168  414 DRRERLQQEIEELLKKLeeaeLKELQAELEELEEELEELQEELERLEEA------LEELREELEEAEQALDAAERELAQL 487

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1677538261 1214 ENKK--LKNELNELRKALSEKSAPEVTAPGAPAYRVLMEQLTSVSEELDVRKEEVLILRSQLV------SQKEAIQ 1281
Cdd:TIGR02168  488 QARLdsLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVvvenlnAAKKAIA 563
Myo5p-like_CBD_afadin cd15471
cargo binding domain of myosin 5-like of afadin; Afadin is an actin filament (F-actin) and ...
 1482-1761 6.25e-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: 6.25e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1482 PAYILFMCVRH---ADYLNDD------QKVRSLLTSTINSIKKVLKKRGDDFETVSFWLSNTCRFLHCLKQysgeegfmk 1552
Cdd:cd15471     25 PAYTLYLAARYrlsTHYRPELtpteraHKLTAFLNKIASLIQQVIQEQRNIAGALAFWMANASELLNFLKQ--------- 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1553 hntsrqnEHCLTNFDLaEYRQVLSDLAIQIYQQLVRVLENILQPMIVSGMLEHETIQGVSGVKPTglrkrtssiadegTY 1632
Cdd:cd15471     96 -------DRDLSAFSV-QAQDVLAEAVQSAFSYLVRCLQEELERSLPAFLDSLVSLDDEPAIGDV-------------LH 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1633 TLDSILRQLNsfhsvmcQHGMDPELIKQVVKQMFYIIGAITLNNLLLRKD--MCSWSKGMQIRYNVSQLEEWLrDKNLMN 1710
Cdd:cd15471    155 TLSSAMRLLR-------RCRVNAALTIQLFSQLFHFINAWLFNSLVSNPDsgLCTRYWGKRLRQRLAHVEAWA-ERQGLE 226

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1677538261 1711 SGAKETLEPLIQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTP 1761
Cdd:cd15471    227 LAADCHLDRIVQAANLLTAPKYSAEDVANLSSTCFKLNSLQLRALLSHYQP 277
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 927-1407 1.56e-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: 75.91  E-value: 1.56e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  927 NKIMQLQRKVDEQNKDYKCLVEKLTNLegiyNSETEKLRSDLER----LQLSEEEAKVATGRVLSLQEEIAKLRKDLEQT 1002
Cdd:pfam05483  268 DKANQLEEKTKLQDENLKELIEKKDHL----TKELEDIKMSLQRsmstQKALEEDLQIATKTICQLTEEKEAQMEELNKA 343

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1003 RSEKKCIeehADRYKQETEQLVSNLKEENTLLKQEKEALNHRIVQQAKEMTETMEKKLVEETKQLELD------LNDERL 1076
Cdd:pfam05483  344 KAAHSFV---VTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEelkkilAEDEKL 420

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1077 RYQNllNEFSRLEERYDDLKEEMTLMVHV-PKPGHKRTDSTHSSNESEYIFSSEIAEMedipsRTEEPSEKKVPLDMSLF 1155
Cdd:pfam05483  421 LDEK--KQFEKIAEELKGKEQELIFLLQArEKEIHDLEIQLTAIKTSEEHYLKEVEDL-----KTELEKEKLKNIELTAH 493

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1156 L-KLQKRVTELEQEKQVMQDELDRKEEQVLRSKaKEEER--PQIRGAElEYESLKRQELESENKKLKNELNELRKAL--S 1230
Cdd:pfam05483  494 CdKLLLENKELTQEASDMTLELKKHQEDIINCK-KQEERmlKQIENLE-EKEMNLRDELESVREEFIQKGDEVKCKLdkS 571

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1231 EKSAPEVTAPGAPAY-------------------------------RVLMEQLTSVSEELDVRKEEVLILRSQLVSQKEA 1279
Cdd:pfam05483  572 EENARSIEYEVLKKEkqmkilenkcnnlkkqienknknieelhqenKALKKKGSAENKQLNAYEIKVNKLELELASAKQK 651

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1280 IQPKDD--KNTMTDSTI----LLEDVQKMK---DKGEIAQAYIGLKETNRLLESQLQSQKRSHE-----NEAEALRGEIQ 1345
Cdd:pfam05483  652 FEEIIDnyQKEIEDKKIseekLLEEVEKAKaiaDEAVKLQKEIDKRCQHKIAEMVALMEKHKHQydkiiEERDSELGLYK 731

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1677538261 1346 SLKEEnnrqqqllaqnlqlppEARIEASLQHEITRLTNENLDLMEQLEKQDKTVRKLKKQLK 1407
Cdd:pfam05483  732 NKEQE----------------QSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAK 777
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 957-1231 4.61e-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: 74.71  E-value: 4.61e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  957 YNSETEKLRSDLERLQLSEEEakvatgrvlsLQEEIAKLRKDLEQTRSEkkciEEHADRYKQETEQLVSNLKEENTLLKQ 1036
Cdd:TIGR02168  675 RRREIEELEEKIEELEEKIAE----------LEKALAELRKELEELEEE----LEQLRKELEELSRQISALRKDLARLEA 740

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1037 EKEALNHRIVQQAKEMTETMEK---------KLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMvhvpk 1107
Cdd:TIGR02168  741 EVEQLEERIAQLSKELTELEAEieeleerleEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL----- 815

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1108 pGHKRTDSTHSSNESEYIFSSEIAEMEDIPSRTEEPSEKkvpldmslFLKLQKRVTELEQEKQVMQDELDRKEEQvlrsK 1187
Cdd:TIGR02168  816 -NEEAANLRERLESLERRIAATERRLEDLEEQIEELSED--------IESLAAEIEELEELIEELESELEALLNE----R 882

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1677538261 1188 AKEEERPQIRGAELEYESLKRQELESENKKLKNELNELRKALSE 1231
Cdd:TIGR02168  883 ASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ 926
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 902-1286 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 1677538261  902 KRELKKLKIEARSVERYKKLHIGMEnkimqlQRKVDEQNKDYKCLVEKLTNLEGIYNSETEKLRSDLERLQLSEEEAKVA 981
Cdd:COG1196    199 ERQLEPLERQAEKAERYRELKEELK------ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEEL 272

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  982 TGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEentlLKQEKEALNHRIVQQAKEMTETMEKKLV 1061
Cdd:COG1196    273 RLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE----LEEELAELEEELEELEEELEELEEELEE 348

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1062 EETK--QLELDLNDERLRYQNLLNEFSRLEERYDDLKEEmtlmvhvpkpghkrtdsthssneseyiFSSEIAEMEDIPSR 1139
Cdd:COG1196    349 AEEEleEAEAELAEAEEALLEAEAELAEAEEELEELAEE---------------------------LLEALRAAAELAAQ 401

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1140 TEEPSEKKvpldmslfLKLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEErpqiRGAELEYESLKRQELESENKKLK 1219
Cdd:COG1196    402 LEELEEAE--------EALLERLERLEEELEELEEALAELEEEEEEEEEALEE----AAEEEAELEEEEEALLELLAELL 469

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1677538261 1220 NELNELRKALSEKSAPEVTApgAPAYRVLMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQPKDDK 1286
Cdd:COG1196    470 EEAALLEAALAELLEELAEA--AARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEA 534
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 902-1281 1.31e-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: 73.18  E-value: 1.31e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  902 KRELKKLKIEARSVERYKKLHI---------------GMENKIMQLQRKVDEQNKDykclVEKLTNLEGIYNSETEKLRS 966
Cdd:TIGR02169  197 RQQLERLRREREKAERYQALLKekreyegyellkekeALERQKEAIERQLASLEEE----LEKLTEEISELEKRLEEIEQ 272

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  967 DLErlQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEkkcIEEHADRYKQETEQLVsNLKEENTLLKQEKEALNHRIV 1046
Cdd:TIGR02169  273 LLE--ELNKKIKDLGEEEQLRVKEKIGELEAEIASLERS---IAEKERELEDAEERLA-KLEAEIDKLLAEIEELEREIE 346

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1047 QQAKEMTETME--KKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMtlmvhvpkpghkrtdsthssNESEY 1124
Cdd:TIGR02169  347 EERKRRDKLTEeyAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREI--------------------NELKR 406

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1125 IFSSEIAEMEDIPSRTEEpsekkvpLDMSLFLKLQKrVTELEQEKQVMQDELDRKEEQVLRSKA-KEEERPQIRGAELEY 1203
Cdd:TIGR02169  407 ELDRLQEELQRLSEELAD-------LNAAIAGIEAK-INELEEEKEDKALEIKKQEWKLEQLAAdLSKYEQELYDLKEEY 478

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1677538261 1204 eslkrQELESENKKLKNELNELRKalsEKSAPEVTAPGAPAyrvlmeqltsVSEELDVRKEEVLILRSQLVSQKEAIQ 1281
Cdd:TIGR02169  479 -----DRVEKELSKLQRELAEAEA---QARASEERVRGGRA----------VEEVLKASIQGVHGTVAQLGSVGERYA 538
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
942-1417 3.41e-12

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 71.63  E-value: 3.41e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  942 DYKCLVEKLTNLEGIYNSETEKLRSDLERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKqETE 1021
Cdd:PRK03918   159 DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE-ELK 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1022 QLVSNLKEENTLLKQEKEALNHRIVQqakemTETMEKKLVEETKQLEldlndERLRYqnlLNEFSRLEERYDDLKEEMTL 1101
Cdd:PRK03918   238 EEIEELEKELESLEGSKRKLEEKIRE-----LEERIEELKKEIEELE-----EKVKE---LKELKEKAEEYIKLSEFYEE 304

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1102 MVHVPKPGHKRTDSTHSSNESeyiFSSEIAEMEDIPSRTEEPSEKKVpldmslflKLQKRVTELEQEKQVMQDELDRKEE 1181
Cdd:PRK03918   305 YLDELREIEKRLSRLEEEING---IEERIKELEEKEERLEELKKKLK--------ELEKRLEELEERHELYEEAKAKKEE 373

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1182 -QVLRSKAKEEERPQIRgAELEYESLKRQELESENKK-------LKNELNELRKALSEKSAPEVTAP--GAP-------- 1243
Cdd:PRK03918   374 lERLKKRLTGLTPEKLE-KELEELEKAKEEIEEEISKitarigeLKKEIKELKKAIEELKKAKGKCPvcGRElteehrke 452

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1244 ---AYRVLMEQLTSVSEELDVRKEEVLI----LRSQLVSQKEAIQPKddknTMTDSTILLEDVQKMKDKGEIAQA---YI 1313
Cdd:PRK03918   453 lleEYTAELKRIEKELKEIEEKERKLRKelreLEKVLKKESELIKLK----ELAEQLKELEEKLKKYNLEELEKKaeeYE 528

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1314 GLKETNRLLESQLQSQKRS------HENEAEALRGEIQSLKEEN---NRQQQLLAQNLQLPPEARIEA--SLQHEITRLT 1382
Cdd:PRK03918   529 KLKEKLIKLKGEIKSLKKElekleeLKKKLAELEKKLDELEEELaelLKELEELGFESVEELEERLKElePFYNEYLELK 608

                          490       500       510
                   ....*....|....*....|....*....|....*
gi 1677538261 1383 NENLDLMEQLEKQDKTVRKLKKQLKVFAKKIGELE 1417
Cdd:PRK03918   609 DAEKELEREEKELKKLEEELDKAFEELAETEKRLE 643
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
902-1418 4.51e-12

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 71.25  E-value: 4.51e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  902 KRELKKLKIEARSVERYKKlhiGMENKIMQLQRKVDEQNKDYKCLVEKLTNLEGI--YNSETEKLRSDLERLQLSEEEAK 979
Cdd:PRK03918   237 KEEIEELEKELESLEGSKR---KLEEKIRELEERIEELKKEIEELEEKVKELKELkeKAEEYIKLSEFYEEYLDELREIE 313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  980 VATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTL--LKQEKEALNHRIVQQAKEMTETME 1057
Cdd:PRK03918   314 KRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAkaKKEELERLKKRLTGLTPEKLEKEL 393

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1058 KKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLmvhVPKPGHKRTDsthssNESEYIFSSEIAEMEDIP 1137
Cdd:PRK03918   394 EELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGK---CPVCGRELTE-----EHRKELLEEYTAELKRIE 465

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1138 SRTEEPSEKKVpldmslflKLQKRVTELEQEKQvmqdeldrKEEQVLRSKAKEEerpQIRGAELEYESLKRQELESENK- 1216
Cdd:PRK03918   466 KELKEIEEKER--------KLRKELRELEKVLK--------KESELIKLKELAE---QLKELEEKLKKYNLEELEKKAEe 526

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1217 --KLKNELNELRKALseksapevtapgapayRVLMEQLTSVsEELDVRKEEVLILRSQLVSQKEAIQPKDDKNTMTDSTI 1294
Cdd:PRK03918   527 yeKLKEKLIKLKGEI----------------KSLKKELEKL-EELKKKLAELEKKLDELEEELAELLKELEELGFESVEE 589

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1295 LLEDVQKMKdkgEIAQAYIGLKETNRLLESQLQSQKRSH-------------ENEAEALRGEIQSLKEENNRQQQLLAQN 1361
Cdd:PRK03918   590 LEERLKELE---PFYNEYLELKDAEKELEREEKELKKLEeeldkafeelaetEKRLEELRKELEELEKKYSEEEYEELRE 666

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1677538261 1362 LQLppearieaSLQHEITRLTNENLDLMEQLEKQDKTVRKLKKQLKVFAKKIGELEV 1418
Cdd:PRK03918   667 EYL--------ELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEK 715
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 896-1415 1.35e-11

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: 69.77  E-value: 1.35e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  896 FRRMMAKRELKKLKIEarsverYKKLHIGMENKIMQLQRKVDEQNKDYKCLVEKLTNLEGIYNSETEKLRSDLERLQL-- 973
Cdd:pfam05557    9 ARLSQLQNEKKQMELE------HKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLkk 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  974 ----------SEEEAKVATGR--VLSLQEEIAKLRK-------DLEQTRSEKKCIEEHADRYK---QETEQLVSNLKEEN 1031
Cdd:pfam05557   83 kylealnkklNEKESQLADARevISCLKNELSELRRqiqraelELQSTNSELEELQERLDLLKakaSEAEQLRQNLEKQQ 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1032 TLLK---QEKEALNHRIVQQA--KEMTETMEKKLVEETkqlELDLNDERLRYQN-----------LLNE----FSRLEER 1091
Cdd:pfam05557  163 SSLAeaeQRIKELEFEIQSQEqdSEIVKNSKSELARIP---ELEKELERLREHNkhlnenienklLLKEevedLKRKLER 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1092 YDDLKEEM-TLMVHVPKPGHK-----RTDSTHSSN-ESEYIFSSEIaemEDIPSRTEEPSEKKVPLDMSLfLKLQKRVTE 1164
Cdd:pfam05557  240 EEKYREEAaTLELEKEKLEQElqswvKLAQDTGLNlRSPEDLSRRI---EQLQQREIVLKEENSSLTSSA-RQLEKARRE 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1165 LEQEKQVMQDELDrkEEQVLRSKAKE-EERPQIRGAELEYE-SLKRQELESENKKLKNELNELRKALSEKSAPEVTApga 1242
Cdd:pfam05557  316 LEQELAQYLKKIE--DLNKKLKRHKAlVRRLQRRVLLLTKErDGYRAILESYDKELTMSNYSPQLLERIEEAEDMTQ--- 390

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1243 pAYRVLMEqltSVSEELDVRKEEVLILRSQLVSQKEAIQPKDDKNTMTDSTILLEDVQKMKDKGEIAQAYIG-LKETNRL 1321
Cdd:pfam05557  391 -KMQAHNE---EMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADPSYSKEEVDSLRRKLETLELERQrLREQKNE 466

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1322 LESQLQSQ------------------------KRSHENEAEALRGEIQSLKEENNRQQQLLAQNLQLPPEARIEASlqhe 1377
Cdd:pfam05557  467 LEMELERRclqgdydpkktkvlhlsmnpaaeaYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNF---- 542

                          570       580       590
                   ....*....|....*....|....*....|....*...
gi 1677538261 1378 itrltNENLDLMEQLEKQDKTVRKLKkqlKVFAKKIGE 1415
Cdd:pfam05557  543 -----KEVLDLRKELESAELKNQRLK---EVFQAKIQE 572
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
900-1418 8.48e-11

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 67.40  E-value: 8.48e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  900 MAKRELKKL----------KIEARSVERYKKlhiGMENKIMQLQRKVDEQNKDYKCLVEKLTNLEGI--YNSETEKLRSD 967
Cdd:PRK03918   225 KLEKEVKELeelkeeieelEKELESLEGSKR---KLEEKIRELEERIEELKKEIEELEEKVKELKELkeKAEEYIKLSEF 301

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  968 LERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTL--LKQEKEALNHRI 1045
Cdd:PRK03918   302 YEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAkaKKEELERLKKRL 381

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1046 VQQAKEMTETMEKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLmvhVPKPGHKRTDsthssNESEYI 1125
Cdd:PRK03918   382 TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGK---CPVCGRELTE-----EHRKEL 453

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1126 FSSEIAEMEDIPSRTEEPSEKKVpldmslflKLQKRVTELE----QEKQVMQDELDRKEEQVLRSKAKEEERPQIRGAEL 1201
Cdd:PRK03918   454 LEEYTAELKRIEKELKEIEEKER--------KLRKELRELEkvlkKESELIKLKELAEQLKELEEKLKKYNLEELEKKAE 525

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1202 EYESLKRQ--ELESENKKLKNELNEL-----RKALSEKSAPEVTAPGAPAYRVLMEQLTSVSEELDVRKEEVLILRSQLV 1274
Cdd:PRK03918   526 EYEKLKEKliKLKGEIKSLKKELEKLeelkkKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYL 605

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1275 SQKEAIQPKDDKntmtdstilLEDVQKMKDKGEIAQAYIGLKETN-RLLESQL-QSQKRSHENEAEALRGEIQSLKEENN 1352
Cdd:PRK03918   606 ELKDAEKELERE---------EKELKKLEEELDKAFEELAETEKRlEELRKELeELEKKYSEEEYEELREEYLELSRELA 676

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1677538261 1353 RQqqllaqnlqlppEARIEaslqhEITRLTNENLDLMEQLEKQDKTVRKLKKQLKVFAKKIGELEV 1418
Cdd:PRK03918   677 GL------------RAELE-----ELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEE 725
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
901-1417 9.88e-11

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 67.01  E-value: 9.88e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  901 AKRELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLVEKLTNLEGiynsETEKLRSDLERL--------Q 972
Cdd:PRK03918   167 LGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELRE----ELEKLEKEVKELeelkeeieE 242

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  973 LSEEEAKVaTGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQ-----ETEQLVSNLKEENTLLKQEKEALNHRIVQ 1047
Cdd:PRK03918   243 LEKELESL-EGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkekaEEYIKLSEFYEEYLDELREIEKRLSRLEE 321

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1048 QAKEMtetmeKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMVHVPKpghkrtdstHSSNESEYIFS 1127
Cdd:PRK03918   322 EINGI-----EERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELER---------LKKRLTGLTPE 387

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1128 SEIAEMEDIPSRTEEPSEKkvpldmslFLKLQKRVTELEQEKQVMQDELDRKEEQ-----VLRSKAKEEERPQIRG---A 1199
Cdd:PRK03918   388 KLEKELEELEKAKEEIEEE--------ISKITARIGELKKEIKELKKAIEELKKAkgkcpVCGRELTEEHRKELLEeytA 459

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1200 ELEYESLKRQELESENKKLKNELNELRKALSEKSAPEVTAPGAPAYRVLMEQLTSVS-EELDVRKEEVLILRSQLVSQKE 1278
Cdd:PRK03918   460 ELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNlEELEKKAEEYEKLKEKLIKLKG 539

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1279 AIQpkddkntmtdstILLEDVQKMKD-KGEIAQAYIGLKETNRLLESQLQSQKRSHENEAEALRGEIQSLKEENNRqqql 1357
Cdd:PRK03918   540 EIK------------SLKKELEKLEElKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNE---- 603

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1358 laQNLQLPPEARIEaSLQHEITRLTNENLDLMEQLEKQDKTVRKLKKQLKVFAKKIGELE 1417
Cdd:PRK03918   604 --YLELKDAEKELE-REEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEE 660
PTZ00121 PTZ00121
MAEBL; Provisional
 897-1459 1.31e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 67.09  E-value: 1.31e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  897 RRMMAKRELKKLKIEARSVERYKKLHigmENKIMQLQRKVDEQNKDYKclvEKLTNLEGIYNSETEKLRSDleRLQLSEE 976
Cdd:PTZ00121  1268 RQAAIKAEEARKADELKKAEEKKKAD---EAKKAEEKKKADEAKKKAE---EAKKADEAKKKAEEAKKKAD--AAKKKAE 1339

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  977 EAKVAtGRVLSLQEEIAKlrKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQEKEAlnhrivQQAKEMTETM 1056
Cdd:PTZ00121  1340 EAKKA-AEAAKAEAEAAA--DEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKA------EEDKKKADEL 1410

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1057 EKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLK---EEMTLMVHVPKPGHKRTDSTHSSNESEyifssEIAEM 1133
Cdd:PTZ00121  1411 KKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKkkaEEAKKAEEAKKKAEEAKKADEAKKKAE-----EAKKA 1485

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1134 EDIPSRTEEPSEKKVPLDMSLFLKlqKRVTELEQ-EKQVMQDELDRKEEQVLRSKAKEEER----PQIRGAELEYESLKR 1208
Cdd:PTZ00121  1486 DEAKKKAEEAKKKADEAKKAAEAK--KKADEAKKaEEAKKADEAKKAEEAKKADEAKKAEEkkkaDELKKAEELKKAEEK 1563

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1209 QELESENKKLKNELNELRKALSEKSAPEvtAPGAPAYRVLMEQLTSVSEELdvRKEEVLILRSQLVSQKEAIQPKDDKNT 1288
Cdd:PTZ00121  1564 KKAEEAKKAEEDKNMALRKAEEAKKAEE--ARIEEVMKLYEEEKKMKAEEA--KKAEEAKIKAEELKKAEEEKKKVEQLK 1639

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1289 MTDStillEDVQKMKdkgEIAQAyiglKETNRLLESQLQSQKRSHENEAEALRGEiqslkEENNRQQQLLAQNLQLppea 1368
Cdd:PTZ00121  1640 KKEA----EEKKKAE---ELKKA----EEENKIKAAEEAKKAEEDKKKAEEAKKA-----EEDEKKAAEALKKEAE---- 1699

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1369 riEASLQHEITRLTNENLDLMEQLEKQDKT----VRKLKKQLKVFAKKIGELEVGQMENISPGQIIDEPIRPVNIPRKEK 1444
Cdd:PTZ00121  1700 --EAKKAEELKKKEAEEKKKAEELKKAEEEnkikAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEK 1777

                          570
                   ....*....|....*
gi 1677538261 1445 DFQGMLEYKKEDEQK 1459
Cdd:PTZ00121  1778 EAVIEEELDEEDEKR 1792
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 856-1477 2.80e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 65.73  E-value: 2.80e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  856 RYRKILREHKAVIIQKRVRGWLARTHYKRSMHAIIylqccfrrmmAKRELKKLKIEARSVERYKKLHIgMENKIMQLQRK 935
Cdd:COG1196    214 RYRELKEELKELEAELLLLKLRELEAELEELEAEL----------EELEAELEELEAELAELEAELEE-LRLELEELELE 282

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  936 VDEQNKDYKCLVEKLTNLEGIYNSETEKLRSDLERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADR 1015
Cdd:COG1196    283 LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1016 YKQETEQLVSNLKEENTLLKQEKEAlnhrivQQAKEMTETMEKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDL 1095
Cdd:COG1196    363 AEEALLEAEAELAEAEEELEELAEE------LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1096 KEEmtlmvhvpkpghkrtdsthsSNESEYIFSSEIAEMEdipsrteepsekkvpldmSLFLKLQKRVTELEQEKQVMQDE 1175
Cdd:COG1196    437 EEE--------------------EEEALEEAAEEEAELE------------------EEEEALLELLAELLEEAALLEAA 478

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1176 LDRKEEQVLRSKAKEE-ERPQIRGAELEYESLKRQELESENKKLKNELNELRKALSEKSAPEVTAPGAPAYRVLMEQLTS 1254
Cdd:COG1196    479 LAELLEELAEAAARLLlLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEV 558

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1255 VSEELDVRKEEVL----ILRSQLVSQKEAIQPKDDKNTMTDSTILLEDVQK---MKDKGEIAQAYIGLKETNRLLESQLQ 1327
Cdd:COG1196    559 AAAAIEYLKAAKAgratFLPLDKIRARAALAAALARGAIGAAVDLVASDLReadARYYVLGDTLLGRTLVAARLEAALRR 638

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1328 SQKRSHENEAEALRGEIQSLKEENNRQQQLLAQNLQLPPEARIEASLQHEITRLTNENLDLMEQLEKQDKTVRKLKKQLK 1407
Cdd:COG1196    639 AVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLE 718

                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1408 VFAKKIGELEVGQMENIspgQIIDEPIRPVNIPRKEKDFQGMLEYKKEDEQKLVKNLILELKPRGvAVNL 1477
Cdd:COG1196    719 EELEEEALEEQLEAERE---ELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALG-PVNL 784
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 902-1209 3.38e-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: 3.38e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  902 KRELKKLKIEARS-VERYKKLHIGMENKIMQLQRKVDEQNKDYKCLVEKLTNLE-GIYNSETE--KLRSDLERLQ----- 972
Cdd:TIGR02169  697 LRRIENRLDELSQeLSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEqEIENVKSElkELEARIEELEedlhk 776

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  973 ----LSEEEAKVATGRVLSLQEEIAKLRK----------DLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQEK 1038
Cdd:TIGR02169  777 leeaLNDLEARLSHSRIPEIQAELSKLEEevsriearlrEIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI 856

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1039 EALNHRivqqaKEMTETMEKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMVHVPKpghkrtdsthS 1118
Cdd:TIGR02169  857 ENLNGK-----KEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLS----------E 921

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1119 SNESEYIFSSEIAEMEDIPSRTEEPSEKKVPLDmslflKLQKRVTELEQEKQVMQ-------DELDRKEEQVLRSKAK-- 1189
Cdd:TIGR02169  922 LKAKLEALEEELSEIEDPKGEDEEIPEEELSLE-----DVQAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDELKEKra 996

                          330       340
                   ....*....|....*....|..
gi 1677538261 1190 --EEERPQIRGAELEYESLKRQ 1209
Cdd:TIGR02169  997 klEEERKAILERIEEYEKKKRE 1018
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 957-1350 8.92e-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: 63.93  E-value: 8.92e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  957 YNSETEKLRSDLERLQLSEEEakvatgrvlsLQEEIAKLRKDLEQTRSEKkcieEHADRYKQeteqLVSNLKE-ENTLLK 1035
Cdd:TIGR02169  168 FDRKKEKALEELEEVEENIER----------LDLIIDEKRQQLERLRRER----EKAERYQA----LLKEKREyEGYELL 229

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1036 QEKEALNHRIVQQAKEMTEtmekkLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMVHvpkpghKRTDS 1115
Cdd:TIGR02169  230 KEKEALERQKEAIERQLAS-----LEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVK------EKIGE 298

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1116 THSsneseyifssEIAEMEDIPSRTEEPSEKkvpldmslfLKLQKRVTELEQEKQVMQ-DELDRKEEQVLRSKAKEEERP 1194
Cdd:TIGR02169  299 LEA----------EIASLERSIAEKERELED---------AEERLAKLEAEIDKLLAEiEELEREIEEERKRRDKLTEEY 359

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1195 QIRGAELEYESLKRQELESENKKLKNELNELRKALSEksapevtapgapayrvLMEQLTSVSEELDVRKEEVLILRSQLV 1274
Cdd:TIGR02169  360 AELKEELEDLRAELEEVDKEFAETRDELKDYREKLEK----------------LKREINELKRELDRLQEELQRLSEELA 423

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1677538261 1275 SQKEAIQPKDDKNTMTDSTilLEDVQKmkdkgEIAQAYIGLKETNRLLESqLQSQKRSHENEAEALRGEIQSLKEE 1350
Cdd:TIGR02169  424 DLNAAIAGIEAKINELEEE--KEDKAL-----EIKKQEWKLEQLAADLSK-YEQELYDLKEEYDRVEKELSKLQRE 491
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 917-1464 1.08e-09

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: 63.50  E-value: 1.08e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  917 RYKKLHIGMENKIMQLQRKVDEQNKDYKCLVEKLTNLEGIYNSETEKLRSDLERLQLSEEEAKVATGRVLSLQEEIAKLR 996
Cdd:TIGR04523   23 GYKNIANKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLN 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  997 KDLEQTRSEKKcieehadrykqETEQLVSNLKEENTLLKQEKEALNHRIvqqakemtetmeKKLVEETKQLELDLNDERL 1076
Cdd:TIGR04523  103 SDLSKINSEIK-----------NDKEQKNKLEVELNKLEKQKKENKKNI------------DKFLTEIKKKEKELEKLNN 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1077 RYQNLLNEFSRLEERYDDLKEEMTlmvhvpKPGHKRTDSTHSSNESEYIFSSEIAEMEDIPSRTEEPSEKKvpldmSLFL 1156
Cdd:TIGR04523  160 KYNDLKKQKEELENELNLLEKEKL------NIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELK-----KQNN 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1157 KLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEE---RPQIRGAELEYESLKRQELESENKKLKNELNELRKalsEKS 1233
Cdd:TIGR04523  229 QLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKikkQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNN---QKE 305

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1234 ApevtapgapayrvlmEQLTSVSEELDVRKEEVLILRSQLVSQKEAI-----QPKDDKNTMTDSTI--------LLEDVQ 1300
Cdd:TIGR04523  306 Q---------------DWNKELKSELKNQEKKLEEIQNQISQNNKIIsqlneQISQLKKELTNSESensekqreLEEKQN 370

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1301 KMKDKGEIAQAYiglKETNRLLESQ---LQSQKRSHENEAEALRGEIQSLKEENNRQqqllaqnlqlppEARIE------ 1371
Cdd:TIGR04523  371 EIEKLKKENQSY---KQEIKNLESQindLESKIQNQEKLNQQKDEQIKKLQQEKELL------------EKEIErlketi 435

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1372 ASLQHEITRLTNENLDLMEQLEKQDKTVRKLKKQLKVFAKKIGELEVGQMENISpgqiidepirpvNIPRKEKDFQGMLE 1451
Cdd:TIGR04523  436 IKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQK------------ELKSKEKELKKLNE 503

                          570
                   ....*....|...
gi 1677538261 1452 YKKEDEQKlVKNL 1464
Cdd:TIGR04523  504 EKKELEEK-VKDL 515
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
924-1350 2.37e-09

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 62.36  E-value: 2.37e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  924 GMENKIMQLQRKVDEqnKDYKCLVEKLTNLEgiynSETEKLRSDLERLQLSEEEAKVATG--------------RVLSLQ 989
Cdd:PRK02224   184 DQRGSLDQLKAQIEE--KEEKDLHERLNGLE----SELAELDEEIERYEEQREQARETRDeadevleeheerreELETLE 257

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  990 EEIAKLRKDLEQTRSEKkciEEHADRYKQETEQLvSNLKEENT--LLKQEKEALNHRIVQQAKemtETMEKKLVEetkqL 1067
Cdd:PRK02224   258 AEIEDLRETIAETERER---EELAEEVRDLRERL-EELEEERDdlLAEAGLDDADAEAVEARR---EELEDRDEE----L 326

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1068 ELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTlmvhvpkpgHKRTDSTHSSNESEyifsseiAEMEDIPSRTEEPSEkk 1147
Cdd:PRK02224   327 RDRLEECRVAAQAHNEEAESLREDADDLEERAE---------ELREEAAELESELE-------EAREAVEDRREEIEE-- 388

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1148 vpldmslflkLQKRVTELEQEKQVMQDELDRKEEqvlRSKAKEEERPQIRGaeleyeslKRQELESENKKLKNELNELRK 1227
Cdd:PRK02224   389 ----------LEEEIEELRERFGDAPVDLGNAED---FLEELREERDELRE--------REAELEATLRTARERVEEAEA 447

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1228 ALSEKSAPEVTAPGAPAYRVlmeqltsvsEELDVRKEEVLILRSQLVSQKEAIQPKDDKNTMTDSTILLED-VQKMKDKG 1306
Cdd:PRK02224   448 LLEAGKCPECGQPVEGSPHV---------ETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDrIERLEERR 518

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*...
gi 1677538261 1307 EIAQAYIGLKET----NRLLESQLQSQKRSHENEAEALRGEIQSLKEE 1350
Cdd:PRK02224   519 EDLEELIAERREtieeKRERAEELRERAAELEAEAEEKREAAAEAEEE 566
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 900-1232 2.70e-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: 62.30  E-value: 2.70e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  900 MAKRELKKLKIEARSVERYKKLHIGMEN-KIMQLQRKVDEQNKDYKCLVEKLTNLEGIYNSETEKLRSDLERLQLSEEEA 978
Cdd:pfam02463  694 ILRRQLEIKKKEQREKEELKKLKLEAEElLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKE 773

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  979 KvatgrvlSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQEKEalnhrivqQAKEMTETMEK 1058
Cdd:pfam02463  774 K-------ELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQE--------EKIKEEELEEL 838

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1059 KLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMVHVPKPGHKRTDSTHSSNESEYIFSSEIAEMEDIPS 1138
Cdd:pfam02463  839 ALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENE 918

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1139 RTEEPSEKKVPLDMSLFLKLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEERPQIRGAELEYESLK--RQELESENK 1216
Cdd:pfam02463  919 IEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEerYNKDELEKE 998

                          330
                   ....*....|....*.
gi 1677538261 1217 KLKNELNELRKALSEK 1232
Cdd:pfam02463  999 RLEEEKKKLIRAIIEE 1014
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 911-1418 4.58e-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: 61.67  E-value: 4.58e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  911 EARSVERYKKLHIGMENKIMQLQRKvdEQNKDYKClveKLTNLEgiynSETEKLRSDLErlqlseEEAKVATGRVLSLQE 990
Cdd:pfam15921  285 EKASSARSQANSIQSQLEIIQEQAR--NQNSMYMR---QLSDLE----STVSQLRSELR------EAKRMYEDKIEELEK 349

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  991 EIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQEKEAlNHRIVQQAKEMTETMEkklveetkQLELD 1070
Cdd:pfam15921  350 QLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQ-NKRLWDRDTGNSITID--------HLRRE 420

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1071 LNDERLRYQnllnefsRLEERYDDLKEEMTLMVhvpkpgHKRTDSTHSSNESEYIFSSEIAEMEDIPSR----TEEPSEK 1146
Cdd:pfam15921  421 LDDRNMEVQ-------RLEALLKAMKSECQGQM------ERQMAAIQGKNESLEKVSSLTAQLESTKEMlrkvVEELTAK 487

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1147 KVPLDMS------LFLKLQKRVTELE---QEKQVMQDELDRKEEQVLRSKAKEEerpQIRGAELEYESLK---------- 1207
Cdd:pfam15921  488 KMTLESSertvsdLTASLQEKERAIEatnAEITKLRSRVDLKLQELQHLKNEGD---HLRNVQTECEALKlqmaekdkvi 564

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1208 ---RQELES-----------------ENKKLKNELNELRKALSEksapevtapgapaYRVLMEQLTSVSEELDVRKEEVL 1267
Cdd:pfam15921  565 eilRQQIENmtqlvgqhgrtagamqvEKAQLEKEINDRRLELQE-------------FKILKDKKDAKIRELEARVSDLE 631

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1268 ILRSQLVSQ--------KEAIQPKDD-----KNTMTDSTILLEDVQKMKdkgeiaQAYIGLKETNRLLESQLQSQKRSHE 1334
Cdd:pfam15921  632 LEKVKLVNAgserlravKDIKQERDQllnevKTSRNELNSLSEDYEVLK------RNFRNKSEEMETTTNKLKMQLKSAQ 705

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1335 NEAEALRGEIQSLKEENNRQQQLLAQNLQLPPEAR--IEAsLQHEITRL----TNENLDlmEQLEKQDKTvrKLKKQLKV 1408
Cdd:pfam15921  706 SELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRgqIDA-LQSKIQFLeeamTNANKE--KHFLKEEKN--KLSQELST 780

                          570
                   ....*....|....
gi 1677538261 1409 FA----KKIGELEV 1418
Cdd:pfam15921  781 VAteknKMAGELEV 794
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 902-1407 1.60e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.95  E-value: 1.60e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  902 KRELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLVEKLTNLEGIYNSETEKLRSDLERLQLSEEEAKVA 981
Cdd:COG1196    305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  982 TGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQEKEALNHRIVQQAKEMTETMEKKLV 1061
Cdd:COG1196    385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1062 EETKQLELDLNDERLryQNLLNEFSRLEERYDDLKEEMTLMVHVPKPGHKRTDSTHSSNESEyifssEIAEMEDIPSRTE 1141
Cdd:COG1196    465 LAELLEEAALLEAAL--AELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAG-----AVAVLIGVEAAYE 537

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1142 EPsekkvpLDMSLFLKLQKRVTELEQE-KQVMQDELDRKEEQV--LRSKAKEEERPQIRGAELEYESLKRQELESENKKL 1218
Cdd:COG1196    538 AA------LEAALAAALQNIVVEDDEVaAAAIEYLKAAKAGRAtfLPLDKIRARAALAAALARGAIGAAVDLVASDLREA 611

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1219 KNELNELRKALSEKSAPEVTAPGAPAYRV-LMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQpkdDKNTMTDSTILLE 1297
Cdd:COG1196    612 DARYYVLGDTLLGRTLVAARLEAALRRAVtLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALL---EAEAELEELAERL 688

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1298 DVQKMKDKGEIAQAYIGLKETNRLLESQLQSQKRSHENEAEALRGEIQSLKEENNRQQQLLAQNLQLPPEARIEASLQHE 1377
Cdd:COG1196    689 AEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERE 768

                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 1677538261 1378 ITRLTNE-------NLDLMEQLEKQDKTVRKLKKQLK 1407
Cdd:COG1196    769 LERLEREiealgpvNLLAIEEYEELEERYDFLSEQRE 805
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 903-1417 1.62e-08

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: 59.65  E-value: 1.62e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  903 RELKKLKieaRSVERYKKLhigMENKIMQLQRKVDEQNKDYKCLVEKLTNLEGiYNSETEKLRSDLERLqlsEEEAKVAT 982
Cdd:TIGR04523  162 NDLKKQK---EELENELNL---LEKEKLNIQKNIDKIKNKLLKLELLLSNLKK-KIQKNKSLESQISEL---KKQNNQLK 231

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  983 GRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQEKEALNhrivqQAKEMTETMEKKLVE 1062
Cdd:TIGR04523  232 DNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLN-----QLKSEISDLNNQKEQ 306

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1063 E-TKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMvhvpkpghkRTDSTHSSNESEYIfSSEIAEMED-IPSRT 1140
Cdd:TIGR04523  307 DwNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQL---------KKELTNSESENSEK-QRELEEKQNeIEKLK 376

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1141 EEPSEKKvpldmslflklqKRVTELEQEKQVMQDELDRKEEQvlrSKAKEEerpQIRGAELEYESLKR--QELESENKKL 1218
Cdd:TIGR04523  377 KENQSYK------------QEIKNLESQINDLESKIQNQEKL---NQQKDE---QIKKLQQEKELLEKeiERLKETIIKN 438

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1219 KNELNELRKALSEKSApevtapgapAYRVLMEQLTSVSEELDVRKEEVLILRSQL-VSQKEAIQPKDDKNTMTDSTILLE 1297
Cdd:TIGR04523  439 NSEIKDLTNQDSVKEL---------IIKNLDNTRESLETQLKVLSRSINKIKQNLeQKQKELKSKEKELKKLNEEKKELE 509

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1298 dvQKMKD-KGEIAQayigLKETnrllESQLQSQKRSHENEAEALRGEIQSLKEENNRQQQLLAQNLQlppEARIEaSLQH 1376
Cdd:TIGR04523  510 --EKVKDlTKKISS----LKEK----IEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEK---NKEIE-ELKQ 575

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1677538261 1377 EITRLTNEN--------------LDLMEQLEKQDKTVRKLKKQLKVFAKKIGELE 1417
Cdd:TIGR04523  576 TQKSLKKKQeekqelidqkekekKDLIKEIEEKEKKISSLEKELEKAKKENEKLS 630
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 902-1417 6.20e-08

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: 58.14  E-value: 6.20e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  902 KRELKKLKIEARSVERYKKLhigMENKIMQLQRKVDEQNKDYKCLVEKLTNLEGIYNSETEKL------RSDLE-RLQLS 974
Cdd:TIGR02168  301 EQQKQILRERLANLERQLEE---LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELeeleaeLEELEsRLEEL 377

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  975 EEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQEKEALNHRIVQQAKEMTE 1054
Cdd:TIGR02168  378 EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELE 457

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1055 TMEKKL------VEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMVHVPK--PGHKRTDSTHSSNESEYIF 1126
Cdd:TIGR02168  458 RLEEALeelreeLEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSglSGILGVLSELISVDEGYEA 537

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1127 SSEIA----------------------------------EMEDIPSRTEEPSEKKVPLDMSLFLKLQKR-VTELEQEKQV 1171
Cdd:TIGR02168  538 AIEAAlggrlqavvvenlnaakkaiaflkqnelgrvtflPLDSIKGTEIQGNDREILKNIEGFLGVAKDlVKFDPKLRKA 617

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1172 MQDELDR-------KEEQVLRSKAKEEER-------------------------PQIRGAELEYESLKRQELESENKKLK 1219
Cdd:TIGR02168  618 LSYLLGGvlvvddlDNALELAKKLRPGYRivtldgdlvrpggvitggsaktnssILERRREIEELEEKIEELEEKIAELE 697

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1220 NELNELRKALSEKSAPEVTAPGAPayRVLMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQPKDDKNTMTDSTILLEDV 1299
Cdd:TIGR02168  698 KALAELRKELEELEEELEQLRKEL--EELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE 775

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1300 QKMKDKGEIAQayigLKETNRLLESQLQSQKRSH---ENEAEALRGEIQSLKE--ENNRQQQLLAQNLQLPPEARIE--- 1371
Cdd:TIGR02168  776 ELAEAEAEIEE----LEAQIEQLKEELKALREALdelRAELTLLNEEAANLRErlESLERRIAATERRLEDLEEQIEels 851

                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1677538261 1372 ---ASLQHEITRLTNENLDLMEQLE-------KQDKTVRKLKKQLKVFAKKIGELE 1417
Cdd:TIGR02168  852 ediESLAAEIEELEELIEELESELEallneraSLEEALALLRSELEELSEELRELE 907
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
900-1273 6.49e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 57.47  E-value: 6.49e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  900 MAKRELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLVEKLTNLEGIYN-----SETEKLRSDLERLQLS 974
Cdd:COG4717     68 LNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllplyQELEALEAELAELPER 147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  975 EEEAKVATGRVLSLQEEIAKLRKDLEQTRSEkkcIEEHADRYKQETEQLVSNLKEENTLLKQEKEALNHRIVQQAKEMTE 1054
Cdd:COG4717    148 LEELEERLEELRELEEELEELEAELAELQEE---LEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEE 224

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1055 TMEKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMVHVP---------------------KPGHKRT 1113
Cdd:COG4717    225 LEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAgvlflvlgllallflllarekASLGKEA 304

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1114 DSTHSSNESEYIFSSEIAEMEDIPSRTEEPSEKKVPLDMSLFLKLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEER 1193
Cdd:COG4717    305 EELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDE 384

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1194 PQIRGAELEYEslKRQELESENKKLKNELNELRKALSEKSAPEVTAPGAPAYRVLMEQLTSVSEELDVRKEEVLILRSQL 1273
Cdd:COG4717    385 EELRAALEQAE--EYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAEL 462
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 992-1278 9.30e-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: 57.06  E-value: 9.30e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  992 IAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQEKE---ALNHRIVQQAKEMTETMEK-KLVEETKQL 1067
Cdd:pfam17380  277 IVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKArqaEMDRQAAIYAEQERMAMEReRELERIRQE 356

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1068 ELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMVHVPKPGHKRTDSTHSSNESEYIFSSEIAEMEDIPSRTEEPSEKK 1147
Cdd:pfam17380  357 ERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQRE 436

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1148 VPLDMSLFLKLQKRVTELEQEKQ-----VMQDELDRKEEQVLRSKAK------EEERPQIrgAELEYESLKRQELESENK 1216
Cdd:pfam17380  437 VRRLEEERAREMERVRLEEQERQqqverLRQQEEERKRKKLELEKEKrdrkraEEQRRKI--LEKELEERKQAMIEEERK 514

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1677538261 1217 K--LKNELNELRKALSEKSAPEV------TAPGAPAYRVLMEQLTSVSEE---LDVRKEEVLILRSQLVSQKE 1278
Cdd:pfam17380  515 RklLEKEMEERQKAIYEEERRREaeeerrKQQEMEERRRIQEQMRKATEErsrLEAMEREREMMRQIVESEKA 587
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 902-1455 1.20e-07

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 56.98  E-value: 1.20e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  902 KRELKKLKIEARSVERykklhigMENKIMQLQRKVDEQNKDYKclvEKLTNLEGiynseTEKLRSDLERLQlseEEAKVA 981
Cdd:TIGR00606  590 RDRLAKLNKELASLEQ-------NKNHINNELESKEEQLSSYE---DKLFDVCG-----SQDEESDLERLK---EEIEKS 651

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  982 TGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADR---YKQETEQLVSNLKEENTLLKQEKEALNHRIVQQAKEMTETMEK 1058
Cdd:TIGR00606  652 SKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRvfqTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGL 731

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1059 KLVE--ETKQLELDLNDERLRYQNLLNEFSRLEeryDDLKEEMTLMvhvpkpghkrtDSTHSSNESEYIFSSEIAEMEDI 1136
Cdd:TIGR00606  732 APGRqsIIDLKEKEIPELRNKLQKVNRDIQRLK---NDIEEQETLL-----------GTIMPEEESAKVCLTDVTIMERF 797

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1137 PSRTEEpSEKKVPLDMSLF--LKLQKRVTELEQEKQVMQDELDRKEEQV-LRSKAKEEERPQIrgaeleyeslkrQELES 1213
Cdd:TIGR00606  798 QMELKD-VERKIAQQAAKLqgSDLDRTVQQVNQEKQEKQHELDTVVSKIeLNRKLIQDQQEQI------------QHLKS 864

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1214 ENKKLKNELNELRKALSEKSAPEVTApgapayRVLMEQLTSVSEELDVRKEEVL----ILRSQLVSQKEAIQPKDDKNTM 1289
Cdd:TIGR00606  865 KTNELKSEKLQIGTNLQRRQQFEEQL------VELSTEVQSLIREIKDAKEQDSpletFLEKDQQEKEELISSKETSNKK 938

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1290 TDstillEDVQKMKDKgeIAQAYIGLKETNRLLESQLQSQKRSHENEaeaLRGEIQSLKEENNRQQQLLAQNLQLppeaR 1369
Cdd:TIGR00606  939 AQ-----DKVNDIKEK--VKNIHGYMKDIENKIQDGKDDYLKQKETE---LNTVNAQLEECEKHQEKINEDMRLM----R 1004

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1370 IEASLQHEITRLTNENLDLMeqleKQDKTVRKLKKQLKVFAKKIGELEVGQMENisPGQIIDEPIRpvNIPRKE-KDFQG 1448
Cdd:TIGR00606 1005 QDIDTQKIQERWLQDNLTLR----KRENELKEVEEELKQHLKEMGQMQVLQMKQ--EHQKLEENID--LIKRNHvLALGR 1076


                   ....*..
gi 1677538261 1449 MLEYKKE 1455
Cdd:TIGR00606 1077 QKGYEKE 1083
Myo5p-like_CBD_Rasip1 cd15472
cargo binding domain of myosin 5-like of Ras-interacting protein 1; Ras-interacting protein 1 ...
 1482-1761 1.29e-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: 55.74  E-value: 1.29e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1482 PAYILFMCVRHADYLNDDQKVRSLLTSTINSIKKVL----KKRGD---------------------DFETVSFWLSNTCR 1536
Cdd:cd15472     25 PAFLLCLCIQHSATHFEPGHFGKLLLKIAKRIQEIVwektKELAEkqpehqdpaslsllsiaelapDLQPLLFWMSNSIE 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1537 FLHCLKQ----YSGEEGFMKHNTSRQNEHCLTNFDLAEYRQVLSDLAIQIYQQLVRVLENILQPmIVSGMLE-----HET 1607
Cdd:cd15472    105 LLYFIQQkvplYEQSMEEELDVGSKESLLSSTLTASEEAMTVLEEVIMYTFQQCVYYLTKTLYV-ALPALLDsnpftAEE 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1608 IQGVSG--VKPTGLRkRTSSIADEgtyTLDsILRQLnsfhsvmCQHgmdPELIKQVVKQMFYIIGAITLNNLLLRKDMCS 1685
Cdd:cd15472    184 RESWSGgsRLPEGVR-RVLEIYQA---TLD-LLRQY-------QVH---PEIASQMFAYLFFFSNASLFNQLMEKGSGGG 248

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1686 ---WSKGMQIRYNVSQLEEWLRDKNLmNSGAKETLEPLIQAAQLLQVKKKTDDDAE--AICSMCNALTTAQIVKVLNLYT 1760
Cdd:cd15472    249 ffqWSRGVQIRANLDLLLDWLQGAGL-GDLAEEFFRKLSSTVNLLATPKEQLLQMSwsSLRAEFPALNPAQLHHLLRQYQ 327


                   .
gi 1677538261 1761 P 1761
Cdd:cd15472    328 L 328
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 898-1339 1.36e-07

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: 56.90  E-value: 1.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  898 RMMAKRELKKLKIEAR-----SVERYKKLHIGMENKIMQLQRKVDEQNK---DYKCLVEKLTNLEGIYNSETEKLRSDLE 969
Cdd:TIGR00618  415 RTSAFRDLQGQLAHAKkqqelQQRYAELCAAAITCTAQCEKLEKIHLQEsaqSLKEREQQLQTKEQIHLQETRKKAVVLA 494

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  970 RLQLSEEEAK--------------------VATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETE-------- 1021
Cdd:TIGR00618  495 RLLELQEEPCplcgscihpnparqdidnpgPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQeiqqsfsi 574

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1022 --QLVSNLKEENTLLKQEKEALNHRIVQQAKEmtetmEKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYddlKEEM 1099
Cdd:TIGR00618  575 ltQCDNRSKEDIPNLQNITVRLQDLTEKLSEA-----EDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELA---LKLT 646

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1100 TLmvhvpkpgHKRTDSTHSSNESEYIFSSEIAEMEDIPSRTEEPSEKKvpldmSLFLKLQKRVTELEQekqvmQDELDRK 1179
Cdd:TIGR00618  647 AL--------HALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQ-----SEKEQLTYWKEMLAQ-----CQTLLRE 708

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1180 EEQVLrskakEEERPQIRGAELEYESLKrQELESENKKLKNELNELRKALSEK-----SAPEVTAPGAPAYRVLMEQLTS 1254
Cdd:TIGR00618  709 LETHI-----EEYDREFNEIENASSSLG-SDLAAREDALNQSLKELMHQARTVlkartEAHFNNNEEVTAALQTGAELSH 782

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1255 VSEELDVRKEEVLILRSQLVSQKEAIQPKDDKN----TMTDSTILLEDVQ-------KMKDKGEIAQAYIGLKETNRLLE 1323
Cdd:TIGR00618  783 LAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDedilNLQCETLVQEEEQflsrleeKSATLGEITHQLLKYEECSKQLA 862

                          490
                   ....*....|....*.
gi 1677538261 1324 SQLQSQKRSHENEAEA 1339
Cdd:TIGR00618  863 QLTQEQAKIIQLSDKL 878
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 928-1259 2.56e-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: 55.84  E-value: 2.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  928 KIMQLQRKVDEQNKDYKCLVEKLTNLEGIYNSETEKLrSDLERlQLSEEEAkvatgRVLSLQEEIAKLRKDLEQTRSEKK 1007
Cdd:TIGR02169  675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQEL-SDASR-KIGEIEK-----EIEQLEQEEEKLKERLEELEEDLS 747

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1008 CIEEHADRYKQETEQLVSNLKEENTLLKQEKEALNH----------RIVQQAKEMTETMEKKLVEETKQLELDLNDERLR 1077
Cdd:TIGR02169  748 SLEQEIENVKSELKELEARIEELEEDLHKLEEALNDlearlshsriPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLE 827

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1078 YQNLLNEFSRLEERYDDLKEEMtlmvhvpkpghkrtdsthssneseyifSSEIAEMEDIPSRTEEPSEKkvpldmslFLK 1157
Cdd:TIGR02169  828 KEYLEKEIQELQEQRIDLKEQI---------------------------KSIEKEIENLNGKKEELEEE--------LEE 872

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1158 LQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEErpqirgAELEYEsLKRQELESENKKLKNELNELRKALSEKSAPEV 1237
Cdd:TIGR02169  873 LEAALRDLESRLGDLKKERDELEAQLRELERKIEE------LEAQIE-KKRKRLSELKAKLEALEEELSEIEDPKGEDEE 945

                          330       340
                   ....*....|....*....|..
gi 1677538261 1238 TAPGAPAYRVLMEQLTSVSEEL 1259
Cdd:TIGR02169  946 IPEEELSLEDVQAELQRVEEEI 967
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 901-1417 2.78e-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: 55.84  E-value: 2.78e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  901 AKRELKKL-KIEARSVERYKKLhigmENKIMQLQRKVDEQNKDYKCLVEKLTNLEgiynSETEKLRSDLERLqlsEEEAK 979
Cdd:TIGR02169  313 KERELEDAeERLAKLEAEIDKL----LAEIEELEREIEEERKRRDKLTEEYAELK----EELEDLRAELEEV---DKEFA 381

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  980 VATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQL---VSNLKEENTLLKQEKEALNHRIvqqakemtetm 1056
Cdd:TIGR02169  382 ETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLnaaIAGIEAKINELEEEKEDKALEI----------- 450

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1057 eKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEM-----TLMVHVPK-PGHKRTDSTHSSN---------- 1120
Cdd:TIGR02169  451 -KKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELaeaeaQARASEERvRGGRAVEEVLKASiqgvhgtvaq 529

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1121 ----ESEYIFSSEIA---EMEDIPSRTEEPSE------KKVPLDMSLFLKLQK-RVTELEQEKQVMQD---------ELD 1177
Cdd:TIGR02169  530 lgsvGERYATAIEVAagnRLNNVVVEDDAVAKeaiellKRRKAGRATFLPLNKmRDERRDLSILSEDGvigfavdlvEFD 609

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1178 RKEE----QVLRS----------------------------------------------KAKEEERPQIRGAELeyESLK 1207
Cdd:TIGR02169  610 PKYEpafkYVFGDtlvvedieaarrlmgkyrmvtlegelfeksgamtggsraprggilfSRSEPAELQRLRERL--EGLK 687

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1208 RQE--LESENKKLKNELNELRKALSEKSApevtapgapAYRVLMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQPKDD 1285
Cdd:TIGR02169  688 RELssLQSELRRIENRLDELSQELSDASR---------KIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKS 758

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1286 KNTMTDSTI--LLEDVQKMKDK-------------GEIAQAYIGLKETNRLLESQLQSQKR---SHENEAEALRGEIQSL 1347
Cdd:TIGR02169  759 ELKELEARIeeLEEDLHKLEEAlndlearlshsriPEIQAELSKLEEEVSRIEARLREIEQklnRLTLEKEYLEKEIQEL 838

                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1677538261 1348 KEENNRQQQLLAQNlqlppEARIE------ASLQHEITRLTNENLDLMEQLEKQDKTVRKLKKQLKVFAKKIGELE 1417
Cdd:TIGR02169  839 QEQRIDLKEQIKSI-----EKEIEnlngkkEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELE 909
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 904-1461 4.14e-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: 55.11  E-value: 4.14e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  904 ELKKLKIEARSVERYKKLHIGMENKIMQLQR---------------KVDEQNKDYKCLVEK------LTNL--------- 953
Cdd:pfam05483   89 KIKKWKVSIEAELKQKENKLQENRKIIEAQRkaiqelqfenekvslKLEEEIQENKDLIKEnnatrhLCNLlketcarsa 168

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  954 --EGIYNSETEKLR-------SDLERLQLSEEEAKVATGRvlSLQEEIAKLRKDLEQTRS-EKKCIEEHADRYKQETEQL 1023
Cdd:pfam05483  169 ekTKKYEYEREETRqvymdlnNNIEKMILAFEELRVQAEN--ARLEMHFKLKEDHEKIQHlEEEYKKEINDKEKQVSLLL 246

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1024 VSNLKEEN-----TLLKQEKEALNHRIVQQAKEMTETMeKKLVEETKQLELDLNDERLRYQNLLNEFSRLEER------- 1091
Cdd:pfam05483  247 IQITEKENkmkdlTFLLEESRDKANQLEEKTKLQDENL-KELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDlqiatkt 325

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1092 -YDDLKEEMTLMVHVPKpghkrTDSTHSSNESEyiFSSEIAEMEDIPSRTEEPSEKKVPLDMSLFLKLQKRVTELEQ--- 1167
Cdd:pfam05483  326 iCQLTEEKEAQMEELNK-----AKAAHSFVVTE--FEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEmtk 398

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1168 ---EKQVMQDELDR--KEEQVLRSKAKEEER--PQIRGAEleyeslkrQELESENKKLKNELNELRKALSEKSAPEvtap 1240
Cdd:pfam05483  399 fknNKEVELEELKKilAEDEKLLDEKKQFEKiaEELKGKE--------QELIFLLQAREKEIHDLEIQLTAIKTSE---- 466

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1241 gapayRVLMEQLTSVSEELDVRKEEVLILRSQlvSQKEAIQPKDDKNTMTDSTILL----EDVQKMKDKGEIAQAYI-GL 1315
Cdd:pfam05483  467 -----EHYLKEVEDLKTELEKEKLKNIELTAH--CDKLLLENKELTQEASDMTLELkkhqEDIINCKKQEERMLKQIeNL 539

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1316 KETNRLLESQLQSQKRSHENEAEALRGEIQslKEENNRQQQLLAQNLQLPPEARIEASLQHEITRLTNENLDLmEQLEKQ 1395
Cdd:pfam05483  540 EEKEMNLRDELESVREEFIQKGDEVKCKLD--KSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNI-EELHQE 616

                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1396 DKTVRKL----KKQLKVFAKKIGELEvgqMENISPGQIIDEPIrpvniprkeKDFQGMLEYKKEDEQKLV 1461
Cdd:pfam05483  617 NKALKKKgsaeNKQLNAYEIKVNKLE---LELASAKQKFEEII---------DNYQKEIEDKKISEEKLL 674
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 896-1258 5.36e-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: 5.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  896 FRRMMAKRELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLVEKLTNLEGIYNS----ETEKLRS----- 966
Cdd:pfam17380  293 FEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEerkrELERIRQeeiam 372

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  967 ------DLERLQLSEeeakvatgrvlslQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQEKEA 1040
Cdd:pfam17380  373 eisrmrELERLQMER-------------QQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRR 439

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1041 LNHrivQQAKEMTETMEKKLvEETKQLELDLNDERLRYQNLLnEFSRlEERYDDLKEEMTLMVhVPKPGHKRTDSTHSSN 1120
Cdd:pfam17380  440 LEE---ERAREMERVRLEEQ-ERQQQVERLRQQEEERKRKKL-ELEK-EKRDRKRAEEQRRKI-LEKELEERKQAMIEEE 512

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1121 ESEYIFSSEIAEMEDipsrteepsekkvpldmSLFLKLQKRVTELEQEKQVMQDELDRKEEQVLRSKakeEERPQIRGAE 1200
Cdd:pfam17380  513 RKRKLLEKEMEERQK-----------------AIYEEERRREAEEERRKQQEMEERRRIQEQMRKAT---EERSRLEAME 572

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1677538261 1201 LEYEsLKRQELESENKKLKNELNELRKALSEKSAPEVTAPGAPAYRVLMEQLTSVSEE 1258
Cdd:pfam17380  573 RERE-MMRQIVESEKARAEYEATTPITTIKPIYRPRISEYQPPDVESHMIRFTTQSPE 629
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
925-1350 5.42e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 54.66  E-value: 5.42e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  925 MENKIMQLQRKVDEQNKDYKCLVEKLTNLEGIYNSETEKLRSDLERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRS 1004
Cdd:PRK02224   256 LEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRV 335

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1005 EKKCIEEHADRYKQETEQlvsnLKEENTLLKQEKEALNHRIvQQAKEMTETMEKKLVEetkqLELDLNDERLRYQNLLNE 1084
Cdd:PRK02224   336 AAQAHNEEAESLREDADD----LEERAEELREEAAELESEL-EEAREAVEDRREEIEE----LEEEIEELRERFGDAPVD 406

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1085 FSRLEERYDDLKEEmtlmvhvpkpghkRTDSTHSSNESEYIFSSE---IAE----------------MEDIP--SRTEEP 1143
Cdd:PRK02224   407 LGNAEDFLEELREE-------------RDELREREAELEATLRTArerVEEaealleagkcpecgqpVEGSPhvETIEED 473

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1144 SEKKVPLDMSL------FLKLQKRVTELEQEKQVmQDELDRKEEQVLRSkakeEERPQIRGAELEYESLKRQELESENKK 1217
Cdd:PRK02224   474 RERVEELEAELedleeeVEEVEERLERAEDLVEA-EDRIERLEERREDL----EELIAERRETIEEKRERAEELRERAAE 548

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1218 LKNELNELRKALSEksAPEVTAPGAPAYRVLMEQLTSVSEELDV--RKEEVLILRSQLVSQKEAIQPK-DDKNTMTDsti 1294
Cdd:PRK02224   549 LEAEAEEKREAAAE--AEEEAEEAREEVAELNSKLAELKERIESleRIRTLLAAIADAEDEIERLREKrEALAELND--- 623

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1677538261 1295 llEDVQKMKDKGEIAQAYIGLKETNRLleSQLQSQKRSHENEAEALRGEIQSLKEE 1350
Cdd:PRK02224   624 --ERRERLAEKRERKRELEAEFDEARI--EEAREDKERAEEYLEQVEEKLDELREE 675
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 901-1099 8.15e-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: 8.15e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  901 AKRELKKLKIEARSVErykklhigmeNKIMQLQRKVDEQNKDYKCLVEKLTNLEG---IYNSETEKLRSDLERLqlsEEE 977
Cdd:TIGR02168  808 LRAELTLLNEEAANLR----------ERLESLERRIAATERRLEDLEEQIEELSEdieSLAAEIEELEELIEEL---ESE 874

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  978 AKVATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLvsnlKEENTLLKQEKEALNHRIVQQAK------- 1050
Cdd:TIGR02168  875 LEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEEL----REKLAQLELRLEGLEVRIDNLQErlseeys 950

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1677538261 1051 ---EMTETMEKKLVEETKQLELDLNDERLRYQNL-------LNEFSRLEERYDDLKEEM 1099
Cdd:TIGR02168  951 ltlEEAEALENKIEDDEEEARRRLKRLENKIKELgpvnlaaIEEYEELKERYDFLTAQK 1009
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 881-1469 1.23e-06

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: 53.82  E-value: 1.23e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  881 HYKRSMHAIIYLQCCFRRMmaKRELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLVEKLTNLEGIYNSE 960
Cdd:pfam02463  221 LEEEYLLYLDYLKLNEERI--DLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEEL 298

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  961 TEKLRSDLERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQEKEA 1040
Cdd:pfam02463  299 KSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAK 378

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1041 LNHRIVQQAKEMTETMEKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLmvhvpkpghkRTDSTHSSN 1120
Cdd:pfam02463  379 KKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESI----------ELKQGKLTE 448

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1121 ESEYIFSSEIAEMEDIPSRTEEPSEKKVPLDMSLFLKLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEERPQIRGAE 1200
Cdd:pfam02463  449 EKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAH 528

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1201 leyESLKRQELESENKKLKNELNELRKALSEKSAPEVTAPGAPAYRVLMEQLTSVSEELDVRKeevLILRSQLVSQKEAI 1280
Cdd:pfam02463  529 ---GRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLK---LPLKSIAVLEIDPI 602

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1281 QPKDDKNTMTDSTILLEDVQKMKDKGEIAQAYIGLKETNRLLESQLQSQKRSHENEAEALRGEIQSLKEENNRQQQLLAQ 1360
Cdd:pfam02463  603 LNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQ 682

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1361 NLQLPPEARIEASLQHEITRLTNENLDLMEQLEKQDKTVRKLKKQLKVFAKKIGELEVGQMENISPGQ----IIDEPIRP 1436
Cdd:pfam02463  683 EKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEeeekSRLKKEEK 762

                          570       580       590
                   ....*....|....*....|....*....|...
gi 1677538261 1437 VNIPRKEKDFQGMLEYKKEDEQKLVKNLILELK 1469
Cdd:pfam02463  763 EEEKSELSLKEKELAEEREKTEKLKVEEEKEEK 795
PRK12704 PRK12704
phosphodiesterase; Provisional
 900-1066 1.52e-06

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 52.86  E-value: 1.52e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  900 MAKRELKKLKIEARSVERYKKLHIgmENKIMQLQRKVDEQNKDYKclvEKLTNLEGIYNSETEKLRSDLERLQLSEEEAK 979
Cdd:PRK12704    39 EAKRILEEAKKEAEAIKKEALLEA--KEEIHKLRNEFEKELRERR---NELQKLEKRLLQKEENLDRKLELLEKREEELE 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  980 VATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQE--TEQLVSNLKEEntlLKQEKEALNHRIVQQAKEMTETME 1057
Cdd:PRK12704   114 KKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEeaKEILLEKVEEE---ARHEAAVLIKEIEEEAKEEADKKA 190


                   ....*....
gi 1677538261 1058 KKLVEETKQ 1066
Cdd:PRK12704   191 KEILAQAIQ 199
PTZ00121 PTZ00121
MAEBL; Provisional
 904-1459 1.55e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.61  E-value: 1.55e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  904 ELKKLKiEARSVERYKKLHigMENKIMQLQRKVDEQNkdykclVEKLTNLEGIYNSE-----TEKLRSDLERLQLSEEEA 978
Cdd:PTZ00121  1192 ELRKAE-DARKAEAARKAE--EERKAEEARKAEDAKK------AEAVKKAEEAKKDAeeakkAEEERNNEEIRKFEEARM 1262

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  979 KVATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQEKEAlnhrivQQAKEMTETMEK 1058
Cdd:PTZ00121  1263 AHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKA------EEAKKKADAAKK 1336

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1059 KLVEETKQLELDLNDERLRYQNLlnEFSRLEERYDDLK--EEMTLMVHVPKPGH--KRTDSTHSSNESEYIFSSEIAEME 1134
Cdd:PTZ00121  1337 KAEEAKKAAEAAKAEAEAAADEA--EAAEEKAEAAEKKkeEAKKKADAAKKKAEekKKADEAKKKAEEDKKKADELKKAA 1414

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1135 DIPSRTEE----PSEKKVPLDMSLFLKLQKRVTELEQ--EKQVMQDELDRKEEQVLRS---KAKEEERPQIRGAELEYES 1205
Cdd:PTZ00121  1415 AAKKKADEakkkAEEKKKADEAKKKAEEAKKADEAKKkaEEAKKAEEAKKKAEEAKKAdeaKKKAEEAKKADEAKKKAEE 1494

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1206 LKRQELESENK-KLKNELNELRKALSEKSAPEVTAPGAPAYRVLMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQPKD 1284
Cdd:PTZ00121  1495 AKKKADEAKKAaEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEE 1574

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1285 DKNTMTDSTILLEDVQKMKDKGEIAQAYIGLKETNRLLESQLQSQKRSHE-NEAEALRGEIQSLKEENNRQQQLLAQNLQ 1363
Cdd:PTZ00121  1575 DKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEElKKAEEEKKKVEQLKKKEAEEKKKAEELKK 1654

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1364 LPPEARIEASlqhEITRLTNENLDLMEQLEKQDKTVRKLKKQLKVF---AKKIGELEVGQMENISPGQII--DEPIRPVN 1438
Cdd:PTZ00121  1655 AEEENKIKAA---EEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEaeeAKKAEELKKKEAEEKKKAEELkkAEEENKIK 1731

                          570       580
                   ....*....|....*....|....*
gi 1677538261 1439 IP----RKEKDFQGMLEYKKEDEQK 1459
Cdd:PTZ00121  1732 AEeakkEAEEDKKKAEEAKKDEEEK 1756
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 980-1244 1.63e-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: 1.63e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  980 VATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEentlLKQEKEALNHRIVQQAKEMTETMEK- 1058
Cdd:COG4942     10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA----LERRIAALARRIRALEQELAALEAEl 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1059 -KLVEETKQLELDLNDERLRYQNLLNEFSRLEERyddlkEEMTLMVHVPKPghkrTDSTHSSNESEYIFSSEIAEMEDIP 1137
Cdd:COG4942     86 aELEKEIAELRAELEAQKEELAELLRALYRLGRQ-----PPLALLLSPEDF----LDAVRRLQYLKYLAPARREQAEELR 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1138 SRTEEpsekkvpldmslflkLQKRVTELEQEKQVMQDELDRKEEQVLR-SKAKEEERPQIRGAELEYESLKRQ--ELESE 1214
Cdd:COG4942    157 ADLAE---------------LAALRAELEAERAELEALLAELEEERAAlEALKAERQKLLARLEKELAELAAElaELQQE 221

                          250       260       270
                   ....*....|....*....|....*....|
gi 1677538261 1215 NKKLKNELNELRKALSEKSAPEVTAPGAPA 1244
Cdd:COG4942    222 AEELEALIARLEAEAAAAAERTPAAGFAAL 251
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 911-1350 1.77e-06

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: 52.90  E-value: 1.77e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  911 EARSVERYKKLHIGMENKIMQL----QRKVDE-------------QNKDYK----CLVEKLTNLE---GIYNSETEKLRS 966
Cdd:pfam10174  273 EIKQMEVYKSHSKFMKNKIDQLkqelSKKESEllalqtkletltnQNSDCKqhieVLKESLTAKEqraAILQTEVDALRL 352

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  967 DLER-----------LQLSEEEAKVATG--------------RVLSLQEEIAKLrkdLEQTRSEKKCIEEHADRYKqETE 1021
Cdd:pfam10174  353 RLEEkesflnkktkqLQDLTEEKSTLAGeirdlkdmldvkerKINVLQKKIENL---QEQLRDKDKQLAGLKERVK-SLQ 428

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1022 QLVSNlkeENTLLKQEKEAL--NHRIVQQAKEMTETMEKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEM 1099
Cdd:pfam10174  429 TDSSN---TDTALTTLEEALseKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHA 505

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1100 TLMVHVPKpghkRTDSTHSSNESEyifsseIAEMEDIPSRTEEPSEKKVPLDMSLFLK--LQKRVTELEQEKQVMQDELD 1177
Cdd:pfam10174  506 SSLASSGL----KKDSKLKSLEIA------VEQKKEECSKLENQLKKAHNAEEAVRTNpeINDRIRLLEQEVARYKEESG 575

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1178 RKEEQV------LRSKAKEEERPQIRGAELEyeSLKRQELESENKK---LKNELNELRK---ALSEKSAPEVTAPGAPAY 1245
Cdd:pfam10174  576 KAQAEVerllgiLREVENEKNDKDKKIAELE--SLTLRQMKEQNKKvanIKHGQQEMKKkgaQLLEEARRREDNLADNSQ 653

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1246 RVLMEQLTsvsEELDVRKEEVLILRSQLVSQKEAIQPKDD--KNTMTDSTILLEDVQKMKDkgEIAQAYIGLKETNRLLE 1323
Cdd:pfam10174  654 QLQLEELM---GALEKTRQELDATKARLSSTQQSLAEKDGhlTNLRAERRKQLEEILEMKQ--EALLAAISEKDANIALL 728

                          490       500       510
                   ....*....|....*....|....*....|.
gi 1677538261 1324 SQLQSQKRSHENEAEALRGE----IQSLKEE 1350
Cdd:pfam10174  729 ELSSSKKKKTQEEVMALKREkdrlVHQLKQQ 759
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 813-835 1.78e-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: 1.78e-06
                            10        20
                    ....*....|....*....|...
gi 1677538261   813 RRTKAATIIQKYWRMYVVRRRYK 835
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRYK 23
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 984-1442 2.89e-06

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: 52.67  E-value: 2.89e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  984 RVLSLQ--EEIAKLRKDLEQTRSE--------KKCIEEHADRYKQETEQLVSNLKEENTLLKQEKEALNHRivQQAKEMT 1053
Cdd:pfam02463  136 NFLVQGgkIEIIAMMKPERRLEIEeeaagsrlKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQA--KKALEYY 213

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1054 ETMEKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLmvhvpkpghKRTDSTHSSNESEYIFSSEIAEM 1133
Cdd:pfam02463  214 QLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIE---------KEEEKLAQVLKENKEEEKEKKLQ 284

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1134 EDIPSRTEEPSEKKVP---LDMSLFLKLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEERPQIRGAELEYESLKRQE 1210
Cdd:pfam02463  285 EEELKLLAKEEEELKSellKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKL 364

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1211 LESENKKLKNELNELRKALSEKSAPEVTAPGAPAYRVLMEQLTSV-----SEELDVRKEEVLILRSQLVSQKEAIQPKDD 1285
Cdd:pfam02463  365 QEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLllelaRQLEDLLKEEKKEELEILEEEEESIELKQG 444

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1286 KNTMTDSTILLEDVQKMKDKGEIAQAYIGLKETNRLLESQLQSQKRSHENEAEALRGEIQSLKEENNRQQQLLAQNLQLP 1365
Cdd:pfam02463  445 KLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRI 524

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1366 PEARIEASLQHEI---------TRLTNENLDLMEQLEKQDKTVRKLKKQLKVFAKKIGELEVGQMENISPGQIIDEPIRP 1436
Cdd:pfam02463  525 ISAHGRLGDLGVAvenykvaisTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILN 604


                   ....*.
gi 1677538261 1437 VNIPRK 1442
Cdd:pfam02463  605 LAQLDK 610
fMyo4p_CBD cd15479
cargo binding domain of fungal myosin 4; Yeast myosin V travels along actin cables, actin ...
 1641-1769 2.93e-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: 2.93e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1641 LNSFHSVMCQHGMDPELIKQVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQIRYNVSQLEEWLRDKnlmNSGAKETLEPL 1720
Cdd:cd15479    168 LNEFDAVLCKFQVVDSMHTKIFNDTLKYLNVMLFNDLITKCPALNWKYGYEVDRNIERLVSWFEPR---IEDVRPNLIQI 244

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1677538261 1721 IQAAQLLQVKKKTDDDAEAICSMCNALTTAQIVKVLNLYTPVNEFEERV 1769
Cdd:cd15479    245 IQAVKILQLKISNLNEFKLLFDFWYALNPAQIQAILLKYKPANKGEAGV 293
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
 639-663 3.12e-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: 3.12e-06
                           10        20
                   ....*....|....*....|....*
gi 1677538261  639 FRNSLHLLMETLNATTPHYVRCIKP 663
Cdd:cd01363    146 INESLNTLMNVLRATRPHFVRCISP 170
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 900-1225 3.54e-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: 3.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  900 MAKRELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLVEKLTNLegIYNSETEKLRSDLERLQLSEEEAK 979
Cdd:TIGR00618  602 KLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTL--TQERVREHALSIRVLPKELLASRQ 679

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  980 VATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQEKEALNHRIVQ-------QAKEM 1052
Cdd:TIGR00618  680 LALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKElmhqartVLKAR 759

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1053 TETMEKKLVEETKQLELDLNDERLRyQNLLNEFSRLEERYDDLKE-EMTLMVHVPKPGHKRTDSTHSSNESEYIFSSEIA 1131
Cdd:TIGR00618  760 TEAHFNNNEEVTAALQTGAELSHLA-AEIQFFNRLREEDTHLLKTlEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLE 838

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1132 E----MEDIPSRTEEPSEKKVPLDMSlfLKLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKE--EERPQIRGAELEYES 1205
Cdd:TIGR00618  839 EksatLGEITHQLLKYEECSKQLAQL--TQEQAKIIQLSDKLNGINQIKIQFDGDALIKFLHEitLYANVRLANQSEGRF 916

                          330       340
                   ....*....|....*....|
gi 1677538261 1206 LKRQELESENKKLKNELNEL 1225
Cdd:TIGR00618  917 HGRYADSHVNARKYQGLALL 936
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 960-1351 5.48e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 5.48e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  960 ETE-KLRS---DLERLQLSEEEakvatgrvlsLQEEIAKLRKDLEQtrsekkcieehADRYKQeteqlvsnLKEENTLLK 1035
Cdd:COG1196    176 EAErKLEAteeNLERLEDILGE----------LERQLEPLERQAEK-----------AERYRE--------LKEELKELE 226

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1036 QEKEALNHRIVQQAKEMTETMEKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEmtlmvhvpkpghkrtds 1115
Cdd:COG1196    227 AELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE----------------- 289

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1116 thssnesEYIFSSEIAEMEdipsrteepSEKKVpldmslflkLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEE-RP 1194
Cdd:COG1196    290 -------EYELLAELARLE---------QDIAR---------LEERRRELEERLEELEEELAELEEELEELEEELEElEE 344

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1195 QIRGAELEYESLkRQELESENKKLKNELNELRKALSEKSApevtapgapAYRVLMEQLTSVSE------ELDVRKEEVLI 1268
Cdd:COG1196    345 ELEEAEEELEEA-EAELAEAEEALLEAEAELAEAEEELEE---------LAEELLEALRAAAElaaqleELEEAEEALLE 414

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1269 LRSQLVSQKEAIQPKDDKNTMTDSTILLEDVQKMKDKGEIAQAyigLKETNRLLESQLQSQKRSHENEAEALRGEIQSLK 1348
Cdd:COG1196    415 RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE---EEALLELLAELLEEAALLEAALAELLEELAEAAA 491


                   ...
gi 1677538261 1349 EEN 1351
Cdd:COG1196    492 RLL 494
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1158-1417 6.71e-06

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: 51.22  E-value: 6.71e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1158 LQKRVTELEQEK------QVMQDELdRKEEQVLRSKAKEEERPQIRGAELEYESLKRQ--ELESENKKLKNELNELRKAL 1229
Cdd:TIGR02169  196 KRQQLERLRRERekaeryQALLKEK-REYEGYELLKEKEALERQKEAIERQLASLEEEleKLTEEISELEKRLEEIEQLL 274

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1230 SEKSApEVTAPGAPAYRVLMEQLTSVSEEL-------DVRKEEVLILRSQLVSQKEAIQPKddKNTMTDSTILLEDVQKM 1302
Cdd:TIGR02169  275 EELNK-KIKDLGEEEQLRVKEKIGELEAEIaslersiAEKERELEDAEERLAKLEAEIDKL--LAEIEELEREIEEERKR 351

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1303 KDKgeIAQAYIGLKETNRLLESQLQSQkrshENEAEALRGEIQSLKEEnnrqqqllaqnlqlppearIEAsLQHEITRLT 1382
Cdd:TIGR02169  352 RDK--LTEEYAELKEELEDLRAELEEV----DKEFAETRDELKDYREK-------------------LEK-LKREINELK 405

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1677538261 1383 NENLDLMEQLEKQDKTVRKLKKQLKVFAKKIGELE 1417
Cdd:TIGR02169  406 RELDRLQEELQRLSEELADLNAAIAGIEAKINELE 440
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
956-1417 6.74e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.92  E-value: 6.74e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  956 IYNSETEKLRSDLERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYK--QETEQLVSNLKEENTL 1033
Cdd:COG4717     68 LNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPER 147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1034 LKQEKEALN--HRIVQQAKEMTETMEKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMtlmvhvpkpghK 1111
Cdd:COG4717    148 LEELEERLEelRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEEL-----------E 216

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1112 RTDSTHSSNESEYIFSSEIAEMEDIPSRTEEPSEkkVPLDMSLFLKLqkrvteleqekQVMQDELDRKEEQVL------- 1184
Cdd:COG4717    217 EAQEELEELEEELEQLENELEAAALEERLKEARL--LLLIAAALLAL-----------LGLGGSLLSLILTIAgvlflvl 283

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1185 -----------RSKAKEEERPQIRGAELEYESLKRQELESENKKLKNElnelrkalseksaPEVTAPGAPAYRVLMEQLT 1253
Cdd:COG4717    284 gllallflllaREKASLGKEAEELQALPALEELEEEELEELLAALGLP-------------PDLSPEELLELLDRIEELQ 350

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1254 SVSEELDVRKEEVLILRSQlvsqkEAIQPKDDKNTMTDSTILLEdvqkmkdKGEIAQAYIGLKETNRLLESQLQSQKRSH 1333
Cdd:COG4717    351 ELLREAEELEEELQLEELE-----QEIAALLAEAGVEDEEELRA-------ALEQAEEYQELKEELEELEEQLEELLGEL 418

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1334 ENEA-----EALRGEIQSLKEENNRQqqllaqnlqlppEARIEAsLQHEITRLTNEnldlMEQLEKqDKTVRKLKKQLKV 1408
Cdd:COG4717    419 EELLealdeEELEEELEELEEELEEL------------EEELEE-LREELAELEAE----LEQLEE-DGELAELLQELEE 480


                   ....*....
gi 1677538261 1409 FAKKIGELE 1417
Cdd:COG4717    481 LKAELRELA 489
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
1129-1270 6.99e-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: 6.99e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1129 EIAEMEDIPSRTEEPSEKKVPLDMSLFLKLQKRVTELEQEKQVMQDELDRKEEQVLR-----SKAKEEERPQIRgAELEY 1203
Cdd:COG2433    389 ELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERlerelSEARSEERREIR-KDREI 467

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1677538261 1204 ESLKR--QELESENKKLKNELNELR------KALSEKSAPEVTAPGAPAYRVLMEQLTSVSEELDVRKEEVLILR 1270
Cdd:COG2433    468 SRLDReiERLERELEEERERIEELKrklerlKELWKLEHSGELVPVKVVEKFTKEAIRRLEEEYGLKEGDVVYLR 542
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
1158-1436 1.16e-05

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 50.40  E-value: 1.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1158 LQKRVTELEQEKQVMQDELDRKEEQVLRSKAKE-----EERPQIRGAELEYESLKRQELESENKKLKNELNELRKALSEK 1232
Cdd:COG3206    173 ARKALEFLEEQLPELRKELEEAEAALEEFRQKNglvdlSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSG 252

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1233 SAPEVTAPGAPAYRVLMEQLTSvseeldvrkeevliLRSQLVSQKEAIQPKDdkntmtdstillEDVQKMKDKgeiaqay 1312
Cdd:COG3206    253 PDALPELLQSPVIQQLRAQLAE--------------LEAELAELSARYTPNH------------PDVIALRAQ------- 299

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1313 igLKETNRLLESQLQSQKRSHENEAEALRGEIQSLKEENNRQQQllaqnlqlppEARIEASLQHEITRLTNEnldlmeql 1392
Cdd:COG3206    300 --IAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEA----------RLAELPELEAELRRLERE-------- 359

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1677538261 1393 ekqdktVRKLKKQLKVFAKKIGELEVGQMENISPGQIIDEPIRP 1436
Cdd:COG3206    360 ------VEVARELYESLLQRLEEARLAEALTVGNVRVIDPAVVP 397
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1156-1397 1.29e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.44  E-value: 1.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1156 LKLQKRVTELEQEKQVMQDELDrKEEQVLRSKAKEEERPQIRGAELEYESlKRQELESENKKLKNELNELRKALSEKSAP 1235
Cdd:TIGR02168  205 LERQAEKAERYKELKAELRELE-LALLVLRLEELREELEELQEELKEAEE-ELEELTAELQELEEKLEELRLEVSELEEE 282

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1236 EVTAPGApayrvlMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQPKDDKNTmTDSTILLEDVQKMKDK-----GEIAQ 1310
Cdd:TIGR02168  283 IEELQKE------LYALANEISRLEQQKQILRERLANLERQLEELEAQLEELE-SKLDELAEELAELEEKleelkEELES 355

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1311 AYIGLKETNRLLEsQLQSQKRSHENEAEALRGEIQSLKEE----NNRQQQLlaqnlqlppEARIEaSLQHEITRLTNENL 1386
Cdd:TIGR02168  356 LEAELEELEAELE-ELESRLEELEEQLETLRSKVAQLELQiaslNNEIERL---------EARLE-RLEDRRERLQQEIE 424

                          250
                   ....*....|.
gi 1677538261 1387 DLMEQLEKQDK 1397
Cdd:TIGR02168  425 ELLKKLEEAEL 435
MyosinXI_CBD cd15475
cargo binding domain of myosin XI; Class XI myosins are a plant specific group, homologous to ...
 1506-1759 1.29e-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: 49.49  E-value: 1.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1506 LTSTINSIKKVlkkrGDDFETVSFWLSNTCRFLhCLKQysgeegfmkhntsrqneHCLTnfdlaeyrqvlsdlAIQIYQQ 1585
Cdd:cd15475     52 IIQTIGSAIED----QDNNDHLAYWLSNTSTLL-FLLQ-----------------RSLP--------------ALLFKQQ 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1586 LVRVLENILqPMI-------VSGMLEhETIQGVSGVKPTGLRKRTSSIADEGTYTL---DSILRQLNSFHSVMCQHGMDP 1655
Cdd:cd15475     96 LTAYVEKIY-GIIrdnlkkeLSPLLS-LCIQAPRTSRGSSSKSSSSANSLGQQSPSshwQSIIKSLNSLLSTLKENHVPP 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1656 ELIKQVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQIRYNVSQLEEWLRDknlmnsgAKET--------LEPLIQAAQLL 1727
Cdd:cd15475    174 FLVQKIFTQVFSFINVQLFNSLLLRRECCSFSNGEYVKAGLAELELWCSQ-------ATEEyagsswdeLKHIRQAVGFL 246

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1677538261 1728 QVKKKTDDDAEAICS-MCNALTTAQIVKVLNLY 1759
Cdd:cd15475    247 VIHQKSRKSYDEITNdLCPVLSVQQLYRICTMY 279
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 959-1402 2.29e-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: 49.58  E-value: 2.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  959 SETEKLRSDLERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEqtrSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQEK 1038
Cdd:TIGR00618  163 KEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQ---LLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQ 239

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1039 EALNH----RIVQQAKEMTETMEKKLVEETKQLE-----LDLNDERLRYQ----NLLNEFSRL-------EERYDDLKEE 1098
Cdd:TIGR00618  240 QSHAYltqkREAQEEQLKKQQLLKQLRARIEELRaqeavLEETQERINRArkaaPLAAHIKAVtqieqqaQRIHTELQSK 319

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1099 MTLMVHVPKPGHKRTDSTHSSNESEYIFSSEIAEMEDIPSRTEEPSEKKVPLDMSL-----FLKLQKRVTELEQEKQVMQ 1173
Cdd:TIGR00618  320 MRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHtltqhIHTLQQQKTTLTQKLQSLC 399

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1174 DELDRKEEQVLRSKAKEEERPQIRG----------AELEYESLKRQELESENKKLKNE---LNELRKALSEKSAPEVTAp 1240
Cdd:TIGR00618  400 KELDILQREQATIDTRTSAFRDLQGqlahakkqqeLQQRYAELCAAAITCTAQCEKLEkihLQESAQSLKEREQQLQTK- 478

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1241 gapayRVLMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQPKddkntMTDSTILLEDVQKMKdkgEIAQAYIGLKETNR 1320
Cdd:TIGR00618  479 -----EQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPA-----RQDIDNPGPLTRRMQ---RGEQTYAQLETSEE 545

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1321 LLESQLQS---QKRSHENEAEALRGEIQSLKEENNRqqqllaqnlqlppearieasLQHEITRLTNENLDLMEQLEKQDK 1397
Cdd:TIGR00618  546 DVYHQLTSerkQRASLKEQMQEIQQSFSILTQCDNR--------------------SKEDIPNLQNITVRLQDLTEKLSE 605


                   ....*
gi 1677538261 1398 TVRKL 1402
Cdd:TIGR00618  606 AEDML 610
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 987-1469 2.65e-05

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 49.25  E-value: 2.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  987 SLQEEIAKLRKDLEQTRSEKKCIeehaDRYKQETEQLVSNLKEENTLLKQEKEALNHRIVQQAKEMTetmekKLVEETKQ 1066
Cdd:TIGR04523   37 QLEKKLKTIKNELKNKEKELKNL----DKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKIN-----KLNSDLSK 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1067 LELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLmvhvpkpghkrtdsthssneseyiFSSEIAEMEDIpsrTEEPSEK 1146
Cdd:TIGR04523  108 INSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDK------------------------FLTEIKKKEKE---LEKLNNK 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1147 kvpldmslFLKLQKRVTELEQEKQVMQDELDRKEEQVLRSK----AKEEERPQIRGAELEYESLKRQ--ELESENKKLKN 1220
Cdd:TIGR04523  161 --------YNDLKKQKEELENELNLLEKEKLNIQKNIDKIKnkllKLELLLSNLKKKIQKNKSLESQisELKKQNNQLKD 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1221 ELNELRKALSEKSAPEVTApgapayrvlMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIqpKDDKNTMTDSTILLEDVQ 1300
Cdd:TIGR04523  233 NIEKKQQEINEKTTEISNT---------QTQLNQLKDEQNKIKKQLSEKQKELEQNNKKI--KELEKQLNQLKSEISDLN 301

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1301 KMKDKgeiaqayiglkETNRLLESQLQSQKRSHENEAEALRGEIQSLKEENNRQqqllaqnlqlppearieASLQHEITR 1380
Cdd:TIGR04523  302 NQKEQ-----------DWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQI-----------------SQLKKELTN 353

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1381 LTNENLDLMEQLEKQDKTVRKLKKQ-------LKVFAKKIGELEVGQMENISPGQIIDEpirpvNIPRKEKDFQgmleyK 1453
Cdd:TIGR04523  354 SESENSEKQRELEEKQNEIEKLKKEnqsykqeIKNLESQINDLESKIQNQEKLNQQKDE-----QIKKLQQEKE-----L 423

                          490
                   ....*....|....*.
gi 1677538261 1454 KEDEQKLVKNLILELK 1469
Cdd:TIGR04523  424 LEKEIERLKETIIKNN 439
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
972-1269 2.99e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 48.36  E-value: 2.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  972 QLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQEKEALNHRI--VQQA 1049
Cdd:COG4372     27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQeeLESL 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1050 KEMTETMEKKLVE---ETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLM---VHVPKPGHKRTDSTHSSNESE 1123
Cdd:COG4372    107 QEEAEELQEELEElqkERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLqeeLAALEQELQALSEAEAEQALD 186

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1124 YIFSSEIAEMEDIPSRTEEPSEKKVPLDMSLFLKLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEERPQIRGAELEY 1203
Cdd:COG4372    187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1677538261 1204 ESLKRQELESENKKLKNELNELRKALSEKSAPEVTAPGAPAYRVLMEQLTSVSEELDVRKEEVLIL 1269
Cdd:COG4372    267 ILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELAL 332
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 897-1234 3.03e-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: 3.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  897 RRMMAKRELKKLKIEARSVERYKKlhiGMENKIMQLQRKVD---EQNKDYKCLVE------KLTNLEGIYNSETEKLRSD 967
Cdd:TIGR00606  320 ELVDCQRELEKLNKERRLLNQEKT---ELLVEQGRLQLQADrhqEHIRARDSLIQslatrlELDGFERGPFSERQIKNFH 396

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  968 LERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLLkQEKEALNHRIVQ 1047
Cdd:TIGR00606  397 TLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKEL-QQLEGSSDRILE 475

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1048 QAKEMTETM-------EKKLVEETKQLELDLNDERLryqNLLNEFSRLEERYDDLKEEMTLMVHVPKPGHKRTDSTHSSN 1120
Cdd:TIGR00606  476 LDQELRKAErelskaeKNSLTETLKKEVKSLQNEKA---DLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIR 552

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1121 ESEYIFSSE-IAEMEDIP-----SRTEEPSEKKVPLDMSLFLKLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKeeerp 1194
Cdd:TIGR00606  553 KIKSRHSDElTSLLGYFPnkkqlEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDK----- 627

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 1677538261 1195 qirgaelEYESLKRQELESENKKLKNELNELRKALSEKSA 1234
Cdd:TIGR00606  628 -------LFDVCGSQDEESDLERLKEEIEKSSKQRAMLAG 660
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
902-1231 3.35e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.91  E-value: 3.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  902 KRELKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLVEKLTNLEGIYNSETEKLRSDLERLQLSEEEAKva 981
Cdd:PRK03918   451 KELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYE-- 528

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  982 tgrvlSLQEEIAKLRKDLEQTRSEKKCIEEhadrYKQETEQLVSNLKEentlLKQEKEALNHRIVQQAKEMTETMEKKLv 1061
Cdd:PRK03918   529 -----KLKEKLIKLKGEIKSLKKELEKLEE----LKKKLAELEKKLDE----LEEELAELLKELEELGFESVEELEERL- 594

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1062 eetKQLElDLNDERLRYQNLLNEFSRLEERYDDLKEEMTlmvhvpkpgHKRTDSTHSSNESEYIfSSEIAEMEDI--PSR 1139
Cdd:PRK03918   595 ---KELE-PFYNEYLELKDAEKELEREEKELKKLEEELD---------KAFEELAETEKRLEEL-RKELEELEKKysEEE 660

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1140 TEEPSEKKVPLDMSLFlKLQKRVTELEQEKQVMQDELDRKEEQvlrskaKEEerpqIRGAELEYESLKR-----QELESE 1214
Cdd:PRK03918   661 YEELREEYLELSRELA-GLRAELEELEKRREEIKKTLEKLKEE------LEE----REKAKKELEKLEKalervEELREK 729

                          330
                   ....*....|....*..
gi 1677538261 1215 NKKLKNELNElrKALSE 1231
Cdd:PRK03918   730 VKKYKALLKE--RALSK 744
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 904-1199 3.99e-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: 3.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  904 ELKKLKI------EARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLVEKLTN----LEGIYN----------SETEK 963
Cdd:pfam15921  631 ELEKVKLvnagseRLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNkseeMETTTNklkmqlksaqSELEQ 710

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  964 LRSDLERLQLSEEEA-KVATGrvlsLQEEIAKLRKDLEQTRSEKKCIEEhadrykqeteqLVSNLKEENTLLKQEKEALN 1042
Cdd:pfam15921  711 TRNTLKSMEGSDGHAmKVAMG----MQKQITAKRGQIDALQSKIQFLEE-----------AMTNANKEKHFLKEEKNKLS 775

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1043 HRIVQQAK---------EMTETMEKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMV-HVPKPGHkr 1112
Cdd:pfam15921  776 QELSTVATeknkmagelEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQHTLDVkELQGPGY-- 853

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1113 tdSTHSSNESEYIFSSEIAEME-DIPSRTEEPSekkvpldmslFLKLQKRVTELEQE------KQVMQD--ELDRKEEQV 1183
Cdd:pfam15921  854 --TSNSSMKPRLLQPASFTRTHsNVPSSQSTAS----------FLSHHSRKTNALKEdptrdlKQLLQElrSVINEEPTV 921

                          330
                   ....*....|....*.
gi 1677538261 1184 LRSKAKEEERPQIRGA 1199
Cdd:pfam15921  922 QLSKAEDKGRAPSLGA 937
Caldesmon pfam02029
Caldesmon;
959-1232 5.36e-05

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 47.94  E-value: 5.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  959 SETEKLRSDLERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADR------------YKQETEQLVSN 1026
Cdd:pfam02029   50 LKPSGQGGLDEEEAFLDRTAKREERRQKRLQEALERQKEFDPTIADEKESVAERKENneeeensswekeEKRDSRLGRYK 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1027 LKEENTLLKQEKEALNHRIVQQAKEMTETMEKKLVEETKQLELDLNDERLRYQNLLNEfsrLEERYDDLK---------- 1096
Cdd:pfam02029  130 EEETEIREKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKE---KKVKYESKVfldqkrghpe 206

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1097 ---EEMTLMVHVPKPGHKRTDSTHSSNESEYIFSSEIAE----MEDIP-SRTEEPSEKKVPLDMslflKLQKRVTELEqe 1168
Cdd:pfam02029  207 vksQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEaeqkLEELRrRRQEKESEEFEKLRQ----KQQEAELELE-- 280

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1677538261 1169 kqvmqdELDRKEEQvlRSKAKEEERPQiRGAEleyESLKRQELESENKKLKNELNELRKALSEK 1232
Cdd:pfam02029  281 ------ELKKKREE--RRKLLEEEEQR-RKQE---EAERKLREEEEKRRMKEEIERRRAEAAEK 332
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
 815-835 5.89e-05

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 459869  Cd Length: 21  Bit Score: 41.53  E-value: 5.89e-05
                           10        20
                   ....*....|....*....|.
gi 1677538261  815 TKAATIIQKYWRMYVVRRRYK 835
Cdd:pfam00612    1 RKAAIKIQAAWRGYLARKRYK 21
FPP pfam05911
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ...
 923-1099 6.29e-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: 6.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  923 IGMENKIMqlqrKVDEQNKdYKCLVEKLTNLEGIYnSETEKLRSDLERLQlseeEAKVATGRVLSLQEEIAKLRKDLEQT 1002
Cdd:pfam05911  624 SSMEDEIK----KHDCIDK-VTLSENKVAQVDNGC-SEIDNLSSDPEIPS----DGPLVSGSNDLKTEENKRLKEEFEQL 693

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1003 RSEKKCIEEHADRYK----------QETEQLVSNLKEENTLLKQEKEALNHRIVQQAkEMTETMEKKLVEetkqLELDLN 1072
Cdd:pfam05911  694 KSEKENLEVELASCTenlestksqlQESEQLIAELRSELASLKESNSLAETQLKCMA-ESYEDLETRLTE----LEAELN 768

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1677538261 1073 DERLRYQNLLNEFS-------RLEERYDDLKEEM 1099
Cdd:pfam05911  769 ELRQKFEALEVELEeekncheELEAKCLELQEQL 802
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 926-1416 6.65e-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: 48.04  E-value: 6.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  926 ENKIMQLQRKVD---EQNKDYKCLVEKLTNLEGiyNSETEKLRSDLERLQLSeeeakVATGRVLSLQEEIAKLRKDLEQT 1002
Cdd:TIGR00618  378 TQHIHTLQQQKTtltQKLQSLCKELDILQREQA--TIDTRTSAFRDLQGQLA-----HAKKQQELQQRYAELCAAAITCT 450

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1003 RSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQEKEalNHRIVQQAKEMTETMEKKLVEETKQLELDLNDERL------ 1076
Cdd:TIGR00618  451 AQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETR--KKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNpgpltr 528

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1077 RYQNLLNEFSRLEERYDDLKEEMTlmvHVPKPGHKRTDSTHSSNESEYIFSSEIAEM-EDIPSRTEEPSEKKVPLDMSLF 1155
Cdd:TIGR00618  529 RMQRGEQTYAQLETSEEDVYHQLT---SERKQRASLKEQMQEIQQSFSILTQCDNRSkEDIPNLQNITVRLQDLTEKLSE 605

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1156 LKLQKRVT--ELEQEKQVMQDELDRKEEQvlRSKAKEEERPQIRGAELEYESLKRQELES-------ENKKLKNELNELR 1226
Cdd:TIGR00618  606 AEDMLACEqhALLRKLQPEQDLQDVRLHL--QQCSQELALKLTALHALQLTLTQERVREHalsirvlPKELLASRQLALQ 683

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1227 KALSEKSAPEVTAPGAPAYRVLMEQLTSVSEELDVRKEEvliLRSQLVSQKEAIQPKDDkntmtdstiLLEDVqkmkdkg 1306
Cdd:TIGR00618  684 KMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNE---IENASSSLGSDLAARED---------ALNQS------- 744

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1307 eiaqayigLKETNRLLESQLQSQKRSHENEAEALRGEIQSLKEENNRQQQLLAQNLQLPPEARIEASLQHEITRLTNENL 1386
Cdd:TIGR00618  745 --------LKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDE 816

                          490       500       510
                   ....*....|....*....|....*....|.
gi 1677538261 1387 DLME-QLEKQDKTVRKLKKQLKVFAKKIGEL 1416
Cdd:TIGR00618  817 DILNlQCETLVQEEEQFLSRLEEKSATLGEI 847
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
905-1100 6.87e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.75  E-value: 6.87e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  905 LKKLKIEARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLVEKLTNLEGIyNSETEKLRSDLERLQ--LSEEEAKVAT 982
Cdd:PRK03918   587 VEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAET-EKRLEELRKELEELEkkYSEEEYEELR 665

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  983 GRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRykqeteqlvsnlkeentlLKQEKEALnhrivQQAKEMTETMEKKLVE 1062
Cdd:PRK03918   666 EEYLELSRELAGLRAELEELEKRREEIKKTLEK------------------LKEELEER-----EKAKKELEKLEKALER 722

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1677538261 1063 ETkqlelDLNDERLRYQNLLNE--FSRLEERYDDLKEEMT 1100
Cdd:PRK03918   723 VE-----ELREKVKKYKALLKEraLSKVGEIASEIFEELT 757
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
957-1099 9.42e-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: 9.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  957 YNSETEKLRSDLERLQL-------------SEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQL 1023
Cdd:COG3206    180 LEEQLPELRKELEEAEAaleefrqknglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL 259

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1024 -----VSNLKEENTLLKQEKEAL------NHRIVQQAKEMTETMEKKLVEETKQLELDLNDERLRYQNLLNEfsrLEERY 1092
Cdd:COG3206    260 lqspvIQQLRAQLAELEAELAELsarytpNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREAS---LQAQL 336


                   ....*..
gi 1677538261 1093 DDLKEEM 1099
Cdd:COG3206    337 AQLEARL 343
PTZ00121 PTZ00121
MAEBL; Provisional
 904-1290 9.56e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.83  E-value: 9.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  904 ELKKLKIEARSVERYKKLhiGMENKIMQLQRKVDEQNKdykclVEKLTNLEGIYNSETEKLRSDL---ERLQLSEEEAKV 980
Cdd:PTZ00121  1494 EAKKKADEAKKAAEAKKK--ADEAKKAEEAKKADEAKK-----AEEAKKADEAKKAEEKKKADELkkaEELKKAEEKKKA 1566

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  981 ATGRVLSLQEEIAkLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNL-KEENTLLKQE---KEALNHRIVQQAKEMTETm 1056
Cdd:PTZ00121  1567 EEAKKAEEDKNMA-LRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAkKAEEAKIKAEelkKAEEEKKKVEQLKKKEAE- 1644

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1057 EKKLVEETKQLEldlNDERLRYQNLLNEFSRLEERYDDLKEEMTLMVHVPKPGHKRTDSTHSSNESEYIFSSEIAEMEDI 1136
Cdd:PTZ00121  1645 EKKKAEELKKAE---EENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEEL 1721

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1137 psRTEEPSEKkvpldmslfLKLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEERPQIRGAELEYESLKRQELESENK 1216
Cdd:PTZ00121  1722 --KKAEEENK---------IKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDE 1790

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1677538261 1217 KLKNELNELRKALSEKSA--PEVTAPGAPAYRVLMEQLTSVSEELDVRKEevlilrSQLVSQKEAIQPKDDKNTMT 1290
Cdd:PTZ00121  1791 KRRMEVDKKIKDIFDNFAniIEGGKEGNLVINDSKEMEDSAIKEVADSKN------MQLEEADAFEKHKFNKNNEN 1860
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 926-1098 1.44e-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: 1.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  926 ENKIMQLQRKVDEQNKDYKCLVEKLTNLEGIYNSETEKLRSDLERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSE 1005
Cdd:COG4942     26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1006 kkcIEEH------------------------ADRYKQETEQLVSNLKEENTLLKQEKEALNHRIVQQAKEMT--ETMEKK 1059
Cdd:COG4942    106 ---LAELlralyrlgrqpplalllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAelEALLAE 182

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1677538261 1060 LVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEE 1098
Cdd:COG4942    183 LEEERAALEALKAERQKLLARLEKELAELAAELAELQQE 221
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 929-1203 1.62e-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: 1.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  929 IMQLQRKVDEQNKDYKCLVEKLTNLEGI--YNSETEKLRSDLERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEK 1006
Cdd:TIGR00606  794 MERFQMELKDVERKIAQQAAKLQGSDLDrtVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEK 873

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1007 KCIEEHADRYKQETEQLVSNLKEENTLLKQEKEALNHRI-VQQAKEMTETMEKKLV----EETKQLELDLNDERLRYQNL 1081
Cdd:TIGR00606  874 LQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSpLETFLEKDQQEKEELIsskeTSNKKAQDKVNDIKEKVKNI 953

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1082 LNEFSRLEERYDDLKEEM---------TLMVHVPK-PGHKRTDSTHSSNESEYIFSSEIAE---MEDIPSRTEEPSEKKV 1148
Cdd:TIGR00606  954 HGYMKDIENKIQDGKDDYlkqketelnTVNAQLEEcEKHQEKINEDMRLMRQDIDTQKIQErwlQDNLTLRKRENELKEV 1033

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1677538261 1149 PLDMSLFLKL--QKRVTELEQEKQVMQDELD--------------RKEEQVLRSKAKEEErPQIRGAELEY 1203
Cdd:TIGR00606 1034 EEELKQHLKEmgQMQVLQMKQEHQKLEENIDlikrnhvlalgrqkGYEKEIKHFKKELRE-PQFRDAEEKY 1103
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 948-1417 1.93e-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: 46.50  E-value: 1.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  948 EKLTNLEGIYNSETEKLRSDLERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNL 1027
Cdd:TIGR00618  389 TTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSL 468

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1028 KEENTLLKQ-----EKEALNHRIVQQAKEMTETMEKKLVEETKQLELDLNDERL------RYQNLLNEFSRLEERYDD-- 1094
Cdd:TIGR00618  469 KEREQQLQTkeqihLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNpgpltrRMQRGEQTYAQLETSEEDvy 548

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1095 ------------LKEEMTLMVH-VPKPGHKRTDSTHS----SNESEYIFSSEIAEMEDIPSRTEEPSEKKVPL-----DM 1152
Cdd:TIGR00618  549 hqltserkqrasLKEQMQEIQQsFSILTQCDNRSKEDipnlQNITVRLQDLTEKLSEAEDMLACEQHALLRKLqpeqdLQ 628

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1153 SLFLKLQKRVTELEQEKQVMQDEL-----DRKEEQVLRSKAKEEERPQIRGAELEYESLKRQELESEnkklKNELNELRK 1227
Cdd:TIGR00618  629 DVRLHLQQCSQELALKLTALHALQltltqERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYW----KEMLAQCQT 704

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1228 ALSEKSAPEVTapgapaYRVLMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQPK-------DDKNTMTDSTILLEDVQ 1300
Cdd:TIGR00618  705 LLRELETHIEE------YDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTvlkarteAHFNNNEEVTAALQTGA 778

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1301 KMKDKGEIAQAYIGLKETNRLLESQLQSQKRSH--ENEAEALRGEIQSLKEENNRQQQLlaqnlqlppeaRIEASLQHEI 1378
Cdd:TIGR00618  779 ELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEipSDEDILNLQCETLVQEEEQFLSRL-----------EEKSATLGEI 847

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 1677538261 1379 TRLT---NENLDLMEQLEKQDKTVRKLKKQLKVFAKKIGELE 1417
Cdd:TIGR00618  848 THQLlkyEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFD 889
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
 809-839 2.37e-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: 2.37e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1677538261  809 AKFLRRTKAATIIQKYWRMYVVRRRYKIRRA 839
Cdd:cd23767      3 EELQRMNRAATLIQALWRGYKVRKELKKKKK 33
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 910-1445 2.47e-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: 46.19  E-value: 2.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  910 IEARSVERYKKLHIGMENKIMQLQRKVDEQNKDYKCLV-EKLTNLEGIYNSETEKLRS---DLERLQLSEEEAKVATGRV 985
Cdd:TIGR00606  185 IKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIrDQITSKEAQLESSREIVKSyenELDPLKNRLKEIEHNLSKI 264

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  986 LSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQEKEA----LNHRIVQQAKEMTETMEKKLV 1061
Cdd:TIGR00606  265 MKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERelvdCQRELEKLNKERRLLNQEKTE 344

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1062 EETKQLELDLNDERLRYQNLLNEFSRLE----------ERYDDLKEEMTLMVHVPKPGHKRTDSTHSSNESEYIFSSEIA 1131
Cdd:TIGR00606  345 LLVEQGRLQLQADRHQEHIRARDSLIQSlatrleldgfERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLK 424

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1132 EmedipSRTEEPSEKKVPLDMSLFLK---LQKRVTELEQEKQVMQ------DELDRKEEQVLRSKA---KEEERPQIRGA 1199
Cdd:TIGR00606  425 Q-----EQADEIRDEKKGLGRTIELKkeiLEKKQEELKFVIKELQqlegssDRILELDQELRKAERelsKAEKNSLTETL 499

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1200 ELEYESLKRQELESENK--KLKNELNEL-RKALSEKSAPEVTAPGAPAYRVLMEQLTSVSEELdVRKEEVLILRSQLvsQ 1276
Cdd:TIGR00606  500 KKEVKSLQNEKADLDRKlrKLDQEMEQLnHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDEL-TSLLGYFPNKKQL--E 576

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1277 KEAIQPKDDKNTMTDStilLEDVQKMKDKGEIAQAYIglketNRLLESQLQSQKRSHENEAEALRGEIQSLKEENNRQQQ 1356
Cdd:TIGR00606  577 DWLHSKSKEINQTRDR---LAKLNKELASLEQNKNHI-----NNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEI 648

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1357 LLAQNLQLPPEARIEASLQHeITRLTNEN------LDLMEQLEKQ-DKTVRKLKKQLKVFAKKIGELE--VGQMENISPG 1427
Cdd:TIGR00606  649 EKSSKQRAMLAGATAVYSQF-ITQLTDENqsccpvCQRVFQTEAElQEFISDLQSKLRLAPDKLKSTEseLKKKEKRRDE 727

                          570
                   ....*....|....*...
gi 1677538261 1428 QIIDEPIRPVNIPRKEKD 1445
Cdd:TIGR00606  728 MLGLAPGRQSIIDLKEKE 745
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 960-1098 5.35e-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: 5.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  960 ETEKLRSDLERL-----QLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRsekkcieehadRYKQETEQLVSNLKEENTLL 1034
Cdd:pfam08614   22 ENAKLQSEPESVlpstsSSKLSKASPQSASIQSLEQLLAQLREELAELY-----------RSRGELAQRLVDLNEELQEL 90

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1035 KQEKEALNHRI------VQQAKEMTETMEKKLVEETKQLElDLNDErlrYQNLLNEFSRLEERYDDLKEE 1098
Cdd:pfam08614   91 EKKLREDERRLaaleaeRAQLEEKLKDREEELREKRKLNQ-DLQDE---LVALQLQLNMAEEKLRKLEKE 156
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 906-1406 6.54e-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: 44.78  E-value: 6.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  906 KKLKIEARSVE-RYKKlhigMENKIMQLQRKVDEQNKDYKCLVEKLTNLEGIYNSETEKLRSdLERLQLSEE----EAKV 980
Cdd:pfam01576  120 QKLQLEKVTTEaKIKK----LEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKS-LSKLKNKHEamisDLEE 194

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  981 ATGRVLSLQEEIAKLRKDLEQTRSEKKciEEHADRYKQETEQLVSNLKEEntllkQEKEALNHRIVQQAKEMTETMEK-- 1058
Cdd:pfam01576  195 RLKKEEKGRQELEKAKRKLEGESTDLQ--EQIAELQAQIAELRAQLAKKE-----EELQAALARLEEETAQKNNALKKir 267

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1059 KLVEETKQLELDLNDERLRYqnllnefSRLEERYDDLKEEMTLMvhvpkpghkRTdsthssneseyifsseiaEMEDIPS 1138
Cdd:pfam01576  268 ELEAQISELQEDLESERAAR-------NKAEKQRRDLGEELEAL---------KT------------------ELEDTLD 313

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1139 RTEEPSEKKvpldmslflklQKRVTELEQEKQVMQDELDRKEEQV--LRSK---AKEEERPQIRGAELEYESLK--RQEL 1211
Cdd:pfam01576  314 TTAAQQELR-----------SKREQEVTELKKALEEETRSHEAQLqeMRQKhtqALEELTEQLEQAKRNKANLEkaKQAL 382

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1212 ESENKKLKNELNELRKALSEKSAPEVTAPGapayrvlmeQLtsvsEELDVRKEEVLILRSQLVSQKEAIQpkddkNTMTD 1291
Cdd:pfam01576  383 ESENAELQAELRTLQQAKQDSEHKRKKLEG---------QL----QELQARLSESERQRAELAEKLSKLQ-----SELES 444

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1292 STILLEDVQK--MKDKGEIAQayiglketnrlLESQLQsqkrsheneaealrgEIQSLKEEnnrqqqllaqnlqlppEAR 1369
Cdd:pfam01576  445 VSSLLNEAEGknIKLSKDVSS-----------LESQLQ---------------DTQELLQE----------------ETR 482

                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 1677538261 1370 IEASLQHEITRLTNENLDLMEQLEKQDKTVRKLKKQL 1406
Cdd:pfam01576  483 QKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQL 519
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 1157-1428 6.82e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.05  E-value: 6.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1157 KLQKRVTELEQEKQVMQDELDRKEEQVlrSKAKEEerpqIRGAELEYESLKRQ--ELESENKKLKNELNELRKALSEK-S 1233
Cdd:COG3883     20 AKQKELSELQAELEAAQAELDALQAEL--EELNEE----YNELQAELEALQAEidKLQAEIAEAEAEIEERREELGERaR 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1234 APEVTAPGAPAYRVLMEQlTSVSEELDvrkeevlilRSQLVSQkeaIQPKDDKntmtdstiLLEDVQKMKDKgeiaqayi 1313
Cdd:COG3883     94 ALYRSGGSVSYLDVLLGS-ESFSDFLD---------RLSALSK---IADADAD--------LLEELKADKAE-------- 144

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1314 gLKETNRLLESQLQSQKRShENEAEALRGEIQSLKEENNRQQqllaqnlqlppearieASLQHEITRLTNENLDLMEQLE 1393
Cdd:COG3883    145 -LEAKKAELEAKLAELEAL-KAELEAAKAELEAQQAEQEALL----------------AQLSAEEAAAEAQLAELEAELA 206

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1677538261 1394 KQDKTVRKLKKQLKVFAKKIGELEVGQMENISPGQ 1428
Cdd:COG3883    207 AAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1174-1416 8.10e-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: 44.67  E-value: 8.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1174 DELDRKEEQVLRSKAKEEERPQIRGAELEYESLKRQELESEnkklKNELNELRKALSEKSAPEVTAPgAPAYRVLMEQLT 1253
Cdd:TIGR02169  166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRE----REKAERYQALLKEKREYEGYEL-LKEKEALERQKE 240

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1254 SVSEELDvRKEEVLILRSQLVSQKEAiqpkddknTMTDSTILLEDV-QKMKDKGEiaQAYIGLKETNRLLESQLQSQKRS 1332
Cdd:TIGR02169  241 AIERQLA-SLEEELEKLTEEISELEK--------RLEEIEQLLEELnKKIKDLGE--EEQLRVKEKIGELEAEIASLERS 309

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1333 ---HENEAEALRGEIQSLKEENNRQQQLLAQNLQLPPEARIE-ASLQHEITRLTNENLDLMEQLEKQDKTVRKLKKQLKV 1408
Cdd:TIGR02169  310 iaeKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRrDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD 389


                   ....*...
gi 1677538261 1409 FAKKIGEL 1416
Cdd:TIGR02169  390 YREKLEKL 397
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 925-1095 9.91e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 42.60  E-value: 9.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  925 MENKIMQLQRKVDEQNKDYKCLVEKLTNLEgiynSETEKLRSDLERLQlsEEEAKVATGRVL-SLQEEIAKLRKDLEQTR 1003
Cdd:COG1579     36 LEDELAALEARLEAAKTELEDLEKEIKRLE----LEIEEVEARIKKYE--EQLGNVRNNKEYeALQKEIESLKRRISDLE 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1004 SEKKCIEEHADRYKQETEQLVSNLKEENTLLKQEKEALNHRIVQQAKEmtetmEKKLVEETKQLELDLNDErlryqnLLN 1083
Cdd:COG1579    110 DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE-----LEELEAEREELAAKIPPE------LLA 178

                          170
                   ....*....|..
gi 1677538261 1084 EFSRLEERYDDL 1095
Cdd:COG1579    179 LYERIRKRKNGL 190
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 926-1098 9.98e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 43.67  E-value: 9.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  926 ENKIMQLQRKVDEQNKDYKCLVEKLTNLegiyNSETEKLRSDLERLQlseeeAKVATgrvlsLQEEIAKLRKDLEQTRSE 1005
Cdd:COG3883     15 DPQIQAKQKELSELQAELEAAQAELDAL----QAELEELNEEYNELQ-----AELEA-----LQAEIDKLQAEIAEAEAE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1006 kkcIEEHADRYKQ----------------------ETEQLVSNLKEENTLLKQEKEALNHriVQQAKEMTETMEKKLVEE 1063
Cdd:COG3883     81 ---IEERREELGEraralyrsggsvsyldvllgseSFSDFLDRLSALSKIADADADLLEE--LKADKAELEAKKAELEAK 155

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1677538261 1064 TKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEE 1098
Cdd:COG3883    156 LAELEALKAELEAAKAELEAQQAEQEALLAQLSAE 190
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1159-1412 1.01e-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: 43.60  E-value: 1.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1159 QKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEErpqirgAELEYESLKRQ--ELESENKKLKNELNELRKALSEksape 1236
Cdd:COG4942     19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKA------LLKQLAALERRiaALARRIRALEQELAALEAELAE----- 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1237 vtapgapayrvLMEQLTSVSEELDVRKEEvliLRSQLVS-QKEAIQPK-------DDKNTMTDSTILLEDVqkMKDKGEI 1308
Cdd:COG4942     88 -----------LEKEIAELRAELEAQKEE---LAELLRAlYRLGRQPPlalllspEDFLDAVRRLQYLKYL--APARREQ 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1309 AQAYIGLKETNRLLESQLQSQKRSHENEAEALRGEIQSLKEENNRQQqllaqnlqlppeaRIEASLQHEITRLTNENLDL 1388
Cdd:COG4942    152 AEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQ-------------KLLARLEKELAELAAELAEL 218

                          250       260
                   ....*....|....*....|....
gi 1677538261 1389 MEQLEKQDKTVRKLKKQLKVFAKK 1412
Cdd:COG4942    219 QQEAEELEALIARLEAEAAAAAER 242
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 960-1225 1.03e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 44.01  E-value: 1.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  960 ETEKLRSDLERLQLSEEEAKVATGR-VLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLkEENTLLKQEK 1038
Cdd:pfam01576  493 QLEDERNSLQEQLEEEEEAKRNVERqLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQL-EEKAAAYDKL 571

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1039 EALNHRIVQQAKEMTETM--EKKLVE--ETKQLELD--LNDERLRYQNLLNEFSRLEErydDLKEEMTLMVHVpkpGHKR 1112
Cdd:pfam01576  572 EKTKNRLQQELDDLLVDLdhQRQLVSnlEKKQKKFDqmLAEEKAISARYAEERDRAEA---EAREKETRALSL---ARAL 645

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1113 TDSTHSSNESEYIFSSEIAEMEDIPSRTE---------EPSEKKVPLDMSlflKLQKRVTELEQEKQVMQDELDRKEEQV 1183
Cdd:pfam01576  646 EEALEAKEELERTNKQLRAEMEDLVSSKDdvgknvhelERSKRALEQQVE---EMKTQLEELEDELQATEDAKLRLEVNM 722

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1184 LRSKAK------------EEERPQIRG------AELEYESLKRQELESENKKLKNELNEL 1225
Cdd:pfam01576  723 QALKAQferdlqardeqgEEKRRQLVKqvreleAELEDERKQRAQAVAAKKKLELDLKEL 782
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 987-1104 1.20e-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: 1.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  987 SLQEEIAKLRKDleqtrsekkciEEHADRYKQETEQLVSNLKEENTLLKQEKEALNHRIVQQAKEMTETMEKKlvEETKQ 1066
Cdd:pfam13851   30 SLKEEIAELKKK-----------EERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENYEKDKQSLKNLK--ARLKV 96

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1677538261 1067 LELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMVH 1104
Cdd:pfam13851   97 LEKELKDLKWEHEVLEQRFEKVERERDELYDKFEAAIQ 134
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
960-1238 1.33e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.88  E-value: 1.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  960 ETEKLRSDLERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSnLKEENTLLkqEKE 1039
Cdd:PRK02224   476 RVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEE-LRERAAEL--EAE 552

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1040 ALNHRivQQAKEMTETMEKKLvEETKQLELDL--NDERL----RYQNLLNEFSRLEERYDDLKEemtlmvhvpkpghKRt 1113
Cdd:PRK02224   553 AEEKR--EAAAEAEEEAEEAR-EEVAELNSKLaeLKERIesleRIRTLLAAIADAEDEIERLRE-------------KR- 615

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1114 dsthssneseyifsSEIAEMEDIP-SRTEEPSEKKVPLDMSLflkLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEE 1192
Cdd:PRK02224   616 --------------EALAELNDERrERLAEKRERKRELEAEF---DEARIEEAREDKERAEEYLEQVEEKLDELREERDD 678

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1677538261 1193 -RPQIRGAELEYESLKrqELESENKKLKNELNELRKALSEKSAPEVT 1238
Cdd:PRK02224   679 lQAEIGAVENELEELE--ELRERREALENRVEALEALYDEAEELESM 723
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
958-1212 1.38e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.97  E-value: 1.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  958 NSETEKLRSDLER----LQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQlvsnLKEENTL 1033
Cdd:COG4372     51 REELEQAREELEQleeeLEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE----LQKERQD 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1034 LKQEKEALNHRIVQQAKEMTETMEKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMVHVPKPGHKRT 1113
Cdd:COG4372    127 LEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAE 206

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1114 DSTHSSNESEYIFSSEIAEM-EDIPSRTEEPSEKKVPLDMSLFLKLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKEEE 1192
Cdd:COG4372    207 KLIESLPRELAEELLEAKDSlEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELE 286

                          250       260
                   ....*....|....*....|
gi 1677538261 1193 RPQIRGAELEYESLKRQELE 1212
Cdd:COG4372    287 ALEEAALELKLLALLLNLAA 306
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1158-1348 1.48e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 1.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1158 LQKRVTELEQEKQVMQDELDRKEEQvlrskaKEEERPQIRGAELEYESLKRQELESenkkLKNELNELRKALSEKSApev 1237
Cdd:COG4913    293 LEAELEELRAELARLEAELERLEAR------LDALREELDELEAQIRGNGGDRLEQ----LEREIERLERELEERER--- 359

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1238 tapgapAYRVLMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQpkddkntmtdstilledvqkmkdkgeiaqayiGLKE 1317
Cdd:COG4913    360 ------RRARLEALLAALGLPLPASAEEFAALRAEAAALLEALE--------------------------------EELE 401

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1677538261 1318 TNRLLESQLQSQKRSHENEAEALRGEIQSLK 1348
Cdd:COG4913    402 ALEEALAEAEAALRDLRRELRELEAEIASLE 432
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 969-1109 1.57e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 43.28  E-value: 1.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  969 ERLQLSE---EEAK-VATGRVLSLQEEIAKL---RKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKE--ENTLLKQEKE 1039
Cdd:PRK00409   495 KRLGLPEniiEEAKkLIGEDKEKLNELIASLeelERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEeeDKLLEEAEKE 574

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1677538261 1040 AlnHRIVQQAKEMTETMEKKLVEETKQLELDLNDerlryQNLLNEFSRLEERYDDLKE---EMTLMVHVPKPG 1109
Cdd:PRK00409   575 A--QQAIKEAKKEADEIIKELRQLQKGGYASVKA-----HELIEARKRLNKANEKKEKkkkKQKEKQEELKVG 640
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 962-1098 1.60e-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: 43.07  E-value: 1.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  962 EKLRSDLER--------LQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQlvsnlkeentL 1033
Cdd:pfam05262  184 EALREDNEKgvnfrrdmTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQ----------K 253

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1677538261 1034 LKQEKEALNHRIVQQAKEMTETMEKKLVE-ETKQLELDLNDERLRYQNllnefsrlEERYDDLKEE 1098
Cdd:pfam05262  254 QQEAKNLPKPADTSSPKEDKQVAENQKREiEKAQIEIKKNDEEALKAK--------DHKAFDLKQE 311
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
932-1091 1.84e-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: 1.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  932 LQRKVDEQNKDYKCLVEKLTNLEgiynSETEKLRSDLERLQlsEEEAKVATGRVLSLQEEIAKLRKDLEQtrsekkcIEE 1011
Cdd:COG4913    293 LEAELEELRAELARLEAELERLE----ARLDALREELDELE--AQIRGNGGDRLEQLEREIERLERELEE-------RER 359

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1012 HADRYkqetEQLVSNLKEENTLLKQEKEALnHRIVQQAKEMTETMEKKLVEETKQLELDLNDERLRYQNLLNEFSRLEER 1091
Cdd:COG4913    360 RRARL----EALLAALGLPLPASAEEFAAL-RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 788-810 1.91e-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: 1.91e-03
                            10        20
                    ....*....|....*....|...
gi 1677538261   788 RMRKAAITMQRYVRGYQARCYAK 810
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRYK 23
Paralemmin pfam03285
Paralemmin;
1160-1282 2.00e-03

Paralemmin;


Pssm-ID: 460875  Cd Length: 301  Bit Score: 42.42  E-value: 2.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1160 KRVTELEQEKQvmQDELDRKEEQVLRSKAKEE----ERPQIRGAElEYESLKRQELESENKK---------LKNELNELR 1226
Cdd:pfam03285    5 KRQTEIENKRR--QLEDDRRQLQHLKSKALRErwllEGPPSSASE-EDEARRRQEEEDEQKKklleeiirrLEEEIELLE 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1677538261 1227 KALSEKSAPEvtapgapayrVLMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQP 1282
Cdd:pfam03285   82 EESSISAKKE----------NLAEKLLEITVEKDKVTGETRVLSSTTLLPDDVQPQ 127
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 765-786 2.10e-03

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


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 36.92  E-value: 2.10e-03
                            10        20
                    ....*....|....*....|..
gi 1677538261   765 KLRAACIRIQKTIRGWLLRKKY 786
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRY 22
PRK12704 PRK12704
phosphodiesterase; Provisional
 971-1104 2.62e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.46  E-value: 2.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  971 LQLSEEEAKVATG-RVLSLQEEIAKLRKDLEQTRSEKkciEEHADRYKQETEQLVSNLKEENTLLKQEKEALNHRIVQQA 1049
Cdd:PRK12704    44 LEEAKKEAEAIKKeALLEAKEEIHKLRNEFEKELRER---RNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELE 120

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1677538261 1050 KEMTETMEKKlvEETKQLELDLNDERLRYQNLLNEFSR---LEERYDDLKEEMTLMVH 1104
Cdd:PRK12704   121 QKQQELEKKE--EELEELIEEQLQELERISGLTAEEAKeilLEKVEEEARHEAAVLIK 176
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 902-1350 2.79e-03

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: 42.90  E-value: 2.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  902 KRELKKLKIEARSVerYKKLHIGMENKIMQLQRKVDEQNKDYKclvEKLTNLEG-----IYNSET-EKLRSDLERLQLSE 975
Cdd:pfam12128  403 REARDRQLAVAEDD--LQALESELREQLEAGKLEFNEEEYRLK---SRLGELKLrlnqaTATPELlLQLENFDERIERAR 477

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  976 EEAKVATGRVLSLQEEIAKLRKDLEQTrsekkciEEHADRYKQETEQLVSNLKEENTLLKQEKEALNHRIVQQAKEMTET 1055
Cdd:pfam12128  478 EEQEAANAEVERLQSELRQARKRRDQA-------SEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEAPDWEQS 550

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1056 MEK--------------KLVEETKQLELDLNDERLRYQNL-LNEFSRLEErydDLKEemtlmvhvpkpghkRTDSTHSSN 1120
Cdd:pfam12128  551 IGKvispellhrtdldpEVWDGSVGGELNLYGVKLDLKRIdVPEWAASEE---ELRE--------------RLDKAEEAL 613

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1121 ESEyifSSEIAEMEdipsrtEEPSEKKVPLD-MSLFLKLQKRVTELEQEKQ-----VMQDELDRKEEQVLRSKAKEEERp 1194
Cdd:pfam12128  614 QSA---REKQAAAE------EQLVQANGELEkASREETFARTALKNARLDLrrlfdEKQSEKDKKNKALAERKDSANER- 683

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1195 qirgaeleyeslkRQELESENKKLKNELNELRKALSEKSApEVTAPGAPAYRVLMEQLtsvSEELDVRKEEVLILRSQLV 1274
Cdd:pfam12128  684 -------------LNSLEAQLKQLDKKHQAWLEEQKEQKR-EARTEKQAYWQVVEGAL---DAQLALLKAAIAARRSGAK 746

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1275 SQKEAIQpKDDKNTMTDSTILLEDVQKMK---------------DKGEIAQAYIGLKETNRLLESQLQSQKRSHENEAEA 1339
Cdd:pfam12128  747 AELKALE-TWYKRDLASLGVDPDVIAKLKreirtlerkieriavRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISE 825

                          490
                   ....*....|.
gi 1677538261 1340 LRGEIQSLKEE 1350
Cdd:pfam12128  826 LQQQLARLIAD 836
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 960-1052 3.07e-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: 3.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  960 ETEKLRSDLERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQEKE 1039
Cdd:COG4942    151 QAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230

                           90
                   ....*....|...
gi 1677538261 1040 ALNHRIVQQAKEM 1052
Cdd:COG4942    231 RLEAEAAAAAERT 243
CBD_MYO6-like cd21759
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, ...
 767-794 3.27e-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: 3.27e-03
                           10        20
                   ....*....|....*....|....*...
gi 1677538261  767 RAACIRIQKTIRGWLLRKKYlRMRKAAI 794
Cdd:cd21759     45 REALIKIQKTVRGYLARKKH-RPRIKGL 71
CBD_MYO6-like cd21759
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, ...
 829-862 3.63e-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: 3.63e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1677538261  829 VVRRRYKI--RRAATIVLQSYLRGFLARNRYRKILR 862
Cdd:cd21759     34 VIKLKNKIlyRREALIKIQKTVRGYLARKKHRPRIK 69
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 900-1242 3.76e-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: 3.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  900 MAKRELKKLKIEArSVERYKKLHIGMENKIMQLQRKVDEqnkdYKCLVEKLTNLEgiynseTEKLRSDLERLQLSEEEAK 979
Cdd:COG5185    217 SESTLLEKAKEII-NIEEALKGFQDPESELEDLAQTSDK----LEKLVEQNTDLR------LEKLGENAESSKRLNENAN 285

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  980 VATGRVLSLQEEIAKLRKDLEQTRS-EKKCIEEHADRYKQETEQLVSNLKEENTLLKQEkealnhrIVQQAKEMTETMEk 1058
Cdd:COG5185    286 NLIKQFENTKEKIAEYTKSIDIKKAtESLEEQLAAAEAEQELEESKRETETGIQNLTAE-------IEQGQESLTENLE- 357

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1059 KLVEETKQLELDLNDERLRyQNLLNEFSRLEERYDDLKEEMTLMVHVPKPGHKRTDSTHSSNESEyiFSSEIAEMEDIPS 1138
Cdd:COG5185    358 AIKEEIENIVGEVELSKSS-EELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQ--IEELQRQIEQATS 434

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1139 RTEEPSEKKVPLDMSlflkLQKRVTELEQEKQVMQDELDRKEEQVLRSKAKE--EERPQIRGAELEYeslkRQELESENK 1216
Cdd:COG5185    435 SNEEVSKLLNELISE----LNKVMREADEESQSRLEEAYDEINRSVRSKKEDlnEELTQIESRVSTL----KATLEKLRA 506

                          330       340
                   ....*....|....*....|....*.
gi 1677538261 1217 KLKNELNELRKALSEKSAPEVTAPGA 1242
Cdd:COG5185    507 KLERQLEGVRSKLDQVAESLKDFMRA 532
HAP1_N pfam04849
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ...
 1161-1353 3.78e-03

HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.


Pssm-ID: 461455 [Multi-domain]  Cd Length: 309  Bit Score: 41.55  E-value: 3.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1161 RVTELEQEKQvMQDEL---------DRKEEQVLRSKAKEEERPQIRGAELEYESLKRQ--ELESENKKLKNELNELRKAL 1229
Cdd:pfam04849  116 EILQLRHELS-KKDDLlqiysndaeESETESSCSTPLRRNESFSSLHGCVQLDALQEKlrGLEEENLKLRSEASHLKTET 194

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1230 SEKSAPE------VTAPGAPA---YRVLMEQLTSVSEELDVRKEEVLILRSQLVSQKEAIQpkddkntmtdstilledvQ 1300
Cdd:pfam04849  195 DTYEEKEqqlmsdCVEQLSEAnqqMAELSEELARKMEENLRQQEEITSLLAQIVDLQHKCK------------------E 256

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1677538261 1301 KMKDKGEIAQAYIGLKETNRLLESQLQSQKRSHENEAEALRGEIQSLKEENNR 1353
Cdd:pfam04849  257 LGIENEELQQHLQASKEAQRQLTSELQELQDRYAECLGMLHEAQEELKELRKK 309
CBD_MYO6-like cd21759
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, ...
 810-837 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: 39.41  E-value: 4.26e-03
                           10        20
                   ....*....|....*....|....*...
gi 1677538261  810 KFLRRTKAATIIQKYWRMYVVRRRYKIR 837
Cdd:cd21759     40 KILYRREALIKIQKTVRGYLARKKHRPR 67
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
900-1098 4.28e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 4.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  900 MAKRELKKLKIEARSVERYKKlhiGMENKIMQLQRKVDEQNKDYKCLVEKLTNLEGIYNSETEKLRSDLERLQLSEEEAK 979
Cdd:COG4372     35 KALFELDKLQEELEQLREELE---QAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAE 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  980 VATGRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQEKEALNHRIVQQAKEMTETMEKK 1059
Cdd:COG4372    112 ELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKE 191

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1677538261 1060 LVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEE 1098
Cdd:COG4372    192 ANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAK 230
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
925-1224 4.71e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 41.05  E-value: 4.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  925 MENKIMQLQRKVDEQNKDYKCLVEKLTNLegiyNSETEKLRsdlERLQLSEEEAKvatgrvlSLQEEIAKLRKDLEQTRS 1004
Cdd:COG1340     20 LREEIEELKEKRDELNEELKELAEKRDEL----NAQVKELR---EEAQELREKRD-------ELNEKVKELKEERDELNE 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1005 EKKCIEEHADRYKQETEQLVSNLKEENTlLKQEKEALNHRivQQAKEMTETMEKKLVEETKQLELDLnDERLRYQNLLNE 1084
Cdd:COG1340     86 KLNELREELDELRKELAELNKAGGSIDK-LRKEIERLEWR--QQTEVLSPEEEKELVEKIKELEKEL-EKAKKALEKNEK 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1085 FSRLEERYDDLKEEMtlmvhvpkpghkrtdSTHSSNESEYifsseiaeMEDIPSRTEEPSEKKVPLDmslflKLQKRVTE 1164
Cdd:COG1340    162 LKELRAELKELRKEA---------------EEIHKKIKEL--------AEEAQELHEEMIELYKEAD-----ELRKEADE 213

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1677538261 1165 LEQEKQVMQDELDRKEEQVLRSKAKEEE-RPQIRGAELEYESLKRQELESENKKLKNELNE 1224
Cdd:COG1340    214 LHKEIVEAQEKADELHEEIIELQKELRElRKELKKLRKKQRALKREKEKEELEEKAEEIFE 274
BMS1 COG5192
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ...
 937-1212 4.81e-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: 4.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  937 DEQNKDYKCLVEKLTNLEGIYNSETEKLRSDLErLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQ------TRSEKKCIE 1010
Cdd:COG5192    439 DENEDVDFTGKKGAINNEDESDNEEVAFDSDSQ-FDESEGNLRWKEGLASKLAYSQSGKRGRNIQkifydeSLSPEECIE 517

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1011 EHADRYKQETEQLVSNLKEENTLLKQEKEALNHRIVQQAKEMTETMEkKLVEETKQleLDLNDERLRYQNLLNEFSRLEE 1090
Cdd:COG5192    518 EYKGESAKSSESDLVVQDEPEDFFDVSKVANESISSNHEKLMESEFE-ELKKKWSS--LAQLKSRFQKDATLDSIEGEEE 594

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1091 RYDDLkEEMTLMVHVPKPGHKRTDSTHSSNESEYIFSSEIAEMEDIPSRTEEPSEKKVPLDMSLflklqkrvtELEQEKQ 1170
Cdd:COG5192    595 LIQDD-EKGNFEDLEDEENSSDNEMEESRGSSVTAENEESADEVDYETEREENARKKEELRGNF---------ELEERGD 664

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1677538261 1171 VMQDELDRKEEQvlrsKAKEEErpQIRGAELEYESL---KRQELE 1212
Cdd:COG5192    665 PEKKDVDWYTEE----KRKIEE--QLKINRSEFETMvpeSRVVIE 703
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 943-1085 5.31e-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: 5.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  943 YKCLVEKLTNLEGIYNSETEKLRSDLERLQL------SEEEAKVATGRVLSLQE-EIAKLRKDLEQTRSEKKCIEEHADR 1015
Cdd:cd16269    144 YQLYLEDREKLVEKYRQVPRKGVKAEEVLQEflqskeAEAEAILQADQALTEKEkEIEAERAKAEAAEQERKLLEEQQRE 223

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1016 YKQETEQLVSNLKEENTLLKQEKEAlnhRIVQQAKEMTETMEKKLVEETKQLELDLNDERLRYQNLLNEF 1085
Cdd:cd16269    224 LEQKLEDQERSYEEHLRQLKEKMEE---ERENLLKEQERALESKLKEQEALLEEGFKEQAELLQEEIRSL 290
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
988-1231 5.57e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 41.05  E-value: 5.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  988 LQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEentllkqekealnhrIVQQAKEMTETMeKKLVEETKQl 1067
Cdd:COG1340     13 LEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKE---------------LREEAQELREKR-DELNEKVKE- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1068 eldLNDERlryQNLLNEFSRLEERYDDLKEEMtlmvhvpkpghkrtDSTHSSNESEYIFSSEIAEMEDipsrteepsekk 1147
Cdd:COG1340     76 ---LKEER---DELNEKLNELREELDELRKEL--------------AELNKAGGSIDKLRKEIERLEW------------ 123

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1148 vpldmslflKLQKRVTELEQEKQVMqDELDRKEEQVLRSKAKEEERPQIRGAELEYESLKRQ--ELESENKKLKNELNEL 1225
Cdd:COG1340    124 ---------RQQTEVLSPEEEKELV-EKIKELEKELEKAKKALEKNEKLKELRAELKELRKEaeEIHKKIKELAEEAQEL 193


                   ....*.
gi 1677538261 1226 RKALSE 1231
Cdd:COG1340    194 HEEMIE 199
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 1039-1422 6.25e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 41.42  E-value: 6.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1039 EALNHRIVQQAKEMTETMeKKLVEETKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMtlmvhvpkpghKRTDSTHS 1118
Cdd:pfam07888   30 ELLQNRLEECLQERAELL-QAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEEL-----------RQSREKHE 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1119 SNESEY----IFSSEIAEMEDIPSRTEEPSEKKVpldmslfLKLQKRVTELEQEKQVMQDELDRKEEQVLRS----KAKE 1190
Cdd:pfam07888   98 ELEEKYkelsASSEELSEEKDALLAQRAAHEARI-------RELEEDIKTLTQRVLERETELERMKERAKKAgaqrKEEE 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1191 EERPQIRgAELEYESLKRQELESENKKLKNELNE-------LRKALSEKSAPEVTAPGAPA-YRVLMEQLTSVSEELDVR 1262
Cdd:pfam07888  171 AERKQLQ-AKLQQTEEELRSLSKEFQELRNSLAQrdtqvlqLQDTITTLTQKLTTAHRKEAeNEALLEELRSLQERLNAS 249

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1263 KEEVLILRSQL---VSQKEAIQpkddkntmtdSTILLEDVQKMKDKGEIAQAYIGLKETnrllESQLQSQKRSHENEAEA 1339
Cdd:pfam07888  250 ERKVEGLGEELssmAAQRDRTQ----------AELHQARLQAAQLTLQLADASLALREG----RARWAQERETLQQSAEA 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1340 LRGEIQSLKEENNRQQQLLAqnlqlppEARIE-ASLQHEITRLTNENLdlmEQLEKQDKTVRKLKKQLKVFAKKIGELEV 1418
Cdd:pfam07888  316 DKDRIEKLSAELQRLEERLQ-------EERMErEKLEVELGREKDCNR---VQLSESRRELQELKASLRVAQKEKEQLQA 385


                   ....
gi 1677538261 1419 GQME 1422
Cdd:pfam07888  386 EKQE 389
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 888-1234 6.85e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 41.36  E-value: 6.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  888 AIIYLQCCFRRMMAKRELKKLKIEARSV----ERYKKLH-IGmenkimQLQRKVDEQNKDYKCLV-EKLTNLEG-IYNSE 960
Cdd:PRK04778    19 AGLILRKRNYKRIDELEERKQELENLPVndelEKVKKLNlTG------QSEEKFEEWRQKWDEIVtNSLPDIEEqLFEAE 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  961 --TEKLRSDLERLQLSEEEAKVAT--GRVLSLQEEIAKLRKDLEQTRSE-----------KKCIEEHADRYKQETEQLVS 1025
Cdd:PRK04778    93 elNDKFRFRKAKHEINEIESLLDLieEDIEQILEELQELLESEEKNREEveqlkdlyrelRKSLLANRFSFGPALDELEK 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1026 NLKEENTLLKQ---EKEALNH----RIVQQAKEMTETMEKKlVEETKQLELDLNDE--------------------RLRY 1078
Cdd:PRK04778   173 QLENLEEEFSQfveLTESGDYvearEILDQLEEELAALEQI-MEEIPELLKELQTElpdqlqelkagyrelveegyHLDH 251

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1079 QNLLNEFSRLEERYDDLKEEMtlmvhvpkpghKRTDSTHSSNESEYIfSSEIAEMEDIpSRTEEPSEKKVpldMSLFLKL 1158
Cdd:PRK04778   252 LDIEKEIQDLKEQIDENLALL-----------EELDLDEAEEKNEEI-QERIDQLYDI-LEREVKARKYV---EKNSDTL 315

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1159 QKRVTELEQEKQVMQDELDR-------KEEQVLRSKAKEEERPQIRG--------------------AELEYESLKRQEL 1211
Cdd:PRK04778   316 PDFLEHAKEQNKELKEEIDRvkqsytlNESELESVRQLEKQLESLEKqydeiteriaeqeiayselqEELEEILKQLEEI 395

                          410       420
                   ....*....|....*....|...
gi 1677538261 1212 ESENKKLKNELNELRKalSEKSA 1234
Cdd:PRK04778   396 EKEQEKLSEMLQGLRK--DELEA 416
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 862-883 6.90e-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: 6.90e-03
                            10        20
                    ....*....|....*....|..
gi 1677538261   862 REHKAVIIQKRVRGWLARTHYK 883
Cdd:smart00015    2 LTRAAIIIQAAWRGYLARKRYK 23
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
899-1233 6.92e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.18  E-value: 6.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  899 MMAKRELKKLKIEARSVERYKklhigMENKIMQLQRKVDEQ-------NKDYKCLVEKLTNLEgiynSETEKLRSDLERL 971
Cdd:PRK02224   298 LLAEAGLDDADAEAVEARREE-----LEDRDEELRDRLEECrvaaqahNEEAESLREDADDLE----ERAEELREEAAEL 368

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  972 QLSEEEAKVAT----GRVLSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKEENTLLKQEKEAL--NHRI 1045
Cdd:PRK02224   369 ESELEEAREAVedrrEEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVeeAEAL 448

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1046 VQQAK-----------EMTETMEKKLvEETKQLELDLNDERLryqnllnEFSRLEERYDDLKEEMTLMVHVPKPGHKRTD 1114
Cdd:PRK02224   449 LEAGKcpecgqpvegsPHVETIEEDR-ERVEELEAELEDLEE-------EVEEVEERLERAEDLVEAEDRIERLEERRED 520

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1115 SthssneseyifSSEIAEMEDipsRTEEPSEKKVpldmslflKLQKRVTELEQEKQVMQDELDRKEEQV--LRSKAKEEE 1192
Cdd:PRK02224   521 L-----------EELIAERRE---TIEEKRERAE--------ELRERAAELEAEAEEKREAAAEAEEEAeeAREEVAELN 578

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1677538261 1193 RpqiRGAEL--EYESLKR------------QELESENKKLKN--ELNELRK-ALSEKS 1233
Cdd:PRK02224   579 S---KLAELkeRIESLERirtllaaiadaeDEIERLREKREAlaELNDERReRLAEKR 633
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 904-1102 7.04e-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: 40.56  E-value: 7.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  904 ELKKL--KIEARSVERYKKlHIGMENKIMQLQRKVDEQNKDYKCLVEKLTNLEGIYN---SETEKLRSDLERLQlseeea 978
Cdd:pfam15905  160 ELMKLrnKLEAKMKEVMAK-QEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIeekSETEKLLEYITELS------ 232

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  979 kvatgrvlSLQEEIAKLRKDLEQtrsekkcIEEHADRYKQETEQLVSNLKEENTLLKqekealnhrivQQAKEMTETMek 1058
Cdd:pfam15905  233 --------CVSEQVEKYKLDIAQ-------LEELLKEKNDEIESLKQSLEEKEQELS-----------KQIKDLNEKC-- 284

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1677538261 1059 KLVEetKQLELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLM 1102
Cdd:pfam15905  285 KLLE--SEKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKL 326
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
925-1018 7.23e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 41.00  E-value: 7.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  925 MENKIMQLQRKVDE---QNKDYKCLVEKLtnlegiyNSETEKLRSDLERLQlSEEEAKVATGRVLS-LQEEIAKLRKDLE 1000
Cdd:COG2433    411 EEEEIRRLEEQVERleaEVEELEAELEEK-------DERIERLERELSEAR-SEERREIRKDREISrLDREIERLERELE 482

                           90
                   ....*....|....*...
gi 1677538261 1001 QTRSEKKCIEEHADRYKQ 1018
Cdd:COG2433    483 EERERIEELKRKLERLKE 500
WEMBL pfam05701
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ...
 968-1350 8.53e-03

Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".


Pssm-ID: 461718 [Multi-domain]  Cd Length: 562  Bit Score: 40.78  E-value: 8.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  968 LERLQLSEEEAKvatgrvlSLQEEIAKLRKDLEQTRSEKKCIEEHADRYKQETEQLVSNLKeentllKQEKEAlnhrivQ 1047
Cdd:pfam05701   34 VERRKLVELELE-------KVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEELKLNLE------RAQTEE------A 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1048 QAKEMTETMEKKlVEETKQ---------LELDLNDERLRYQNLLNEFSRLEERYDDLKEEMTLMVHVPKPGHKRT-DSTH 1117
Cdd:pfam05701   95 QAKQDSELAKLR-VEEMEQgiadeasvaAKAQLEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAeEAVS 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1118 SSNESEYIFssEIAEMEDIPSRTE---------EPSEKKVPLDMSL---FLKLQKrvtELEQekqvMQDELDRKEEQVLR 1185
Cdd:pfam05701  174 ASKEIEKTV--EELTIELIATKESlesahaahlEAEEHRIGAALAReqdKLNWEK---ELKQ----AEEELQRLNQQLLS 244

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1186 SKAKEeerpqirgAELEYESLKRQELESE-NKKLKNELNELRKALSEKSAPEVTAPGApayrvlmeqLTSVSEEL-DVR- 1262
Cdd:pfam05701  245 AKDLK--------SKLETASALLLDLKAElAAYMESKLKEEADGEGNEKKTSTSIQAA---------LASAKKELeEVKa 307

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1263 -----KEEVLI-------LRSQLVSQKEAIQPKDDKNTMTDSTILLEDVQKMKDKGEIAQAYIGLKETN-RLLESQLQSQ 1329
Cdd:pfam05701  308 niekaKDEVNClrvaaasLRSELEKEKAELASLRQREGMASIAVSSLEAELNRTKSEIALVQAKEKEAReKMVELPKQLQ 387

                          410       420
                   ....*....|....*....|....*.
gi 1677538261 1330 KRSHENE-----AEALRGEIQSLKEE 1350
Cdd:pfam05701  388 QAAQEAEeakslAQAAREELRKAKEE 413
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 960-1413 8.72e-03

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: 40.98  E-value: 8.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261  960 ETEKLRSDLERLQLSEEEAKVATGRVLSLQEEIAKLRKDLEQT-RSEKKCIEEHADRYKQETEQL---VSNLKEENTLLK 1035
Cdd:pfam12128  249 EFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLlRTLDDQWKEKRDELNGELSAAdaaVAKDRSELEALE 328

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1036 QEKEALNHRIVQQAK---EMTETMEKKLVEETKQLELDLNDER-----------LRYQNLLNEFSRLEERYDDLKEEMTL 1101
Cdd:pfam12128  329 DQHGAFLDADIETAAadqEQLPSWQSELENLEERLKALTGKHQdvtakynrrrsKIKEQNNRDIAGIKDKLAKIREARDR 408

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1102 MVHVPKPG---------HKRTDSTHSSNESEYIFSSEIAEME---DIPSRTEEpsekkvpldmslfLKLQKRVTELEQEK 1169
Cdd:pfam12128  409 QLAVAEDDlqaleselrEQLEAGKLEFNEEEYRLKSRLGELKlrlNQATATPE-------------LLLQLENFDERIER 475

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1170 qvMQDELDRKEEQVLRSkakEEERPQIRGAElEYESLKRQELESENKKLKNELNELRKALSEKSAP--EVTAPGAPAYRV 1247
Cdd:pfam12128  476 --AREEQEAANAEVERL---QSELRQARKRR-DQASEALRQASRRLEERQSALDELELQLFPQAGTllHFLRKEAPDWEQ 549

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1248 LMEQLTSVSeeldvrkeevLILRSQLVSQKEAIQPKDDkNTMTDSTILLEDVqkmkDKGEIAQAYIGLKETNRLLESQLQ 1327
Cdd:pfam12128  550 SIGKVISPE----------LLHRTDLDPEVWDGSVGGE-LNLYGVKLDLKRI----DVPEWAASEEELRERLDKAEEALQ 614

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677538261 1328 SQKRSHENEAEAL---RGEIQSLKEEnnrqqqllaqnlqlppEARIEASLQH---EITRLTNENLDLMEQLEKQ------ 1395
Cdd:pfam12128  615 SAREKQAAAEEQLvqaNGELEKASRE----------------ETFARTALKNarlDLRRLFDEKQSEKDKKNKAlaerkd 678

                          490       500
                   ....*....|....*....|
gi 1677538261 1396 --DKTVRKLKKQLKVFAKKI 1413
Cdd:pfam12128  679 saNERLNSLEAQLKQLDKKH 698
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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