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Conserved domains on  [gi|568955249|ref|XP_006509632|]
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unconventional myosin-IXb isoform X4 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MYSc_Myo9 cd01385
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ...
160-977 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: 1324.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISG 239
Cdd:cd01385     1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  240 ESGSGKTQSTNFLIHCLTALSQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRGAVVEKYL 319
Cdd:cd01385    81 ESGSGKTESTNFLLHHLTALSQKGYGSGVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVEKYL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  320 LEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDLKHDFERLQQAMEMVGFLPATKK 399
Cdd:cd01385   161 LEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNQSDCYTLEGEDEKYEFERLKQAMEMVGFLPETQR 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  400 QIFSVLSAILYLGNVTYKKRATGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILPYSLSEAITARD 479
Cdd:cd01385   241 QIFSVLSAVLHLGNIEYKKKAYHRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLILPYKLPEAIATRD 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  480 SMAKSLYSALFDWIVLRINHALLNKKDMEEaVSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQEE 559
Cdd:cd01385   321 AMAKCLYSALFDWIVLRINHALLNKKDLEE-AKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIFKLEQEE 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  560 YQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPVLEPAFIIQHFAGR 639
Cdd:cd01385   400 YKKEGISWHNIEYTDNTGCLQLISKKPTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNKYYEKPQVMEPAFIIAHYAGK 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  640 VKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLIGMDPVAVFRWAVLRAAIRAMAVLREAGRlraeraekaaagissp 719
Cdd:cd01385   480 VKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVRELIGIDPVAVFRWAVLRAFFRAMAAFREAGR---------------- 543
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  720 atrshmeelprgastpseklyrctgldfsferseeldvnafedimafyESRKARGQSdlhnqiikslkglpwqgedprrl 799
Cdd:cd01385   544 ------------------------------------------------RRAQRTAGH----------------------- 552
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  800 lqslslfqkprtsflkskgikqkqiipknlldskslrliiSMTLHDRTTKSLLHLHKKKKPPSISAQFQTSLNKLLEALG 879
Cdd:cd01385   553 ----------------------------------------SLTLHDRTTKSLLHLHKKKKPPSVSAQFQTSLSKLMETLG 592
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  880 KAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPKDVQPCREAIAALLEK 959
Cdd:cd01385   593 QAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVLLPKGLISSKEDIKDFLEK 672
                         810
                  ....*....|....*...
gi 568955249  960 LQVDRQNYQIGKTKVFLK 977
Cdd:cd01385   673 LNLDRDNYQIGKTKVFLK 690
RhoGAP_myosin_IXB cd04407
RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
1704-1889 4.73e-128

RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in myosins IXB. Class IX myosins contain a characteristic head domain, a neck domain and a tail domain which contains a C6H2-zinc binding motif and a Rho-GAP domain. Class IX myosins are single-headed, processive myosins that are partly cytoplasmic, and partly associated with membranes and the actin cytoskeleton. Class IX myosins are implicated in the regulation of neuronal morphogenesis and function of sensory systems, like the inner ear. There are two major isoforms, myosin IXA and IXB with several splice variants, which are both expressed in developing neurons Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


:

Pssm-ID: 239872 [Multi-domain]  Cd Length: 186  Bit Score: 399.37  E-value: 4.73e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1704 FGVCVDSLTSDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKLEDFPIHAITGVLKQWLRE 1783
Cdd:cd04407     1 FGVRVGSLTSNKTSVPIVLEKLLEHVEMHGLYTEGIYRKSGSANRMKELHQLLQADPENVKLENYPIHAITGLLKQWLRE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1784 LPEPLMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRC 1863
Cdd:cd04407    81 LPEPLMTFAQYNDFLRAVELPEKQEQLQAIYRVLEQLPTANHNTLERLIFHLVKVALEEDVNRMSPNALAIVFAPCLLRC 160
                         170       180
                  ....*....|....*....|....*.
gi 568955249 1864 PDNSDPLTSMKDVLKITTCVEMLIKE 1889
Cdd:cd04407   161 PDSSDPLTSMKDVAKTTTCVEMLIKE 186
RA_Myosin-IXb cd17217
Ras-associating (RA) domain found in Myosin-IXb; Myosin-IXb, also termed myosin-9b (Myo9b), is ...
16-112 1.68e-55

Ras-associating (RA) domain found in Myosin-IXb; Myosin-IXb, also termed myosin-9b (Myo9b), is a motor protein with a Rho GTPase activating domain (RhoGAP); it is an actin-dependent motor protein of the unconventional myosin IX class. It is expressed abundantly in tissues of the immune system, like lymph nodes, thymus, and spleen and in several immune cells including dendritic cells, macrophages and CD4+ T. Myosin-IXb contains a Ras-associating (RA) domain, a motor domain, a protein kinase C conserved region 1 (C1), and a RhoGAP domain. Its RA domain is located at its head domain and has the beta-grasp ubiquitin-like fold with unknown function. Myosin-IXb acts as a motorized signaling molecule that links Rho signaling to the dynamic actin cytoskeleton. It regulates leukocyte migration by controlling RhoA signaling. Myosin-IXb is also involved in the development of autoimmune diseases, including rheumatoid arthritis, systemic lupus erythematosus and type 1 diabetes. Moreover, Myosin-IXb is a ROBO-interacting protein that suppresses RhoA activity in lung cancer cells.


:

Pssm-ID: 340737  Cd Length: 96  Bit Score: 188.08  E-value: 1.68e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249   16 TYHLHIYPQLSSAgSQTSCRVTATKDSTTSDVIQDVVASLHLDGSKHYVLVEVKESGGEEWVLDASDSPVHRVLLWPRRA 95
Cdd:cd17217     1 VYALQIYPQLSAE-SSTCCIVLATKEATASDVIKDAVATLGLDSSKPYVLAEVKESGGEEWVLDANDSPVQRVLLWPRKA 79
                          90
                  ....*....|....*..
gi 568955249   96 QDEHPQEDGYYFLLQER 112
Cdd:cd17217    80 QDDHPQSDGYYFLLQER 96
C1_Myosin-IXb cd20884
protein kinase C conserved region 1 (C1 domain) found in unconventional myosin-IXb and similar ...
1634-1691 1.87e-36

protein kinase C conserved region 1 (C1 domain) found in unconventional myosin-IXb and similar proteins; Myosin-IXb, also called unconventional myosin-9b (Myo9b), is an actin-dependent motor protein of the unconventional myosin IX class. It is expressed abundantly in tissues of the immune system, like lymph nodes, thymus, and spleen, and in several immune cells including dendritic cells, macrophages and CD4+ T cells. Myosin-IXb contains a Ras-associating (RA) domain, a motor domain, a protein kinase C conserved region 1 (C1), and a Rho GTPase activating (RhoGAP) domain. Myosin-IXb acts as a motorized signaling molecule that links Rho signaling to the dynamic actin cytoskeleton. It regulates leukocyte migration by controlling RhoA signaling. Myosin-IXb is also involved in the development of autoimmune diseases, including rheumatoid arthritis, systemic lupus erythematosus, and type 1 diabetes. Moreover, Myosin-IXb is a ROBO-interacting protein that suppresses RhoA activity in lung cancer cells. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


:

Pssm-ID: 410434  Cd Length: 58  Bit Score: 132.29  E-value: 1.87e-36
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568955249 1634 QEHNGHVFASYQVNIPQSCEQCLSYIWLMDKALLCSVCKMTCHKKCVHKIQSYCSYTG 1691
Cdd:cd20884     1 EEYNGHVFTSYQVNIMQSCEQCSSYIWAMEKALLCSVCKMTCHKKCLSKIQSHCSSTC 58
PHA02682 super family cl31817
ORF080 virion core protein; Provisional
2027-2121 4.24e-05

ORF080 virion core protein; Provisional


The actual alignment was detected with superfamily member PHA02682:

Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 47.55  E-value: 4.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 2027 PAPALPCPISPTLSPLPEAAAPPRGRPTSFVTVRVKTPRR-TPIMPMANIKLPPGLPLHLTSWAPALQEAVVPvKRREPP 2105
Cdd:PHA02682   96 PACAPAAPAPAVTCPAPAPACPPATAPTCPPPAVCPAPARpAPACPPSTRQCPPAPPLPTPKPAPAAKPIFLH-NQLPPP 174
                          90
                  ....*....|....*.
gi 568955249 2106 ARRQDQVHSVYIAPGA 2121
Cdd:PHA02682  175 DYPAASCPTIETAPAA 190
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
1036-1058 1.14e-04

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


:

Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 40.77  E-value: 1.14e-04
                            10        20
                    ....*....|....*....|...
gi 568955249   1036 ERTQAAVYLQAAWRGYLQRQAYH 1058
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRYK 23
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
1014-1035 5.49e-03

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


:

Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 36.15  E-value: 5.49e-03
                            10        20
                    ....*....|....*....|..
gi 568955249   1014 QMKHAALTIQACWRSYRVRRAL 1035
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRY 22
 
Name Accession Description Interval E-value
MYSc_Myo9 cd01385
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ...
160-977 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: 1324.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISG 239
Cdd:cd01385     1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  240 ESGSGKTQSTNFLIHCLTALSQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRGAVVEKYL 319
Cdd:cd01385    81 ESGSGKTESTNFLLHHLTALSQKGYGSGVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVEKYL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  320 LEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDLKHDFERLQQAMEMVGFLPATKK 399
Cdd:cd01385   161 LEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNQSDCYTLEGEDEKYEFERLKQAMEMVGFLPETQR 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  400 QIFSVLSAILYLGNVTYKKRATGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILPYSLSEAITARD 479
Cdd:cd01385   241 QIFSVLSAVLHLGNIEYKKKAYHRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLILPYKLPEAIATRD 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  480 SMAKSLYSALFDWIVLRINHALLNKKDMEEaVSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQEE 559
Cdd:cd01385   321 AMAKCLYSALFDWIVLRINHALLNKKDLEE-AKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIFKLEQEE 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  560 YQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPVLEPAFIIQHFAGR 639
Cdd:cd01385   400 YKKEGISWHNIEYTDNTGCLQLISKKPTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNKYYEKPQVMEPAFIIAHYAGK 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  640 VKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLIGMDPVAVFRWAVLRAAIRAMAVLREAGRlraeraekaaagissp 719
Cdd:cd01385   480 VKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVRELIGIDPVAVFRWAVLRAFFRAMAAFREAGR---------------- 543
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  720 atrshmeelprgastpseklyrctgldfsferseeldvnafedimafyESRKARGQSdlhnqiikslkglpwqgedprrl 799
Cdd:cd01385   544 ------------------------------------------------RRAQRTAGH----------------------- 552
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  800 lqslslfqkprtsflkskgikqkqiipknlldskslrliiSMTLHDRTTKSLLHLHKKKKPPSISAQFQTSLNKLLEALG 879
Cdd:cd01385   553 ----------------------------------------SLTLHDRTTKSLLHLHKKKKPPSVSAQFQTSLSKLMETLG 592
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  880 KAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPKDVQPCREAIAALLEK 959
Cdd:cd01385   593 QAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVLLPKGLISSKEDIKDFLEK 672
                         810
                  ....*....|....*...
gi 568955249  960 LQVDRQNYQIGKTKVFLK 977
Cdd:cd01385   673 LNLDRDNYQIGKTKVFLK 690
MYSc smart00242
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...
141-986 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: 887.27  E-value: 0e+00
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249    141 LPRPQADFDDLCNLPELTEANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALAD 220
Cdd:smart00242    1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249    221 VAYYAMLRKHVNQCIVISGESGSGKTQSTNFLIHCLTALS-QKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKF 299
Cdd:smart00242   81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSgSNTEVGSVEDQILESNPILEAFGNAKTLRNNNSSRFGKF 160
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249    300 IQVNYLENGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDLKH 379
Cdd:smart00242  161 IEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQGGCLTVDGIDDAE 240
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249    380 DFERLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKRATGRDEGlEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTV 459
Cdd:smart00242  241 EFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAAS-TVKDKEELSNAAELLGVDPEELEKALTKRKIK 319
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249    460 TVNDKLILPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDmeeavSCLSIGVLDIFGFEDFERNSFEQFCINY 539
Cdd:smart00242  320 TGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDG-----STYFIGVLDIYGFEIFEVNSFEQLCINY 394
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249    540 ANEQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNK 619
Cdd:smart00242  395 ANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFFDNQDCIDLIEKKPPGILSLLDEECRFPKGTDQTFLEKLNQHHKKHP 474
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249    620 YFLGTPVL-EPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLigmdpvavfrwavlraairamavl 698
Cdd:smart00242  475 HFSKPKKKgRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASL------------------------ 530
                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249    699 reagrlraeraekaaagisspatrshmeelprgastpseklyrctgldfsferseeldvnaFEDimafYESRKargqsdl 778
Cdd:smart00242  531 -------------------------------------------------------------FPS----GVSNA------- 538
                           650       660       670       680       690       700       710       720
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249    779 hnqiikslkglpwqgedprrllqslslfqkprtsflkskgikqkqiipknlldskslrliismtlhdrttksllhlHKKK 858
Cdd:smart00242  539 ----------------------------------------------------------------------------GSKK 542
                           730       740       750       760       770       780       790       800
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249    859 KPPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQF 938
Cdd:smart00242  543 RFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFDEFLQRY 622
                           810       820       830       840       850
                    ....*....|....*....|....*....|....*....|....*....|..
gi 568955249    939 QVLLPKDVQPC----REAIAALLEKLQVDRQNYQIGKTKVFLKETERQTLQE 986
Cdd:smart00242  623 RVLLPDTWPPWggdaKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEE 674
Myosin_head pfam00063
Myosin head (motor domain);
149-977 0e+00

Myosin head (motor domain);


Pssm-ID: 395017  Cd Length: 674  Bit Score: 677.85  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249   149 DDLCNLPELTEANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLR 228
Cdd:pfam00063    2 EDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSMLQ 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249   229 KHVNQCIVISGESGSGKTQSTNFLIHCLTALSQKGYASGVER---TILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYL 305
Cdd:pfam00063   82 DKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGNVGRleeQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQFD 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249   306 ENGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDLKHDFERLQ 385
Cdd:pfam00063  162 AKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQSGCYTIDGIDDSEEFKITD 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249   386 QAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKRAtgRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKL 465
Cdd:pfam00063  242 KAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKER--NDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGRETV 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249   466 ILPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEAVsclsIGVLDIFGFEDFERNSFEQFCINYANEQLQ 545
Cdd:pfam00063  320 SKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASF----IGVLDIYGFEIFEKNSFEQLCINYVNEKLQ 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249   546 YYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDN-KYFLGT 624
Cdd:pfam00063  396 QFFNHHMFKLEQEEYVREGIEWTFIDFGDNQPCIDLIEKKPLGILSLLDEECLFPKATDQTFLDKLYSTFSKHpHFQKPR 475
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249   625 PVLEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLigmdpvavfrwavlraairamavlreagrl 704
Cdd:pfam00063  476 LQGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAEL------------------------------ 525
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249   705 raeraekaaagisspatrshmeelprgastpseklyrctgldfsferseeldvnafedimafyesrkargqsdlhnqiik 784
Cdd:pfam00063      --------------------------------------------------------------------------------
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249   785 slkglpWQGEDPrrllQSLSLFQKPRTSFLKSKgikqkqiipknlldskslrliismtlhdrttksllhlhKKKKPPSIS 864
Cdd:pfam00063  526 ------FPDYET----AESAAANESGKSTPKRT--------------------------------------KKKRFITVG 557
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249   865 AQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL--- 941
Cdd:pfam00063  558 SQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRYRILapk 637
                          810       820       830
                   ....*....|....*....|....*....|....*..
gi 568955249   942 -LPKDVQPCREAIAALLEKLQVDRQNYQIGKTKVFLK 977
Cdd:pfam00063  638 tWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
COG5022 COG5022
Myosin heavy chain [General function prediction only];
149-1079 0e+00

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 647.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  149 DDLCNLPELTEANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLR 228
Cdd:COG5022    69 DDLTELSYLNEPAVLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLS 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  229 KHVNQCIVISGESGSGKTQSTNFLIHCLTAL--SQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLE 306
Cdd:COG5022   149 EKENQTIIISGESGAGKTENAKRIMQYLASVtsSSTVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDE 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  307 NGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDLKHDFERLQQ 386
Cdd:COG5022   229 NGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDKIDGIDDAKEFKITLD 308
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  387 AMEMVGFLPATKKQIFSVLSAILYLGNVTYKKratGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLI 466
Cdd:COG5022   309 ALKTIGIDEEEQDQIFKILAAILHIGNIEFKE---DRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIV 385
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  467 LPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEavsclSIGVLDIFGFEDFERNSFEQFCINYANEQLQY 546
Cdd:COG5022   386 VPLNLEQALAIRDSLAKALYSNLFDWIVDRINKSLDHSAAASN-----FIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQ 460
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  547 YFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKK-PTGLFYLLDEESNFPHATSHTLLAKFKQQ--HEDNKYFLG 623
Cdd:COG5022   461 FFNQHMFKLEQEEYVKEGIEWSFIDYFDNQPCIDLIEKKnPLGILSLLDEECVMPHATDESFTSKLAQRlnKNSNPKFKK 540
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  624 TPVLEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLigmdpvavfrwavlraairamavlreagr 703
Cdd:COG5022   541 SRFRDNKFVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTL----------------------------- 591
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  704 lraeraekaaagisspatrshmeelprgastpseklyrctgldfsFERSEELDvnafedimafyesrkargqsdlhnqii 783
Cdd:COG5022   592 ---------------------------------------------FDDEENIE--------------------------- 599
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  784 kslkglpwqgedprrllqslslfqkprtsflkskgikqkqiipknlldskslrliismtlhdrttksllhlhKKKKPPSI 863
Cdd:COG5022   600 ------------------------------------------------------------------------SKGRFPTL 607
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  864 SAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLP 943
Cdd:COG5022   608 GSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSP 687
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  944 --------KDVQPCREAIAALLEKLQVDRQNYQIGKTKVFLKeTERQTLQEKLHGEVLRRIL-QLQSWFRMVLERKHFVQ 1014
Cdd:COG5022   688 skswtgeyTWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFK-AGVLAALEDMRDAKLDNIAtRIQRAIRGRYLRRRYLQ 766
                         890       900       910       920       930       940
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568955249 1015 MKHAALTIQACWRSYRVRRALER---TQAAVYLQAAWRGYLQRQAYHHQRHSIIRLQSLCRGHLQRRS 1079
Cdd:COG5022   767 ALKRIKKIQVIQHGFRLRRLVDYelkWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIKREKKLRE 834
PTZ00014 PTZ00014
myosin-A; Provisional
148-1052 3.25e-132

myosin-A; Provisional


Pssm-ID: 240229 [Multi-domain]  Cd Length: 821  Bit Score: 436.38  E-value: 3.25e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  148 FDDLCNLPELTEANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYEN-QQLGKLEPHVFALADVAYYAM 226
Cdd:PTZ00014   98 YGDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDaKDSDKLPPHVFTTARRALENL 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  227 LRKHVNQCIVISGESGSGKTQSTNFLIhcltalsqKGYASGV--------ERTILGAGPVLEAFGNAKTAHNNNSSRFGK 298
Cdd:PTZ00014  178 HGVKKSQTIIVSGESGAGKTEATKQIM--------RYFASSKsgnmdlkiQNAIMAANPVLEAFGNAKTIRNNNSSRFGR 249
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  299 FIQVNYLENGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDLK 378
Cdd:PTZ00014  250 FMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPKCLDVPGIDDVK 329
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  379 hDFERLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKRAT-GRDEGLEVGP--PEVLDTLSQLLKVKRETLVEVLTK 455
Cdd:PTZ00014  330 -DFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEgGLTDAAAISDesLEVFNEACELLFLDYESLKKELTV 408
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  456 RKTVTVNDKLILPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEeavscLSIGVLDIFGFEDFERNSFEQF 535
Cdd:PTZ00014  409 KVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFK-----VFIGMLDIFGFEVFKNNSLEQL 483
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  536 CINYANEQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQH 615
Cdd:PTZ00014  484 FINITNEMLQKNFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGKSVLSILEDQCLAPGGTDEKFVSSCNTNL 563
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  616 EDNKYFLGTPV-LEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLigmdpvavfrwavlraaira 694
Cdd:PTZ00014  564 KNNPKYKPAKVdSNKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDL-------------------- 623
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  695 mavlreagrlraeraekaaagisspatrshmeelprgastpseklyrctgldfsferseeldvnaFEDIMAfYESRKARG 774
Cdd:PTZ00014  624 -----------------------------------------------------------------FEGVEV-EKGKLAKG 637
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  775 QsdlhnqiikslkglpwqgedprrllqslslfqkprtsflkskgikqkqiipknlldskslrLIISmtlhdrttksllhl 854
Cdd:PTZ00014  638 Q-------------------------------------------------------------LIGS-------------- 642
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  855 hkkkkppsisaQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDF 934
Cdd:PTZ00014  643 -----------QFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEF 711
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  935 TEQFQVL-LP----KDVQPcREAIAALLEKLQVDRQNYQIGKTKVFLKETERQTLQEKLHgevlrriLQLQSWfrmvler 1009
Cdd:PTZ00014  712 LSQFKYLdLAvsndSSLDP-KEKAEKLLERSGLPKDSYAIGKTMVFLKKDAAKELTQIQR-------EKLAAW------- 776
                         890       900       910       920
                  ....*....|....*....|....*....|....*....|....
gi 568955249 1010 KHFVQMkhaaltIQACWRSYRVRRAL-ERTQAAVYLQAAWRGYL 1052
Cdd:PTZ00014  777 EPLVSV------LEALILKIKKKRKVrKNIKSLVRIQAHLRRHL 814
RhoGAP_myosin_IXB cd04407
RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
1704-1889 4.73e-128

RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in myosins IXB. Class IX myosins contain a characteristic head domain, a neck domain and a tail domain which contains a C6H2-zinc binding motif and a Rho-GAP domain. Class IX myosins are single-headed, processive myosins that are partly cytoplasmic, and partly associated with membranes and the actin cytoskeleton. Class IX myosins are implicated in the regulation of neuronal morphogenesis and function of sensory systems, like the inner ear. There are two major isoforms, myosin IXA and IXB with several splice variants, which are both expressed in developing neurons Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239872 [Multi-domain]  Cd Length: 186  Bit Score: 399.37  E-value: 4.73e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1704 FGVCVDSLTSDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKLEDFPIHAITGVLKQWLRE 1783
Cdd:cd04407     1 FGVRVGSLTSNKTSVPIVLEKLLEHVEMHGLYTEGIYRKSGSANRMKELHQLLQADPENVKLENYPIHAITGLLKQWLRE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1784 LPEPLMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRC 1863
Cdd:cd04407    81 LPEPLMTFAQYNDFLRAVELPEKQEQLQAIYRVLEQLPTANHNTLERLIFHLVKVALEEDVNRMSPNALAIVFAPCLLRC 160
                         170       180
                  ....*....|....*....|....*.
gi 568955249 1864 PDNSDPLTSMKDVLKITTCVEMLIKE 1889
Cdd:cd04407   161 PDSSDPLTSMKDVAKTTTCVEMLIKE 186
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
1717-1890 3.63e-58

GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases. etter domain limits and outliers.


Pssm-ID: 214618  Cd Length: 174  Bit Score: 198.64  E-value: 3.63e-58
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249   1717 SVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVK-LEDFPIHAITGVLKQWLRELPEPLMTFAQYG 1795
Cdd:smart00324    2 PIPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDPDLdLSEYDVHDVAGLLKLFLRELPEPLITYELYE 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249   1796 DFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRCPDNSDPltSMKD 1875
Cdd:smart00324   82 EFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGEVA--SLKD 159
                           170
                    ....*....|....*
gi 568955249   1876 VLKITTCVEMLIKEQ 1890
Cdd:smart00324  160 IRHQNTVIEFLIENA 174
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
1719-1868 8.19e-56

RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.


Pssm-ID: 425782  Cd Length: 152  Bit Score: 191.25  E-value: 8.19e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  1719 PIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAV-KLEDFPIHAITGVLKQWLRELPEPLMTFAQYGDF 1797
Cdd:pfam00620    1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDSGEDVDlDLEEEDVHDVASLLKLFLRELPEPLLTFELYEEF 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568955249  1798 LRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRCPDNSD 1868
Cdd:pfam00620   81 IEAAKSEDEEERIEALRELLEKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLLRPPDSES 151
RA_Myosin-IXb cd17217
Ras-associating (RA) domain found in Myosin-IXb; Myosin-IXb, also termed myosin-9b (Myo9b), is ...
16-112 1.68e-55

Ras-associating (RA) domain found in Myosin-IXb; Myosin-IXb, also termed myosin-9b (Myo9b), is a motor protein with a Rho GTPase activating domain (RhoGAP); it is an actin-dependent motor protein of the unconventional myosin IX class. It is expressed abundantly in tissues of the immune system, like lymph nodes, thymus, and spleen and in several immune cells including dendritic cells, macrophages and CD4+ T. Myosin-IXb contains a Ras-associating (RA) domain, a motor domain, a protein kinase C conserved region 1 (C1), and a RhoGAP domain. Its RA domain is located at its head domain and has the beta-grasp ubiquitin-like fold with unknown function. Myosin-IXb acts as a motorized signaling molecule that links Rho signaling to the dynamic actin cytoskeleton. It regulates leukocyte migration by controlling RhoA signaling. Myosin-IXb is also involved in the development of autoimmune diseases, including rheumatoid arthritis, systemic lupus erythematosus and type 1 diabetes. Moreover, Myosin-IXb is a ROBO-interacting protein that suppresses RhoA activity in lung cancer cells.


Pssm-ID: 340737  Cd Length: 96  Bit Score: 188.08  E-value: 1.68e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249   16 TYHLHIYPQLSSAgSQTSCRVTATKDSTTSDVIQDVVASLHLDGSKHYVLVEVKESGGEEWVLDASDSPVHRVLLWPRRA 95
Cdd:cd17217     1 VYALQIYPQLSAE-SSTCCIVLATKEATASDVIKDAVATLGLDSSKPYVLAEVKESGGEEWVLDANDSPVQRVLLWPRKA 79
                          90
                  ....*....|....*..
gi 568955249   96 QDEHPQEDGYYFLLQER 112
Cdd:cd17217    80 QDDHPQSDGYYFLLQER 96
C1_Myosin-IXb cd20884
protein kinase C conserved region 1 (C1 domain) found in unconventional myosin-IXb and similar ...
1634-1691 1.87e-36

protein kinase C conserved region 1 (C1 domain) found in unconventional myosin-IXb and similar proteins; Myosin-IXb, also called unconventional myosin-9b (Myo9b), is an actin-dependent motor protein of the unconventional myosin IX class. It is expressed abundantly in tissues of the immune system, like lymph nodes, thymus, and spleen, and in several immune cells including dendritic cells, macrophages and CD4+ T cells. Myosin-IXb contains a Ras-associating (RA) domain, a motor domain, a protein kinase C conserved region 1 (C1), and a Rho GTPase activating (RhoGAP) domain. Myosin-IXb acts as a motorized signaling molecule that links Rho signaling to the dynamic actin cytoskeleton. It regulates leukocyte migration by controlling RhoA signaling. Myosin-IXb is also involved in the development of autoimmune diseases, including rheumatoid arthritis, systemic lupus erythematosus, and type 1 diabetes. Moreover, Myosin-IXb is a ROBO-interacting protein that suppresses RhoA activity in lung cancer cells. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410434  Cd Length: 58  Bit Score: 132.29  E-value: 1.87e-36
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568955249 1634 QEHNGHVFASYQVNIPQSCEQCLSYIWLMDKALLCSVCKMTCHKKCVHKIQSYCSYTG 1691
Cdd:cd20884     1 EEYNGHVFTSYQVNIMQSCEQCSSYIWAMEKALLCSVCKMTCHKKCLSKIQSHCSSTC 58
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
15-114 1.36e-15

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Recent evidence (not yet in MEDLINE) shows that some RA domains do NOT bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase.


Pssm-ID: 425871  Cd Length: 93  Bit Score: 73.91  E-value: 1.36e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249    15 ATYHLHIYPQLSSAGSqTSCRVTATKDSTTSDVIQDVVASLHLDGSK-HYVLVEVKESGGEEWVLDASDSPVHRVLLWPR 93
Cdd:pfam00788    1 DDGVLKVYTEDGKPGT-TYKTILVSSSTTAEEVIEALLEKFGLEDDPrDYVLVEVLERGGGERRLPDDECPLQIQLQWPR 79
                           90       100
                   ....*....|....*....|.
gi 568955249    94 RAQDehpqedgYYFLLQERNA 114
Cdd:pfam00788   80 DASD-------SRFLLRKRDD 93
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
15-113 6.63e-15

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Kalhammer et al. have shown that not all RA domains bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase. Predicted RA domains in PLC210 and nore1 found to bind RasGTP. Included outliers (Grb7, Grb14, adenylyl cyclases etc.)


Pssm-ID: 214612  Cd Length: 90  Bit Score: 71.95  E-value: 6.63e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249     15 ATYHLHIYPQLSSagSQTSCRVTATKDSTTSDVIQDVVASLHLDGS-KHYVLVEVKEsGGEEWVLDASDSPVHRVLLWPR 93
Cdd:smart00314    1 DTFVLRVYVDDLP--GGTYKTLRVSSRTTARDVIQQLLEKFHLTDDpEEYVLVEVLP-DGKERVLPDDENPLQLQKLWPR 77
                            90       100
                    ....*....|....*....|
gi 568955249     94 RaqdehpqEDGYYFLLQERN 113
Cdd:smart00314   78 R-------GPNLRFVLRKRD 90
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
1639-1687 2.02e-12

Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.


Pssm-ID: 197519  Cd Length: 50  Bit Score: 63.64  E-value: 2.02e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 568955249   1639 HVFASYQVNIPQSCEQCLSYIWLMDK-ALLCSVCKMTCHKKCVHKIQSYC 1687
Cdd:smart00109    1 HKHVFRTFTKPTFCCVCRKSIWGSFKqGLRCSECKVKCHKKCADKVPKAC 50
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
1639-1687 2.24e-07

Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the Protein kinase C conserved region 1 (C1) domain.


Pssm-ID: 395079  Cd Length: 53  Bit Score: 49.36  E-value: 2.24e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 568955249  1639 HVFASYQVNIPQSCEQCLSYIWLMDK-ALLCSVCKMTCHKKCVHKIQSYC 1687
Cdd:pfam00130    1 HHFVHRNFKQPTFCDHCGEFLWGLGKqGLKCSWCKLNVHKRCHEKVPPEC 50
PHA02682 PHA02682
ORF080 virion core protein; Provisional
2027-2121 4.24e-05

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 47.55  E-value: 4.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 2027 PAPALPCPISPTLSPLPEAAAPPRGRPTSFVTVRVKTPRR-TPIMPMANIKLPPGLPLHLTSWAPALQEAVVPvKRREPP 2105
Cdd:PHA02682   96 PACAPAAPAPAVTCPAPAPACPPATAPTCPPPAVCPAPARpAPACPPSTRQCPPAPPLPTPKPAPAAKPIFLH-NQLPPP 174
                          90
                  ....*....|....*.
gi 568955249 2106 ARRQDQVHSVYIAPGA 2121
Cdd:PHA02682  175 DYPAASCPTIETAPAA 190
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
1036-1058 1.14e-04

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


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 40.77  E-value: 1.14e-04
                            10        20
                    ....*....|....*....|...
gi 568955249   1036 ERTQAAVYLQAAWRGYLQRQAYH 1058
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRYK 23
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
1038-1058 1.92e-03

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 425778  Cd Length: 21  Bit Score: 37.30  E-value: 1.92e-03
                           10        20
                   ....*....|....*....|.
gi 568955249  1038 TQAAVYLQAAWRGYLQRQAYH 1058
Cdd:pfam00612    1 RKAAIKIQAAWRGYLARKRYK 21
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
1014-1035 5.49e-03

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


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 36.15  E-value: 5.49e-03
                            10        20
                    ....*....|....*....|..
gi 568955249   1014 QMKHAALTIQACWRSYRVRRAL 1035
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRY 22
 
Name Accession Description Interval E-value
MYSc_Myo9 cd01385
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ...
160-977 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: 1324.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISG 239
Cdd:cd01385     1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  240 ESGSGKTQSTNFLIHCLTALSQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRGAVVEKYL 319
Cdd:cd01385    81 ESGSGKTESTNFLLHHLTALSQKGYGSGVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVEKYL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  320 LEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDLKHDFERLQQAMEMVGFLPATKK 399
Cdd:cd01385   161 LEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNQSDCYTLEGEDEKYEFERLKQAMEMVGFLPETQR 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  400 QIFSVLSAILYLGNVTYKKRATGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILPYSLSEAITARD 479
Cdd:cd01385   241 QIFSVLSAVLHLGNIEYKKKAYHRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLILPYKLPEAIATRD 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  480 SMAKSLYSALFDWIVLRINHALLNKKDMEEaVSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQEE 559
Cdd:cd01385   321 AMAKCLYSALFDWIVLRINHALLNKKDLEE-AKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIFKLEQEE 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  560 YQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPVLEPAFIIQHFAGR 639
Cdd:cd01385   400 YKKEGISWHNIEYTDNTGCLQLISKKPTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNKYYEKPQVMEPAFIIAHYAGK 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  640 VKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLIGMDPVAVFRWAVLRAAIRAMAVLREAGRlraeraekaaagissp 719
Cdd:cd01385   480 VKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVRELIGIDPVAVFRWAVLRAFFRAMAAFREAGR---------------- 543
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  720 atrshmeelprgastpseklyrctgldfsferseeldvnafedimafyESRKARGQSdlhnqiikslkglpwqgedprrl 799
Cdd:cd01385   544 ------------------------------------------------RRAQRTAGH----------------------- 552
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  800 lqslslfqkprtsflkskgikqkqiipknlldskslrliiSMTLHDRTTKSLLHLHKKKKPPSISAQFQTSLNKLLEALG 879
Cdd:cd01385   553 ----------------------------------------SLTLHDRTTKSLLHLHKKKKPPSVSAQFQTSLSKLMETLG 592
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  880 KAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPKDVQPCREAIAALLEK 959
Cdd:cd01385   593 QAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVLLPKGLISSKEDIKDFLEK 672
                         810
                  ....*....|....*...
gi 568955249  960 LQVDRQNYQIGKTKVFLK 977
Cdd:cd01385   673 LNLDRDNYQIGKTKVFLK 690
MYSc smart00242
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...
141-986 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: 887.27  E-value: 0e+00
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249    141 LPRPQADFDDLCNLPELTEANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALAD 220
Cdd:smart00242    1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249    221 VAYYAMLRKHVNQCIVISGESGSGKTQSTNFLIHCLTALS-QKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKF 299
Cdd:smart00242   81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSgSNTEVGSVEDQILESNPILEAFGNAKTLRNNNSSRFGKF 160
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249    300 IQVNYLENGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDLKH 379
Cdd:smart00242  161 IEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQGGCLTVDGIDDAE 240
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249    380 DFERLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKRATGRDEGlEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTV 459
Cdd:smart00242  241 EFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAAS-TVKDKEELSNAAELLGVDPEELEKALTKRKIK 319
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249    460 TVNDKLILPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDmeeavSCLSIGVLDIFGFEDFERNSFEQFCINY 539
Cdd:smart00242  320 TGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDG-----STYFIGVLDIYGFEIFEVNSFEQLCINY 394
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249    540 ANEQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNK 619
Cdd:smart00242  395 ANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFFDNQDCIDLIEKKPPGILSLLDEECRFPKGTDQTFLEKLNQHHKKHP 474
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249    620 YFLGTPVL-EPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLigmdpvavfrwavlraairamavl 698
Cdd:smart00242  475 HFSKPKKKgRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASL------------------------ 530
                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249    699 reagrlraeraekaaagisspatrshmeelprgastpseklyrctgldfsferseeldvnaFEDimafYESRKargqsdl 778
Cdd:smart00242  531 -------------------------------------------------------------FPS----GVSNA------- 538
                           650       660       670       680       690       700       710       720
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249    779 hnqiikslkglpwqgedprrllqslslfqkprtsflkskgikqkqiipknlldskslrliismtlhdrttksllhlHKKK 858
Cdd:smart00242  539 ----------------------------------------------------------------------------GSKK 542
                           730       740       750       760       770       780       790       800
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249    859 KPPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQF 938
Cdd:smart00242  543 RFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFDEFLQRY 622
                           810       820       830       840       850
                    ....*....|....*....|....*....|....*....|....*....|..
gi 568955249    939 QVLLPKDVQPC----REAIAALLEKLQVDRQNYQIGKTKVFLKETERQTLQE 986
Cdd:smart00242  623 RVLLPDTWPPWggdaKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEE 674
MYSc cd00124
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ...
160-977 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  Cd Length: 633  Bit Score: 768.68  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGK-LEPHVFALADVAYYAMLRKHVNQCIVIS 238
Cdd:cd00124     1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSAdLPPHVFAVADAAYRAMLRDGQNQSILIS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  239 GESGSGKTQSTNFLIHCLTALSQKG------YASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRG 312
Cdd:cd00124    81 GESGAGKTETTKLVLKYLAALSGSGssksssSASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLVG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  313 AVVEKYLLEKSRLVSQEKDERNYHVFYYLL----LGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDLKHDFERLQQAM 388
Cdd:cd00124   161 ASIETYLLEKSRVVSQAPGERNFHIFYQLLaglsDGAREELKLELLLSYYYLNDYLNSSGCDRIDGVDDAEEFQELLDAL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  389 EMVGFLPATKKQIFSVLSAILYLGNVTYKKRATGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILP 468
Cdd:cd00124   241 DVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEDSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETITKP 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  469 YSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDmeeAVSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYF 548
Cdd:cd00124   321 LTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDA---AESTSFIGILDIFGFENFEVNSFEQLCINYANEKLQQFF 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  549 TQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPVLE 628
Cdd:cd00124   398 NQHVFKLEQEEYEEEGIDWSFIDFPDNQDCLDLIEGKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKRKA 477
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  629 P-AFIIQHFAGRVKYQIKDFREKNmdymrpdivallrgsdssyvrqligmdpvavfrwavlraairamavlreagrlrae 707
Cdd:cd00124   478 KlEFGIKHYAGDVTYDADGFLEKN-------------------------------------------------------- 501
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  708 raekaaagisspatrshmeelprgastpseklyrctgldfsferseeldvnafedimafyesrkargqsdlhnqiikslk 787
Cdd:cd00124       --------------------------------------------------------------------------------
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  788 glpwqgedprrllqslslfqkprtsflkskgikqKQIIPKNLLDskslrliismtlhdrttksLLhlhkkkkppSISAQF 867
Cdd:cd00124   502 ----------------------------------KDTLPPDLVD-------------------LL---------RSGSQF 519
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  868 QTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPKDVQ 947
Cdd:cd00124   520 RSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAPGATE 599
                         810       820       830
                  ....*....|....*....|....*....|....
gi 568955249  948 PCR----EAIAALLEKLQVDRQNYQIGKTKVFLK 977
Cdd:cd00124   600 KASdskkAAVLALLLLLKLDSSGYQLGKTKVFLR 633
MYSc_Myo7 cd01381
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ...
160-977 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: 693.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISG 239
Cdd:cd01381     1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  240 ESGSGKTQSTNFLIHCLTALSqkGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRGAVVEKYL 319
Cdd:cd01381    81 ESGAGKTESTKLILQYLAAIS--GQHSWIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKIEQYL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  320 LEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDLKHDFERLQQAMEMVGFLPATKK 399
Cdd:cd01381   159 LEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGNCLTCEGRDDAAEFADIRSAMKVLMFTDEEIW 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  400 QIFSVLSAILYLGNVTYKKRATGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILPYSLSEAITARD 479
Cdd:cd01381   239 DIFKLLAAILHLGNIKFEATVVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAEQALDVRD 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  480 SMAKSLYSALFDWIVLRINHALlnKKDMEEAVSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQEE 559
Cdd:cd01381   319 AFVKGIYGRLFIWIVNKINSAI--YKPRGTDSSRTSIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFKLEQEE 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  560 YQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLgTP--VLEPAFIIQHFA 637
Cdd:cd01381   397 YDKEGINWQHIEFVDNQDVLDLIALKPMNIMSLIDEESKFPKGTDQTMLEKLHSTHGNNKNYL-KPksDLNTSFGINHFA 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  638 GRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLIGmdpvavfrwavlraairamavlreagrlraeraekaaagis 717
Cdd:cd01381   476 GVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFN----------------------------------------- 514
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  718 spatrshmEELPRGASTpseklyrctgldfsferseeldvnafedimafyesrkargqsdlhnqiikslkglpwqgedpr 797
Cdd:cd01381   515 --------EDISMGSET--------------------------------------------------------------- 523
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  798 rllqslslfqkprtsflkskgikqkqiipknlldskslrliismtlhdrttksllhlhkKKKPPSISAQFQTSLNKLLEA 877
Cdd:cd01381   524 -----------------------------------------------------------RKKSPTLSSQFRKSLDQLMKT 544
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  878 LGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPkDVQP-----CREA 952
Cdd:cd01381   545 LSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVP-GIPPahktdCRAA 623
                         810       820
                  ....*....|....*....|....*
gi 568955249  953 IAALLEKLQVDRQNYQIGKTKVFLK 977
Cdd:cd01381   624 TRKICCAVLGGDADYQLGKTKIFLK 648
Myosin_head pfam00063
Myosin head (motor domain);
149-977 0e+00

Myosin head (motor domain);


Pssm-ID: 395017  Cd Length: 674  Bit Score: 677.85  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249   149 DDLCNLPELTEANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLR 228
Cdd:pfam00063    2 EDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSMLQ 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249   229 KHVNQCIVISGESGSGKTQSTNFLIHCLTALSQKGYASGVER---TILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYL 305
Cdd:pfam00063   82 DKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGNVGRleeQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQFD 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249   306 ENGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDLKHDFERLQ 385
Cdd:pfam00063  162 AKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQSGCYTIDGIDDSEEFKITD 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249   386 QAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKRAtgRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKL 465
Cdd:pfam00063  242 KAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKER--NDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGRETV 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249   466 ILPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEAVsclsIGVLDIFGFEDFERNSFEQFCINYANEQLQ 545
Cdd:pfam00063  320 SKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASF----IGVLDIYGFEIFEKNSFEQLCINYVNEKLQ 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249   546 YYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDN-KYFLGT 624
Cdd:pfam00063  396 QFFNHHMFKLEQEEYVREGIEWTFIDFGDNQPCIDLIEKKPLGILSLLDEECLFPKATDQTFLDKLYSTFSKHpHFQKPR 475
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249   625 PVLEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLigmdpvavfrwavlraairamavlreagrl 704
Cdd:pfam00063  476 LQGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAEL------------------------------ 525
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249   705 raeraekaaagisspatrshmeelprgastpseklyrctgldfsferseeldvnafedimafyesrkargqsdlhnqiik 784
Cdd:pfam00063      --------------------------------------------------------------------------------
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249   785 slkglpWQGEDPrrllQSLSLFQKPRTSFLKSKgikqkqiipknlldskslrliismtlhdrttksllhlhKKKKPPSIS 864
Cdd:pfam00063  526 ------FPDYET----AESAAANESGKSTPKRT--------------------------------------KKKRFITVG 557
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249   865 AQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL--- 941
Cdd:pfam00063  558 SQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRYRILapk 637
                          810       820       830
                   ....*....|....*....|....*....|....*..
gi 568955249   942 -LPKDVQPCREAIAALLEKLQVDRQNYQIGKTKVFLK 977
Cdd:pfam00063  638 tWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
COG5022 COG5022
Myosin heavy chain [General function prediction only];
149-1079 0e+00

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 647.52  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  149 DDLCNLPELTEANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLR 228
Cdd:COG5022    69 DDLTELSYLNEPAVLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLS 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  229 KHVNQCIVISGESGSGKTQSTNFLIHCLTAL--SQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLE 306
Cdd:COG5022   149 EKENQTIIISGESGAGKTENAKRIMQYLASVtsSSTVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDE 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  307 NGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDLKHDFERLQQ 386
Cdd:COG5022   229 NGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDKIDGIDDAKEFKITLD 308
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  387 AMEMVGFLPATKKQIFSVLSAILYLGNVTYKKratGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLI 466
Cdd:COG5022   309 ALKTIGIDEEEQDQIFKILAAILHIGNIEFKE---DRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIV 385
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  467 LPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEavsclSIGVLDIFGFEDFERNSFEQFCINYANEQLQY 546
Cdd:COG5022   386 VPLNLEQALAIRDSLAKALYSNLFDWIVDRINKSLDHSAAASN-----FIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQ 460
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  547 YFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKK-PTGLFYLLDEESNFPHATSHTLLAKFKQQ--HEDNKYFLG 623
Cdd:COG5022   461 FFNQHMFKLEQEEYVKEGIEWSFIDYFDNQPCIDLIEKKnPLGILSLLDEECVMPHATDESFTSKLAQRlnKNSNPKFKK 540
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  624 TPVLEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLigmdpvavfrwavlraairamavlreagr 703
Cdd:COG5022   541 SRFRDNKFVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTL----------------------------- 591
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  704 lraeraekaaagisspatrshmeelprgastpseklyrctgldfsFERSEELDvnafedimafyesrkargqsdlhnqii 783
Cdd:COG5022   592 ---------------------------------------------FDDEENIE--------------------------- 599
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  784 kslkglpwqgedprrllqslslfqkprtsflkskgikqkqiipknlldskslrliismtlhdrttksllhlhKKKKPPSI 863
Cdd:COG5022   600 ------------------------------------------------------------------------SKGRFPTL 607
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  864 SAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLP 943
Cdd:COG5022   608 GSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSP 687
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  944 --------KDVQPCREAIAALLEKLQVDRQNYQIGKTKVFLKeTERQTLQEKLHGEVLRRIL-QLQSWFRMVLERKHFVQ 1014
Cdd:COG5022   688 skswtgeyTWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFK-AGVLAALEDMRDAKLDNIAtRIQRAIRGRYLRRRYLQ 766
                         890       900       910       920       930       940
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568955249 1015 MKHAALTIQACWRSYRVRRALER---TQAAVYLQAAWRGYLQRQAYHHQRHSIIRLQSLCRGHLQRRS 1079
Cdd:COG5022   767 ALKRIKKIQVIQHGFRLRRLVDYelkWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIKREKKLRE 834
MYSc_Myo15 cd01387
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ...
160-977 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: 630.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISG 239
Cdd:cd01387     1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  240 ESGSGKTQSTNFLIHCLTALSQKGYASGVERtILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVnYLENGIVRGAVVEKYL 319
Cdd:cd01387    81 ESGSGKTEATKLIMQYLAAVNQRRNNLVTEQ-ILEATPLLEAFGNAKTVRNDNSSRFGKYLEV-FFEGGVIVGAITSQYL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  320 LEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDLKHDFERLQQAMEMVGFLPATKK 399
Cdd:cd01387   159 LEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGGNCEIAGKSDADDFRRLLAAMQVLGFSSEEQD 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  400 QIFSVLSAILYLGNVTYKKR-ATGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILPYSLSEAITAR 478
Cdd:cd01387   239 SIFRILASVLHLGNVYFHKRqLRHGQEGVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRERIFTPLTIDQALDAR 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  479 DSMAKSLYSALFDWIVLRINHALLNKKDmeeavSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQE 558
Cdd:cd01387   319 DAIAKALYALLFSWLVTRVNAIVYSGTQ-----DTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVFKLEQE 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  559 EYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPVLEPAFIIQHFAG 638
Cdd:cd01387   394 EYIREQIDWTEIAFADNQPVINLISKKPVGILHILDDECNFPQATDHSFLEKCHYHHALNELYSKPRMPLPEFTIKHYAG 473
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  639 RVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLigmdpvavfrwavlraairamavlreagrlraeraekaaagiSS 718
Cdd:cd01387   474 QVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHL------------------------------------------FS 511
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  719 PATRSHMEELPRGAStpseklyrctgldfsferseeldvnafedimafyesrkargqsdlhnqiikslkglpwqgedprr 798
Cdd:cd01387   512 SHRAQTDKAPPRLGK----------------------------------------------------------------- 526
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  799 llqSLSLFQKPRTsflkskgikqkqiipknlldskslrliismtlhdrttksllhlhkkkkpPSISAQFQTSLNKLLEAL 878
Cdd:cd01387   527 ---GRFVTMKPRT-------------------------------------------------PTVAARFQDSLLQLLEKM 554
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  879 GKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLL------PKDVQPCREA 952
Cdd:cd01387   555 ERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLValklprPAPGDMCVSL 634
                         810       820
                  ....*....|....*....|....*
gi 568955249  953 IAALLEklQVDRQNYQIGKTKVFLK 977
Cdd:cd01387   635 LSRLCT--VTPKDMYRLGATKVFLR 657
MYSc_Myo22 cd14883
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ...
162-977 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: 629.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  162 LLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISGES 241
Cdd:cd14883     3 INTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGES 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  242 GSGKTQSTNFLIHCLTALSQKgyASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRGAVVEKYLLE 321
Cdd:cd14883    83 GAGKTETTKLILQYLCAVTNN--HSWVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGAIIQDYLLE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  322 KSRLVSQEKDERNYHVFYYLLLG--VSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDLKHDFERLQQAMEMVGFLPATKK 399
Cdd:cd14883   161 QSRITFQAPGERNYHVFYQLLAGakHSKELKEKLKLGEPEDYHYLNQSGCIRIDNINDKKDFDHLRLAMNVLGIPEEMQE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  400 QIFSVLSAILYLGNVTYKKrATGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILPYSLSEAITARD 479
Cdd:cd14883   241 GIFSVLSAILHLGNLTFED-IDGETGALTVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQEARDNRD 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  480 SMAKSLYSALFDWIVLRINhallnkkdmeeavSCLS--------IGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQH 551
Cdd:cd14883   320 AMAKALYSRTFAWLVNHIN-------------SCTNpgqknsrfIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHY 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  552 IFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFL-GTPVL-EP 629
Cdd:cd14883   387 VFKLEQEEYEKEGINWSHIVFTDNQECLDLIEKPPLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEkPDRRRwKT 466
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  630 AFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLigmdpvavfrwavlraairamavlreagrlraera 709
Cdd:cd14883   467 EFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKEL----------------------------------- 511
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  710 ekaaagisspatrshmeelprgastpseklyrctgldFSFERSEELDvnafedimafyesrkargqsdlhnqiikslkgl 789
Cdd:cd14883   512 -------------------------------------FTYPDLLALT--------------------------------- 521
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  790 pwqgedprrllqslslfqkprtsflkskgikQKQIIPKNLLDSKSlrliismtlhdrttksllhlhKKKKPPSISAQFQT 869
Cdd:cd14883   522 -------------------------------GLSISLGGDTTSRG---------------------TSKGKPTVGDTFKH 549
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  870 SLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPK--DVQ 947
Cdd:cd14883   550 QLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPRarSAD 629
                         810       820       830
                  ....*....|....*....|....*....|..
gi 568955249  948 PCREAIA--ALLEKLQVDRQNYQIGKTKVFLK 977
Cdd:cd14883   630 HKETCGAvrALMGLGGLPEDEWQVGKTKVFLR 661
MYSc_Myo5 cd01380
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ...
163-977 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: 615.70  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  163 LQNLKLRFMQQK-IYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISGES 241
Cdd:cd01380     4 LHNLKVRFCQRNaIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSGES 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  242 GSGKTQSTNFLIHCLTALS-QKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRGAVVEKYLL 320
Cdd:cd01380    84 GAGKTVSAKYAMRYFATVGgSSSGETQVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANMRTYLL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  321 EKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDLKHDFERLQQAMEMVGFLPATKKQ 400
Cdd:cd01380   164 EKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPVIDGVDDAAEFEETRKALTLLGISEEEQME 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  401 IFSVLSAILYLGNVTYKKRatgRDEGLEVGPPEV-LDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILPYSLSEAITARD 479
Cdd:cd01380   244 IFRILAAILHLGNVEIKAT---RNDSASISPDDEhLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQAIVARD 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  480 SMAKSLYSALFDWIVLRINHALLNKKDmEEAVSClsIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQEE 559
Cdd:cd01380   321 ALAKHIYAQLFDWIVDRINKALASPVK-EKQHSF--IGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQEE 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  560 YQGEGISWHNIDYTDNVGCIHLISKKPtGLFYLLDEESNFPHATSHTLLAKFKQQHE--DNKYFLGTPVLEPAFIIQHFA 637
Cdd:cd01380   398 YVKEEIEWSFIDFYDNQPCIDLIEGKL-GILDLLDEECRLPKGSDENWAQKLYNQHLkkPNKHFKKPRFSNTAFIVKHFA 476
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  638 GRVKYQIKDFREKNMDYMRPDIVALLRGSDSsyvrqligmdpvavfrwavlraairamavlreagrlraeraekaaagis 717
Cdd:cd01380   477 DDVEYQVEGFLEKNRDTVSEEHLNVLKASKN------------------------------------------------- 507
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  718 spatrshmeelprgastpseklyrctgldfsferseeldvnafedimafyesrkargqsdlhnqiikslkglpwqgedpr 797
Cdd:cd01380       --------------------------------------------------------------------------------
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  798 rllqslslfqkprtsflkskgikqkqiipknlldskslrliismtlhdrttksllhlHKkkkpPSISAQFQTSLNKLLEA 877
Cdd:cd01380   508 ---------------------------------------------------------RK----KTVGSQFRDSLILLMET 526
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  878 LGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPKDV---QPCREAIA 954
Cdd:cd01380   527 LNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSKEwlrDDKKKTCE 606
                         810       820
                  ....*....|....*....|...
gi 568955249  955 ALLEKLQVDRQNYQIGKTKVFLK 977
Cdd:cd01380   607 NILENLILDPDKYQFGKTKIFFR 629
MYSc_Myo3 cd01379
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ...
162-977 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: 605.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  162 LLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISGES 241
Cdd:cd01379     3 IVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGES 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  242 GSGKTQSTNFLIHCLTALSQKGYASgVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRGAVVEKYLLE 321
Cdd:cd01379    83 GAGKTESANLLVQQLTVLGKANNRT-LEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEYLLE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  322 KSRLVSQEKDERNYHVFYYLLLGVSEEERLE-FQLKQPQDYFYLNQHNLNIEDGEDL---KHDFERLQQAMEMVGFLPAT 397
Cdd:cd01379   162 KSRVVHQAIGERNFHIFYYIYAGLAEDKKLAkYKLPENKPPRYLQNDGLTVQDIVNNsgnREKFEEIEQCFKVIGFTKEE 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  398 KKQIFSVLSAILYLGNVTYKKRATG--RDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILPYSLSEAI 475
Cdd:cd01379   242 VDSVYSILAAILHIGDIEFTEVESNhqTDKSSRISNPEALNNVAKLLGIEADELQEALTSHSVVTRGETIIRNNTVEEAT 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  476 TARDSMAKSLYSALFDWIVLRINhALLnKKDMEEAVSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKL 555
Cdd:cd01379   322 DARDAMAKALYGRLFSWIVNRIN-SLL-KPDRSASDEPLSIGILDIFGFENFQKNSFEQLCINIANEQIQYYFNQHIFAW 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  556 EQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFkqqhEDN---KYFLGTPVLEPAFI 632
Cdd:cd01379   400 EQQEYLNEGIDVDLIEYEDNRPLLDMFLQKPMGLLALLDEESRFPKATDQTLVEKF----HNNiksKYYWRPKSNALSFG 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  633 IQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQligmdpvavfrwavlraairamavlreagrlraeraeka 712
Cdd:cd01379   476 IHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVRQ--------------------------------------- 516
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  713 aagisspatrshmeelprgastpseklyrctgldfsferseeldvnafedimafyesrkargqsdlhnqiikslkglpwq 792
Cdd:cd01379       --------------------------------------------------------------------------------
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  793 gedprrllqslslfqkprtsflkskgikqkqiipknlldskslrliismtlhdrttksllhlhkkkkppSISAQFQTSLN 872
Cdd:cd01379   517 ---------------------------------------------------------------------TVATYFRYSLM 527
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  873 KLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL---LPKDVQPC 949
Cdd:cd01379   528 DLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYYFLafkWNEEVVAN 607
                         810       820
                  ....*....|....*....|....*...
gi 568955249  950 REAIAALLEKLQVDrqNYQIGKTKVFLK 977
Cdd:cd01379   608 RENCRLILERLKLD--NWALGKTKVFLK 633
MYSc_Myo8 cd01383
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ...
162-977 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: 603.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  162 LLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYenQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISGES 241
Cdd:cd01383     3 VLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAY--RQKLLDSPHVYAVADTAYREMMRDEINQSIIISGES 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  242 GSGKTQSTNFLIHCLTALSqkGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRGAVVEKYLLE 321
Cdd:cd01383    81 GAGKTETAKIAMQYLAALG--GGSSGIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQTYLLE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  322 KSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDLKHDFERLQQAMEMVGFLPATKKQI 401
Cdd:cd01383   159 KSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNQSNCLTIDGVDDAKKFHELKEALDTVGISKEDQEHI 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  402 FSVLSAILYLGNVTYKkrATGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILPYSLSEAITARDSM 481
Cdd:cd01383   239 FQMLAAVLWLGNISFQ--VIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAIDARDAL 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  482 AKSLYSALFDWIVLRINHALlnkkDMEEAVSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQEEYQ 561
Cdd:cd01383   317 AKAIYASLFDWLVEQINKSL----EVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEEYE 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  562 GEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPvlEPAFIIQHFAGRVK 641
Cdd:cd01383   393 LDGIDWTKVDFEDNQECLDLIEKKPLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCFKGER--GGAFTIRHYAGEVT 470
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  642 YQIKDFREKNMDYMRPDIVALLrgsdssyvrqligmdpvavfrwavlraairamavlreagrlraeraekaaagisspat 721
Cdd:cd01383   471 YDTSGFLEKNRDLLHSDLIQLL---------------------------------------------------------- 492
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  722 rshmeelprgaSTPSEKLYRCTgldfsferseeldvnafedimafyeSRKARGQSdlhnqiikslkglpwqgedprrllq 801
Cdd:cd01383   493 -----------SSCSCQLPQLF-------------------------ASKMLDAS------------------------- 511
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  802 slslfQKPRTSFLKSKGIKQKQiipknlldskslrliismtlhdrttksllhlhkkkkppSISAQFQTSLNKLLEALGKA 881
Cdd:cd01383   512 -----RKALPLTKASGSDSQKQ--------------------------------------SVATKFKGQLFKLMQRLENT 548
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  882 EPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPKDVQPCREAIA---ALLE 958
Cdd:cd01383   549 TPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDVSASQDPLStsvAILQ 628
                         810
                  ....*....|....*....
gi 568955249  959 KLQVDRQNYQIGKTKVFLK 977
Cdd:cd01383   629 QFNILPEMYQVGYTKLFFR 647
MYSc_Myo10 cd14873
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ...
160-977 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: 589.07  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLP-IYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVIS 238
Cdd:cd14873     1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  239 GESGSGKTQSTNFLIHCLTALSQ-------KGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVR 311
Cdd:cd14873    81 GESGAGKTESTKLILKFLSVISQqslelslKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  312 GAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDLKHDFERLQQAMEMV 391
Cdd:cd14873   161 GGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNQSGCVEDKTISDQESFREVITAMEVM 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  392 GFLPATKKQIFSVLSAILYLGNVTYKKRAtgrdeGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILPYSL 471
Cdd:cd14873   241 QFSKEEVREVSRLLAGILHLGNIEFITAG-----GAQVSFKTALGRSAELLGLDPTQLTDALTQRSMFLRGEEILTPLNV 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  472 SEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEeavsclSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQH 551
Cdd:cd14873   316 QQAVDSRDSLAMALYARCFEWVIKKINSRIKGKEDFK------SIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKH 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  552 IFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKpTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPVLEPAF 631
Cdd:cd14873   390 IFSLEQLEYSREGLVWEDIDWIDNGECLDLIEKK-LGLLALINEESHFPQATDSTLLEKLHSQHANNHFYVKPRVAVNNF 468
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  632 IIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDssyvrqligmdpvavfrwavlraairamavlreagrlraeraek 711
Cdd:cd14873   469 GVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESR-------------------------------------------- 504
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  712 aaagisspatrshmeelprgastpseklyrctgLDFSFErseeldvnafedimafyesrkargqsdlhnqiikslkglpw 791
Cdd:cd14873   505 ---------------------------------FDFIYD----------------------------------------- 510
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  792 qgedprrllqslsLFQKprtsflkskgikqkqiipknllDSKslrliismtlhdRTTKSLLHLHKKKKPPSISAQFQTSL 871
Cdd:cd14873   511 -------------LFEH----------------------VSS------------RNNQDTLKCGSKHRRPTVSSQFKDSL 543
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  872 NKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLP--KDVQPC 949
Cdd:cd14873   544 HSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRnlALPEDV 623
                         810       820
                  ....*....|....*....|....*...
gi 568955249  950 REAIAALLEKLQVDRQNYQIGKTKVFLK 977
Cdd:cd14873   624 RGKCTSLLQLYDASNSEWQLGKTKVFLR 651
MYSc_Myo1 cd01378
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ...
162-977 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: 576.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  162 LLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISGES 241
Cdd:cd01378     3 INENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGES 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  242 GSGKTQSTNFLIHCLTALSQKGYAS--GVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRGAVVEKYL 319
Cdd:cd01378    83 GAGKTEASKRIMQYIAAVSGGSESEveRVKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGHITNYL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  320 LEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDLKHDFERLQQAMEMVGFLPATKK 399
Cdd:cd01378   163 LEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVIGFTEEEQD 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  400 QIFSVLSAILYLGNVTYKKRATGrdeGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDK---LILPYSLSEAIT 476
Cdd:cd01378   243 SIFRILAAILHLGNIQFAEDEEG---NAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvYEVPLNVEQAAY 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  477 ARDSMAKSLYSALFDWIVLRINHALLNKKDMEEAVsclsIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLE 556
Cdd:cd01378   320 ARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKV----IGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELTLKAE 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  557 QEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPH-ATSHTLLAKFKQQHEDNKYFLGTP----VLEPAF 631
Cdd:cd01378   396 QEEYVREGIEWTPIKYFNNKIICDLIEEKPPGIFAILDDACLTAGdATDQTFLQKLNQLFSNHPHFECPSghfeLRRGEF 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  632 IIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLigmdpvavfrwavlraairamavlreagrlraeraek 711
Cdd:cd01378   476 RIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSL------------------------------------- 518
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  712 aaagisspatrshmeeLPRGASTPSeklyrctgldfsferseeldvnafedimafyesrkargqsdlhnqiikslkglpw 791
Cdd:cd01378   519 ----------------FPEGVDLDS------------------------------------------------------- 527
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  792 qgedprrllqslslfqkprtsflkskgikqkqiipknlldskslrliismtlhdrttksllhlhkKKKPPSISAQFQTSL 871
Cdd:cd01378   528 -----------------------------------------------------------------KKRPPTAGTKFKNSA 542
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  872 NKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPK------- 944
Cdd:cd01378   543 NALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPKtwpawdg 622
                         810       820       830
                  ....*....|....*....|....*....|...
gi 568955249  945 DVQpcrEAIAALLEKLQVDRQNYQIGKTKVFLK 977
Cdd:cd01378   623 TWQ---GGVESILKDLNIPPEEYQMGKTKIFIR 652
MYSc_class_II cd01377
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ...
160-977 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: 575.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISG 239
Cdd:cd01377     1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  240 ESGSGKTQST----NFLIHCLTALSQKGYASG----VERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVR 311
Cdd:cd01377    81 ESGAGKTENTkkviQYLASVAASSKKKKESGKkkgtLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKIA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  312 GAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQ-PQDYFYLNQHNLNIEDGEDlKHDFERLQQAMEM 390
Cdd:cd01377   161 GADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGdPSYYFFLSQGELTIDGVDD-AEEFKLTDEAFDI 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  391 VGFLPATKKQIFSVLSAILYLGNVTYKKRatGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTK------RKTVTVNdk 464
Cdd:cd01377   240 LGFSEEEKMSIFKIVAAILHLGNIKFKQR--RREEQAELDGTEEADKAAHLLGVNSSDLLKALLKprikvgREWVTKG-- 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  465 lilpYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEeavscLSIGVLDIFGFEDFERNSFEQFCINYANEQL 544
Cdd:cd01377   316 ----QNKEQVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQ-----YFIGVLDIAGFEIFEFNSFEQLCINYTNEKL 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  545 QYYFTQHIFKLEQEEYQGEGISWHNIDYtdnvG-----CIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNK 619
Cdd:cd01377   387 QQFFNHHMFVLEQEEYKKEGIEWTFIDF----GldlqpTIDLIEKPNMGILSILDEECVFPKATDKTFVEKLYSNHLGKS 462
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  620 YFLGTPV---LEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLIgmdpvavfrwavlraairama 696
Cdd:cd01377   463 KNFKKPKpkkSEAHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLF--------------------- 521
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  697 vlreagrlraeraekaaagisspatrshmeelprgastpseklyrctgldfsferseeldVNAFEDIMAFYESRKARGqs 776
Cdd:cd01377   522 ------------------------------------------------------------KDYEESGGGGGKKKKKGG-- 539
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  777 dlhnqiikslkglpwqgedprrllqslslfqkprtSFlkskgikqkqiipknlldskslrliismtlhdRTtksllhlhk 856
Cdd:cd01377   540 -----------------------------------SF--------------------------------RT--------- 543
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  857 kkkppsISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTE 936
Cdd:cd01377   544 ------VSQLHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQ 617
                         810       820       830       840
                  ....*....|....*....|....*....|....*....|....*
gi 568955249  937 QFQVLLPKDVQPC----REAIAALLEKLQVDRQNYQIGKTKVFLK 977
Cdd:cd01377   618 RYSILAPNAIPKGfddgKAACEKILKALQLDPELYRIGNTKVFFK 662
MYSc_Myo11 cd01384
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ...
163-977 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: 574.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  163 LQNLKLRFMQQKIYTYAGSILVAINPFKFLP-IYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISGES 241
Cdd:cd01384     4 LHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVSGES 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  242 GSGKTQSTNFLIHCLTALSQKGYASG--VERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRGAVVEKYL 319
Cdd:cd01384    84 GAGKTETTKMLMQYLAYMGGRAVTEGrsVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAAIRTYL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  320 LEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDLKHDFERLQQAMEMVGFLPATKK 399
Cdd:cd01384   164 LERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNQSKCFELDGVDDAEEYRATRRAMDVVGISEEEQD 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  400 QIFSVLSAILYLGNVTYKKRAtgRDEGLEVGPPEV---LDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILPYSLSEAIT 476
Cdd:cd01384   244 AIFRVVAAILHLGNIEFSKGE--EDDSSVPKDEKSefhLKAAAELLMCDEKALEDALCKRVIVTPDGIITKPLDPDAATL 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  477 ARDSMAKSLYSALFDWIVLRINHALLNKKDmeeavSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLE 556
Cdd:cd01384   322 SRDALAKTIYSRLFDWLVDKINRSIGQDPN-----SKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQHVFKME 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  557 QEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFlGTPVLEP-AFIIQH 635
Cdd:cd01384   397 QEEYTKEEIDWSYIEFVDNQDVLDLIEKKPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHKRF-SKPKLSRtDFTIDH 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  636 FAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLigmdpvavfrwavlraairamavlreagrlraeraekaaag 715
Cdd:cd01384   476 YAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGL----------------------------------------- 514
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  716 isspatrshMEELPRGASTPSEKlyrctgldFSferseeldvnafedimafyesrkargqsdlhnqiikslkglpwqged 795
Cdd:cd01384   515 ---------FPPLPREGTSSSSK--------FS----------------------------------------------- 530
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  796 prrllqslslfqkprtsflkskgikqkqiipknlldskslrliismtlhdrttksllhlhkkkkppSISAQFQTSLNKLL 875
Cdd:cd01384   531 ------------------------------------------------------------------SIGSRFKQQLQELM 544
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  876 EALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLP---KDVQPCREA 952
Cdd:cd01384   545 ETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPevlKGSDDEKAA 624
                         810       820
                  ....*....|....*....|....*
gi 568955249  953 IAALLEKLQVdrQNYQIGKTKVFLK 977
Cdd:cd01384   625 CKKILEKAGL--KGYQIGKTKVFLR 647
MYSc_Myo36 cd14897
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ...
160-977 6.77e-163

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: 515.78  E-value: 6.77e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQL-GKLEPHVFALADVAYYAMLRKHVNQCIVIS 238
Cdd:cd14897     1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSVrSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  239 GESGSGKTQSTNFLIHCLTALSQKGYASGVERtILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRGAVVEKY 318
Cdd:cd14897    81 GESGAGKTESTKYMIKHLMKLSPSDDSDLLDK-IVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAKIDDY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  319 LLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYL---NQHNLNIEDGEDLKHD---FERLQQAMEMVG 392
Cdd:cd14897   160 LLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILrddNRNRPVFNDSEELEYYrqmFHDLTNIMKLIG 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  393 FLPATKKQIFSVLSAILYLGNVTYKKraTGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILPYSLS 472
Cdd:cd14897   240 FSEEDISVIFTILAAILHLTNIVFIP--DEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNTIRGERIQSWKSLR 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  473 EAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEAVSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHI 552
Cdd:cd14897   318 QANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDFQIMTRGPSIGILDMSGFENFKINSFDQLCINLSNERLQQYFNDYV 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  553 FKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPVLEPAFI 632
Cdd:cd14897   398 FPRERSEYEIEGIEWRDIEYHDNDDVLELFFKKPLGILPLLDEESTFPQSTDSSLVQKLNKYCGESPRYVASPGNRVAFG 477
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  633 IQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDssyvrqligmdpvavfrwavlraairamavlreagrlraeraeka 712
Cdd:cd14897   478 IRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSN--------------------------------------------- 512
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  713 aagisspatrshmeelprgastpseklyrctgldfsferseeldvnafedimafyesrkargqsdlhNQIIKSLkglpwq 792
Cdd:cd14897   513 -------------------------------------------------------------------NEFISDL------ 519
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  793 gedprrllqslslfqkprtsFLKskgikqkqiipknlldskslrliismtlhdrttksllhlhkkkkppsisaQFQTSLN 872
Cdd:cd14897   520 --------------------FTS--------------------------------------------------YFKRSLS 529
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  873 KLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPKdvqpCREA 952
Cdd:cd14897   530 DLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRYKEICDF----SNKV 605
                         810       820       830
                  ....*....|....*....|....*....|
gi 568955249  953 IAALLEKLQV-----DRQNYQIGKTKVFLK 977
Cdd:cd14897   606 RSDDLGKCQKilktaGIKGYQFGKTKVFLK 635
MYSc_Myo28 cd14889
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ...
162-977 1.34e-158

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: 504.83  E-value: 1.34e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  162 LLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAML----RKHVNQCIVI 237
Cdd:cd14889     3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  238 SGESGSGKTQSTNFLIHCLTALSQKGyaSGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYlENGIVRGAVVEK 317
Cdd:cd14889    83 SGESGAGKTESTKLLLRQIMELCRGN--SQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RNGHVKGAKINE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  318 YLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDLKHDFERLQQAMEMVGFLPAT 397
Cdd:cd14889   160 YLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLLDPGKYRYLNNGAGCKREVQYWKKKYDEVCNAMDMVGFTEQE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  398 KKQIFSVLSAILYLGNVTYKKRATG--RDEGLEVGPpevLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILPYSLSEAI 475
Cdd:cd14889   240 EVDMFTILAGILSLGNITFEMDDDEalKVENDSNGW---LKAAAGQFGVSEEDLLKTLTCTVTFTRGEQIQRHHTKQQAE 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  476 TARDSMAKSLYSALFDWIVLRINHALLNKKDMEeaVSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKL 555
Cdd:cd14889   317 DARDSIAKVAYGRVFGWIVSKINQLLAPKDDSS--VELREIGILDIFGFENFAVNRFEQACINLANEQLQYFFNHHIFLM 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  556 EQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPVLEPAFIIQH 635
Cdd:cd14889   395 EQKEYKKEGIDWKEITYKDNKPILDLFLNKPIGILSLLDEQSHFPQATDESFVDKLNIHFKGNSYYGKSRSKSPKFTVNH 474
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  636 FAGRVKYQIKDFREKNMDYMRPDIVALLRGSdssyvrqligmdpvavfrwavlraAIRAMAVLREagrlraeraekaaag 715
Cdd:cd14889   475 YAGKVTYNASGFLEKNRDTIPASIRTLFINS------------------------ATPLLSVLFT--------------- 515
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  716 isspATRSHmeelpRGASTPseklyrctgldfsferseeldvnafedimafyesRKARGQSDLHNqiikslkglpwqged 795
Cdd:cd14889   516 ----ATRSR-----TGTLMP----------------------------------RAKLPQAGSDN--------------- 537
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  796 prrllqslslfqkprtsflksKGIKQKQiipknlldskslrliismtlhdrttksllhlhkkkkppSISAQFQTSLNKLL 875
Cdd:cd14889   538 ---------------------FNSTRKQ--------------------------------------SVGAQFKHSLGVLM 558
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  876 EALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPK-DVQPCREAIA 954
Cdd:cd14889   559 EKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAERYKILLCEpALPGTKQSCL 638
                         810       820
                  ....*....|....*....|...
gi 568955249  955 ALLEKLQVdrQNYQIGKTKVFLK 977
Cdd:cd14889   639 RILKATKL--VGWKCGKTRLFFK 659
MYSc_Myo6 cd01382
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ...
160-977 1.90e-157

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: 501.39  E-value: 1.90e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLP-IYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVIS 238
Cdd:cd01382     1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  239 GESGSGKTQSTNFLIHCLTAlSQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRGAVVEKY 318
Cdd:cd01382    81 GESGAGKTESTKYILRYLTE-SWGSGAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  319 LLEKSRLVSQEKDERNYHVFYYLLLGVSEEERlEFQLKQPQdyfyLNQHNlniedgedlkhDFERLQQAMEMVGFLPATK 398
Cdd:cd01382   160 LLEKSRICVQSKEERNYHIFYRLCAGAPEDLR-EKLLKDPL----LDDVG-----------DFIRMDKAMKKIGLSDEEK 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  399 KQIFSVLSAILYLGNVTYKKRATGRDEGLEVGP--PEVLDTLSQLLKVKRETLVEVLTKRKTVT----VNDKLIL-PYSL 471
Cdd:cd01382   224 LDIFRVVAAVLHLGNIEFEENGSDSGGGCNVKPksEQSLEYAAELLGLDQDELRVSLTTRVMQTtrggAKGTVIKvPLKV 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  472 SEAITARDSMAKSLYSALFDWIVLRINHALLNKKdmeeavSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQH 551
Cdd:cd01382   304 EEANNARDALAKAIYSKLFDHIVNRINQCIPFET------SSYFIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQFFNER 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  552 IFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNkYFLGTPVL---- 627
Cdd:cd01382   378 ILKEEQELYEKEGLGVKEVEYVDNQDCIDLIEAKLVGILDLLDEESKLPKPSDQHFTSAVHQKHKNH-FRLSIPRKsklk 456
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  628 -------EPAFIIQHFAGRVKYQIKDFREKNMDymrpdivallrgsdssyvrqligmdpvavfrwavlraairamavlre 700
Cdd:cd01382   457 ihrnlrdDEGFLIRHFAGAVCYETAQFIEKNND----------------------------------------------- 489
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  701 agrlraeraekaaagisspatrshmeelprgastpseklyrctgldfsferseeldvnafedimafyesrkargqsDLHN 780
Cdd:cd01382   490 ----------------------------------------------------------------------------ALHA 493
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  781 qiikSLKGLPWQGEDPrrLLQslSLFQKPRTSFLKSKGIKQKqiipknlldsksLRLIismtlhdrttksllhlhkkkkp 860
Cdd:cd01382   494 ----SLESLICESKDK--FIR--SLFESSTNNNKDSKQKAGK------------LSFI---------------------- 531
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  861 pSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQV 940
Cdd:cd01382   532 -SVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSFHDLYNMYKK 610
                         810       820       830       840
                  ....*....|....*....|....*....|....*....|...
gi 568955249  941 LLPKDV---QP---CReaiaALLEKLQVDRQNYQIGKTKVFLK 977
Cdd:cd01382   611 YLPPKLarlDPrlfCK----ALFKALGLNENDFKFGLTKVFFR 649
MYSc_Myo46 cd14907
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ...
160-977 1.29e-155

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: 497.25  E-value: 1.29e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLP-IYNPKYVKMYENQ--------QLGKLEPHVFALADVAYYAMLRKH 230
Cdd:cd14907     1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQiiqngeyfDIKKEPPHIYAIAALAFKQLFENN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  231 VNQCIVISGESGSGKTQSTNFLIHCLTALSQKGYAS------------------GVERTILGAGPVLEAFGNAKTAHNNN 292
Cdd:cd14907    81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQQEQNSeevltltssiratskstkSIEQKILSCNPILEAFGNAKTVRNDN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  293 SSRFGKF--IQVNYLENGIVrGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQP--QD-YFYLNQ- 366
Cdd:cd14907   161 SSRFGKYvsILVDKKKRKIL-GARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNQlsGDrYDYLKKs 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  367 --HNLNIEDGEDLkhdFERLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKRATGRDEGLEVGPPEVLDTLSQLLKV 444
Cdd:cd14907   240 ncYEVDTINDEKL---FKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTLDDNSPCCVKNKETLQIIAKLLGI 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  445 KRETLVEVLTKRKTVTVNDKLILPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNK---KDMEEAVSCLSIGVLDI 521
Cdd:cd14907   317 DEEELKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTIMPKdekDQQLFQNKYLSIGLLDI 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  522 FGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQEEYQGEGISWH--NIDYTDNVGCIHLISKKPTGLFYLLDEESNF 599
Cdd:cd14907   397 FGFEVFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYlnQLSYTDNQDVIDLLDKPPIGIFNLLDDSCKL 476
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  600 PHATSHTLLAKFKQQHEDNKYFLGTPVL-EPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDssyvrqligmd 678
Cdd:cd14907   477 ATGTDEKLLNKIKKQHKNNSKLIFPNKInKDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSK----------- 545
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  679 pvavfrwavlraairamavlreagrlraeraekaaagisspatrshmeelprgastpseklyrctgldfsferseeldvn 758
Cdd:cd14907       --------------------------------------------------------------------------------
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  759 afedimafyesrkargqsdlhNQIIKSLkglpWQGEDprrlLQSLSLFQKPRTSFLKSKgikqkqiipknlldskslrli 838
Cdd:cd14907   546 ---------------------NRIISSI----FSGED----GSQQQNQSKQKKSQKKDK--------------------- 575
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  839 ismtlhdrttksllhlhkkkkppSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETV 918
Cdd:cd14907   576 -----------------------FLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLESI 632
                         810       820       830       840       850
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568955249  919 RIRRSGYSAKYTFQDFTEQFQVLlpkdvqpcreaiaalleklqvdRQNYQIGKTKVFLK 977
Cdd:cd14907   633 RVRKQGYPYRKSYEDFYKQYSLL----------------------KKNVLFGKTKIFMK 669
MYSc_Myo4 cd14872
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ...
160-974 9.43e-152

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: 485.43  E-value: 9.43e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISG 239
Cdd:cd14872     1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  240 ESGSGKTQSTNfliHCLTALSQ-KGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRGAVVEKY 318
Cdd:cd14872    81 ESGAGKTEATK---QCLSFFAEvAGSTNGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGASTENY 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  319 LLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQhNLNIEdGEDLKHDFERLQQAMEMVGFLPATK 398
Cdd:cd14872   158 LLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGWGSSAAYGYLSLSG-CIEVE-GVDDVADFEEVVLAMEQLGFDDADI 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  399 KQIFSVLSAILYLGNVTYKKRATGRD-EGLEVGPPEVLDTLSQLLKVKRETLVEVLT-KRKTVTVNDKLILPYSLSEAIT 476
Cdd:cd14872   236 NNVMSLIAAILKLGNIEFASGGGKSLvSGSTVANRDVLKEVATLLGVDAATLEEALTsRLMEIKGCDPTRIPLTPAQATD 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  477 ARDSMAKSLYSALFDWIVLRINHALlnkKDMEEAVSCLsIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLE 556
Cdd:cd14872   316 ACDALAKAAYSRLFDWLVKKINESM---RPQKGAKTTF-IGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTFKLE 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  557 QEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPVL--EPAFIIQ 634
Cdd:cd14872   392 EALYQSEGVKFEHIDFIDNQPVLDLIEKKQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKSTFVYAEVRtsRTEFIVK 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  635 HFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDssyvrqligmdpvavfrwavlraairamavlreagrlraeraekaaa 714
Cdd:cd14872   472 HYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSK----------------------------------------------- 504
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  715 gisspatrshmeelprgastpseklyrctgldfsferseeldvnafedimafyesrkargqsdlhNQIIKSLKglpwqge 794
Cdd:cd14872   505 -----------------------------------------------------------------NKLIAVLF------- 512
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  795 dprrllqslslfqkprtsflkskgikqkqiiPKNLLDSKSLRliismtlhdrttksllhlhkkkkpPSISAQFQTSLNKL 874
Cdd:cd14872   513 -------------------------------PPSEGDQKTSK------------------------VTLGGQFRKQLSAL 537
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  875 LEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLL-------PKDVq 947
Cdd:cd14872   538 MTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFLVktiakrvGPDD- 616
                         810       820
                  ....*....|....*....|....*..
gi 568955249  948 pcREAIAALLEKLQVDRQNYQIGKTKV 974
Cdd:cd14872   617 --RQRCDLLLKSLKQDFSKVQVGKTRV 641
MYSc_Myo29 cd14890
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ...
160-977 1.21e-147

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: 474.65  E-value: 1.21e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLP-IYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHV----NQC 234
Cdd:cd14890     1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQSGVldpsNQS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  235 IVISGESGSGKTQSTNFLIHCL---TALSQKGYASG--------------VERTILGAGPVLEAFGNAKTAHNNNSSRFG 297
Cdd:cd14890    81 IIISGESGAGKTEATKIIMQYLariTSGFAQGASGEgeaaseaieqtlgsLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  298 KFIQVNYLENGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLnQHNLNIEDGEDL 377
Cdd:cd14890   161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYL-RGECSSIPSCDD 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  378 KHDFERLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYKkrATGRDEGLE-VGPPEVLDTLSQLLKVKRETLVEVLTKR 456
Cdd:cd14890   240 AKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFE--SENDTTVLEdATTLQSLKLAAELLGVNEDALEKALLTR 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  457 kTVTVNDKLIL-PYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEavsclSIGVLDIFGFEDFERNSFEQF 535
Cdd:cd14890   318 -QLFVGGKTIVqPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWG-----FIGVLDIYGFEKFEWNTFEQL 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  536 CINYANEQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPT---GLFYLLD-------EESNfphatsH 605
Cdd:cd14890   392 CINYANEKLQRHFNQHMFEVEQVEYSNEGIDWQYITFNDNQACLELIEGKVNgkpGIFITLDdcwrfkgEEAN------K 465
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  606 TLLAKFKQQH-------------EDNKYFLgTPVLEPA--FIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSy 670
Cdd:cd14890   466 KFVSQLHASFgrksgsggtrrgsSQHPHFV-HPKFDADkqFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSRRS- 543
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  671 vrqligmdpvavfrwavlraairamavLREAgrlraeraekaaagisspatrshmeelprgastpseklyrctgldfsfe 750
Cdd:cd14890   544 ---------------------------IREV------------------------------------------------- 547
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  751 rseeldvnafedimafyesrkargqsdlhnqiikslkglpwqgedprrllqslslfqkprtsflkskgikqkqiipknll 830
Cdd:cd14890       --------------------------------------------------------------------------------
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  831 dskslrliismtlhdrttksllhlhkkkkppSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLR 910
Cdd:cd14890   548 -------------------------------SVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLK 596
                         810       820       830       840       850       860
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568955249  911 YTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPkDVQPCREAIAALLEKLQVDRQNYQIGKTKVFLK 977
Cdd:cd14890   597 YSGMMEAIQIRQQGFALREEHDSFFYDFQVLLP-TAENIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662
MYSc_Myo27 cd14888
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ...
160-977 9.67e-147

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: 472.25  E-value: 9.67e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPiynpkyvKMYENQQLGKL-------EPHVFALADVAYYAMLRKHVN 232
Cdd:cd14888     1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIP-------GLYSDEMLLKFiqpsiskSPHVFSTASSAYQGMCNNKKS 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  233 QCIVISGESGSGKTQSTNF---LIHCLTALSQKGYaSGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGI 309
Cdd:cd14888    74 QTILISGESGAGKTESTKYvmkFLACAGSEDIKKR-SLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSKLKS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  310 VR---------GAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSE--------EERLE--------------FQLKQP 358
Cdd:cd14888   153 KRmsgdrgrlcGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREakntglsyEENDEklakgadakpisidMSSFEP 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  359 QDYF-YLNQHNLNIEDGEDLKHDFERLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKRAtGRDEG--LEVGPPEVL 435
Cdd:cd14888   233 HLKFrYLTKSSCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNE-ACSEGavVSASCTDDL 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  436 DTLSQLLKVKRETLVEVLTKRKTVTVNDKLILPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMeeavSCLS 515
Cdd:cd14888   312 EKVASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDN----SLLF 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  516 IGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDE 595
Cdd:cd14888   388 CGVLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFPDNQDCVDLLQEKPLGIFCMLDE 467
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  596 ESNFPHATSHTLLAKFKQQHEDNKYFLGTPVLEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLI 675
Cdd:cd14888   468 ECFVPGGKDQGLCNKLCQKHKGHKRFDVVKTDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNLF 547
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  676 gmdpvavfrwavlraairamavlreagrlraeraekaaagisspatrshmeelprgastpSEKLYRCTGLDFsferseel 755
Cdd:cd14888   548 ------------------------------------------------------------SAYLRRGTDGNT-------- 559
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  756 dvnafedimafyesrkargqsdlhnqiikslkglpwqgedprrllqslslfqkprtsflkskgikqkqiipknlldsksl 835
Cdd:cd14888       --------------------------------------------------------------------------------
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  836 rliismtlhdrttksllhlhKKKKPPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGML 915
Cdd:cd14888   560 --------------------KKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGVL 619
                         810       820       830       840       850       860
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568955249  916 ETVRIRRSGYSAKYTFQDFTEQFQVLLPKDvqpcreaiaallEKLQVdrQNYQIGKTKVFLK 977
Cdd:cd14888   620 QAVQVSRAGYPVRLSHAEFYNDYRILLNGE------------GKKQL--SIWAVGKTLCFFK 667
MYSc_Myo40 cd14901
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ...
160-976 7.87e-143

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: 460.79  E-value: 7.87e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYN----PKYVKMYENQQLG--KLEPHVFALADVAYYAMLRKHV-- 231
Cdd:cd14901     1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDdetkEAYYEHGERRAAGerKLPPHVYAVADKAFRAMLFASRgq 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  232 --NQCIVISGESGSGKTQSTNFLIHCLTALS--QKGYASGVERT-----ILGAGPVLEAFGNAKTAHNNNSSRFGKFIQV 302
Cdd:cd14901    81 kcDQSILVSGESGAGKTETTKIIMNYLASVSsaTTHGQNATEREnvrdrVLESNPILEAFGNARTNRNNNSSRFGKFIRL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  303 NYLENGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNI-EDGEDLKHDF 381
Cdd:cd14901   161 GFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLNSSQCYDrRDGVDDSVQY 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  382 ERLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKrATGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTV 461
Cdd:cd14901   241 AKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVK-KDGEGGTFSMSSLANVRAACDLLGLDMDVLEKTLCTREIRAG 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  462 NDKLILPYSLSEAITARDSMAKSLYSALFDWIVLRINHALlnkKDMEEAVSCLSIGVLDIFGFEDFERNSFEQFCINYAN 541
Cdd:cd14901   320 GEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESI---AYSESTGASRFIGIVDIFGFEIFATNSLEQLCINFAN 396
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  542 EQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYF 621
Cdd:cd14901   397 EKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYPNNDACVAMFEARPTGLFSLLDEQCLLPRGNDEKLANKYYDLLAKHASF 476
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  622 lGTPVLEPA---FIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVrqligmdpvavfrwavlraairamavl 698
Cdd:cd14901   477 -SVSKLQQGkrqFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFL--------------------------- 528
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  699 reagrlraeraekaaagisspatrshmeelprgastpseklyrctgldfsferseeldvnafedimafyesrkargqsdl 778
Cdd:cd14901       --------------------------------------------------------------------------------
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  779 hnqiikslkglpwqgedprrllqslslfqkprtsflkskgikqkqiipknlldskslrliismtlhdrttksllhlhkkk 858
Cdd:cd14901       --------------------------------------------------------------------------------
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  859 kPPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQF 938
Cdd:cd14901   529 -SSTVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHTY 607
                         810       820       830       840
                  ....*....|....*....|....*....|....*....|....*..
gi 568955249  939 QVLLP---KDVQPCREAIAALLEKLQV------DRQNYQIGKTKVFL 976
Cdd:cd14901   608 SCLAPdgaSDTWKVNELAERLMSQLQHselnieHLPPFQVGKTKVFL 654
MYSc_Myo42 cd14903
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ...
160-977 1.62e-142

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: 460.01  E-value: 1.62e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLP-IYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVIS 238
Cdd:cd14903     1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  239 GESGSGKTQSTNFLIHCLTALsqkgyASGVE----RTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRGAV 314
Cdd:cd14903    81 GESGAGKTETTKILMNHLATI-----AGGLNdstiKKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLVGAK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  315 VEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQhNLNIEDGEDLKHdFERLQQAMEMVGFL 394
Cdd:cd14903   156 CRTYLLEKTRVISHERPERNYHIFYQLLASPDVEERLFLDSANECAYTGANK-TIKIEGMSDRKH-FARTKEALSLIGVS 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  395 PATKKQIFSVLSAILYLGNVTYKKRATGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILPYSLSEA 474
Cdd:cd14903   234 EEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSAIAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKKDQA 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  475 ITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEavsclSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFK 554
Cdd:cd14903   314 EDCRDALAKAIYSNVFDWLVATINASLGNDAKMAN-----HIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFK 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  555 LEQEEYQGEGISWHNIDYTDNVGCIHLISKKpTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPVLEPA-FII 633
Cdd:cd14903   389 TVQIEYEEEGIRWAHIDFADNQDVLAVIEDR-LGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFPRTSRTqFTI 467
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  634 QHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLIGmdpvavfrwavLRAAIRAMAVLREAGRlraeraekaa 713
Cdd:cd14903   468 KHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFK-----------EKVESPAAASTSLARG---------- 526
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  714 agisspatrshmeelprgastpseklyrctgldfsferseeldvnafedimafyeSRKARGQsdlhnqiikslkglpwqg 793
Cdd:cd14903   527 -------------------------------------------------------ARRRRGG------------------ 533
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  794 edprrllqslslfqkprtsflkskgikqkqiipknlldskslrliismTLHDRTtksllhlhkkkkppsISAQFQTSLNK 873
Cdd:cd14903   534 ------------------------------------------------ALTTTT---------------VGTQFKDSLNE 550
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  874 LLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLP---KDVQPCR 950
Cdd:cd14903   551 LMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFLPegrNTDVPVA 630
                         810       820
                  ....*....|....*....|....*...
gi 568955249  951 EAIAALLEKLQVDR-QNYQIGKTKVFLK 977
Cdd:cd14903   631 ERCEALMKKLKLESpEQYQMGLTRIYFQ 658
MYSc_Myo31 cd14892
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ...
160-977 1.70e-142

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: 460.00  E-value: 1.70e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLP-IYN-PKYVKMYENQQLGKL-EPHVFALADVAYYAMLR----KHVN 232
Cdd:cd14892     1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPlLYDvPGFDSQRKEEATASSpPPHVFSIAERAYRAMKGvgkgQGTP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  233 QCIVISGESGSGKTQSTNFLIHCLTALSQ-----------KGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQ 301
Cdd:cd14892    81 QSIVVSGESGAGKTEASKYIMKYLATASKlakgastskgaANAHESIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  302 VNYLENGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDLKHDF 381
Cdd:cd14892   161 IHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGNCVEVDGVDDATEF 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  382 ERLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKRATGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTV 461
Cdd:cd14892   241 KQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDVFAQSADGVNVAKAAGLLGVDAAELMFKLVTQTTSTA 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  462 NDK-LILPYSLSEAITARDSMAKSLYSALFDWIVLRINHA------LLNKKDMEEAVSCLsIGVLDIFGFEDFERNSFEQ 534
Cdd:cd14892   321 RGSvLEIKLTAREAKNALDALCKYLYGELFDWLISRINAChkqqtsGVTGGAASPTFSPF-IGILDIFGFEIMPTNSFEQ 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  535 FCINYANEQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATS-HTLLAKFKQ 613
Cdd:cd14892   400 LCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQDNQDCLDLIQKKPLGLLPLLEEQMLLKRKTTdKQLLTIYHQ 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  614 QHEDNKYFLGTPVLE-PAFIIQHFAGRVKYQIKDFREKNMDymrpdivallrgsdssyvrqligmdpvavfrwavlraai 692
Cdd:cd14892   480 THLDKHPHYAKPRFEcDEFVLRHYAGDVTYDVHGFLAKNND--------------------------------------- 520
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  693 ramavlreagrlraeraekaaagisspatrshmeelprgastpseklyrctgldfsferseeldvnafedimafyesrka 772
Cdd:cd14892       --------------------------------------------------------------------------------
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  773 rgqsDLHNQIIkslkglpwqgedprrllqslslfqkprtsflkskgikqkqiipkNLLDSKSlrliismtlhdrttksll 852
Cdd:cd14892   521 ----NLHDDLR--------------------------------------------DLLRSSS------------------ 534
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  853 hlhkkkkppsisaQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQ 932
Cdd:cd14892   535 -------------KFRTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREGFPIRRQFE 601
                         810       820       830       840       850
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568955249  933 DFTEQFQVLL-----------PKDVQPCREAIAALLEKlQVDRQNYQIGKTKVFLK 977
Cdd:cd14892   602 EFYEKFWPLArnkagvaaspdACDATTARKKCEEIVAR-ALERENFQLGRTKVFLR 656
MYSc_Myo35 cd14896
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ...
163-977 1.64e-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: 450.77  E-value: 1.64e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  163 LQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISGESG 242
Cdd:cd14896     4 LLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSGHSG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  243 SGKTQSTNFLIHCLTALSQKGyASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVnYLENGIVRGAVVEKYLLEK 322
Cdd:cd14896    84 SGKTEAAKKIVQFLSSLYQDQ-TEDRLRQPEDVLPILESFGHAKTILNANASRFGQVLRL-HLQHGVIVGASVSHYLLET 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  323 SRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDLKHDFERLQQAMEMVGFLPATKKQIF 402
Cdd:cd14896   162 SRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGACRLQGKEDAQDFEGLLKALQGLGLCAEELTAIW 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  403 SVLSAILYLGNVTYKKRATGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILPYSLSEAITARDSMA 482
Cdd:cd14896   242 AVLAAILQLGNICFSSSERESQEVAAVSSWAEIHTAARLLQVPPERLEGAVTHRVTETPYGRVSRPLPVEGAIDARDALA 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  483 KSLYSALFDWIVLRINhALLNKKDMEEAVSclSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQEEYQG 562
Cdd:cd14896   322 KTLYSRLFTWLLKRIN-AWLAPPGEAESDA--TIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLLAQEEEECQR 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  563 EGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPVLEPAFIIQHFAGRVKY 642
Cdd:cd14896   399 ELLPWVPIPQPPRESCLDLLVDQPHSLLSILDDQTWLSQATDHTFLQKCHYHHGDHPSYAKPQLPLPVFTVRHYAGTVTY 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  643 QIKDFREKNMDYMRPDIVALLRGSDssyvRQLIGmdpvavfrwavlraairamavlreagrlraeraekaaagisspatr 722
Cdd:cd14896   479 QVHKFLNRNRDQLDPAVVEMLAQSQ----LQLVG---------------------------------------------- 508
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  723 shmeelprgastpseklyrctgldfsferseeldvnafedimafyesrkargqsdlhnqiikslkglpwqgedprrllqs 802
Cdd:cd14896       --------------------------------------------------------------------------------
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  803 lSLFQKPRTSFlkskgikqkqiipknlldskslrliismtlhdrttksllhlHKKKKPPSISAQFQTSLNKLLEALGKAE 882
Cdd:cd14896   509 -SLFQEAEPQY-----------------------------------------GLGQGKPTLASRFQQSLGDLTARLGRSH 546
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  883 PFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLpKDVQPC---REAIAALLEK 959
Cdd:cd14896   547 VYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALG-SERQEAlsdRERCGAILSQ 625
                         810
                  ....*....|....*....
gi 568955249  960 -LQVDRQNYQIGKTKVFLK 977
Cdd:cd14896   626 vLGAESPLYHLGATKVLLK 644
MYSc_Myo30 cd14891
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ...
160-666 4.11e-135

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: 438.32  E-value: 4.11e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  160 ANLLQNLKLRFM--QQKIYTYAGSILVAINPFKFLPiyNPKyVKMYENQQLGKLEPHVFALADVAYYAM-LRKHV--NQC 234
Cdd:cd14891     1 AGILHNLEERSKldNQRPYTFMANVLIAVNPLRRLP--EPD-KSDYINTPLDPCPPHPYAIAEMAYQQMcLGSGRmqNQS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  235 IVISGESGSGKTQSTNFLIHCLT-----------------ALSQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFG 297
Cdd:cd14891    78 IVISGESGAGKTETSKIILRFLTtravggkkasgqdieqsSKKRKLSVTSLDERLMDTNPILESFGNAKTLRNHNSSRFG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  298 KFIQVNYLENGI-VRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGED 376
Cdd:cd14891   158 KFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNQSGCVSDDNID 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  377 LKHDFERLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKRAT--GRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLT 454
Cdd:cd14891   238 DAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTseGEAEIASESDKEALATAAELLGVDEEALEKVIT 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  455 KRKTVTVNDKLILPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDmeeavSCLSIGVLDIFGFEDFER-NSFE 533
Cdd:cd14891   318 QREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPD-----PLPYIGVLDIFGFESFETkNDFE 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  534 QFCINYANEQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQ 613
Cdd:cd14891   393 QLLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWPDNRECLDLIASKPNGILPLLDNEARNPNPSDAKLNETLHK 472
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568955249  614 QHEDNKYFLGTPV--LEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGS 666
Cdd:cd14891   473 THKRHPCFPRPHPkdMREMFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASS 527
PTZ00014 PTZ00014
myosin-A; Provisional
148-1052 3.25e-132

myosin-A; Provisional


Pssm-ID: 240229 [Multi-domain]  Cd Length: 821  Bit Score: 436.38  E-value: 3.25e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  148 FDDLCNLPELTEANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYEN-QQLGKLEPHVFALADVAYYAM 226
Cdd:PTZ00014   98 YGDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDaKDSDKLPPHVFTTARRALENL 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  227 LRKHVNQCIVISGESGSGKTQSTNFLIhcltalsqKGYASGV--------ERTILGAGPVLEAFGNAKTAHNNNSSRFGK 298
Cdd:PTZ00014  178 HGVKKSQTIIVSGESGAGKTEATKQIM--------RYFASSKsgnmdlkiQNAIMAANPVLEAFGNAKTIRNNNSSRFGR 249
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  299 FIQVNYLENGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDLK 378
Cdd:PTZ00014  250 FMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPKCLDVPGIDDVK 329
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  379 hDFERLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKRAT-GRDEGLEVGP--PEVLDTLSQLLKVKRETLVEVLTK 455
Cdd:PTZ00014  330 -DFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEgGLTDAAAISDesLEVFNEACELLFLDYESLKKELTV 408
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  456 RKTVTVNDKLILPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEeavscLSIGVLDIFGFEDFERNSFEQF 535
Cdd:PTZ00014  409 KVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFK-----VFIGMLDIFGFEVFKNNSLEQL 483
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  536 CINYANEQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQH 615
Cdd:PTZ00014  484 FINITNEMLQKNFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGKSVLSILEDQCLAPGGTDEKFVSSCNTNL 563
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  616 EDNKYFLGTPV-LEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLigmdpvavfrwavlraaira 694
Cdd:PTZ00014  564 KNNPKYKPAKVdSNKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDL-------------------- 623
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  695 mavlreagrlraeraekaaagisspatrshmeelprgastpseklyrctgldfsferseeldvnaFEDIMAfYESRKARG 774
Cdd:PTZ00014  624 -----------------------------------------------------------------FEGVEV-EKGKLAKG 637
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  775 QsdlhnqiikslkglpwqgedprrllqslslfqkprtsflkskgikqkqiipknlldskslrLIISmtlhdrttksllhl 854
Cdd:PTZ00014  638 Q-------------------------------------------------------------LIGS-------------- 642
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  855 hkkkkppsisaQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDF 934
Cdd:PTZ00014  643 -----------QFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEF 711
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  935 TEQFQVL-LP----KDVQPcREAIAALLEKLQVDRQNYQIGKTKVFLKETERQTLQEKLHgevlrriLQLQSWfrmvler 1009
Cdd:PTZ00014  712 LSQFKYLdLAvsndSSLDP-KEKAEKLLERSGLPKDSYAIGKTMVFLKKDAAKELTQIQR-------EKLAAW------- 776
                         890       900       910       920
                  ....*....|....*....|....*....|....*....|....
gi 568955249 1010 KHFVQMkhaaltIQACWRSYRVRRAL-ERTQAAVYLQAAWRGYL 1052
Cdd:PTZ00014  777 EPLVSV------LEALILKIKKKRKVrKNIKSLVRIQAHLRRHL 814
MYSc_Myo43 cd14904
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ...
160-977 3.00e-129

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: 422.04  E-value: 3.00e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLP-IYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVIS 238
Cdd:cd14904     1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  239 GESGSGKTQSTNFLIHCLTALSQKGYASGVERTIlGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRGAVVEKY 318
Cdd:cd14904    81 GESGAGKTETTKIVMNHLASVAGGRKDKTIAKVI-DVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAKCETY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  319 LLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIE-DGEDLKHDFERLQQAMEMVGFLPAT 397
Cdd:cd14904   160 LLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLGDSLAQMQiPGLDDAKLFASTQKSLSLIGLDNDA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  398 KKQIFSVLSAILYLGNVTYKKRAtgrDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILPYSLSEAITA 477
Cdd:cd14904   240 QRTLFKILSGVLHLGEVMFDKSD---ENGSRISNGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLAPVEAEEN 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  478 RDSMAKSLYSALFDWIVLRINHALLNKKDMEEAvsclSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQ 557
Cdd:cd14904   317 RDALAKAIYSKLFDWMVVKINAAISTDDDRIKG----QIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKTVE 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  558 EEYQGEGISWHNIDYTDNVGCIHLISKKpTGLFYLLDEESNFPHATSHTLLAKFKQQHE---DNKYFLGTPVLEPAFIIQ 634
Cdd:cd14904   393 EEYIREGLQWDHIEYQDNQGIVEVIDGK-MGIIALMNDHLRQPRGTEEALVNKIRTNHQtkkDNESIDFPKVKRTQFIIN 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  635 HFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLIGmdpvavfrwavlraairamavlreagrlraeraekaaa 714
Cdd:cd14904   472 HYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFG-------------------------------------- 513
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  715 giSSPATRSHMEelprgasTPSEKlyrctgldfsferseeldvnafedimafyesrkargqsdlhnqiikslkglpwqge 794
Cdd:cd14904   514 --SSEAPSETKE-------GKSGK-------------------------------------------------------- 528
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  795 dprrllqslslfqkprtsflkskgikqkqiipknlldskslrliismtlhdrttksllhlhKKKKPPSISAQFQTSLNKL 874
Cdd:cd14904   529 -------------------------------------------------------------GTKAPKSLGSQFKTSLSQL 547
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  875 LEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLP-----KDV-QP 948
Cdd:cd14904   548 MDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFPpsmhsKDVrRT 627
                         810       820
                  ....*....|....*....|....*....
gi 568955249  949 CREAIAALLEKLQVDrqnYQIGKTKVFLK 977
Cdd:cd14904   628 CSVFMTAIGRKSPLE---YQIGKSLIYFK 653
RhoGAP_myosin_IXB cd04407
RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
1704-1889 4.73e-128

RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in myosins IXB. Class IX myosins contain a characteristic head domain, a neck domain and a tail domain which contains a C6H2-zinc binding motif and a Rho-GAP domain. Class IX myosins are single-headed, processive myosins that are partly cytoplasmic, and partly associated with membranes and the actin cytoskeleton. Class IX myosins are implicated in the regulation of neuronal morphogenesis and function of sensory systems, like the inner ear. There are two major isoforms, myosin IXA and IXB with several splice variants, which are both expressed in developing neurons Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239872 [Multi-domain]  Cd Length: 186  Bit Score: 399.37  E-value: 4.73e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1704 FGVCVDSLTSDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKLEDFPIHAITGVLKQWLRE 1783
Cdd:cd04407     1 FGVRVGSLTSNKTSVPIVLEKLLEHVEMHGLYTEGIYRKSGSANRMKELHQLLQADPENVKLENYPIHAITGLLKQWLRE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1784 LPEPLMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRC 1863
Cdd:cd04407    81 LPEPLMTFAQYNDFLRAVELPEKQEQLQAIYRVLEQLPTANHNTLERLIFHLVKVALEEDVNRMSPNALAIVFAPCLLRC 160
                         170       180
                  ....*....|....*....|....*.
gi 568955249 1864 PDNSDPLTSMKDVLKITTCVEMLIKE 1889
Cdd:cd04407   161 PDSSDPLTSMKDVAKTTTCVEMLIKE 186
MYSc_Myh10 cd14920
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ...
160-977 9.24e-128

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: 418.65  E-value: 9.24e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISG 239
Cdd:cd14920     1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  240 ESGSGKTQSTNFLIHCLT--ALSQKGYASG-----VERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRG 312
Cdd:cd14920    81 ESGAGKTENTKKVIQYLAhvASSHKGRKDHnipgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  313 AVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDlKHDFERLQQAMEMVG 392
Cdd:cd14920   161 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQD-KDNFQETMEAMHIMG 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  393 FLPATKKQIFSVLSAILYLGNVTYKKRATGRDEGLevgpPE--VLDTLSQLLKVK-RETLVEVLTKRKTVTvNDKLILPY 469
Cdd:cd14920   240 FSHEEILSMLKVVSSVLQFGNISFKKERNTDQASM----PEntVAQKLCHLLGMNvMEFTRAILTPRIKVG-RDYVQKAQ 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  470 SLSEAITARDSMAKSLYSALFDWIVLRINHALlnkkDMEEAVSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFT 549
Cdd:cd14920   315 TKEQADFAVEALAKATYERLFRWLVHRINKAL----DRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  550 QHIFKLEQEEYQGEGISWHNIDY-TDNVGCIHLISK--KPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGT-- 624
Cdd:cd14920   391 HTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPrq 470
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  625 PVLEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLigmdpvavfrwavlraairamavlreagrl 704
Cdd:cd14920   471 LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAEL------------------------------ 520
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  705 raeraekaaagisspatrshmeelprgastpseklyrctgldfsferseeldvnafedimafyesrkargqsdlhnqiik 784
Cdd:cd14920       --------------------------------------------------------------------------------
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  785 slkglpWQGEDprRLLQSLSLFQKPRTSFlkSKGIKQKqiipKNLLdskslrliismtlhdRTTKSLlhlhkkkkppsis 864
Cdd:cd14920   521 ------WKDVD--RIVGLDQVTGMTETAF--GSAYKTK----KGMF---------------RTVGQL------------- 558
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  865 aqFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL--- 941
Cdd:cd14920   559 --YKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILtpn 636
                         810       820       830
                  ....*....|....*....|....*....|....*..
gi 568955249  942 -LPKDVQPCREAIAALLEKLQVDRQNYQIGKTKVFLK 977
Cdd:cd14920   637 aIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
MYSc_Myo41 cd14902
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ...
160-952 1.52e-127

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: 419.30  E-value: 1.52e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLP-IYNPKYVKMYE--------NQQLGKLEPHVFALADVAYYAMLR-K 229
Cdd:cd14902     1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKpE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  230 HVNQCIVISGESGSGKTQSTNFLIHCLTAL--------SQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQ 301
Cdd:cd14902    81 RRNQSILVSGESGSGKTESTKFLMQFLTSVgrdqssteQEGSDAVEIGKRILQTNPILESFGNAQTIRNDNSSRFGKFIK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  302 VNYLENGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDLKHDF 381
Cdd:cd14902   161 IQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELLNSYGPSFARKRAVADKY 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  382 ERLQ----QAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKrATGRDEGLEVGPP--EVLDTLSQLLKVKRETLVEVLTK 455
Cdd:cd14902   241 AQLYvetvRAFEDTGVGELERLDIFKILAALLHLGNVNFTA-ENGQEDATAVTAAsrFHLAKCAELMGVDVDKLETLLSS 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  456 RKTVTVNDKLILPYSLSEAITARDSMAKSLYSALFDWIVLR----INHALLNKKDMEEAVSCLSIGVLDIFGFEDFERNS 531
Cdd:cd14902   320 REIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRlsdeINYFDSAVSISDEDEELATIGILDIFGFESLNRNG 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  532 FEQFCINYANEQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKF 611
Cdd:cd14902   400 FEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYPSNAACLALFDDKSNGLFSLLDQECLMPKGSNQALSTKF 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  612 KQqhednkYFLGtpvlEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVrQLIGMDPvavfrwavlraa 691
Cdd:cd14902   480 YR------YHGG----LGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVV-VAIGADE------------ 536
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  692 iramavlreagrlraeraekaaaGISSPatrshmeelprgASTPSEKLYRctgldfsferseeldvnafedimafyesrk 771
Cdd:cd14902   537 -----------------------NRDSP------------GADNGAAGRR------------------------------ 551
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  772 argqsdlhnqiikslkglpwqgedprrllqslslfqkpRTSFLKSkgikqkqiipknlldskslrliismtlhdrttksl 851
Cdd:cd14902   552 --------------------------------------RYSMLRA----------------------------------- 558
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  852 lhlhkkkkpPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTF 931
Cdd:cd14902   559 ---------PSVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRIARHGYSVRLAH 629
                         810       820
                  ....*....|....*....|.
gi 568955249  932 QDFTEQFQVLLPKDVQPCREA 952
Cdd:cd14902   630 ASFIELFSGFKCFLSTRDRAA 650
MYSc_Myo34 cd14895
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ...
166-977 2.96e-126

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: 415.51  E-value: 2.96e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  166 LKLRFMQQKIYTYAGSILVAINPFKFLP-IYNpkyVKMYENQQLG--KLEPHVFALADVAYYAMLRK-------HVNQCI 235
Cdd:cd14895     7 LAQRYGVDQVYCRSGAVLIAVNPFKHIPgLYD---LHKYREEMPGwtALPPHVFSIAEGAYRSLRRRlhepgasKKNQTI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  236 VISGESGSGKTQSTNFLIHCLTALSQKGYA---SGVERTILG-----AGPVLEAFGNAKTAHNNNSSRFGKFIQVNY--- 304
Cdd:cd14895    84 LVSGESGAGKTETTKFIMNYLAESSKHTTAtssSKRRRAISGsellsANPILESFGNARTLRNDNSSRFGKFVRMFFegh 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  305 -LENGI-VRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLK--QPQDYFYLN-----QHNLNIEDGE 375
Cdd:cd14895   164 eLDTSLrMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLEllSAQEFQYISggqcyQRNDGVRDDK 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  376 DlkhdFERLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTY---KKRATGRDEGLEVGPP-------------EVLDTLS 439
Cdd:cd14895   244 Q----FQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFvasSEDEGEEDNGAASAPCrlasaspssltvqQHLDIVS 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  440 QLLKVKRETLVEVLTKRKTVTVNDKLILPYSLSEAITARDSMAKSLYSALFDWIVLRINHAL--------LNKKDMEEAV 511
Cdd:cd14895   320 KLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASpqrqfalnPNKAANKDTT 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  512 SClsIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFY 591
Cdd:cd14895   400 PC--IAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDNSVCLEMLEQRPSGIFS 477
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  592 LLDEESNFPHATSHTLLAKFKQQHEDNKYFLG--TPVLEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSS 669
Cdd:cd14895   478 LLDEECVVPKGSDAGFARKLYQRLQEHSNFSAsrTDQADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAELFSVLGKTSDA 557
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  670 YVRQLigmdpvavfrwavlraairamavlreagrlraeraekaaagisspatrshmeelprgastpseklyrctgldfsf 749
Cdd:cd14895   558 HLREL--------------------------------------------------------------------------- 562
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  750 erseeldvnaFEDIMAFYESRKARGQSDLhnqiikslkglpwqgedpRRllqslslfqkpRTSFLKSKGikqkqiipknl 829
Cdd:cd14895   563 ----------FEFFKASESAELSLGQPKL------------------RR-----------RSSVLSSVG----------- 592
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  830 ldskslrliismtlhdrttksllhlhkkkkppsISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQL 909
Cdd:cd14895   593 ---------------------------------IGSQFKQQLASLLDVVQQTQTHYIRCIKPNDESASDQFDMAKVSSQL 639
                         810       820       830       840       850       860
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568955249  910 RYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPKDVQPCREAiAALLEKLQVDrqNYQIGKTKVFLK 977
Cdd:cd14895   640 RYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKNASDATA-SALIETLKVD--HAELGKTRVFLR 704
MYSc_Myh2_insects_mollusks cd14911
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ...
160-977 3.54e-122

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: 402.44  E-value: 3.54e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISG 239
Cdd:cd14911     1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  240 ESGSGKTQSTNFLIHCL----------------TALSQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVN 303
Cdd:cd14911    81 ESGAGKTENTKKVIQFLayvaaskpkgsgavphPAVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  304 YLENGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEdGEDLKHDFER 383
Cdd:cd14911   161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVP-GVDDYAEFQA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  384 LQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKRATGRDEGLevgpPE--VLDTLSQLLKVKRETLVEVLTKRKTVTV 461
Cdd:cd14911   240 TVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATL----PDntVAQKIAHLLGLSVTDMTRAFLTPRIKVG 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  462 NDKLILPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEAVsclsIGVLDIFGFEDFERNSFEQFCINYAN 541
Cdd:cd14911   316 RDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASF----IGILDMAGFEIFELNSFEQLCINYTN 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  542 EQLQYYFTQHIFKLEQEEYQGEGISWHNIDY-TDNVGCIHLIsKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKY 620
Cdd:cd14911   392 EKLQQLFNHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLI-DKPGGIMALLDEECWFPKATDKTFVDKLVSAHSMHPK 470
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  621 FLGTPVLEPA-FIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDssyvrqligmDPVAVFRWAvlRAAIRAMAvlr 699
Cdd:cd14911   471 FMKTDFRGVAdFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQ----------DPFVVNIWK--DAEIVGMA--- 535
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  700 eagrlraeraekaaagisspatRSHMEELPRGAstpseklyrctgldfsferseeldvnafedimafyesrkargqsdlh 779
Cdd:cd14911   536 ----------------------QQALTDTQFGA----------------------------------------------- 546
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  780 nqiikslkglpwqgedprrllqslslfqkprtsflkskgikqkqiipknlldskslrliismtlhdRTTKSLLHlhkkkk 859
Cdd:cd14911   547 ------------------------------------------------------------------RTRKGMFR------ 554
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  860 ppSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQ 939
Cdd:cd14911   555 --TVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYE 632
                         810       820       830       840
                  ....*....|....*....|....*....|....*....|..
gi 568955249  940 VL----LPKDVQPCREAIAALLEKLQVDRQNYQIGKTKVFLK 977
Cdd:cd14911   633 LLtpnvIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
MYSc_Myo39 cd14900
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ...
162-663 3.18e-121

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: 398.14  E-value: 3.18e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  162 LLQNLKLRFMQQKIYTYAGSILVAINPFKFLP-IYNP----KYVKMYE-------NQQLGKLEPHVFALADVAYYAMLR- 228
Cdd:cd14900     3 ILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSdtmaKYLLSFEarssstrNKGSDPMPPHIYQVAGEAYKAMMLg 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  229 ---KHVNQCIVISGESGSGKTQSTNFLIHCLT---------ALSQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRF 296
Cdd:cd14900    83 lngVMSDQSILVSGESGSGKTESTKFLMEYLAqagdnnlaaSVSMGKSTSGIAAKVLQTNILLESFGNARTLRNDNSSRF 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  297 GKFIQVNYLENGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLefqlkqpqdyfylnqhnlniedged 376
Cdd:cd14900   163 GKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARK------------------------- 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  377 lKHDFERLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKRATGRDEG---LEVGPPEV--LDTLSQLLKVKRETLVE 451
Cdd:cd14900   218 -RDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGqlkSDLAPSSIwsRDAAATLLSVDATKLEK 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  452 VLTKRKTVTVNDKLILPYSLSEAITARDSMAKSLYSALFDWIVLRINHaLLNKKDMEEAVSCLS-IGVLDIFGFEDFERN 530
Cdd:cd14900   297 ALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNA-FLKMDDSSKSHGGLHfIGILDIFGFEVFPKN 375
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  531 SFEQFCINYANEQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAK 610
Cdd:cd14900   376 SFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFCDNQDCVNLISQRPTGILSLIDEECVMPKGSDTTLASK 455
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568955249  611 FKQQHEDNKYFLGTPVLEPA--FIIQHFAGRVKYQIKDFREKNMDYMRPDIVALL 663
Cdd:cd14900   456 LYRACGSHPRFSASRIQRARglFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDLF 510
MYSc_Myh15_mammals cd14929
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ...
160-977 3.44e-121

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: 399.35  E-value: 3.44e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISG 239
Cdd:cd14929     1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  240 ESGSGKTQSTNFLIH---CLTALSQKGYASGV-ERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRGAVV 315
Cdd:cd14929    81 ESGAGKTVNTKHIIQyfaTIAAMIESKKKLGAlEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSADI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  316 EKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDLKhDFERLQQAMEMVGFLP 395
Cdd:cd14929   161 DIYLLEKSRVIFQQPGERNYHIFYQILSGKKELRDLLLVSANPSDFHFCSCGAVAVESLDDAE-ELLATEQAMDILGFLP 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  396 ATKKQIFSVLSAILYLGNVTYKKRAtgRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILPYSLSEAI 475
Cdd:cd14929   240 DEKYGCYKLTGAIMHFGNMKFKQKP--REEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIEQVT 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  476 TARDSMAKSLYSALFDWIVLRINHALLNKkdmeeAVSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKL 555
Cdd:cd14929   318 YAVGALSKSIYERMFKWLVARINRVLDAK-----LSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVL 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  556 EQEEYQGEGISWHNIDY-TDNVGCIHLIsKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPV-----LEP 629
Cdd:cd14929   393 EQEEYRKEGIDWVSIDFgLDLQACIDLI-EKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKpdkkkFEA 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  630 AFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSdssyvrqligmdpvavfrwavlraairamavlreagrlraera 709
Cdd:cd14929   472 HFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKS------------------------------------------- 508
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  710 ekaaagisspatrshmeelprgastpseklyrctgldfsferSEELDVNAFEDIMAfyesrkargqSDLHNQIikslkgl 789
Cdd:cd14929   509 ------------------------------------------SNRLLASLFENYIS----------TDSAIQF------- 529
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  790 pwqGEDPRRllqslslfqkprtsflksKGikqkqiipknlldsKSLRLIISmtlhdrttksllhLHKKkkppsisaqfqt 869
Cdd:cd14929   530 ---GEKKRK------------------KG--------------ASFQTVAS-------------LHKE------------ 549
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  870 SLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPK----- 944
Cdd:cd14929   550 NLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRtfpks 629
                         810       820       830
                  ....*....|....*....|....*....|...
gi 568955249  945 DVQPCREAIAALLEKLQVDRQNYQIGKTKVFLK 977
Cdd:cd14929   630 KFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
MYSc_Myo14 cd14876
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ...
166-977 7.20e-121

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: 397.82  E-value: 7.20e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  166 LKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYEN-QQLGKLEPHVFALADVAYYAMLRKHVNQCIVISGESGSG 244
Cdd:cd14876     7 LKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDaPDLTKLPPHVFYTARRALENLHGVNKSQTIIVSGESGAG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  245 KTQSTNFLIHCLtALSQKGYASG-VERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYL-ENGIVRGAVVeKYLLEK 322
Cdd:cd14876    87 KTEATKQIMRYF-ASAKSGNMDLrIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVAsEGGIRYGSVV-AFLLEK 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  323 SRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIeDGEDLKHDFERLQQAMEMVGFLPATKKQIF 402
Cdd:cd14876   165 SRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLNPKCLDV-PGIDDVADFEEVLESLKSMGLTEEQIDTVF 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  403 SVLSAILYLGNVTY-KKRATGRDEGLEVGP--PEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILPYSLSEAITARD 479
Cdd:cd14876   244 SIVSGVLLLGNVKItGKTEQGVDDAAAISNesLEVFKEACSLLFLDPEALKRELTVKVTKAGGQEIEGRWTKDDAEMLKL 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  480 SMAKSLYSALFDWIVLRINHALLNKKDMEEAvsclsIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQEE 559
Cdd:cd14876   324 SLAKAMYDKLFLWIIRNLNSTIEPPGGFKNF-----MGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFIDIVFERESKL 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  560 YQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLgtpvlePA-------FI 632
Cdd:cd14876   399 YKDEGIPTAELEYTSNAEVIDVLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSKLKSNGKFK------PAkvdsninFI 472
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  633 IQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLIGMDPVavfrwavlraairamavlrEAGRLraeraeka 712
Cdd:cd14876   473 VVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVVV-------------------EKGKI-------- 525
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  713 aagisspatrshmeelprgastpseklyrctgldfsferseeldvnafedimafyesrkARGQsdlhnqiikslkglpwq 792
Cdd:cd14876   526 -----------------------------------------------------------AKGS----------------- 529
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  793 gedprrllqslslfqkprtsflkskgikqkqiipknlldskslrLIISmtlhdrttksllhlhkkkkppsisaQFQTSLN 872
Cdd:cd14876   530 --------------------------------------------LIGS-------------------------QFLKQLE 540
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  873 KLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLP-----KDVQ 947
Cdd:cd14876   541 SLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFLDLgiandKSLD 620
                         810       820       830
                  ....*....|....*....|....*....|
gi 568955249  948 PcREAIAALLEKLQVDRQNYQIGKTKVFLK 977
Cdd:cd14876   621 P-KVAALKLLESSGLSEDEYAIGKTMVFLK 649
MYSc_Myh18 cd14932
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ...
160-977 1.31e-119

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: 395.17  E-value: 1.31e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISG 239
Cdd:cd14932     1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  240 ESGSGKTQSTNFLIHCLTAL-----SQKGYASGV------ERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENG 308
Cdd:cd14932    81 ESGAGKTENTKKVIQYLAYVassfkTKKDQSSIAlshgelEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  309 IVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDlKHDFERLQQAM 388
Cdd:cd14932   161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQD-KELFAETMEAF 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  389 EMVGFLPATKKQIFSVLSAILYLGNVTYKKRATGRDEGLevgpPEvlDTLSQ----LLKVKRETLVEVLTKRKTVTVNDK 464
Cdd:cd14932   240 RIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASM----PD--DTAAQkvchLLGMNVTDFTRAILSPRIKVGRDY 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  465 LILPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEAVsclsIGVLDIFGFEDFERNSFEQFCINYANEQL 544
Cdd:cd14932   314 VQKAQTQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASF----IGILDIAGFEIFELNSFEQLCINYTNEKL 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  545 QYYFTQHIFKLEQEEYQGEGISWHNIDY-TDNVGCIHLISKK--PTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYF 621
Cdd:cd14932   390 QQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIELIEKPngPPGILALLDEECWFPKATDKSFVEKVVQEQGNNPKF 469
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  622 LGTPVL--EPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLigmdpvavfrWavlraairamavlR 699
Cdd:cd14932   470 QKPKKLkdDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSEL----------W-------------K 526
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  700 EAGRLraeraekaaagisspatrshmeelprgastpseklyrcTGLDfsferseeldvnafedimafyesrKARGQSDLH 779
Cdd:cd14932   527 DVDRI--------------------------------------VGLD------------------------KVAGMGESL 544
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  780 NQIIKSLKGLpwqgedprrllqslslfqkprtsflkskgikqkqiipknlldskslrliismtlhDRTTKSLlhlhkkkk 859
Cdd:cd14932   545 HGAFKTRKGM-------------------------------------------------------FRTVGQL-------- 561
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  860 ppsisaqFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQ 939
Cdd:cd14932   562 -------YKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 634
                         810       820       830       840
                  ....*....|....*....|....*....|....*....|..
gi 568955249  940 VL----LPKDVQPCREAIAALLEKLQVDRQNYQIGKTKVFLK 977
Cdd:cd14932   635 ILtpnaIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
MYSc_Myh3 cd14913
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ...
162-977 6.86e-117

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: 387.10  E-value: 6.86e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  162 LLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISGES 241
Cdd:cd14913     3 VLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  242 GSGKTQSTNFLIHCLTALSQKGYASG---------VERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRG 312
Cdd:cd14913    83 GAGKTVNTKRVIQYFATIAATGDLAKkkdskmkgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  313 AVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGvSEEERLEFQL--KQPQDYFYLNQHNL---NIEDGEDLKhdfeRLQQA 387
Cdd:cd14913   163 ADIETYLLEKSRVTFQLKAERSYHIFYQILSN-KKPELIELLLitTNPYDYPFISQGEIlvaSIDDAEELL----ATDSA 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  388 MEMVGFLPATKKQIFSVLSAILYLGNVTYKKRAtgRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLIL 467
Cdd:cd14913   238 IDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQ--REEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTK 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  468 PYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEAvsclsIGVLDIFGFEDFERNSFEQFCINYANEQLQYY 547
Cdd:cd14913   316 GQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHF-----IGVLDIAGFEIFEYNSLEQLCINFTNEKLQQF 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  548 FTQHIFKLEQEEYQGEGISWHNIDY-TDNVGCIHLIsKKPTGLFYLLDEESNFPHATSHTLLAKFKQQH--EDNKYFLGT 624
Cdd:cd14913   391 FNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYDQHlgKSNNFQKPK 469
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  625 PV---LEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRgsdssyvrqligmdpvavfrwavlRAAIRAMAVLrea 701
Cdd:cd14913   470 VVkgrAEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQ------------------------KSSNRLLAHL--- 522
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  702 grlraeraekaaagisspatrshmeelprgastpseklyrctgldfsferseeldvnafediMAFYESRKARGQsdlhnq 781
Cdd:cd14913   523 --------------------------------------------------------------YATFATADADSG------ 534
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  782 iikslkglpwqgedprrllqslslfqkprtsflKSKGIKQKqiipknlldSKSLRliismtlhdrttksllhlhkkkkpp 861
Cdd:cd14913   535 ---------------------------------KKKVAKKK---------GSSFQ------------------------- 547
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  862 SISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL 941
Cdd:cd14913   548 TVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVL 627
                         810       820       830       840
                  ....*....|....*....|....*....|....*....|.
gi 568955249  942 LPKDVQP-----CREAIAALLEKLQVDRQNYQIGKTKVFLK 977
Cdd:cd14913   628 NASAIPEgqfidSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
MYSc_Myo17 cd14879
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ...
157-666 3.91e-116

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: 384.21  E-value: 3.91e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  157 LTEANLLQNLKLRFMQQKIYTYAGS-ILVAINPFKFLPIYNPKYVKMYEN-------QQLGKLEPHVFALADVAYYAMLR 228
Cdd:cd14879     1 PSDDAITSHLASRFRSDLPYTRLGSsALVAVNPYKYLSSNSDASLGEYGSeyydttsGSKEPLPPHAYDLAARAYLRMRR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  229 KHVNQCIVISGESGSGKT----QSTNFLIHcLTALSQKGYASGVErtILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNY 304
Cdd:cd14879    81 RSEDQAVVFLGETGSGKSesrrLLLRQLLR-LSSHSKKGTKLSSQ--ISAAEFVLDSFGNAKTLTNPNASRFGRYTELQF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  305 LENGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYL---NQHNLNIEDGEDLKHDF 381
Cdd:cd14879   158 NERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLasyGCHPLPLGPGSDDAEGF 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  382 ERLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKRATGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKrKTVTV 461
Cdd:cd14879   238 QELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFTYDHEGGEESAVVKNTDVLDIVAAFLGVSPEDLETSLTY-KTKLV 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  462 NdklilpyslSEAITA----------RDSMAKSLYSALFDWIVLRINHALLNKkdmEEAVScLSIGVLDIFGFEDF---E 528
Cdd:cd14879   317 R---------KELCTVfldpegaaaqRDELARTLYSLLFAWVVETINQKLCAP---EDDFA-TFISLLDFPGFQNRsstG 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  529 RNSFEQFCINYANEQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEE-SNFPHATSHTL 607
Cdd:cd14879   384 GNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSYFDNSDCVRLLRGKPGGLLGILDDQtRRMPKKTDEQM 463
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568955249  608 LAKFKQQHEDNKYF-----LGTPVLEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGS 666
Cdd:cd14879   464 LEALRKRFGNHSSFiavgnFATRSGSASFTVNHYAGEVTYSVEGFLERNGDVLSPDFVNLLRGA 527
MYSc_Myh7b cd14927
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ...
160-977 3.06e-115

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: 382.38  E-value: 3.06e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISG 239
Cdd:cd14927     1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  240 ESGSGKTQSTNFLIHCLTALSQKGYASG-------------VERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLE 306
Cdd:cd14927    81 ESGAGKTVNTKRVIQYFAIVAALGDGPGkkaqflatktggtLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  307 NGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEE-ERLEFQLKQPQDYFYLNQHNL---NIEDGEDLKhdfe 382
Cdd:cd14927   161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPElQDMLLVSMNPYDYHFCSQGVTtvdNMDDGEELM---- 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  383 RLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKRAtgRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVN 462
Cdd:cd14927   237 ATDHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQ--REEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGN 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  463 DKLILPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEeavscLSIGVLDIFGFEDFERNSFEQFCINYANE 542
Cdd:cd14927   315 EYVTKGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQ-----FFIGVLDIAGFEIFEFNSFEQLCINFTNE 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  543 QLQYYFTQHIFKLEQEEYQGEGISWHNIDY-TDNVGCIHLIsKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYF 621
Cdd:cd14927   390 KLQQFFNHHMFILEQEEYKREGIEWVFIDFgLDLQACIDLI-EKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPN 468
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  622 LGTPVL------EPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSsyvrqligmdpvavfrwavlraaiRAM 695
Cdd:cd14927   469 FQKPRPdkkrkyEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQN------------------------KLL 524
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  696 AVLREagrlraeraekaaagisspatrshmeelprgastpseklyrctgldfSFERSEELDvnafedimafyesrkargq 775
Cdd:cd14927   525 ATLYE-----------------------------------------------NYVGSDSTE------------------- 538
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  776 sdlhnqiikslkglpwqgeDPRrllqslslfqkprtsflksKGIKqkqiipknlldskslrliismtlhdrttksllhlH 855
Cdd:cd14927   539 -------------------DPK-------------------SGVK----------------------------------E 546
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  856 KKKKppsiSAQFQT-------SLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAK 928
Cdd:cd14927   547 KRKK----AASFQTvsqlhkeNLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNR 622
                         810       820       830       840       850
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568955249  929 YTFQDFTEQFQVLLPKDVQP-----CREAIAALLEKLQVDRQNYQIGKTKVFLK 977
Cdd:cd14927   623 ILYADFKQRYRILNPSAIPDdkfvdSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
MYSc_Myh16 cd14934
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ...
160-977 3.80e-115

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: 381.68  E-value: 3.80e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISG 239
Cdd:cd14934     1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  240 ESGSGKTQSTNFLIHCLTALSQKGYAS-----GVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRGAV 314
Cdd:cd14934    81 ESGAGKTENTKKVIQYFANIGGTGKQSsdgkgSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGAD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  315 VEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEE--ERLeFQLKQPQDYFYLNQHNL---NIEDGEDLkhdfERLQQAME 389
Cdd:cd14934   161 IESYLLEKSRVISQQAAERGYHIFYQILSNKKPEliESL-LLVPNPKEYHWVSQGVTvvdNMDDGEEL----QITDVAFD 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  390 MVGFLPATKKQIFSVLSAILYLGNVTYKKRAtgRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILPY 469
Cdd:cd14934   236 VLGFSAEEKIGVYKLTGGIMHFGNMKFKQKP--REEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQ 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  470 SLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEeavscLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFT 549
Cdd:cd14934   314 NMEQCNNSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQ-----FFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFN 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  550 QHIFKLEQEEYQGEGISWHNIDY-TDNVGCIHLIsKKPTGLFYLLDEESNFPHATShtllAKFKQQHEDNKYFLGTPVLE 628
Cdd:cd14934   389 HHMFVLEQEEYKREGIEWVFIDFgLDLQACIDLL-EKPMGIFSILEEQCVFPKATD----ATFKAALYDNHLGKSSNFLK 463
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  629 PA----------FIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRgsdssyvrqligmdpvavfrwavlRAAIRAMAVL 698
Cdd:cd14934   464 PKggkgkgpeahFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQ------------------------KSSLGLLALL 519
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  699 REAgrlraeraekaaagisspatrshmEELPRGASTpseklyrctgldfsferseeldvnafedimafyesrkargqsdl 778
Cdd:cd14934   520 FKE------------------------EEAPAGSKK-------------------------------------------- 531
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  779 hnqiikslkglpwqgedprrllqslslfQKPRTSFLkskgikqkqiipknlldskslrliismtlhdrttksllhlhkkk 858
Cdd:cd14934   532 ----------------------------QKRGSSFM-------------------------------------------- 539
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  859 kppSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQF 938
Cdd:cd14934   540 ---TVSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRY 616
                         810       820       830       840
                  ....*....|....*....|....*....|....*....|...
gi 568955249  939 QVL----LPKDVQPCREAIAALLEKLQVDRQNYQIGKTKVFLK 977
Cdd:cd14934   617 QVLnpnvIPQGFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
MYSc_Myh9 cd14919
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ...
160-977 3.21e-113

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: 376.36  E-value: 3.21e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISG 239
Cdd:cd14919     1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  240 ESGSGKTQST----NFLIHCLTALSQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRGAVV 315
Cdd:cd14919    81 ESGAGKTENTkkviQYLAHVASSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  316 EKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDlKHDFERLQQAMEMVGFLP 395
Cdd:cd14919   161 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQD-KDMFQETMEAMRIMGIPE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  396 ATKKQIFSVLSAILYLGNVTYKKRatgRDEGLEVGPPEV-LDTLSQLLKVKRETLVE-VLTKRKTVTvNDKLILPYSLSE 473
Cdd:cd14919   240 EEQMGLLRVISGVLQLGNIVFKKE---RNTDQASMPDNTaAQKVSHLLGINVTDFTRgILTPRIKVG-RDYVQKAQTKEQ 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  474 AITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEAVsclsIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIF 553
Cdd:cd14919   316 ADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASF----IGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMF 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  554 KLEQEEYQGEGISWHNIDY-TDNVGCIHLISKK--PTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPVLEPA 630
Cdd:cd14919   392 ILEQEEYQREGIEWNFIDFgLDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDK 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  631 --FIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQL-------IGMDPVAvfrwavlraairamavlrea 701
Cdd:cd14919   472 adFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELwkdvdriIGLDQVA-------------------- 531
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  702 grlraeraekaaaGISSPAtrshmeeLPrGASTPSEKLYRCTGldfsferseeldvnafedimafyesrkargqsdlhnq 781
Cdd:cd14919   532 -------------GMSETA-------LP-GAFKTRKGMFRTVG------------------------------------- 553
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  782 iikslkglpwqgedprrllqslslfqkprtsflkskgikqkqiipknlldskslrliismtlhdrttksllHLHKKKkpp 861
Cdd:cd14919   554 -----------------------------------------------------------------------QLYKEQ--- 559
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  862 sisaqfqtsLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL 941
Cdd:cd14919   560 ---------LAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEIL 630
                         810       820       830       840
                  ....*....|....*....|....*....|....*....|
gi 568955249  942 ----LPKDVQPCREAIAALLEKLQVDRQNYQIGKTKVFLK 977
Cdd:cd14919   631 tpnsIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
RhoGAP_myosin_IX cd04377
RhoGAP_myosin_IX: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
1704-1889 2.29e-112

RhoGAP_myosin_IX: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in class IX myosins. Class IX myosins contain a characteristic head domain, a neck domain, a tail domain which contains a C6H2-zinc binding motif and a RhoGAP domain. Class IX myosins are single-headed, processive myosins that are partly cytoplasmic, and partly associated with membranes and the actin cytoskeleton. Class IX myosins are implicated in the regulation of neuronal morphogenesis and function of sensory systems, like the inner ear. There are two major isoforms, myosin IXA and IXB with several splice variants, which are both expressed in developing neurons. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239842  Cd Length: 186  Bit Score: 354.44  E-value: 2.29e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1704 FGVCVDSLTSDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKLEDFPIHAITGVLKQWLRE 1783
Cdd:cd04377     1 FGVSLSSLTSEDRSVPLVLEKLLEHIEMHGLYTEGIYRKSGSANKIKELRQGLDTDPDSVNLEDYPIHVITSVLKQWLRE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1784 LPEPLMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRC 1863
Cdd:cd04377    81 LPEPLMTFELYENFLRAMELEEKQERVRALYSVLEQLPRANLNTLERLIFHLVRVALQEEVNRMSANALAIVFAPCILRC 160
                         170       180
                  ....*....|....*....|....*.
gi 568955249 1864 PDNSDPLTSMKDVLKITTCVEMLIKE 1889
Cdd:cd04377   161 PDTADPLQSLQDVSKTTTCVETLIKE 186
MYSc_Myh1_insects_crustaceans cd14909
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ...
160-977 1.69e-111

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: 371.48  E-value: 1.69e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISG 239
Cdd:cd14909     1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  240 ESGSGKTQSTNFLIHCLTAL--SQKGYASG-----VERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRG 312
Cdd:cd14909    81 ESGAGKTENTKKVIAYFATVgaSKKTDEAAkskgsLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  313 AVVEKYLLEKSRLVSQEKDERNYHVFYYLLLG-VSEEERLEFQLKQPQDYFYLNQHNL---NIEDGEdlkhDFERLQQAM 388
Cdd:cd14909   161 ADIETYLLEKARVISQQSLERSYHIFYQIMSGsVPGVKEMCLLSDNIYDYYIVSQGKVtvpNVDDGE----EFSLTDQAF 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  389 EMVGFLPATKKQIFSVLSAILYLGNVTYKKRatGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILP 468
Cdd:cd14909   237 DILGFTKQEKEDVYRITAAVMHMGGMKFKQR--GREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQG 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  469 YSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEAvsclsIGVLDIFGFEDFERNSFEQFCINYANEQLQYYF 548
Cdd:cd14909   315 RNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHF-----IGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFF 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  549 TQHIFKLEQEEYQGEGISWHNIDY-TDNVGCIHLIsKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHednkyfLG--TP 625
Cdd:cd14909   390 NHHMFVLEQEEYKREGIDWAFIDFgMDLLACIDLI-EKPMGILSILEEESMFPKATDQTFSEKLTNTH------LGksAP 462
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  626 VLEPA----------FIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLIGMDPvavfrwavlraairam 695
Cdd:cd14909   463 FQKPKppkpgqqaahFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHA---------------- 526
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  696 avlreagrlraeraekaaagisspatrshmeelprGASTPSEklyrctgldfsferseeldvnafedimafyESRKARGQ 775
Cdd:cd14909   527 -----------------------------------GQSGGGE------------------------------QAKGGRGK 541
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  776 sdlhnqiikslKGLPWQgedprrllqslslfqkprtsflkskgikqkqiipknlldskslrliismtlhdrttksllhlh 855
Cdd:cd14909   542 -----------KGGGFA--------------------------------------------------------------- 547
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  856 kkkkppSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFT 935
Cdd:cd14909   548 ------TVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFK 621
                         810       820       830       840
                  ....*....|....*....|....*....|....*....|....*
gi 568955249  936 EQFQVLLPKDVQP---CREAIAALLEKLQVDRQNYQIGKTKVFLK 977
Cdd:cd14909   622 MRYKILNPAGIQGeedPKKAAEIILESIALDPDQYRLGHTKVFFR 666
MYSc_Myo47 cd14908
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ...
160-653 5.08e-111

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: 370.39  E-value: 5.08e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQL---------GKLEPHVFALADVAYYAMLRK- 229
Cdd:cd14908     1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRQEGLlrsqgiespQALGPHVFAIADRSYRQMMSEi 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  230 HVNQCIVISGESGSGKTQSTNFLIHCLTAL-----------SQKGYASGVERtILGAGPVLEAFGNAKTAHNNNSSRFGK 298
Cdd:cd14908    81 RASQSILISGESGAGKTESTKIVMLYLTTLgngeegapnegEELGKLSIMDR-VLQSNPILEAFGNARTLRNDNSSRFGK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  299 FIQVNYLENGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQ--------PQDYFYLNQ---- 366
Cdd:cd14908   160 FIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEKYEFHDgitgglqlPNEFHYTGQggap 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  367 HNLNIEDgEDlkhDFERLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYK-KRATGRDEGLEVGPPEVLDTLSQLLKVK 445
Cdd:cd14908   240 DLREFTD-ED---GLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFEsKEEDGAAEIAEEGNEKCLARVAKLLGVD 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  446 RETLVEVLTKRKTVTVNDKLILPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEAVSClsiGVLDIFGFE 525
Cdd:cd14908   316 VDKLLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKDIRSSV---GVLDIFGFE 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  526 DFERNSFEQFCINYANEQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEE--------- 596
Cdd:cd14908   393 CFAHNSFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFPDNQDCLDTIQAKKKGILTMLDDEcrlgirgsd 472
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  597 SNFPHATSHTLLAKFKQQHEDNKYFLGTPVLEPA--FIIQHFAGRVKYQIKD-FREKNMD 653
Cdd:cd14908   473 ANYASRLYETYLPEKNQTHSENTRFEATSIQKTKliFAVRHFAGQVQYTVETtFCEKNKD 532
MYSc_Myh11 cd14921
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ...
160-977 5.60e-111

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: 370.12  E-value: 5.60e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISG 239
Cdd:cd14921     1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  240 ESGSGKTQSTNFLIHCLT--ALSQKGYASG-----VERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRG 312
Cdd:cd14921    81 ESGAGKTENTKKVIQYLAvvASSHKGKKDTsitgeLEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  313 AVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDlKHDFERLQQAMEMVG 392
Cdd:cd14921   161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQD-DEMFQETLEAMSIMG 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  393 FLPATKKQIFSVLSAILYLGNVTYKKRATGRDEGLevgpPEvlDTLSQ----LLKVKRETLVE-VLTKRKTVTvNDKLIL 467
Cdd:cd14921   240 FSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASM----PD--NTAAQkvchLMGINVTDFTRsILTPRIKVG-RDVVQK 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  468 PYSLSEAITARDSMAKSLYSALFDWIVLRINHALlnKKDMEEAVSCLsiGVLDIFGFEDFERNSFEQFCINYANEQLQYY 547
Cdd:cd14921   313 AQTKEQADFAIEALAKATYERLFRWILTRVNKAL--DKTHRQGASFL--GILDIAGFEIFEVNSFEQLCINYTNEKLQQL 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  548 FTQHIFKLEQEEYQGEGISWHNIDY-TDNVGCIHLISK--KPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGT 624
Cdd:cd14921   389 FNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIELIERpnNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKP 468
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  625 PVL--EPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLigmdpvavfrWavlraairamavlreag 702
Cdd:cd14921   469 KQLkdKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADL----------W----------------- 521
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  703 rlraeraekaaagisspatrshmeelprgastpsEKLYRCTGLDFSFERSEeldvnafedimafyesrkargqsdlhnqi 782
Cdd:cd14921   522 ----------------------------------KDVDRIVGLDQMAKMTE----------------------------- 538
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  783 ikslkglpwqgedprrllQSLSLFQKPRTSFLKSKGikqkqiipknlldskslrliismtlhdrttksllHLHKKKkpps 862
Cdd:cd14921   539 ------------------SSLPSASKTKKGMFRTVG----------------------------------QLYKEQ---- 562
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  863 isaqfqtsLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL- 941
Cdd:cd14921   563 --------LGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILa 634
                         810       820       830
                  ....*....|....*....|....*....|....*....
gi 568955249  942 ---LPKDVQPCREAIAALLEKLQVDRQNYQIGKTKVFLK 977
Cdd:cd14921   635 anaIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
MYSc_Myo45 cd14906
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ...
160-976 9.63e-111

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: 370.85  E-value: 9.63e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLP-IYNPKYVKMYENQQLGKLE-PHVFALADVAYYAMLRKHVNQCIVI 237
Cdd:cd14906     1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQNKSPiPHIYAVALRAYQSMVSEKKNQSIII 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  238 SGESGSGKTQSTNFLIHCLTALSQKGYASG---------VERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLE-N 307
Cdd:cd14906    81 SGESGSGKTEASKTILQYLINTSSSNQQQNnnnnnnnnsIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSsD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  308 GIVRGAVVEKYLLEKSRlVSQEKDERN--YHVFYYLLLGVSEEERLEFQLKQ-PQDYFYLNQH--------------NLN 370
Cdd:cd14906   161 GKIDGASIETYLLEKSR-ISHRPDNINlsYHIFYYLVYGASKDERSKWGLNNdPSKYRYLDARddvissfksqssnkNSN 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  371 IEDGEDLKHDFERLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKRATGrDEGLEVGPP--EVLDTLSQLLKVKRET 448
Cdd:cd14906   240 HNNKTESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDF-SKYAYQKDKvtASLESVSKLLGYIESV 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  449 LVEVLTKRKTVTVNDKLIL--PYSLSEAITARDSMAKSLYSALFDWIVLRINHALLN---KKDMEEAVS---CLSIGVLD 520
Cdd:cd14906   319 FKQALLNRNLKAGGRGSVYcrPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQntqSNDLAGGSNkknNLFIGVLD 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  521 IFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFP 600
Cdd:cd14906   399 IFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNFIDNKECIELIEKKSDGILSLLDDECIMP 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  601 HATSHTLLAKFKQQ-HEDNKYFLGTpVLEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDssyvrqligmdp 679
Cdd:cd14906   479 KGSEQSLLEKYNKQyHNTNQYYQRT-LAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASS------------ 545
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  680 vavfrwavlraairamavlreagrlraeraekaaagisspatrshmeelprgastpseklyrctgldfsferseeldvna 759
Cdd:cd14906       --------------------------------------------------------------------------------
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  760 fedimafyesrkargqsdlhNQIIKSlkglpwqgedprrlLQSLSLFQKPRTSflkskgikqkqiipknlldskslrlii 839
Cdd:cd14906   546 --------------------NFLKKS--------------LFQQQITSTTNTT--------------------------- 564
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  840 smtlhDRTTKSLlhlhkkkkppSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVR 919
Cdd:cd14906   565 -----KKQTQSN----------TVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLNTIK 629
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  920 IRRSGYSAKYTFQDFTEQFQVLL----------PKD-VQPCREAIAALLEKLQV-----------------DRQNYQIGK 971
Cdd:cd14906   630 VRKMGYSYRRDFNQFFSRYKCIVdmynrknnnnPKLaSQLILQNIQSKLKTMGIsnnkkknnsnsnsnttnDKPLFQIGK 709

                  ....*
gi 568955249  972 TKVFL 976
Cdd:cd14906   710 TKIFI 714
MYSc_Myh19 cd15896
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ...
160-977 2.61e-110

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: 368.24  E-value: 2.61e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISG 239
Cdd:cd15896     1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  240 ESGSGKTQSTNFLIHCLTALSQK-----------GYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENG 308
Cdd:cd15896    81 ESGAGKTENTKKVIQYLAHVASShktkkdqnslaLSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  309 IVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDlKHDFERLQQAM 388
Cdd:cd15896   161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQD-KDLFTETMEAF 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  389 EMVGFLPATKKQIFSVLSAILYLGNVTYKKRAtgRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILP 468
Cdd:cd15896   240 RIMGIPEDEQIGMLKVVASVLQLGNMSFKKER--HTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKA 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  469 YSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEAVsclsIGVLDIFGFEDFERNSFEQFCINYANEQLQYYF 548
Cdd:cd15896   318 QTQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASF----IGILDIAGFEIFELNSFEQLCINYTNEKLQQLF 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  549 TQHIFKLEQEEYQGEGISWHNIDY-TDNVGCIHLISK--KPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTP 625
Cdd:cd15896   394 NHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIEKpaSPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPK 473
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  626 VL--EPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLigmdpvavfrWavlraairamavlreagr 703
Cdd:cd15896   474 KLkdEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSEL----------W------------------ 525
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  704 lraeraekaaagisspatrshmeelprgastpsEKLYRCTGLDfsferseeldvnafedimafyesrKARGQSDLHNqii 783
Cdd:cd15896   526 ---------------------------------KDVDRIVGLD------------------------KVSGMSEMPG--- 545
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  784 kslkglpwqgedprrllqslslfqkprtSFLKSKGIKqkqiipknlldskslrliismtlhdRTTKSLlhlhkkkkppsi 863
Cdd:cd15896   546 ----------------------------AFKTRKGMF-------------------------RTVGQL------------ 560
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  864 saqFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL-- 941
Cdd:cd15896   561 ---YKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILtp 637
                         810       820       830
                  ....*....|....*....|....*....|....*...
gi 568955249  942 --LPKDVQPCREAIAALLEKLQVDRQNYQIGKTKVFLK 977
Cdd:cd15896   638 naIPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
MYSc_Myo19 cd14880
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ...
160-976 1.52e-107

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: 359.55  E-value: 1.52e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLP-IYNPKYVKMYENQ-QLGKLEPHVFALADVAYYAM--LRKHVNQCI 235
Cdd:cd14880     1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAApQPQKLKPHIFTVGEQTYRNVksLIEPVNQSI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  236 VISGESGSGKTQSTNFLIH-------CLTALSQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENG 308
Cdd:cd14880    81 VVSGESGAGKTWTSRCLMKfyavvaaSPTSWESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  309 IVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEdgEDlkhDFERLQQAM 388
Cdd:cd14880   161 QMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPNPERNLE--ED---CFEVTREAM 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  389 EMVGFLPATKKQIFSVLSAILYLGNVTYKkratgrDEGLEVGPPEVLD-------TLSQLLKVKRETLVEVLTKRkTVTV 461
Cdd:cd14880   236 LHLGIDTPTQNNIFKVLAGLLHLGNIQFA------DSEDEAQPCQPMDdtkesvrTSALLLKLPEDHLLETLQIR-TIRA 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  462 NDKLIL---PYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEAVsclsIGVLDIFGFEDFERNSFEQFCIN 538
Cdd:cd14880   309 GKQQQVfkkPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTF----IGLLDVYGFESFPENSLEQLCIN 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  539 YANEQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLakfkqQHEDN 618
Cdd:cd14880   385 YANEKLQQHFVAHYLRAQQEEYAVEGLEWSFINYQDNQTCLDLIEGSPISICSLINEECRLNRPSSAAQL-----QTRIE 459
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  619 KYFLGTPVL-------EPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLIGMDPvavfrwavlraa 691
Cdd:cd14880   460 SALAGNPCLghnklsrEPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANP------------ 527
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  692 iramavlreagrlraeraekaaagisspatRSHMEELPRGAStpseklyRCTGLdfsferseeldvnafedimafyesrk 771
Cdd:cd14880   528 ------------------------------EEKTQEEPSGQS-------RAPVL-------------------------- 544
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  772 argqsdlhnqiikslkglpwqgedprrllqslslfqkprtsflkskgikqkqiipknlldskslrliismtlhdrttksl 851
Cdd:cd14880       --------------------------------------------------------------------------------
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  852 lhlhkkkkppSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTF 931
Cdd:cd14880   545 ----------TVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSH 614
                         810       820       830       840
                  ....*....|....*....|....*....|....*....|....*
gi 568955249  932 QDFTEQFQVLLPKdvQPCREAIAALLEKLQVDRQNYQIGKTKVFL 976
Cdd:cd14880   615 QNFVERYKLLRRL--RPHTSSGPHSPYPAKGLSEPVHCGRTKVFM 657
MYSc_Myh8 cd14918
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ...
162-977 5.68e-106

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: 355.58  E-value: 5.68e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  162 LLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISGES 241
Cdd:cd14918     3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  242 GSGKTQSTNFLIHCLTALS--------QKGYASG-VERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRG 312
Cdd:cd14918    83 GAGKTVNTKRVIQYFATIAvtgekkkeESGKMQGtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  313 AVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGvSEEERLEFQL--KQPQDYFYLNQHNLNIEDGEDlKHDFERLQQAMEM 390
Cdd:cd14918   163 ADIETYLLEKSRVTFQLKAERSYHIFYQITSN-KKPDLIEMLLitTNPYDYAFVSQGEITVPSIDD-QEELMATDSAIDI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  391 VGFLPATKKQIFSVLSAILYLGNVTYKKRAtgRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILPYS 470
Cdd:cd14918   241 LGFTPEEKVSIYKLTGAVMHYGNMKFKQKQ--REEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  471 LSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEeavscLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQ 550
Cdd:cd14918   319 VQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQ-----YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNH 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  551 HIFKLEQEEYQGEGISWHNIDY-TDNVGCIHLIsKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPVL-- 627
Cdd:cd14918   394 HMFVLEQEEYKKEGIEWTFIDFgMDLAACIELI-EKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVvk 472
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  628 ---EPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRgsdssyvrqligmdpvavfrwavlRAAIRAMAVLreagrl 704
Cdd:cd14918   473 gkaEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQ------------------------KSAMKTLASL------ 522
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  705 raeraekaaagisspatrshmeelprgastpseklyrctgldFSFERSEELDVNAfedimafYESRKARGQSdlhnqiik 784
Cdd:cd14918   523 ------------------------------------------FSTYASAEADSGA-------KKGAKKKGSS-------- 545
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  785 slkglpwqgedprrllqslslFQkprtsflkskgikqkqiipknlldskslrliismtlhdrttksllhlhkkkkppSIS 864
Cdd:cd14918   546 ---------------------FQ------------------------------------------------------TVS 550
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  865 AQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL--- 941
Cdd:cd14918   551 ALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLnas 630
                         810       820       830
                  ....*....|....*....|....*....|....*...
gi 568955249  942 -LPK-DVQPCREAIAALLEKLQVDRQNYQIGKTKVFLK 977
Cdd:cd14918   631 aIPEgQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
MYSc_Myo13 cd14875
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ...
160-684 9.52e-106

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: 354.50  E-value: 9.52e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  160 ANLLQNLKLRFMQ-QKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQ-QLGKLEPHVFALADVAYYAM-LRKHVNQCIV 236
Cdd:cd14875     1 ATLLHCIKERFEKlHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYLALpDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  237 ISGESGSGKTQSTNFLIHCLTALS--------QKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVnYLE-- 306
Cdd:cd14875    81 ISGESGSGKTENAKMLIAYLGQLSymhssntsQRSIADKIDENLKWSNPVMESFGNARTVRNDNSSRFGKYIKL-YFDpt 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  307 NGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEF-QLKQPQDYFYLNQHNLNIEDGEDLK-----HD 380
Cdd:cd14875   160 SGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKCLNGGNTFVRRGVDGKtlddaHE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  381 FERLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKRATGRDEGLEVGPpevLDTLSQLLKVKRETLVEV-LTKRKTV 459
Cdd:cd14875   240 FQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQNDKAQIADETP---FLTACRLLQLDPAKLRECfLVKSKTS 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  460 TVNdklILPySLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEavsCLSIGVLDIFGFEDFERNSFEQFCINY 539
Cdd:cd14875   317 LVT---ILA-NKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITPQGDCSG---CKYIGLLDIFGFENFTRNSFEQLCINY 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  540 ANEQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHED-N 618
Cdd:cd14875   390 ANESLQNHYNKYTFINDEEECRREGIQIPKIEFPDNSECVNMFDQKRTGIFSMLDEECNFKGGTTERFTTNLWDQWANkS 469
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568955249  619 KYFLGTPVLEP-AFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLIGMDPVAVFR 684
Cdd:cd14875   470 PYFVLPKSTIPnQFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTEKGLARR 536
MYSc_Myh4 cd14915
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ...
162-977 7.71e-105

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: 352.11  E-value: 7.71e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  162 LLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISGES 241
Cdd:cd14915     3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  242 GSGKTQSTNFLIHCLTALSQKG------YASG-----VERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIV 310
Cdd:cd14915    83 GAGKTVNTKRVIQYFATIAVTGekkkeeAASGkmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  311 RGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGvSEEERLEFQL--KQPQDYFYLNQHNLNIEDGEDlKHDFERLQQAM 388
Cdd:cd14915   163 ASADIETYLLEKSRVTFQLKAERSYHIFYQIMSN-KKPELIEMLLitTNPYDFAFVSQGEITVPSIDD-QEELMATDSAV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  389 EMVGFLPATKKQIFSVLSAILYLGNVTYKKRAtgRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILP 468
Cdd:cd14915   241 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQ--REEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKG 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  469 YSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEeavscLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYF 548
Cdd:cd14915   319 QTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQ-----YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFF 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  549 TQHIFKLEQEEYQGEGISWHNIDY-TDNVGCIHLIsKKPTGLFYLLDEESNFPHATSHTLLAKFKQQH--EDNKYFLGTP 625
Cdd:cd14915   394 NHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYEQHlgKSNNFQKPKP 472
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  626 V---LEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRgsdssyvrqligmdpvavfrwavlRAAIRAMAVLREAG 702
Cdd:cd14915   473 AkgkAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQ------------------------KSGMKTLAFLFSGG 528
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  703 RLRaeraekaaagisspatrshmeelprgastpseklyrctgldfsferseeldvnafedimafyESRKARGQsdlhnqi 782
Cdd:cd14915   529 QTA--------------------------------------------------------------EAEGGGGK------- 539
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  783 ikslKGLPWQGedprrllqslSLFQkprtsflkskgikqkqiipknlldskslrliismtlhdrttksllhlhkkkkppS 862
Cdd:cd14915   540 ----KGGKKKG----------SSFQ------------------------------------------------------T 551
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  863 ISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL- 941
Cdd:cd14915   552 VSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLn 631
                         810       820       830       840
                  ....*....|....*....|....*....|....*....|
gi 568955249  942 ---LPK-DVQPCREAIAALLEKLQVDRQNYQIGKTKVFLK 977
Cdd:cd14915   632 asaIPEgQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
MYSc_Myh2_mammals cd14912
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ...
162-977 8.36e-105

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: 352.11  E-value: 8.36e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  162 LLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISGES 241
Cdd:cd14912     3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  242 GSGKTQSTNFLIHCLTALSQKG------YASG-----VERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIV 310
Cdd:cd14912    83 GAGKTVNTKRVIQYFATIAVTGekkkeeITSGkmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  311 RGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGvSEEERLEFQL--KQPQDYFYLNQHNLNIEDGEDlKHDFERLQQAM 388
Cdd:cd14912   163 ASADIETYLLEKSRVTFQLKAERSYHIFYQITSN-KKPELIEMLLitTNPYDYPFVSQGEISVASIDD-QEELMATDSAI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  389 EMVGFLPATKKQIFSVLSAILYLGNVTYKKRAtgRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILP 468
Cdd:cd14912   241 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQ--REEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKG 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  469 YSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEeavscLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYF 548
Cdd:cd14912   319 QTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQ-----YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFF 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  549 TQHIFKLEQEEYQGEGISWHNIDY-TDNVGCIHLIsKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPVL 627
Cdd:cd14912   394 NHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKV 472
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  628 -----EPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRgsdssyvrqligmdpvavfrwavlRAAIRAMAvlreag 702
Cdd:cd14912   473 vkgkaEAHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQ------------------------KSAMKTLA------ 522
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  703 rlraeraekaaagisspatrshmeELPRGASTPseklyrctgldfsferseeldvnafedimafyESRKARGQSDlhnqi 782
Cdd:cd14912   523 ------------------------YLFSGAQTA--------------------------------EGASAGGGAK----- 541
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  783 ikslKGLPWQGedprrllqslSLFQkprtsflkskgikqkqiipknlldskslrliismtlhdrttksllhlhkkkkppS 862
Cdd:cd14912   542 ----KGGKKKG----------SSFQ------------------------------------------------------T 553
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  863 ISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL- 941
Cdd:cd14912   554 VSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLn 633
                         810       820       830       840
                  ....*....|....*....|....*....|....*....|
gi 568955249  942 ---LPK-DVQPCREAIAALLEKLQVDRQNYQIGKTKVFLK 977
Cdd:cd14912   634 asaIPEgQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
MYSc_Myh7 cd14917
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ...
162-977 1.36e-104

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: 351.33  E-value: 1.36e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  162 LLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISGES 241
Cdd:cd14917     3 VLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGES 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  242 GSGKTQSTNFLIHCLTAL------SQKGYASG---VERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRG 312
Cdd:cd14917    83 GAGKTVNTKRVIQYFAVIaaigdrSKKDQTPGkgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLAS 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  313 AVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGvSEEERLEFQL--KQPQDYFYLNQHNL---NIEDGEDLKhdfeRLQQA 387
Cdd:cd14917   163 ADIETYLLEKSRVIFQLKAERDYHIFYQILSN-KKPELLDMLLitNNPYDYAFISQGETtvaSIDDAEELM----ATDNA 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  388 MEMVGFLPATKKQIFSVLSAILYLGNVTYKKRAtgRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLIL 467
Cdd:cd14917   238 FDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQ--REEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTK 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  468 PYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEeavscLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYY 547
Cdd:cd14917   316 GQNVQQVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQ-----YFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQF 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  548 FTQHIFKLEQEEYQGEGISWHNIDY-TDNVGCIHLIsKKPTGLFYLLDEESNFPHATSHTLLAKFKQQH-------EDNK 619
Cdd:cd14917   391 FNHHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLI-EKPMGIMSILEEECMFPKATDMTFKAKLFDNHlgksnnfQKPR 469
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  620 YFLGTPvlEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLIGmdpvavfRWAvlraairamavlr 699
Cdd:cd14917   470 NIKGKP--EAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFA-------NYA------------- 527
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  700 eagrlraeraekaaagisspatrshmeelprGASTPSEklyrctgldfsferseeldvnafedimafyesrKARGqsdlh 779
Cdd:cd14917   528 -------------------------------GADAPIE---------------------------------KGKG----- 538
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  780 nqiiKSLKGLPWQgedprrllqslslfqkprtsflkskgikqkqiipknlldskslrliismtlhdrttksllhlhkkkk 859
Cdd:cd14917   539 ----KAKKGSSFQ------------------------------------------------------------------- 547
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  860 ppSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQ 939
Cdd:cd14917   548 --TVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYR 625
                         810       820       830       840
                  ....*....|....*....|....*....|....*....|...
gi 568955249  940 VLLPKDVQP-----CREAIAALLEKLQVDRQNYQIGKTKVFLK 977
Cdd:cd14917   626 ILNPAAIPEgqfidSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
MYSc_Myh1_mammals cd14910
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ...
162-977 5.70e-104

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: 349.80  E-value: 5.70e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  162 LLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISGES 241
Cdd:cd14910     3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  242 GSGKTQSTNFLIHCLTALSQKG------YASG-----VERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIV 310
Cdd:cd14910    83 GAGKTVNTKRVIQYFATIAVTGekkkeeATSGkmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  311 RGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGvSEEERLEFQL--KQPQDYFYLNQHNLNIEDGEDlKHDFERLQQAM 388
Cdd:cd14910   163 ASADIETYLLEKSRVTFQLKAERSYHIFYQIMSN-KKPDLIEMLLitTNPYDYAFVSQGEITVPSIDD-QEELMATDSAI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  389 EMVGFLPATKKQIFSVLSAILYLGNVTYKKRAtgRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILP 468
Cdd:cd14910   241 EILGFTSDERVSIYKLTGAVMHYGNMKFKQKQ--REEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKG 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  469 YSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEeavscLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYF 548
Cdd:cd14910   319 QTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQ-----YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFF 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  549 TQHIFKLEQEEYQGEGISWHNIDY-TDNVGCIHLIsKKPTGLFYLLDEESNFPHATSHTLLAKFKQQH--EDNKYFLGTP 625
Cdd:cd14910   394 NHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYEQHlgKSNNFQKPKP 472
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  626 V---LEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRgsdssyvrqligmdpvavfrwavlRAAIRAMAVLreag 702
Cdd:cd14910   473 AkgkVEAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQ------------------------KSSMKTLALL---- 524
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  703 rlraeraekaaagisspatrshmeelprgastpseklyrctgldFSFERSEELDVNAFEdimafyESRKARGQSdlhnqi 782
Cdd:cd14910   525 --------------------------------------------FSGAAAAEAEEGGGK------KGGKKKGSS------ 548
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  783 ikslkglpwqgedprrllqslslFQkprtsflkskgikqkqiipknlldskslrliismtlhdrttksllhlhkkkkppS 862
Cdd:cd14910   549 -----------------------FQ------------------------------------------------------T 551
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  863 ISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL- 941
Cdd:cd14910   552 VSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLn 631
                         810       820       830       840
                  ....*....|....*....|....*....|....*....|
gi 568955249  942 ---LPK-DVQPCREAIAALLEKLQVDRQNYQIGKTKVFLK 977
Cdd:cd14910   632 asaIPEgQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
MYSc_Myh6 cd14916
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ...
162-977 9.94e-103

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: 345.89  E-value: 9.94e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  162 LLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISGES 241
Cdd:cd14916     3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGES 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  242 GSGKTQSTNFLIHCLTALSQKGY----------ASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVR 311
Cdd:cd14916    83 GAGKTVNTKRVIQYFASIAAIGDrskkenpnanKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  312 GAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGvSEEERLEFQL--KQPQDYFYLNQHNLNIEDGEDlKHDFERLQQAME 389
Cdd:cd14916   163 SADIETYLLEKSRVIFQLKAERNYHIFYQILSN-KKPELLDMLLvtNNPYDYAFVSQGEVSVASIDD-SEELLATDSAFD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  390 MVGFLPATKKQIFSVLSAILYLGNVTYKKRAtgRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILPY 469
Cdd:cd14916   241 VLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQ--REEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  470 SLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEeavscLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFT 549
Cdd:cd14916   319 SVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQ-----YFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFN 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  550 QHIFKLEQEEYQGEGISWHNIDY-TDNVGCIHLIsKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTP--- 625
Cdd:cd14916   394 HHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLI-EKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPrnv 472
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  626 --VLEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRgsdssyvrqligmdpvavfrwavlRAAIRAMAVLreagr 703
Cdd:cd14916   473 kgKQEAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQ------------------------KSSLKLMATL----- 523
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  704 lraeraekaaagISSPAtrshmeelprGASTpseklyrctgldfsferseeldvnafedimafyesrkarGQSDlhnqii 783
Cdd:cd14916   524 ------------FSTYA----------SADT---------------------------------------GDSG------ 536
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  784 kslkglpwqgedprrllqslslfqkprtsflKSKGIKQKqiipknlldSKSLRliismtlhdrttksllhlhkkkkppSI 863
Cdd:cd14916   537 -------------------------------KGKGGKKK---------GSSFQ-------------------------TV 551
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  864 SAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLP 943
Cdd:cd14916   552 SALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNP 631
                         810       820       830
                  ....*....|....*....|....*....|....*....
gi 568955249  944 KDVQP-----CREAIAALLEKLQVDRQNYQIGKTKVFLK 977
Cdd:cd14916   632 AAIPEgqfidSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
MYSc_Myh14_mammals cd14930
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ...
160-977 5.69e-102

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: 344.00  E-value: 5.69e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISG 239
Cdd:cd14930     1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  240 ESGSGKTQSTNFLIHCLTALS-------QKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRG 312
Cdd:cd14930    81 ESGAGKTENTKKVIQYLAHVAsspkgrkEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  313 AVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNqHNLNIEDGEDlKHDFERLQQAMEMVG 392
Cdd:cd14930   161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLT-NGPSSSPGQE-RELFQETLESLRVLG 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  393 FLPATKKQIFSVLSAILYLGNVTYKKRatgRDEGLEVGPPEV-LDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILPYSL 471
Cdd:cd14930   239 FSHEEITSMLRMVSAVLQFGNIVLKRE---RNTDQATMPDNTaAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTK 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  472 SEAITARDSMAKSLYSALFDWIVLRINHALlnkkDMEEAVSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQH 551
Cdd:cd14930   316 EQADFALEALAKATYERLFRWLVLRLNRAL----DRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHT 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  552 IFKLEQEEYQGEGISWHNIDY-TDNVGCIHLISK--KPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPVL- 627
Cdd:cd14930   392 MFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLr 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  628 -EPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSdssyvrqligmdpvavfrwavlraairamavlreagrlra 706
Cdd:cd14930   472 dQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQS---------------------------------------- 511
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  707 eraekaaagisspatrshmeelprgastpseklyrctgldfsferSEELDVNAFEDIMAFYESRKARGQSDlhnqiiksl 786
Cdd:cd14930   512 ---------------------------------------------TDRLTAEIWKDVEGIVGLEQVSSLGD--------- 537
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  787 kGLPwqGEDPRRllqslSLFqkprtsflkskgikqkqiipknlldskslrliismtlhdRTTKSLlhlhkkkkppsisaq 866
Cdd:cd14930   538 -GPP--GGRPRR-----GMF---------------------------------------RTVGQL--------------- 555
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  867 FQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL----L 942
Cdd:cd14930   556 YKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILtpnaI 635
                         810       820       830
                  ....*....|....*....|....*....|....*
gi 568955249  943 PKDVQPCREAIAALLEKLQVDRQNYQIGKTKVFLK 977
Cdd:cd14930   636 PKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
MYSc_Myo25 cd14886
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ...
166-977 2.91e-101

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: 341.10  E-value: 2.91e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  166 LKLRFMQQKIYTYAGSILVAINPFKFLP-IYNPKYVKMYE--NQQLG---KLEPHVFALADVAYYAMLRKHVNQCIVISG 239
Cdd:cd14886     7 LRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRqaDTSRGfpsDLPPHSYAVAQSALNGLISDGISQSCIVSG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  240 ESGSGKTQSTNFLIHCLtALSQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRGAVVEKYL 319
Cdd:cd14886    87 ESGAGKTETAKQLMNFF-AYGHSTSSTDVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGLKGGKITSYM 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  320 LEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDLKHDFERLQQAMEMVgFLPATKK 399
Cdd:cd14886   166 LELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCYDAPGIDDQKEFAPVRSQLEKL-FSKNEID 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  400 QIFSVLSAILYLGNVTYKKR-ATGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILPYSLSEAITAR 478
Cdd:cd14886   245 SFYKCISGILLAGNIEFSEEgDMGVINAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNETIISPVTQAQAEVNI 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  479 DSMAKSLYSALFDWIVLRINHALlnkkdMEEAVSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQE 558
Cdd:cd14886   325 RAVAKDLYGALFELCVDTLNEII-----QFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFINQVFKSEIQ 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  559 EYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPVlEPAFIIQHFAG 638
Cdd:cd14886   400 EYEIEGIDHSMITFTDNSNVLAVFDKPNLSIFSFLEEQCLIQTGSSEKFTSSCKSKIKNNSFIPGKGS-QCNFTIVHTAA 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  639 RVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQligmdpvavfrwavlraairamavlreagrlraeraekaaagiss 718
Cdd:cd14886   479 TVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNK--------------------------------------------- 513
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  719 patrshmeelprgastpseklyrctgldfsferseeldvnAFEDIMAfyesrkargqsdlhnqiikslkglpwqgEDPRR 798
Cdd:cd14886   514 ----------------------------------------AFSDIPN----------------------------EDGNM 525
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  799 llqslslfqkpRTSFLKSKgikqkqiipknlldskslrliismtlhdrttksllhlhkkkkppsisaqFQTSLNKLLEAL 878
Cdd:cd14886   526 -----------KGKFLGST-------------------------------------------------FQLSIDQLMKTL 545
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  879 GKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLL---------PKDVqpc 949
Cdd:cd14886   546 SATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILIshnsssqnaGEDL--- 622
                         810       820
                  ....*....|....*....|....*...
gi 568955249  950 REAIAALLEKLQVDRQNYQIGKTKVFLK 977
Cdd:cd14886   623 VEAVKSILENLGIPCSDYRIGKTKVFLR 650
MYSc_Myh13 cd14923
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ...
162-977 5.88e-100

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: 337.81  E-value: 5.88e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  162 LLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISGES 241
Cdd:cd14923     3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGES 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  242 GSGKTQSTNFLIHCLTALS---------QKGYASG-VERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVR 311
Cdd:cd14923    83 GAGKTVNTKRVIQYFATIAvtgdkkkeqQPGKMQGtLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  312 GAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGvSEEERLEFQL--KQPQDYFYLNQHNL---NIEDGEDLKhdfeRLQQ 386
Cdd:cd14923   163 SADIETYLLEKSRVTFQLSSERSYHIFYQIMSN-KKPELIDLLLisTNPFDFPFVSQGEVtvaSIDDSEELL----ATDN 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  387 AMEMVGFLPATKKQIFSVLSAILYLGNVTYKKRAtgRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLI 466
Cdd:cd14923   238 AIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQ--REEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVT 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  467 LPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEAvsclsIGVLDIFGFEDFERNSFEQFCINYANEQLQY 546
Cdd:cd14923   316 KGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYF-----IGVLDIAGFEIFDFNSLEQLCINFTNEKLQQ 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  547 YFTQHIFKLEQEEYQGEGISWHNIDY-TDNVGCIHLIsKKPTGLFYLLDEESNFPHATSHTLLAKFKQQH--EDNKYFLG 623
Cdd:cd14923   391 FFNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYDQHlgKSNNFQKP 469
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  624 TPV---LEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRgsdssyvrqligmdpvavfrwavlRAAIRAMAVLre 700
Cdd:cd14923   470 KPAkgkAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQ------------------------KSSLKLLSFL-- 523
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  701 agrlraeraekaaagisspatRSHMEELPRGASTPSEKlyrctgldfsferseeldvnafedimafyeSRKARGQSdlhn 780
Cdd:cd14923   524 ---------------------FSNYAGAEAGDSGGSKK------------------------------GGKKKGSS---- 548
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  781 qiikslkglpwqgedprrllqslslFQkprtsflkskgikqkqiipknlldskslrliismtlhdrttksllhlhkkkkp 860
Cdd:cd14923   549 -------------------------FQ----------------------------------------------------- 550
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  861 pSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQV 940
Cdd:cd14923   551 -TVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRI 629
                         810       820       830       840
                  ....*....|....*....|....*....|....*....|..
gi 568955249  941 LLPKDVQP-----CREAIAALLEKLQVDRQNYQIGKTKVFLK 977
Cdd:cd14923   630 LNASAIPEgqfidSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
MYSc_Myo24A cd14937
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ...
160-674 3.82e-95

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: 322.73  E-value: 3.82e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYnpkyVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISG 239
Cdd:cd14937     1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVD----INEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  240 ESGSGKTQSTNFLIhcltalsqKGYASGVER------TILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRGA 313
Cdd:cd14937    77 ESGSGKTEASKLVI--------KYYLSGVKEdneisnTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSS 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  314 VVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDLKhDFERLqqameMVGF 393
Cdd:cd14937   149 SIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKNVVIPEIDDAK-DFGNL-----MISF 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  394 ----LPATKKQIFSVLSAILYLGNVTYKKRATGRDEG---LEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLI 466
Cdd:cd14937   223 dkmnMHDMKDDLFLTLSGLLLLGNVEYQEIEKGGKTNcseLDKNNLELVNEISNLLGINYENLKDCLVFTEKTIANQKIE 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  467 LPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEavsclSIGVLDIFGFEDFERNSFEQFCINYANEQLQY 546
Cdd:cd14937   303 IPLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNKELNN-----YIGILDIFGFEIFSKNSLEQLLINIANEEIHS 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  547 YFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKpTGLFYLLDEESNFPHATSHTLLAKFKQQHEDN-KYFLGTP 625
Cdd:cd14937   378 IYLYIVYEKETELYKAEDILIESVKYTTNESIIDLLRGK-TSIISILEDSCLGPVKNDESIVSVYTNKFSKHeKYASTKK 456
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 568955249  626 VLEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQL 674
Cdd:cd14937   457 DINKNFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSL 505
MYSc_Myo26 cd14887
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ...
160-977 6.35e-93

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: 319.29  E-value: 6.35e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  160 ANLLQNLKLRFMQ--------QKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHV 231
Cdd:cd14887     1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  232 NQCIVISGESGSGKTQSTNFLIHCLTALS--QKGYAS-GVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENG 308
Cdd:cd14887    81 SQSILISGESGAGKTETSKHVLTYLAAVSdrRHGADSqGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGRG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  309 IVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLlgVSEEERLEFQLKQPQDYFYLnqhnlniedgedlkHDFERLQQAM 388
Cdd:cd14887   161 KLTRASVATYLLANERVVRIPSDEFSFHIFYALC--NAAVAAATQKSSAGEGDPES--------------TDLRRITAAM 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  389 EMVGFLPATKKQIFSVLSAILYLGNV---------TYKKRatgRDEGLEVGPPEVLDTLSQLLKVK-------------- 445
Cdd:cd14887   225 KTVGIGGGEQADIFKLLAAILHLGNVefttdqepeTSKKR---KLTSVSVGCEETAADRSHSSEVKclssglkvteasrk 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  446 -RETLVEVLTKRKTVTVNDKLILP------------YSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEAVS 512
Cdd:cd14887   302 hLKTVARLLGLPPGVEGEEMLRLAlvsrsvretrsfFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKPSESDS 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  513 ---------CLSIGVLDIFGFEDFE---RNSFEQFCINYANEQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGcih 580
Cdd:cd14887   382 dedtpsttgTQTIGILDLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDCSAFPFS--- 458
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  581 liskkptglFYLLDEESNFPHATSHtllakfkqqhednkyFLGTPvlepafiiqhfagrvkyQIKDFREKNMDYMRPDIV 660
Cdd:cd14887   459 ---------FPLASTLTSSPSSTSP---------------FSPTP-----------------SFRSSSAFATSPSLPSSL 497
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  661 ALLRGSDSSYVRQLIGMDPVAVFrwavlraairamavlreagrlraeraekaaagisspatrshMEELPRGASTPSEklY 740
Cdd:cd14887   498 SSLSSSLSSSPPVWEGRDNSDLF-----------------------------------------YEKLNKNIINSAK--Y 534
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  741 RCTGLDFSFERSEELDVNAFEDIMafYESRkargqsDLHNQIIKSLKglpwqgEDPRRLLQSLSLFqkprtsflkskgik 820
Cdd:cd14887   535 KNITPALSRENLEFTVSHFACDVT--YDAR------DFCRANREATS------DELERLFLACSTY-------------- 586
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  821 qkqiIPKNLLDSKSLRLIISmtlhdrttksllhlhkkKKPPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCF 900
Cdd:cd14887   587 ----TRLVGSKKNSGVRAIS-----------------SRRSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIF 645
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  901 DDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPKDVQ---PCREAIAALLEKLQVDRQNYQIGKTKVFLK 977
Cdd:cd14887   646 EDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYETKLPMALRealTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
MYSc_Myo37 cd14898
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ...
162-651 2.57e-92

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: 312.60  E-value: 2.57e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  162 LLQNLKLRFMQQKIYTYAGSILVAINPFKflPIYNPKYVKMYENQQlGKLEPHVFALADVAYYAMLrKHVNQCIVISGES 241
Cdd:cd14898     3 TLEILEKRYASGKIYTKSGLVFLALNPYE--TIYGAGAMKAYLKNY-SHVEPHVYDVAEASVQDLL-VHGNQTIVISGES 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  242 GSGKTQSTNFLIHCLtaLSQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYleNGIVRGAVVEKYLLE 321
Cdd:cd14898    79 GSGKTENAKLVIKYL--VERTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKF--DGKITGAKFETYLLE 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  322 KSRLVSQEKDERNYHVFYYlllgVSEEERLEFQlkqpQDYFYLNQHNLNIEDGEDLKHDFERLQQAMEMVGFlpATKKQI 401
Cdd:cd14898   155 KSRVTHHEKGERNFHIFYQ----FCASKRLNIK----NDFIDTSSTAGNKESIVQLSEKYKMTCSAMKSLGI--ANFKSI 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  402 FSVLSAILYLGNVTYKkratgrDEG-LEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILPYSLSEAITARDS 480
Cdd:cd14898   225 EDCLLGILYLGSIQFV------NDGiLKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQARTIRNS 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  481 MAKSLYSALFDWIVLRINHALlnkkdmeEAVSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQEEY 560
Cdd:cd14898   299 MARLLYSNVFNYITASINNCL-------EGSGERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGMY 371
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  561 QGEGISWHNIDYTDNVGCIHLIsKKPTGLFYLLDEESNFPHATSHTLLAKFKQQhedNKYFLGTPVlEPAFIIQHFAGRV 640
Cdd:cd14898   372 KEEGIEWPDVEFFDNNQCIRDF-EKPCGLMDLISEESFNAWGNVKNLLVKIKKY---LNGFINTKA-RDKIKVSHYAGDV 446
                         490
                  ....*....|.
gi 568955249  641 KYQIKDFREKN 651
Cdd:cd14898   447 EYDLRDFLDKN 457
MYSc_Myo38 cd14899
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ...
160-674 2.05e-91

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: 314.34  E-value: 2.05e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLP-IYNPKYVKMY---ENQQLGK-------LEPHVFALADVAYYAMLR 228
Cdd:cd14899     1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydHNSQFGDrvtstdpREPHLFAVARAAYIDIVQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  229 KHVNQCIVISGESGSGKTQSTN-----FLIHCLTALSQKGYASG-----------VERTILGAGPVLEAFGNAKTAHNNN 292
Cdd:cd14899    81 NGRSQSILISGESGAGKTEATKiimtyFAVHCGTGNNNLTNSESisppaspsrttIEEQVLQSNPILEAFGNARTVRNDN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  293 SSRFGKFIQVNYL-ENGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLG----VSEEERLEFQLKQ-PQDYFYLNQ 366
Cdd:cd14899   161 SSRFGKFIELRFRdERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncVSKEQKQVLALSGgPQSFRLLNQ 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  367 HNLNIE-DGEDLKHDFERLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKRATGRDEGLEVGPPEVLDT-------- 437
Cdd:cd14899   241 SLCSKRrDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQIPHKGDDTVFADEARVMSSttgafdhf 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  438 --LSQLLKVKRETLVEVLTKRKTVTVNDKLILPYSLSEAITARDSMAKSLYSALFDWIVLRINHAL----------LNKK 505
Cdd:cd14899   321 tkAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLqrqasapwgaDESD 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  506 DMEEAVSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKK 585
Cdd:cd14899   401 VDDEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNNRACLELFEHR 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  586 PTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNK---YFLGTPVLEPA--FIIQHFAGRVKYQIKDFREKNMDYMRPDIV 660
Cdd:cd14899   481 PIGIFSLTDQECVFPQGTDRALVAKYYLEFEKKNshpHFRSAPLIQRTtqFVVAHYAGCVTYTIDGFLAKNKDSFCESAA 560
                         570
                  ....*....|....
gi 568955249  661 ALLRGSDSSYVRQL 674
Cdd:cd14899   561 QLLAGSSNPLIQAL 574
MYSc_Myo16 cd14878
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ...
160-674 1.78e-87

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


Pssm-ID: 276844 [Multi-domain]  Cd Length: 656  Bit Score: 300.96  E-value: 1.78e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYEN---QQLGKLEPHVFALADVAYYAMLRKHVNQCIV 236
Cdd:cd14878     1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLSssgQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  237 ISGESGSGKTQSTNFLIHCLTAlsqkgyASGVERTILG-----AGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLE-NGIV 310
Cdd:cd14878    81 LSGERGSGKTEASKQIMKHLTC------RASSSRTTFDsrfkhVNCILEAFGHAKTTLNDLSSCFIKYFELQFCErKKHL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  311 RGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLniEDGEDLKHDFER-----LQ 385
Cdd:cd14878   155 TGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTMR--EDVSTAERSLNReklavLK 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  386 QAMEMVGFLPATKKQIFSVLSAILYLGNVTYKkrATGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKL 465
Cdd:cd14878   233 QALNVVGFSSLEVENLFVILSAILHLGDIRFT--ALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMI 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  466 ILPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKkDMEEAVSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQ 545
Cdd:cd14878   311 IRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLQSQ-DEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMH 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  546 YYFTQHIFKLEQEEYQGEGISWHNIDYTDN-VGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHED---NKYF 621
Cdd:cd14878   390 HYINEVLFLQEQTECVQEGVTMETAYSPGNqTGVLDFFFQKPSGFLSLLDEESQMIWSVEPNLPKKLQSLLESsntNAVY 469
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568955249  622 L------GTPVLE---PAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQL 674
Cdd:cd14878   470 SpmkdgnGNVALKdqgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHL 531
MYSc_Myo12 cd14874
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ...
160-977 4.71e-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: 278.29  E-value: 4.71e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYenqqlgklepHVFALADVAYYAMLRKHVN-QCIVIS 238
Cdd:cd14874     1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  239 GESGSGKTQSTNFLIHCLTALSQKGYASGVERTIlgaGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRGAVVEKY 318
Cdd:cd14874    71 GESGSGKSYNAFQVFKYLTSQPKSKVTTKHSSAI---ESVFKSFGCAKTLKNDEATRFGCSIDLLYKRNVLTGLNLKYTV 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  319 LLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDLKHdFERLQQAMEMVGFLPATK 398
Cdd:cd14874   148 PLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTENIQSDVNH-FKHLEDALHVLGFSDDHC 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  399 KQIFSVLSAILYLGNVTYKKRATGRDEG--LEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVndklilPYSLSEAIT 476
Cdd:cd14874   227 ISIYKIISTILHIGNIYFRTKRNPNVEQdvVEIGNMSEVKWVAFLLEVDFDQLVNFLLPKSEDGT------TIDLNAALD 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  477 ARDSMAKSLYSALFDWIVLRINHALlnKKDMEEAVsclsIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLE 556
Cdd:cd14874   301 NRDSFAMLIYEELFKWVLNRIGLHL--KCPLHTGV----ISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHSFHDQ 374
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  557 QEEYQGEGISwhnIDYT-----DNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPVLEP-A 630
Cdd:cd14874   375 LVDYAKDGIS---VDYKvpnsiENGKTVELLFKKPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSSYGKARNKERlE 451
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  631 FIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLIgmdpvavfrwavlraairamavlreagrlraerae 710
Cdd:cd14874   452 FGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLF----------------------------------- 496
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  711 kaaagisspatRSHmeelprgastpseklyrctgldfSFERSEELdvnafedimafyesrkargqsdlhnqiikslkglp 790
Cdd:cd14874   497 -----------ESY-----------------------SSNTSDMI----------------------------------- 507
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  791 wqgedprrllqslslfqkprtsflkskgIKQKQIIPKNlldskslrliiSMTLHDRTTKSLLHlhkkkkppsisaqfqts 870
Cdd:cd14874   508 ----------------------------VSQAQFILRG-----------AQEIADKINGSHAH----------------- 531
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  871 lnkllealgkaepfFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPKDVQPC- 949
Cdd:cd14874   532 --------------FVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCLLPGDIAMCq 597
                         810       820       830
                  ....*....|....*....|....*....|.
gi 568955249  950 --REAIAALLEKLQVDRQN-YQIGKTKVFLK 977
Cdd:cd14874   598 neKEIIQDILQGQGVKYENdFKIGTEYVFLR 628
MYSc_Myo20 cd14881
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ...
163-664 3.82e-79

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: 275.84  E-value: 3.82e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  163 LQNLKLRFMQQKIYTYAGSILVAINPFKFLPiyNPKYVKMYENQQLGKLephvfaLADVAYYAMlRKHVN----QCIVIS 238
Cdd:cd14881     4 MKCLQARFYAKEFFTNVGPILLSVNPYRDVG--NPLTLTSTRSSPLAPQ------LLKVVQEAV-RQQSEtgypQAIILS 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  239 GESGSGKTQSTNFLIHCLTALSQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRGAVvEKY 318
Cdd:cd14881    75 GTSGSGKTYASMLLLRQLFDVAGGGPETDAFKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQVTDGALYRTKI-HCY 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  319 LLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLK--QPQDYFYLNQHnlniEDGEDLKHDFERLQQAMEMVGFLPA 396
Cdd:cd14881   154 FLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDgySPANLRYLSHG----DTRQNEAEDAARFQAWKACLGILGI 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  397 TKKQIFSVLSAILYLGNVTYKKRATGrdeGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRktvTVNDKLILPYSLSEAIT 476
Cdd:cd14881   230 PFLDVVRVLAAVLLLGNVQFIDGGGL---EVDVKGETELKSVAALLGVSGAALFRGLTTR---THNARGQLVKSVCDANM 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  477 A---RDSMAKSLYSALFDWIVLRIN-----HALLNKKDMEEavsclSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYF 548
Cdd:cd14881   304 SnmtRDALAKALYCRTVATIVRRANslkrlGSTLGTHATDG-----FIGILDMFGFEDPKPSQLEHLCINLCAETMQHFY 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  549 TQHIFKLEQEEYQGEGISWH-NIDYTDNVGCIHLISKKPTGLFYLLDEESNfPHATSHTLLAKFKQQHEDNKYFLGT-PV 626
Cdd:cd14881   379 NTHIFKSSIESCRDEGIQCEvEVDYVDNVPCIDLISSLRTGLLSMLDVECS-PRGTAESYVAKIKVQHRQNPRLFEAkPQ 457
                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 568955249  627 LEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLR 664
Cdd:cd14881   458 DDRMFGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFY 495
MYSc_Myo44 cd14905
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ...
162-671 5.84e-78

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: 273.51  E-value: 5.84e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  162 LLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGkLEPHVFALADVAYYAMLRKHVNQCIVISGES 241
Cdd:cd14905     3 LINIIQARYKKEIIYTYIGPILVSVNPLRYLPFLHSQELVRNYNQRRG-LPPHLFALAAKAISDMQDFRRDQLIFIGGES 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  242 GSGKTQSTNFLIHCL--TALSQKGYasgVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRGAVVEKYL 319
Cdd:cd14905    82 GSGKSENTKIIIQYLltTDLSRSKY---LRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKLYSYF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  320 LEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQ-HNLNIEDGEDlKHDFERLQQAMEMVGFLPATK 398
Cdd:cd14905   159 LDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQgGSISVESIDD-NRVFDRLKMSFVFFDFPSEKI 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  399 KQIFSVLSAILYLGNVTYKKratgRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNdklilpyslsEAITAR 478
Cdd:cd14905   238 DLIFKTLSFIIILGNVTFFQ----KNGKTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVN----------EAVENR 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  479 DSMAKSLYSALFDWIVlrinhALLNKKdMEEAVSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQE 558
Cdd:cd14905   304 DSLARSLYSALFHWII-----DFLNSK-LKPTQYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQR 377
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  559 EYQGEGISWHN-IDYTDNVGCIHLISKkptgLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPvlePAFIIQHFA 637
Cdd:cd14905   378 EYQTERIPWMTpISFKDNEESVEMMEK----IINLLDQESKNINSSDQIFLEKLQNFLSRHHLFGKKP---NKFGIEHYF 450
                         490       500       510
                  ....*....|....*....|....*....|....
gi 568955249  638 GRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYV 671
Cdd:cd14905   451 GQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYL 484
MYSc_Myo21 cd14882
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ...
161-977 3.29e-73

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: 258.90  E-value: 3.29e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  161 NLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISGE 240
Cdd:cd14882     2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  241 SGSGKTqsTNFLiHCLTALSQKGYA-SGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRGAVVEKYL 319
Cdd:cd14882    82 SYSGKT--TNAR-LLIKHLCYLGDGnRGATGRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFWMYQ 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  320 LEKSRLVSQEKDERNYHVFYYLLLGVSEEERL-EFQLKQPQDYFYLNQHNLNIEDG-----EDLKHDFERLQQAMEMVGF 393
Cdd:cd14882   159 LEKLRVSTTDGNQSNFHIFYYFYDFIEAQNRLkEYNLKAGRNYRYLRIPPEVPPSKlkyrrDDPEGNVERYKEFEEILKD 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  394 LPATKKQ---IFSVLSAILYLGNVTYKKratGRDEGlEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILPYS 470
Cdd:cd14882   239 LDFNEEQletVRKVLAAILNLGEIRFRQ---NGGYA-ELENTEIASRVAELLRLDEKKFMWALTNYCLIKGGSAERRKHT 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  471 LSEAITARDSMAKSLYSALFDWIVLRINHALLnkkdMEEAV--SCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYF 548
Cdd:cd14882   315 TEEARDARDVLASTLYSRLVDWIINRINMKMS----FPRAVfgDKYSISIHDMFGFECFHRNRLEQLMVNTLNEQMQYHY 390
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  549 TQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLlakfKQQHEDNKYFLgTPVLE 628
Cdd:cd14882   391 NQRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPDGLFYIIDDASRSCQDQNYIM----DRIKEKHSQFV-KKHSA 465
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  629 PAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLIgmdpvavfrwavlraairamavlreagrlraer 708
Cdd:cd14882   466 HEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMF--------------------------------- 512
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  709 aekaaagisspaTRSHMEELPRGASTpseklYRCTGLdfsferseeldvnafedimafyesrkargqsdlhnQIIKSLkg 788
Cdd:cd14882   513 ------------TNSQVRNMRTLAAT-----FRATSL-----------------------------------ELLKML-- 538
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  789 lpwqgedprrllqslslfqkprtsflkskgikqkqiipknlldskslrliismtlhdrttksllhlhkkkkppSISAqfq 868
Cdd:cd14882   539 -------------------------------------------------------------------------SIGA--- 542
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  869 tslnkllealGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL---LPKD 945
Cdd:cd14882   543 ----------NSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQEFLRRYQFLafdFDET 612
                         810       820       830
                  ....*....|....*....|....*....|..
gi 568955249  946 VQPCREAIAALLEKLQVdrQNYQIGKTKVFLK 977
Cdd:cd14882   613 VEMTKDNCRLLLIRLKM--EGWAIGKTKVFLK 642
MYSc_Myo23 cd14884
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ...
160-673 2.42e-72

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: 257.53  E-value: 2.42e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLP-IYNPK----YVKMYENQQLGK---LEPHVFALADVAYYAMLRKHV 231
Cdd:cd14884     1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDvmnvYLHKKSNSAASAapfPKAHIYDIANMAYKNMRGKLK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  232 NQCIVISGESGSGKTQSTNFLIHCLTALSQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLE----- 306
Cdd:cd14884    81 RQTIVVSGHSGSGKTENCKFLFKYFHYIQTDSQMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFEEventq 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  307 ----NGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEE----RL--------------EFQLKQPQDYFYL 364
Cdd:cd14884   161 knmfNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDlarrNLvrncgvygllnpdeSHQKRSVKGTLRL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  365 NQHNLNIEDGEDLKHD--FERLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYKkratgrdeglevgppevldTLSQLL 442
Cdd:cd14884   241 GSDSLDPSEEEKAKDEknFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRAYK-------------------AAAECL 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  443 KVKRETLVEVLTKRKTVTVNDKLILPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEAVSCLS------- 515
Cdd:cd14884   302 QIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEKDESDNEDIysineai 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  516 IGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKkptgLFYLLDE 595
Cdd:cd14884   382 ISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAPSYSDTLIFIAK----IFRRLDD 457
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  596 ESNFpHATSHT---------LLAKFKQQHEDNKYFLG-------------TPVLEPAFIIQHFAGRVKYQIKDFREKNMD 653
Cdd:cd14884   458 ITKL-KNQGQKktddhffryLLNNERQQQLEGKVSYGfvlnhdadgtakkQNIKKNIFFIRHYAGLVTYRINNWIDKNSD 536
                         570       580
                  ....*....|....*....|
gi 568955249  654 YMRPDIVALLRGSDSSYVRQ 673
Cdd:cd14884   537 KIETSIETLISCSSNRFLRE 556
RhoGAP_myosin_IXA cd04406
RhoGAP_myosin_IXA: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
1704-1889 7.50e-70

RhoGAP_myosin_IXA: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in myosins IXA. Class IX myosins contain a characteristic head domain, a neck domain and a tail domain which contains a C6H2-zinc binding motif and a Rho-GAP domain. Class IX myosins are single-headed, processive myosins that are partly cytoplasmic, and partly associated with membranes and the actin cytoskeleton. Class IX myosins are implicated in the regulation of neuronal morphogenesis and function of sensory systems, like the inner ear. There are two major isoforms, myosin IXA and IXB with several splice variants, which are both expressed in developing neurons. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239871  Cd Length: 186  Bit Score: 232.58  E-value: 7.50e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1704 FGVCVDSLTSDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKLEDFPIHAITGVLKQWLRE 1783
Cdd:cd04406     1 FGVELSRLTSEDRSVPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDANSVNLDDYNIHVIASVFKQWLRD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1784 LPEPLMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRC 1863
Cdd:cd04406    81 LPNPLMTFELYEEFLRAMGLQERRETVRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEETNRMSANALAIVFAPCILRC 160
                         170       180
                  ....*....|....*....|....*.
gi 568955249 1864 PDNSDPLTSMKDVLKITTCVEMLIKE 1889
Cdd:cd04406   161 PDTTDPLQSVQDISKTTTCVELIVCE 186
MYSc_Myo18 cd01386
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ...
163-642 8.08e-70

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: 249.92  E-value: 8.08e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  163 LQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISGESG 242
Cdd:cd01386     4 LHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLGRSG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  243 SGKTQSTNFLIH--CLTALSQKGYASgVERtILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRGAVVEKYLL 320
Cdd:cd01386    84 SGKTTNCRHILEylVTAAGSVGGVLS-VEK-LNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASIQTLLL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  321 EKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQ--PQDYFYLNQHnLNIEDGEDLKHDFERLQQAMEMVGFLPATK 398
Cdd:cd01386   162 ERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQlaESNSFGIVPL-QKPEDKQKAAAAFSKLQAAMKTLGISEEEQ 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  399 KQIFSVLSAILYLGnvtykkrATGRDEGLEVGPPEVLDTLS-----QLLKVKRETLVEVLTK--------RKTVTVNDKL 465
Cdd:cd01386   241 RAIWSILAAIYHLG-------AAGATKAASAGRKQFARPEWaqraaYLLGCTLEELSSAIFKhhlsggpqQSTTSSGQES 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  466 ILPYSLSE----AITARDSMAKSLYSALFDWIVlrinhALLNKKDMEEAVSCLSIGVLDIFGFED-----FERNS-FEQF 535
Cdd:cd01386   314 PARSSSGGpkltGVEALEGFAAGLYSELFAAVV-----SLINRSLSSSHHSTSSITIVDTPGFQNpahsgSQRGAtFEDL 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  536 CINYANEQLQYYFTQHIFKLEQEEYQGEGIswhNIDYTDNVGCIH----LISKKPT--------------GLFYLLDEES 597
Cdd:cd01386   389 CHNYAQERLQLLFHERTFVAPLERYKQENV---EVDFDLPELSPGalvaLIDQAPQqalvrsdlrdedrrGLLWLLDEEA 465
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568955249  598 NFPHATSHTLLAKFKQQHEDNKYFLGTPVLEPA-----FIIQHFAGR--VKY 642
Cdd:cd01386   466 LYPGSSDDTFLERLFSHYGDKEGGKGHSLLRRSegplqFVLGHLLGTnpVEY 517
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
1717-1890 3.63e-58

GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases. etter domain limits and outliers.


Pssm-ID: 214618  Cd Length: 174  Bit Score: 198.64  E-value: 3.63e-58
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249   1717 SVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVK-LEDFPIHAITGVLKQWLRELPEPLMTFAQYG 1795
Cdd:smart00324    2 PIPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDPDLdLSEYDVHDVAGLLKLFLRELPEPLITYELYE 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249   1796 DFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRCPDNSDPltSMKD 1875
Cdd:smart00324   82 EFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGEVA--SLKD 159
                           170
                    ....*....|....*
gi 568955249   1876 VLKITTCVEMLIKEQ 1890
Cdd:smart00324  160 IRHQNTVIEFLIENA 174
MYSc_Myo32 cd14893
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ...
162-666 2.33e-57

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: 214.06  E-value: 2.33e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  162 LLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQ----------LGKLEPHVFALADVAYYAMLRKHV 231
Cdd:cd14893     3 ALYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSReqtplyekdtVNDAPPHVFALAQNALRCMQDAGE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  232 NQCIVISGESGSGKTQSTNFLIHCLT-----------ALSQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFI 300
Cdd:cd14893    83 DQAVILLGGMGAGKSEAAKLIVQYLCeigdeteprpdSEGASGVLHPIGQQILHAFTILEAFGNAATRQNRNSSRFAKMI 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  301 QVNYLENGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQL---KQPQDYFYLNQHNLNIEDGEDL 377
Cdd:cd14893   163 SVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHDPTLRDSLemnKCVNEFVMLKQADPLATNFALD 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  378 KHDFERLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKRATGRDEGLEVGPPEVLDTLSQLLKVKRE-TLVEVLTKR 456
Cdd:cd14893   243 ARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFVPDPEGGKSVGGANSTTVSDAQSCALKDPAQiLLAAKLLEV 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  457 KTVTV-------------NDKLILPY---SLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEE----AVSCLSI 516
Cdd:cd14893   323 EPVVLdnyfrtrqffskdGNKTVSSLkvvTVHQARKARDTFVRSLYESLFNFLVETLNGILGGIFDRYEksniVINSQGV 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  517 GVLDIFGFEDFE--RNSFEQFCINYANEQLQYYFTQHIFK-----LEQEEYQGEG-ISWH-NIDYT-DNVGCIHLISKKP 586
Cdd:cd14893   403 HVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYVQNTLAinfsfLEDESQQVENrLTVNsNVDITsEQEKCLQLFEDKP 482
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  587 TGLFYLLDEESNFPHATSHTLLAKFKQQHED---------NKYFLGTPVLEPA-----FIIQHFAGRVKYQIKDFREKNM 652
Cdd:cd14893   483 FGIFDLLTENCKVRLPNDEDFVNKLFSGNEAvgglsrpnmGADTTNEYLAPSKdwrllFIVQHHCGKVTYNGKGLSSKNM 562
                         570
                  ....*....|....
gi 568955249  653 DYMRPDIVALLRGS 666
Cdd:cd14893   563 LSISSTCAAIMQSS 576
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
1719-1868 8.19e-56

RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.


Pssm-ID: 425782  Cd Length: 152  Bit Score: 191.25  E-value: 8.19e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  1719 PIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAV-KLEDFPIHAITGVLKQWLRELPEPLMTFAQYGDF 1797
Cdd:pfam00620    1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDSGEDVDlDLEEEDVHDVASLLKLFLRELPEPLLTFELYEEF 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568955249  1798 LRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRCPDNSD 1868
Cdd:pfam00620   81 IEAAKSEDEEERIEALRELLEKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLLRPPDSES 151
RA_Myosin-IXb cd17217
Ras-associating (RA) domain found in Myosin-IXb; Myosin-IXb, also termed myosin-9b (Myo9b), is ...
16-112 1.68e-55

Ras-associating (RA) domain found in Myosin-IXb; Myosin-IXb, also termed myosin-9b (Myo9b), is a motor protein with a Rho GTPase activating domain (RhoGAP); it is an actin-dependent motor protein of the unconventional myosin IX class. It is expressed abundantly in tissues of the immune system, like lymph nodes, thymus, and spleen and in several immune cells including dendritic cells, macrophages and CD4+ T. Myosin-IXb contains a Ras-associating (RA) domain, a motor domain, a protein kinase C conserved region 1 (C1), and a RhoGAP domain. Its RA domain is located at its head domain and has the beta-grasp ubiquitin-like fold with unknown function. Myosin-IXb acts as a motorized signaling molecule that links Rho signaling to the dynamic actin cytoskeleton. It regulates leukocyte migration by controlling RhoA signaling. Myosin-IXb is also involved in the development of autoimmune diseases, including rheumatoid arthritis, systemic lupus erythematosus and type 1 diabetes. Moreover, Myosin-IXb is a ROBO-interacting protein that suppresses RhoA activity in lung cancer cells.


Pssm-ID: 340737  Cd Length: 96  Bit Score: 188.08  E-value: 1.68e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249   16 TYHLHIYPQLSSAgSQTSCRVTATKDSTTSDVIQDVVASLHLDGSKHYVLVEVKESGGEEWVLDASDSPVHRVLLWPRRA 95
Cdd:cd17217     1 VYALQIYPQLSAE-SSTCCIVLATKEATASDVIKDAVATLGLDSSKPYVLAEVKESGGEEWVLDANDSPVQRVLLWPRKA 79
                          90
                  ....*....|....*..
gi 568955249   96 QDEHPQEDGYYFLLQER 112
Cdd:cd17217    80 QDDHPQSDGYYFLLQER 96
RhoGAP cd00159
RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like ...
1719-1889 1.88e-53

RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like small GTPases. Small GTPases (G proteins) cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when bound to GDP. The Rho family of small G proteins, which includes Cdc42Hs, activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. G proteins generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude. The RhoGAPs are one of the major classes of regulators of Rho G proteins.


Pssm-ID: 238090  Cd Length: 169  Bit Score: 185.20  E-value: 1.88e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1719 PIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKLEDFPIHAITGVLKQWLRELPEPLMTFAQYGDFL 1798
Cdd:cd00159     1 PLIIEKCIEYLEKNGLNTEGIFRVSGSASKIEELKKKFDRGEDIDDLEDYDVHDVASLLKLYLRELPEPLIPFELYDEFI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1799 RAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRCPDNSDplTSMKDVLK 1878
Cdd:cd00159    81 ELAKIEDEEERIEALKELLKSLPPENRDLLKYLLKLLHKISQNSEVNKMTASNLAIVFAPTLLRPPDSDD--ELLEDIKK 158
                         170
                  ....*....|.
gi 568955249 1879 ITTCVEMLIKE 1889
Cdd:cd00159   159 LNEIVEFLIEN 169
MYSc_Myo24B cd14938
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ...
162-674 4.16e-52

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: 197.75  E-value: 4.16e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  162 LLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMY---ENQQLGKLEPHVFALADVAYYAMLRKhvNQCIVIS 238
Cdd:cd14938     3 VLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYkciDCIEDLSLNEYHVVHNALKNLNELKR--NQSIIIS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  239 GESGSGKTQSTNFLIHCL----------------------TALSQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRF 296
Cdd:cd14938    81 GESGSGKSEIAKNIINFIayqvkgsrrlptnlndqeedniHNEENTDYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  297 GKFIQVnYLENGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYfylnqHNLNIEDGED 376
Cdd:cd14938   161 SKFCTI-HIENEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENY-----SMLNNEKGFE 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  377 LKHDFE-RLQQAMEMVGFLPATKKQI---FSVLSAILYLGNV----TYKKRAT---GRDEGLEVGPPEVLDTLS------ 439
Cdd:cd14938   235 KFSDYSgKILELLKSLNYIFDDDKEIdfiFSVLSALLLLGNTeivkAFRKKSLlmgKNQCGQNINYETILSELEnsedig 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  440 ------------QLLKVKRETLVEVLTKRktVTVNDKLILPYSLSEAITAR-DSMAKSLYSALFDWIVLRINHALLNKKD 506
Cdd:cd14938   315 ldenvknlllacKLLSFDIETFVKYFTTN--YIFNDSILIKVHNETKIQKKlENFIKTCYEELFNWIIYKINEKCTQLQN 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  507 MEEAVSclSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQEEYQGEGISW-HNIDYTDNVG-CIHLISK 584
Cdd:cd14938   393 ININTN--YINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCeYNSENIDNEPlYNLLVGP 470
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  585 KPTGLFYLLDEESN---FPHATSHTL-LAKFKQqheDNKYFLGTPVLE--PAFIIQHFAGRVKYQIKDFREKNMDYMRPD 658
Cdd:cd14938   471 TEGSLFSLLENVSTktiFDKSNLHSSiIRKFSR---NSKYIKKDDITGnkKTFVITHSCGDIIYNAENFVEKNIDILTNR 547
                         570
                  ....*....|....*.
gi 568955249  659 IVALLRGSDSSYVRQL 674
Cdd:cd14938   548 FIDMVKQSENEYMRQF 563
RhoGAP_ARAP cd04385
RhoGAP_ARAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
1711-1861 2.23e-38

RhoGAP_ARAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in ARAPs. ARAPs (also known as centaurin deltas) contain, besides the RhoGAP domain, an Arf GAP, ankyrin repeat ras-associating, and PH domains. Since their ArfGAP activity is PIP3-dependent, ARAPs are considered integration points for phosphoinositide, Arf and Rho signaling. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239850  Cd Length: 184  Bit Score: 142.45  E-value: 2.23e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1711 LTSDkaSVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKL---EDFPiHAITGVLKQWLRELPEP 1787
Cdd:cd04385    10 LTDN--DIPVIVDKCIDFITQHGLMSEGIYRKNGKNSSVKKLLEAFRKDARSVQLregEYTV-HDVADVLKRFLRDLPDP 86
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568955249 1788 LMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLL 1861
Cdd:cd04385    87 LLTSELHAEWIEAAELENKDERIARYKELIRRLPPINRATLKVLIGHLYRVQKHSDENQMSVHNLALVFGPTLF 160
C1_Myosin-IXb cd20884
protein kinase C conserved region 1 (C1 domain) found in unconventional myosin-IXb and similar ...
1634-1691 1.87e-36

protein kinase C conserved region 1 (C1 domain) found in unconventional myosin-IXb and similar proteins; Myosin-IXb, also called unconventional myosin-9b (Myo9b), is an actin-dependent motor protein of the unconventional myosin IX class. It is expressed abundantly in tissues of the immune system, like lymph nodes, thymus, and spleen, and in several immune cells including dendritic cells, macrophages and CD4+ T cells. Myosin-IXb contains a Ras-associating (RA) domain, a motor domain, a protein kinase C conserved region 1 (C1), and a Rho GTPase activating (RhoGAP) domain. Myosin-IXb acts as a motorized signaling molecule that links Rho signaling to the dynamic actin cytoskeleton. It regulates leukocyte migration by controlling RhoA signaling. Myosin-IXb is also involved in the development of autoimmune diseases, including rheumatoid arthritis, systemic lupus erythematosus, and type 1 diabetes. Moreover, Myosin-IXb is a ROBO-interacting protein that suppresses RhoA activity in lung cancer cells. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410434  Cd Length: 58  Bit Score: 132.29  E-value: 1.87e-36
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568955249 1634 QEHNGHVFASYQVNIPQSCEQCLSYIWLMDKALLCSVCKMTCHKKCVHKIQSYCSYTG 1691
Cdd:cd20884     1 EEYNGHVFTSYQVNIMQSCEQCSSYIWAMEKALLCSVCKMTCHKKCLSKIQSHCSSTC 58
RA_Myosin-IX cd01779
Ras-associating (RA) domain found in Myosin-IX; Myosins IX (Myo9) is a class of unique motor ...
18-112 3.52e-36

Ras-associating (RA) domain found in Myosin-IX; Myosins IX (Myo9) is a class of unique motor proteins with a common structure of an N-terminal extension preceding a myosin head homologous to the Ras-association (RA) domain, a head (motor) domain, a neck with IQ motifs that bind light chains and a C-terminal tail containing a Rho-GTPase activating protein (RhoGAP) domain. The RA domain is located at its head domain and has the beta-grasp ubiquitin-like fold with unknown function. There are two genes for myosins IX in humans, IXa and IXb, that are different in their expression and localization. IXa is expressed abundantly in brain and testis and IXb is expressed abundantly in tissues of the immune system.


Pssm-ID: 340477  Cd Length: 97  Bit Score: 132.83  E-value: 3.52e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249   18 HLHIYPQLSSAgSQTSCRVTATKDSTTSDVIQDVVASLHLDGSKHYVLVEVKESGG---EEWVLDASDSPVHRVLLWPRR 94
Cdd:cd01779     1 MVRVYPGALSP-ETEFLSVEATKQTTASEVIECLVAKLRLDKAECYELAEVCGSGGqgcKERRLGPSENPVQVQLLWPKM 79
                          90
                  ....*....|....*...
gi 568955249   95 AQDEHPQEDGYYFLLQER 112
Cdd:cd01779    80 AGDSDNQVTSYRFFLREK 97
RhoGAP_nadrin cd04386
RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1704-1889 1.36e-35

RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Nadrin-like proteins. Nadrin, also named Rich-1, has been shown to be involved in the regulation of Ca2+-dependent exocytosis in neurons and recently has been implicated in tight junction maintenance in mammalian epithelium. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239851  Cd Length: 203  Bit Score: 135.28  E-value: 1.36e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1704 FGVCV-DSLTSDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKLEDF---PiHAITGVLKQ 1779
Cdd:cd04386     5 FGTPLeEHLKRTGREIALPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKAALDAGTFSLPLDEFysdP-HAVASALKS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1780 WLRELPEPLMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPC 1859
Cdd:cd04386    84 YLRELPDPLLTYNLYEDWVQAANKPDEDERLQAIWRILNKLPRENRDNLRYLIKFLSKLAQKSDENKMSPSNIAIVLAPN 163
                         170       180       190
                  ....*....|....*....|....*....|.
gi 568955249 1860 LLRCP-DNSDPLTSMKDVLKITTCVEMLIKE 1889
Cdd:cd04386   164 LLWAKnEGSLAEMAAGTSVHVVAIVELIISH 194
RhoGAP_fRGD1 cd04398
RhoGAP_fRGD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1704-1873 2.41e-35

RhoGAP_fRGD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal RGD1-like proteins. Yeast Rgd1 is a GAP protein for Rho3 and Rho4 and plays a role in low-pH response. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239863  Cd Length: 192  Bit Score: 134.07  E-value: 2.41e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1704 FGVCVDSLTS-DKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKL---EDF--PIHAITGVL 1777
Cdd:cd04398     1 FGVPLEDLILrEGDNVPNIVYQCIQAIENFGLNLEGIYRLSGNVSRVNKLKELFDKDPLNVLLispEDYesDIHSVASLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1778 KQWLRELPEPLMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFA 1857
Cdd:cd04398    81 KLFFRELPEPLLTKALSREFIEAAKIEDESRRRDALHGLINDLPDANYATLRALMFHLARIKEHESVNRMSVNNLAIIWG 160
                         170
                  ....*....|....*.
gi 568955249 1858 PCLLrcPDNSDPLTSM 1873
Cdd:cd04398   161 PTLM--NAAPDNAADM 174
RhoGAP_ARHGAP27_15_12_9 cd04403
RhoGAP_ARHGAP27_15_12_9: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
1704-1873 2.95e-34

RhoGAP_ARHGAP27_15_12_9: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ARHGAP27 (also called CAMGAP1), ARHGAP15, 12 and 9-like proteins; This subgroup of ARHGAPs are multidomain proteins that contain RhoGAP, PH, SH3 and WW domains. Most members that are studied show GAP activity towards Rac1, some additionally show activity towards Cdc42. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239868 [Multi-domain]  Cd Length: 187  Bit Score: 130.59  E-value: 2.95e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1704 FGVCVDSLTS-DKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAA----VKLEDfpIHAITGVLK 1778
Cdd:cd04403     1 FGCHLEALCQrENSTVPKFVRLCIEAVEKRGLDVDGIYRVSGNLAVIQKLRFAVDHDEKLdlddSKWED--IHVITGALK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1779 QWLRELPEPLMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAP 1858
Cdd:cd04403    79 LFFRELPEPLFPYSLFNDFVAAIKLSDYEQRVSAVKDLIKSLPKPNHDTLKMLFRHLCRVIEHGEKNRMTTQNLAIVFGP 158
                         170
                  ....*....|....*..
gi 568955249 1859 CLLRcP--DNSDPLTSM 1873
Cdd:cd04403   159 TLLR-PeqETGNIAVHM 174
RhoGAP_chimaerin cd04372
RhoGAP_chimaerin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1711-1888 5.01e-33

RhoGAP_chimaerin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of chimaerins. Chimaerins are a family of phorbolester- and diacylglycerol-responsive GAPs specific for the Rho-like GTPase Rac. Chimaerins exist in two alternative splice forms that each contain a C-terminal GAP domain, and a central C1 domain which binds phorbol esters, inducing a conformational change that activates the protein; one splice form is lacking the N-terminal Src homology-2 (SH2) domain. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239837  Cd Length: 194  Bit Score: 127.63  E-value: 5.01e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1711 LTSDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTD--PAAVKLEDFP-IHAITGVLKQWLRELPEP 1787
Cdd:cd04372     9 VKAHNTQRPMVVDMCIREIEARGLQSEGLYRVSGFAEEIEDVKMAFDRDgeKADISATVYPdINVITGALKLYFRDLPIP 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1788 LMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRCPDnS 1867
Cdd:cd04372    89 VITYDTYPKFIDAAKISNPDERLEAVHEALMLLPPAHYETLRYLMEHLKRVTLHEKDNKMNAENLGIVFGPTLMRPPE-D 167
                         170       180
                  ....*....|....*....|.
gi 568955249 1868 DPLTSMKDVLKITTCVEMLIK 1888
Cdd:cd04372   168 SALTTLNDMRYQILIVQLLIT 188
MYSc_Myo33 cd14894
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ...
272-675 4.84e-31

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: 133.33  E-value: 4.84e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  272 ILGAGPVLEAFGNAKTAHNNNSSRFGKF--IQVNYlenGI------VRGAVVEKYLLEKSRLVSQ------EKDERNYHV 337
Cdd:cd14894   249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAF---GLhpwefqICGCHISPFLLEKSRVTSErgresgDQNELNFHI 325
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  338 FYYLLLGVSEEERLEFQLKQPQ---------DYFYLNQHNLN--IEDGEDLKHDFERLQQAMEMVGFL---PATKKQIFS 403
Cdd:cd14894   326 LYAMVAGVNAFPFMRLLAKELHldgidcsalTYLGRSDHKLAgfVSKEDTWKKDVERWQQVIDGLDELnvsPDEQKTIFK 405
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  404 VLSAILYLGNVTYKKR-ATGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTV---NDKLILPYSLSEAITARD 479
Cdd:cd14894   406 VLSAVLWLGNIELDYReVSGKLVMSSTGALNAPQKVVELLELGSVEKLERMLMTKSVSLqstSETFEVTLEKGQVNHVRD 485
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  480 SMAKSLYSALFDWIVLRINHALL--------NKKDME------EAVSCLSIgvLDIFGFEDFERNSFEQFCINYANEQLq 545
Cdd:cd14894   486 TLARLLYQLAFNYVVFVMNEATKmsalstdgNKHQMDsnasapEAVSLLKI--VDVFGFEDLTHNSLDQLCINYLSEKL- 562
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  546 yyftqhiFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLdEESNFPHATSHTllaKFKQQHEDNKYFL--- 622
Cdd:cd14894   563 -------YAREEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASL-EELTILHQSENM---NAQQEEKRNKLFVrni 631
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568955249  623 --------------------GTPVLEPA--FIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLI 675
Cdd:cd14894   632 ydrnssrlpepprvlsnakrHTPVLLNVlpFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRML 706
RhoGAP_SYD1 cd04379
RhoGAP_SYD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
1704-1871 8.63e-31

RhoGAP_SYD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in SYD-1_like proteins. Syd-1, first identified and best studied in C.elegans, has been shown to play an important role in neuronal development by specifying axonal properties. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239844  Cd Length: 207  Bit Score: 121.42  E-value: 8.63e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1704 FGVCVDSLT---SDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKL--EDFP-IHAITGVL 1777
Cdd:cd04379     1 FGVPLSRLVereGESRDVPIVLQKCVQEIERRGLDVIGLYRLCGSAAKKKELRDAFERNSAAVELseELYPdINVITGVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1778 KQWLRELPEPLMTFAQYGDFLRA--VELP-EKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAI 1854
Cdd:cd04379    81 KDYLRELPEPLITPQLYEMVLEAlaVALPnDVQTNTHLTLSIIDCLPLSAKATLLLLLDHLSLVLSNSERNKMTPQNLAV 160
                         170
                  ....*....|....*..
gi 568955249 1855 IFAPCLLRCPDNSDPLT 1871
Cdd:cd04379   161 CFGPVLMFCSQEFSRYG 177
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
182-302 1.16e-30

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: 119.76  E-value: 1.16e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249  182 ILVAINPFKFLPIYNP-KYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISGESGSGKTQSTNFLIHCLTALS 260
Cdd:cd01363     1 VLVRVNPFKELPIYRDsKIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568955249  261 QKGYASG--------------VERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQV 302
Cdd:cd01363    81 FNGINKGetegwvylteitvtLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEI 136
RhoGAP_ARHGAP20 cd04402
RhoGAP_ARHGAP20: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1704-1887 1.09e-29

RhoGAP_ARHGAP20: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP20-like proteins. ArhGAP20, also known as KIAA1391 and RA-RhoGAP, contains a RhoGAP, a RA, and a PH domain, and ANXL repeats. ArhGAP20 is activated by Rap1 and induces inactivation of Rho, which in turn leads to neurite outgrowth. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239867  Cd Length: 192  Bit Score: 117.78  E-value: 1.09e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1704 FGVCVDSLTSDkASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDpAAVKLEDFPIHAITGVLKQWLRE 1783
Cdd:cd04402     2 FGQPLSNICED-DNLPKPILDMLSLLYQKGPSTEGIFRRSANAKACKELKEKLNSG-VEVDLKAEPVLLLASVLKDFLRN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1784 LPEPLMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRC 1863
Cdd:cd04402    80 IPGSLLSSDLYEEWMSALDQENEEEKIAELQRLLDKLPRPNVLLLKHLICVLHNISQNSETNKMDAFNLAVCIAPSLLWP 159
                         170       180
                  ....*....|....*....|....
gi 568955249 1864 PDNSDPLtsMKDVLKITTCVEMLI 1887
Cdd:cd04402   160 PASSELQ--NEDLKKVTSLVQFLI 181
RhoGAP_ARHGAP21 cd04395
RhoGAP_ARHGAP21: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1704-1887 1.74e-29

RhoGAP_ARHGAP21: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP21-like proteins. ArhGAP21 is a multi-domain protein, containing RhoGAP, PH and PDZ domains, and is believed to play a role in the organization of the cell-cell junction complex. It has been shown to function as a GAP of Cdc42 and RhoA, and to interact with alpha-catenin and Arf6. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239860  Cd Length: 196  Bit Score: 117.50  E-value: 1.74e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1704 FGVCVDS--LTSDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKLED---FPIHAITGVLK 1778
Cdd:cd04395     2 FGVPLDDcpPSSENPYVPLIVEVCCNIVEARGLETVGIYRVPGNNAAISALQEELNRGGFDIDLQDprwRDVNVVSSLLK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1779 QWLRELPEPLMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAP 1858
Cdd:cd04395    82 SFFRKLPEPLFTNELYPDFIEANRIEDPVERLKELRRLIHSLPDHHYETLKHLIRHLKTVADNSEVNKMEPRNLAIVFGP 161
                         170       180       190
                  ....*....|....*....|....*....|.
gi 568955249 1859 CLLRCPDNS--DPLTSMKDVLKIttcVEMLI 1887
Cdd:cd04395   162 TLVRTSDDNmeTMVTHMPDQCKI---VETLI 189
RhoGAP_GMIP_PARG1 cd04378
RhoGAP_GMIP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
1717-1888 7.80e-29

RhoGAP_GMIP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP (Gem interacting protein) and PARG1 (PTPL1-associated RhoGAP1). GMIP plays important roles in neurite growth and axonal guidance, and interacts with Gem, a member of the RGK subfamily of the Ras small GTPase superfamily, through the N-terminal half of the protein. GMIP contains a C-terminal RhoGAP domain. GMIP inhibits RhoA function, but is inactive towards Rac1 and Cdc41. PARG1 interacts with Rap2, also a member of the Ras small GTPase superfamily whose exact function is unknown, and shows strong preference for Rho. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239843  Cd Length: 203  Bit Score: 115.60  E-value: 7.80e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1717 SVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKLEDFPIHAITGVLKQWLRELPEPLMTFAQYGD 1796
Cdd:cd04378    15 EVPFIIKKCTSEIENRALGVQGIYRVSGSKARVEKLCQAFENGKDLVELSELSPHDISSVLKLFLRQLPEPLILFRLYND 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1797 FL----RAVELPEKQEQL-------SAIYAV---LDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLR 1862
Cdd:cd04378    95 FIalakEIQRDTEEDKAPntpievnRIIRKLkdlLRQLPASNYNTLQHLIAHLYRVAEQFEENKMSPNNLGIVFGPTLIR 174
                         170       180
                  ....*....|....*....|....*...
gi 568955249 1863 CPDNSDP--LTSMKDVLKITTCVEMLIK 1888
Cdd:cd04378   175 PRPGDADvsLSSLVDYGYQARLVEFLIT 202
C1_Myosin-IX cd20818
protein kinase C conserved region 1 (C1 domain) found in the unconventional myosin-IX family; ...
1636-1691 1.68e-28

protein kinase C conserved region 1 (C1 domain) found in the unconventional myosin-IX family; Myosins IX (Myo9) is a class of unique motor proteins with a common structure of an N-terminal extension preceding a myosin head homologous to the Ras-association (RA) domain, a head (motor) domain, a neck with IQ motifs that bind light chains, and a C-terminal tail containing cysteine-rich zinc binding (C1) and Rho-GTPase activating protein (RhoGAP) domains. There are two genes for myosins IX in humans, IXa and IXb, that are different in their expression and localization. IXa is expressed abundantly in brain and testis, and IXb is expressed abundantly in tissues of the immune system. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410368  Cd Length: 56  Bit Score: 109.31  E-value: 1.68e-28
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568955249 1636 HNGHVFASYQVNIPQSCEQCLSYIWLMDKALLCSVCKMTCHKKCVHKIQSYCSYTG 1691
Cdd:cd20818     1 HNGHKFATVQFNIPTYCEVCNSFIWLMEKGLVCQVCKFTCHKKCYSKITAPCKGNS 56
RhoGAP-p50rhoGAP cd04404
RhoGAP-p50rhoGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1704-1891 6.44e-28

RhoGAP-p50rhoGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of p50RhoGAP-like proteins; p50RhoGAP, also known as RhoGAP-1, contains a C-terminal RhoGAP domain and an N-terminal Sec14 domain which binds phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3). It is ubiquitously expressed and preferentially active on Cdc42. This subgroup also contains closely related ARHGAP8. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239869  Cd Length: 195  Bit Score: 112.82  E-value: 6.44e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1704 FGVCVDSLTS---DKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQAL-QTDPaaVKLEDFP-IHAITGVLK 1778
Cdd:cd04404     6 FGVSLQFLKEknpEQEPIPPVVRETVEYLQAHALTTEGIFRRSANTQVVKEVQQKYnMGEP--VDFDQYEdVHLPAVILK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1779 QWLRELPEPLMTFAQYGDFLRAVELPeKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAP 1858
Cdd:cd04404    84 TFLRELPEPLLTFDLYDDIVGFLNVD-KEERVERVKQLLQTLPEENYQVLKYLIKFLVQVSAHSDQNKMTNSNLAVVFGP 162
                         170       180       190
                  ....*....|....*....|....*....|...
gi 568955249 1859 CLLRCPDNSdplTSMKDVLKITTCVEMLIKEQM 1891
Cdd:cd04404   163 NLLWAKDAS---MSLSAINPINTFTKFLLDHQD 192
RhoGAP_MgcRacGAP cd04382
RhoGAP_MgcRacGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
1705-1876 2.11e-27

RhoGAP_MgcRacGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in MgcRacGAP proteins. MgcRacGAP plays an important dual role in cytokinesis: i) it is part of centralspindlin-complex, together with the mitotic kinesin MKLP1, which is critical for the structure of the central spindle by promoting microtuble bundling. ii) after phosphorylation by aurora B MgcRacGAP becomes an effective regulator of RhoA and plays an important role in the assembly of the contractile ring and the initiation of cytokinesis. MgcRacGAP-like proteins contain a N-terminal C1-like domain, and a C-terminal RhoGAP domain. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239847  Cd Length: 193  Bit Score: 111.23  E-value: 2.11e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1705 GVCVDSLTSDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKLEDFPIHAITGVLKQWLREL 1784
Cdd:cd04382     4 GELADFDPSTSPMIPALIVHCVNEIEARGLTEEGLYRVSGSEREVKALKEKFLRGKTVPNLSKVDIHVICGCLKDFLRSL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1785 PEPLMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDvNRMSPGALAIIFAPCLLRCP 1864
Cdd:cd04382    84 KEPLITFALWKEFMEAAEILDEDNSRAALYQAISELPQPNRDTLAFLILHLQRVAQSPE-CKMDINNLARVFGPTIVGYS 162
                         170
                  ....*....|...
gi 568955249 1865 D-NSDPLTSMKDV 1876
Cdd:cd04382   163 VpNPDPMTILQDT 175
RhoGAP_GMIP cd04408
RhoGAP_GMIP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP ...
1704-1887 4.96e-27

RhoGAP_GMIP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP (Gem interacting protein). GMIP plays important roles in neurite growth and axonal guidance, and interacts with Gem, a member of the RGK subfamily of the Ras small GTPase superfamily, through the N-terminal half of the protein. GMIP contains a C-terminal RhoGAP domain. GMIP inhibits RhoA function, but is inactive towards Rac1 and Cdc41. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239873  Cd Length: 200  Bit Score: 110.29  E-value: 4.96e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1704 FGVCVDSLTSD-KASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKLEDFPIHAITGVLKQWLR 1782
Cdd:cd04408     1 FGVDFSQLPRDfPEEVPFVVVRCTAEIENRALGVQGIYRISGSKARVEKLCQAFENGRDLVDLSGHSPHDITSVLKHFLK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1783 ELPEPLMTFAQYGDFL-----------RAVELPE-KQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPG 1850
Cdd:cd04408    81 ELPEPVLPFQLYDDFIalakelqrdseKAAESPSiVENIIRSLKELLGRLPVSNYNTLRHLMAHLYRVAERFEDNKMSPN 160
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 568955249 1851 ALAIIFAPCLLRCPDNSD-PLTSMKDVLKITTCVEMLI 1887
Cdd:cd04408   161 NLGIVFGPTLLRPLVGGDvSMICLLDTGYQAQLVEFLI 198
RA_Myosin-IXa cd17216
Ras-associating (RA) domain found in Myosin-IXa; Myosin-IXa, also termed myosin-9a (Myo9a), is ...
19-112 1.76e-26

Ras-associating (RA) domain found in Myosin-IXa; Myosin-IXa, also termed myosin-9a (Myo9a), is a single-headed, actin-dependent motor protein of the unconventional myosin IX class. It is expressed in several tissues and is enriched in the brain and testes. Myosin-IXa contains a Ras-associating (RA) domain, a motor domain, a protein kinase C conserved region 1 (C1), and a Rho GTPase activating domain (RhoGAP). Its RA domain is located at its head domain and has the beta-grasp ubiquitin-like fold with unknown function. Myosin-IXa binds the alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptor (AMPAR) GluA2 subunit, and plays a key role in controlling the molecular structure and function of hippocampal synapses. Moreover, Myosin-IXa functions in epithelial cell morphology and differentiation such that its knockout mice develop hydrocephalus and kidney dysfunction. Myosin-IXa regulates collective epithelial cell migration by targeting RhoGAP activity to cell-cell junctions. Myosin-IXa negatively regulates Rho GTPase signaling, and functions as a regulator of kidney tubule function.


Pssm-ID: 340736  Cd Length: 96  Bit Score: 105.01  E-value: 1.76e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249   19 LHIYPQLSSAGSqTSCRVTATKDSTTSDVIQDVVASLHLDGSKHYVLVEVKESGGEEWVLDASDSPVHRVLLWPRRAQDE 98
Cdd:cd17216     4 LRIYPGNIAEGT-IYCPVPARKNTTAAEVIESLINKLQLDKTKCYVLAEVKEFGGEEWILNPTDCPVQRMMLWPRMALEN 82
                          90
                  ....*....|....
gi 568955249   99 HPQEDGYYFLLQER 112
Cdd:cd17216    83 RFSGEDYRFLLREK 96
RhoGAP_Graf cd04374
RhoGAP_Graf: GTPase-activator protein (GAP) domain for Rho-like GTPases found in GRAF (GTPase ...
1714-1887 1.98e-26

RhoGAP_Graf: GTPase-activator protein (GAP) domain for Rho-like GTPases found in GRAF (GTPase regulator associated with focal adhesion kinase); Graf is a multi-domain protein, containing SH3 and PH domains, that binds focal adhesion kinase and influences cytoskeletal changes mediated by Rho proteins. Graf exhibits GAP activity toward RhoA and Cdc42, but only weakly activates Rac1. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239839  Cd Length: 203  Bit Score: 108.63  E-value: 1.98e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1714 DKASVPIVlEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQAL----QTDPAAVKLE--DFPIHAITGVLKQWLRELPEP 1787
Cdd:cd04374    25 DDIGFKFV-RKCIEAVETRGINEQGLYRVVGVNSKVQKLLSLGldpkTSTPGDVDLDnsEWEIKTITSALKTYLRNLPEP 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1788 LMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRCPDNS 1867
Cdd:cd04374   104 LMTYELHNDFINAAKSENLESRVNAIHSLVHKLPEKNREMLELLIKHLTNVSDHSKKNLMTVSNLGVVFGPTLLRPQEET 183
                         170       180
                  ....*....|....*....|
gi 568955249 1868 dpLTSMKDVLKITTCVEMLI 1887
Cdd:cd04374   184 --VAAIMDIKFQNIVVEILI 201
RhoGAP_p190 cd04373
RhoGAP_p190: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1704-1887 2.55e-26

RhoGAP_p190: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of p190-like proteins. p190, also named RhoGAP5, plays a role in neuritogenesis and axon branch stability. p190 shows a preference for Rho, over Rac and Cdc42, and consists of an N-terminal GTPase domain and a C-terminal GAP domain. The central portion of p190 contains important regulatory phosphorylation sites. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239838  Cd Length: 185  Bit Score: 107.93  E-value: 2.55e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1704 FGVCVDSLTSDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTREL-RQALQTDPAAVKLEDFPIHAITGVLKQWLR 1782
Cdd:cd04373     1 FGVPLANVVTSEKPIPIFLEKCVEFIEATGLETEGIYRVSGNKTHLDSLqKQFDQDHNLDLVSKDFTVNAVAGALKSFFS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1783 ELPEPLMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLR 1862
Cdd:cd04373    81 ELPDPLIPYSMHLELVEAAKINDREQRLHALKELLKKFPPENFDVFKYVITHLNKVSQNSKVNLMTSENLSICFWPTLMR 160
                         170       180
                  ....*....|....*....|....*..
gi 568955249 1863 cPD--NSDPLTSMKDVlkiTTCVEMLI 1887
Cdd:cd04373   161 -PDftSMEALSATRIY---QTIIETFI 183
RhoGAP_Bcr cd04387
RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr ...
1704-1875 3.26e-26

RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr (breakpoint cluster region protein)-like proteins. Bcr is a multidomain protein with a variety of enzymatic functions. It contains a RhoGAP and a Rho GEF domain, a Ser/Thr kinase domain, an N-terminal oligomerization domain, and a C-terminal PDZ binding domain, in addition to PH and C2 domains. Bcr is a negative regulator of: i) RacGTPase, via the Rho GAP domain, ii) the Ras-Raf-MEK-ERK pathway, via phosphorylation of the Ras binding protein AF-6, and iii) the Wnt signaling pathway through binding beta-catenin. Bcr can form a complex with beta-catenin and Tcf1. The Wnt signaling pathway is involved in cell proliferation, differentiation, and cell renewal. Bcr was discovered as a fusion partner of Abl. The Bcr-Abl fusion is characteristic for a large majority of chronic myelogenous leukemias (CML). Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239852 [Multi-domain]  Cd Length: 196  Bit Score: 108.09  E-value: 3.26e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1704 FGVCVDSLTSDKAS-VPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTD--PAAVKLEDFPIHAITGVLKQW 1780
Cdd:cd04387     1 FGVKISTVTKRERSkVPYIVRQCVEEVERRGMEEVGIYRISGVATDIQALKAAFDTNnkDVSVMLSEMDVNAIAGTLKLY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1781 LRELPEPLMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCL 1860
Cdd:cd04387    81 FRELPEPLFTDELYPNFAEGIALSDPVAKESCMLNLLLSLPDPNLVTFLFLLHHLKRVAEREEVNKMSLHNLATVFGPTL 160
                         170
                  ....*....|....*..
gi 568955249 1861 LRCP--DNSDPLTSMKD 1875
Cdd:cd04387   161 LRPSekESKIPTNTMTD 177
RhoGAP_CdGAP cd04384
RhoGAP_CdGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1718-1864 2.43e-24

RhoGAP_CdGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of CdGAP-like proteins; CdGAP contains an N-terminal RhoGAP domain and a C-terminal proline-rich region, and it is active on both Cdc42 and Rac1 but not RhoA. CdGAP is recruited to focal adhesions via the interaction with the scaffold protein actopaxin (alpha-parvin). Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239849 [Multi-domain]  Cd Length: 195  Bit Score: 102.58  E-value: 2.43e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1718 VPIVLEKLLEHVEMHGLYTeGLYRKSGAANRTRELRQALQTDpAAVKLEDFP----IHAITGVLKQWLRELPEPLMTFAQ 1793
Cdd:cd04384    18 VPQVLKSCTEFIEKHGIVD-GIYRLSGIASNIQRLRHEFDSE-QIPDLTKDVyiqdIHSVSSLCKLYFRELPNPLLTYQL 95
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568955249 1794 YGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRCP 1864
Cdd:cd04384    96 YEKFSEAVSAASDEERLEKIHDVIQQLPPPHYRTLEFLMRHLSRLAKYCSITNMHAKNLAIVWAPNLLRSK 166
RhoGAP_ARHGAP18 cd04391
RhoGAP_ARHGAP18: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1704-1890 4.72e-24

RhoGAP_ARHGAP18: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP18-like proteins. The function of ArhGAP18 is unknown. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239856  Cd Length: 216  Bit Score: 102.42  E-value: 4.72e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1704 FGVCVDSL------TSDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTD--PAAVKLEDFPIHAITG 1775
Cdd:cd04391     2 FGVPLSTLlerdqkKVPGSKVPLIFQKLINKLEERGLETEGILRIPGSAQRVKFLCQELEAKfyEGTFLWDQVKQHDAAS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1776 VLKQWLRELPEPLMTfAQYGDFLRAVE-LPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAI 1854
Cdd:cd04391    82 LLKLFIRELPQPLLT-VEYLPAFYSVQgLPSKKDQLQALNLLVLLLPEANRDTLKALLEFLQKVVDHEEKNKMNLWNVAM 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 568955249 1855 IFAPCLLRC--PDNSDPLTSMKDVLKITTC---VEMLIKEQ 1890
Cdd:cd04391   161 IMAPNLFPPrgKHSKDNESLQEEVNMAAGCaniMRLLIRYQ 201
RhoGAP-ARHGAP11A cd04394
RhoGAP-ARHGAP11A: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1704-1887 2.27e-23

RhoGAP-ARHGAP11A: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP11A-like proteins. The mouse homolog of human ArhGAP11A has been detected as a gene exclusively expressed in immature ganglion cells, potentially playing a role in retinal development. The exact function of ArhGAP11A is unknown. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239859 [Multi-domain]  Cd Length: 202  Bit Score: 99.85  E-value: 2.27e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1704 FGVCVDSLT----SDKASVPIVLEKLLEHVEMHgLYTEGLYRKSGAANRTRELRqaLQTDPAAVKLEDFPIHAITGVLKQ 1779
Cdd:cd04394     2 FGVPLHSLPhstvPEYGNVPKFLVDACTFLLDH-LSTEGLFRKSGSVVRQKELK--AKLEGGEACLSSALPCDVAGLLKQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1780 WLRELPEPLMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPC 1859
Cdd:cd04394    79 FFRELPEPLLPYDLHEALLKAQELPTDEERKSATLLLTCLLPDEHVNTLRYFFSFLYDVAQRCSENKMDSSNLAVIFAPN 158
                         170       180       190
                  ....*....|....*....|....*....|
gi 568955249 1860 LLRCPDNSDPLTS--MKDVLKITTCVEMLI 1887
Cdd:cd04394   159 LFQSEEGGEKMSSstEKRLRLQAAVVQTLI 188
RhoGAP_ARHGAP22_24_25 cd04390
RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
1718-1889 3.27e-23

RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ARHGAP22, 24 and 25-like proteins; longer isoforms of these proteins contain an additional N-terminal pleckstrin homology (PH) domain. ARHGAP25 (KIA0053) has been identified as a GAP for Rac1 and Cdc42. Short isoforms (without the PH domain) of ARHGAP24, called RC-GAP72 and p73RhoGAP, and of ARHGAP22, called p68RacGAP, has been shown to be involved in angiogenesis and endothelial cell capillary formation. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239855 [Multi-domain]  Cd Length: 199  Bit Score: 99.44  E-value: 3.27e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1718 VPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKLEDFPIHAITGVLKQWLRELPEPLMTFAQYGDF 1797
Cdd:cd04390    22 VPILVEQCVDFIREHGLKEEGLFRLPGQANLVKQLQDAFDAGERPSFDSDTDVHTVASLLKLYLRELPEPVIPWAQYEDF 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1798 LRAVELPEKQEQ--LSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRcPDNSDPLTSMKD 1875
Cdd:cd04390   102 LSCAQLLSKDEEkgLGELMKQVSILPKVNYNLLSYICRFLDEVQSNSSVNKMSVQNLATVFGPNILR-PKVEDPATIMEG 180
                         170
                  ....*....|....
gi 568955249 1876 VLKITTCVEMLIKE 1889
Cdd:cd04390   181 TPQIQQLMTVMISK 194
RhoGAP_PARG1 cd04409
RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1718-1888 2.75e-22

RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of PARG1 (PTPL1-associated RhoGAP1). PARG1 was originally cloned as an interaction partner of PTPL1, an intracellular protein-tyrosine phosphatase. PARG1 interacts with Rap2, also a member of the Ras small GTPase superfamily whose exact function is unknown, and shows strong preference for Rho. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239874  Cd Length: 211  Bit Score: 97.19  E-value: 2.75e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1718 VPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKLEDFPIHAITGVLKQWLRELPEPLMTFAQYGDF 1797
Cdd:cd04409    16 IPFIIKKCTSEIESRALCLKGIYRVNGAKSRVEKLCQAFENGKDLVELSELSPHDISNVLKLYLRQLPEPLILFRLYNEF 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1798 L-------------RAVELPEKQEQ---------LSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAII 1855
Cdd:cd04409    96 IglakesqhvnetqEAKKNSDKKWPnmctelnriLLKSKDLLRQLPAPNYNTLQFLIVHLHRVSEQAEENKMSASNLGII 175
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 568955249 1856 FAPCLLRcPDNSDP---LTSMKDVLKITTCVEMLIK 1888
Cdd:cd04409   176 FGPTLIR-PRPTDAtvsLSSLVDYPHQARLVELLIT 210
RhoGAP_ARHGAP6 cd04376
RhoGAP_ARHGAP6: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1717-1887 1.59e-21

RhoGAP_ARHGAP6: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP6-like proteins. ArhGAP6 shows GAP activity towards RhoA, but not towards Cdc42 and Rac1. ArhGAP6 is often deleted in microphthalmia with linear skin defects syndrome (MLS); MLS is a severe X-linked developmental disorder. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239841  Cd Length: 206  Bit Score: 94.81  E-value: 1.59e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1717 SVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKLEDFPIHAITGVLKQWLRELPEPLMTFAQYGD 1796
Cdd:cd04376     8 QVPRLVESCCQHLEKHGLQTVGIFRVGSSKKRVRQLREEFDRGIDVVLDENHSVHDVAALLKEFFRDMPDPLLPRELYTA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1797 FLRAVELpEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVAL-LEDV----------NRMSPGALAIIFAPCLLRCPD 1865
Cdd:cd04376    88 FIGTALL-EPDEQLEALQLLIYLLPPCNCDTLHRLLKFLHTVAEhAADSidedgqevsgNKMTSLNLATIFGPNLLHKQK 166
                         170       180
                  ....*....|....*....|....*..
gi 568955249 1866 NSDPLTS-----MKDVLKITTCVEMLI 1887
Cdd:cd04376   167 SGEREFVqaslrIEESTAIINVVQTMI 193
RhoGAP_FAM13A1a cd04393
RhoGAP_FAM13A1a: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1704-1880 3.87e-21

RhoGAP_FAM13A1a: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of FAM13A1, isoform a-like proteins. The function of FAM13A1a is unknown. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by up several orders of magnitude.


Pssm-ID: 239858 [Multi-domain]  Cd Length: 189  Bit Score: 93.30  E-value: 3.87e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1704 FGVCVDSLTSD---KASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKLEDFPIHAITGVLKQW 1780
Cdd:cd04393     3 FGVPLQELQQAgqpENGVPAVVRHIVEYLEQHGLEQEGLFRVNGNAETVEWLRQRLDSGEEVDLSKEADVCSAASLLRLF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1781 LRELPEPLMTFAQYGDFLRAV-ELPEKQEQLSAIYAVLDHLPEANHtSLERLIFH-LVKVALLEDVNRMSPGALAIIFAP 1858
Cdd:cd04393    83 LQELPEGLIPASLQIRLMQLYqDYNGEDEFGRKLRDLLQQLPPVNY-SLLKFLCHfLSNVASQHHENRMTAENLAAVFGP 161
                         170       180
                  ....*....|....*....|..
gi 568955249 1859 CLLRCPDNSDPLTSMKDVLKIT 1880
Cdd:cd04393   162 DVFHVYTDVEDMKEQEICSRIM 183
RhoGAP_ARHGAP19 cd04392
RhoGAP_ARHGAP19: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1724-1895 5.85e-21

RhoGAP_ARHGAP19: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP19-like proteins. The function of ArhGAP19 is unknown. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239857  Cd Length: 208  Bit Score: 93.29  E-value: 5.85e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1724 KLLEHVEMHgLYTEGLYRKSGAANRTRELRQALQTD-PAAVKLEDFPIHAITGVLKQWLRELPEPLMTFAQYGDFLRAVE 1802
Cdd:cd04392    15 QLIEYLEKN-LRVEGLFRKPGNSARQQELRDLLNSGtDLDLESGGFHAHDCATVLKGFLGELPEPLLTHAHYPAHLQIAD 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1803 L------------PEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLrCPDNSDPL 1870
Cdd:cd04392    94 LcqfdekgnktsaPDKERLLEALQLLLLLLPEENRNLLKLILDLLYQTAKHEDKNKMSADNLALLFTPHLI-CPRNLTPE 172
                         170       180
                  ....*....|....*....|....*
gi 568955249 1871 TSMKDVLKITTCVEMLIKEQMRKYK 1895
Cdd:cd04392   173 DLHENAQKLNSIVTFMIKHSQKLFK 197
RhoGAP_fBEM3 cd04400
RhoGAP_fBEM3: RhoGAP (GTPase-activator [GAP] protein for Rho-like small GTPases) domain of ...
1717-1860 3.28e-20

RhoGAP_fBEM3: RhoGAP (GTPase-activator [GAP] protein for Rho-like small GTPases) domain of fungal BEM3-like proteins. Bem3 is a GAP protein of Cdc42, and is specifically involved in the control of the initial assembly of the septin ring in yeast bud formation. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239865 [Multi-domain]  Cd Length: 190  Bit Score: 90.50  E-value: 3.28e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1717 SVPIVLEKLLEHVEMHG-LYTEGLYRKSGAANRTRELRQALQTDPAAVKLED---FPIHAITGVLKQWLRELPEPLMTFA 1792
Cdd:cd04400    21 DLPSVVYRCIEYLDKNRaIYEEGIFRLSGSASVIKQLKERFNTEYDVDLFSSslyPDVHTVAGLLKLYLRELPTLILGGE 100
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568955249 1793 QYGDFLRAVELPEKQEQLSAIYAVL-DHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCL 1860
Cdd:cd04400   101 LHNDFKRLVEENHDRSQRALELKDLvSQLPQANYDLLYVLFSFLRKIIEHSDVNKMNLRNVCIVFSPTL 169
RhoGAP_KIAA1688 cd04389
RhoGAP_KIAA1688: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
1718-1888 2.13e-19

RhoGAP_KIAA1688: GTPase-activator protein (GAP) domain for Rho-like GTPases found in KIAA1688-like proteins; KIAA1688 is a protein of unknown function that contains a RhoGAP domain and a myosin tail homology 4 (MyTH4) domain. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239854  Cd Length: 187  Bit Score: 87.83  E-value: 2.13e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1718 VPIVLEKLLEHV-EMHGLYTEGLYRKSGAANRTRELRqaLQTDPAAV---KLEDfpIHAITGVLKQWLRELPEPLMTFAQ 1793
Cdd:cd04389    21 LPWILTFLSEKVlALGGFQTEGIFRVPGDIDEVNELK--LRVDQWDYplsGLED--PHVPASLLKLWLRELEEPLIPDAL 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1794 YGDFLRAVELPEKqeqlsaIYAVLDHLPEANHTSLERLIfHLVKVALLEDV---NRMSPGALAIIFAPCLLRCpDNSDPL 1870
Cdd:cd04389    97 YQQCISASEDPDK------AVEIVQKLPIINRLVLCYLI-NFLQVFAQPENvahTKMDVSNLAMVFAPNILRC-TSDDPR 168
                         170
                  ....*....|....*...
gi 568955249 1871 TSMKDVLKITTCVEMLIK 1888
Cdd:cd04389   169 VIFENTRKEMSFLRTLIE 186
C1_Myosin-IXa cd20883
protein kinase C conserved region 1 (C1 domain) found in unconventional myosin-IXa and similar ...
1634-1688 2.45e-19

protein kinase C conserved region 1 (C1 domain) found in unconventional myosin-IXa and similar proteins; Myosin-IXa, also called unconventional myosin-9a (Myo9a), is a single-headed, actin-dependent motor protein of the unconventional myosin IX class. It is expressed in several tissues and is enriched in the brain and testes. Myosin-IXa contains a Ras-associating (RA) domain, a motor domain, a protein kinase C conserved region 1 (C1), and a Rho GTPase activating domain (RhoGAP). Myosin-IXa binds the alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptor (AMPAR) GluA2 subunit, and plays a key role in controlling the molecular structure and function of hippocampal synapses. Moreover, Myosin-IXa functions in epithelial cell morphology and differentiation, such that its knockout mice develop hydrocephalus and kidney dysfunction. Myosin-IXa regulates collective epithelial cell migration by targeting RhoGAP activity to cell-cell junctions. Myosin-IXa negatively regulates Rho GTPase signaling, and functions as a regulator of kidney tubule function. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410433  Cd Length: 58  Bit Score: 83.48  E-value: 2.45e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568955249 1634 QEHNGHVFASYQVNIPQSCEQCLSYIWLMDKALLCSVCKMTCHKKCVHKIQSYCS 1688
Cdd:cd20883     1 EEHNGHIFKSTQYSIPTYCEYCSSLIWMMDRAYVCKLCRYACHKKCCLKTTTKCS 55
RhoGap_RalBP1 cd04381
RhoGap_RalBP1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
1704-1860 8.90e-19

RhoGap_RalBP1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in RalBP1 proteins, also known as RLIP, RLIP76 or cytocentrin. RalBP1 plays an important role in endocytosis during interphase. During mitosis, RalBP1 transiently associates with the centromere and has been shown to play an essential role in the proper assembly of the mitotic apparatus. RalBP1 is an effector of the Ral GTPase which itself is an effector of Ras. RalBP1 contains a RhoGAP domain, which shows weak activity towards Rac1 and Cdc42, but not towards Ral, and a Ral effector domain binding motif. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239846 [Multi-domain]  Cd Length: 182  Bit Score: 85.95  E-value: 8.90e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1704 FGVCVD-----SLTSDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRqALQTDPAAVKLEDFPIHAITGVLK 1778
Cdd:cd04381     1 FGASLSlaverSRCHDGIDLPLVFRECIDYVEKHGMKCEGIYKVSGIKSKVDELK-AAYNRRESPNLEEYEPPTVASLLK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1779 QWLRELPEPLMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAP 1858
Cdd:cd04381    80 QYLRELPEPLLTKELMPRFEEACGRPTEAEREQELQRLLKELPECNRLLLAWLIVHMDHVIAQELETKMNIQNISIVLSP 159

                  ..
gi 568955249 1859 CL 1860
Cdd:cd04381   160 TV 161
RhoGAP_DLC1 cd04375
RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1704-1860 2.65e-18

RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of DLC1-like proteins. DLC1 shows in vitro GAP activity towards RhoA and CDC42. Beside its C-terminal GAP domain, DLC1 also contains a SAM (sterile alpha motif) and a START (StAR-related lipid transfer action) domain. DLC1 has tumor suppressor activity in cell culture. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239840  Cd Length: 220  Bit Score: 85.93  E-value: 2.65e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1704 FGVCVD-SLTSDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKLEDFPIHAITGVLKQWLR 1782
Cdd:cd04375     5 FGVPLLvNLQRTGQPLPRSIQQAMRWLRNNALDQVGLFRKSGVKSRIQKLRSMIESSTDNVNYDGQQAYDVADMLKQYFR 84
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568955249 1783 ELPEPLMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCL 1860
Cdd:cd04375    85 DLPEPLLTNKLSETFIAIFQYVPKEQRLEAVQCAILLLPDENREVLQTLLYFLSDVAANSQENQMTATNLAVCLAPSL 162
RhoGAP_p85 cd04388
RhoGAP_p85: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
1719-1869 4.52e-18

RhoGAP_p85: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in the p85 isoforms of the regulatory subunit of the class IA PI3K (phosphatidylinositol 3'-kinase). This domain is also called Bcr (breakpoint cluster region protein) homology (BH) domain. Class IA PI3Ks are heterodimers, containing a regulatory subunit (p85) and a catalytic subunit (p110) and are activated by growth factor receptor tyrosine kinases (RTKs); this activation is mediated by the p85 subunit. p85 isoforms, alpha and beta, contain a C-terminal p110-binding domain flanked by two SH2 domains, an N-terminal SH3 domain, and a RhoGAP domain flanked by two proline-rich regions. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239853  Cd Length: 200  Bit Score: 84.54  E-value: 4.52e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1719 PIVLEKLLEHVEMHGLYTEGLYRKSGAANRTrELRQALQTDPAAVKLEDFPIHAITGVLKQWLRELPEPLMTFAQYGDFL 1798
Cdd:cd04388    16 PPLLIKLVEAIEKKGLESSTLYRTQSSSSLT-ELRQILDCDAASVDLEQFDVAALADALKRYLLDLPNPVIPAPVYSEMI 94
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568955249 1799 RA---VELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRCPDNSDP 1869
Cdd:cd04388    95 SRaqeVQSSDEYAQLLRKLIRSPNLPHQYWLTLQYLLKHFFRLCQSSSKNLLSARALAEIFSPLLFRFQPASSD 168
RhoGAP_srGAP cd04383
RhoGAP_srGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
1718-1869 7.13e-17

RhoGAP_srGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in srGAPs. srGAPs are components of the intracellular part of Slit-Robo signalling pathway that is important for axon guidance and cell migration. srGAPs contain an N-terminal FCH domain, a central RhoGAP domain and a C-terminal SH3 domain; this SH3 domain interacts with the intracellular proline-rich-tail of the Roundabout receptor (Robo). This interaction with Robo then activates the rhoGAP domain which in turn inhibits Cdc42 activity. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239848  Cd Length: 188  Bit Score: 80.93  E-value: 7.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1718 VPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQ--TDPAAVKLEDFPIHAITGVLKQWLRELPEPLMTFAQYG 1795
Cdd:cd04383    18 IPLVVESCIRFINLYGLQHQGIFRVSGSQVEVNDIKNAFErgEDPLADDQNDHDINSVAGVLKLYFRGLENPLFPKERFE 97
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568955249 1796 DFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRCPDNSDP 1869
Cdd:cd04383    98 DLMSCVKLENPTERVHQIREILSTLPRSVIIVMRYLFAFLNHLSQFSDENMMDPYNLAICFGPTLMPVPEGQDQ 171
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
15-114 1.36e-15

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Recent evidence (not yet in MEDLINE) shows that some RA domains do NOT bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase.


Pssm-ID: 425871  Cd Length: 93  Bit Score: 73.91  E-value: 1.36e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249    15 ATYHLHIYPQLSSAGSqTSCRVTATKDSTTSDVIQDVVASLHLDGSK-HYVLVEVKESGGEEWVLDASDSPVHRVLLWPR 93
Cdd:pfam00788    1 DDGVLKVYTEDGKPGT-TYKTILVSSSTTAEEVIEALLEKFGLEDDPrDYVLVEVLERGGGERRLPDDECPLQIQLQWPR 79
                           90       100
                   ....*....|....*....|.
gi 568955249    94 RAQDehpqedgYYFLLQERNA 114
Cdd:pfam00788   80 DASD-------SRFLLRKRDD 93
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
15-113 6.63e-15

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Kalhammer et al. have shown that not all RA domains bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase. Predicted RA domains in PLC210 and nore1 found to bind RasGTP. Included outliers (Grb7, Grb14, adenylyl cyclases etc.)


Pssm-ID: 214612  Cd Length: 90  Bit Score: 71.95  E-value: 6.63e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249     15 ATYHLHIYPQLSSagSQTSCRVTATKDSTTSDVIQDVVASLHLDGS-KHYVLVEVKEsGGEEWVLDASDSPVHRVLLWPR 93
Cdd:smart00314    1 DTFVLRVYVDDLP--GGTYKTLRVSSRTTARDVIQQLLEKFHLTDDpEEYVLVEVLP-DGKERVLPDDENPLQLQKLWPR 77
                            90       100
                    ....*....|....*....|
gi 568955249     94 RaqdehpqEDGYYFLLQERN 113
Cdd:smart00314   78 R-------GPNLRFVLRKRD 90
RhoGAP_fLRG1 cd04397
RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1695-1887 1.62e-13

RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal LRG1-like proteins. Yeast Lrg1p is required for efficient cell fusion, and mother-daughter cell separation, possibly through acting as a RhoGAP specifically regulating 1,3-beta-glucan synthesis. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239862  Cd Length: 213  Bit Score: 71.63  E-value: 1.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1695 SELGAEPGHFgvcvdsltsdkaSVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVK--LEDFPIHa 1772
Cdd:cd04397    16 STLGVGPGKL------------RIPALIDDIISAMRQMDMSVEGVFRKNGNIRRLKELTEEIDKNPTEVPdlSKENPVQ- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1773 ITGVLKQWLRELPEPLMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDV-----NRM 1847
Cdd:cd04397    83 LAALLKKFLRELPDPLLTFKLYRLWISSQKIEDEEERKRVLHLVYCLLPKYHRDTMEVLFSFLKWVSSFSHIdeetgSKM 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 568955249 1848 SPGALAIIFAPCLLRcPDNSDPLTSMKDVLKITTcVEMLI 1887
Cdd:cd04397   163 DIHNLATVITPNILY-SKTDNPNTGDEYFLAIEA-VNYLI 200
RhoGAP_fSAC7_BAG7 cd04396
RhoGAP_fSAC7_BAG7: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
1717-1865 5.87e-13

RhoGAP_fSAC7_BAG7: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal SAC7 and BAG7-like proteins. Both proteins are GTPase activating proteins of Rho1, but differ functionally in vivo: SAC7, but not BAG7, is involved in the control of Rho1-mediated activation of the PKC-MPK1 pathway. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239861  Cd Length: 225  Bit Score: 70.52  E-value: 5.87e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1717 SVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDP---AAVKLEDFPIHAITGVLKQWLRELPEPLMTFAQ 1793
Cdd:cd04396    31 YIPVVVAKCGVYLKENATEVEGIFRVAGSSKRIRELQLIFSTPPdygKSFDWDGYTVHDAASVLRRYLNNLPEPLVPLDL 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1794 YGDFLRAVE----------------LPEKQEQLSAIY-AVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIF 1856
Cdd:cd04396   111 YEEFRNPLRkrprilqymkgrinepLNTDIDQAIKEYrDLITRLPNLNRQLLLYLLDLLAVFARNSDKNLMTASNLAAIF 190

                  ....*....
gi 568955249 1857 APCLLRCPD 1865
Cdd:cd04396   191 QPGILSHPD 199
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
1639-1687 2.02e-12

Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.


Pssm-ID: 197519  Cd Length: 50  Bit Score: 63.64  E-value: 2.02e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 568955249   1639 HVFASYQVNIPQSCEQCLSYIWLMDK-ALLCSVCKMTCHKKCVHKIQSYC 1687
Cdd:smart00109    1 HKHVFRTFTKPTFCCVCRKSIWGSFKqGLRCSECKVKCHKKCADKVPKAC 50
C1 cd00029
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ...
1639-1687 7.96e-12

protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains. It contains the motif HX12CX2CXnCX2CX4HX2CX7C, where C and H are cysteine and histidine, respectively; X represents other residues; and n is either 13 or 14. C1 has a globular fold with two separate Zn(2+)-binding sites. It was originally discovered as lipid-binding modules in protein kinase C (PKC) isoforms. C1 domains that bind and respond to phorbol esters (PE) and diacylglycerol (DAG) are referred to as typical, and those that do not respond to PE and DAG are deemed atypical. A C1 domain may also be referred to as PKC or non-PKC C1, based on the parent protein's activity. Most C1 domain-containing non-PKC proteins act as lipid kinases and scaffolds, except PKD which acts as a protein kinase. PKC C1 domains play roles in membrane translocation and activation of the enzyme.


Pssm-ID: 410341  Cd Length: 50  Bit Score: 61.76  E-value: 7.96e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 568955249 1639 HVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYC 1687
Cdd:cd00029     1 HRFVPTTFSSPTFCDVCGKLIWgLFKQGLKCSDCGLVCHKKCLDKAPSPC 50
C1_PDZD8 cd20825
protein kinase C conserved region 1 (C1 domain) found in PDZ domain-containing protein 8 ...
1636-1689 2.55e-11

protein kinase C conserved region 1 (C1 domain) found in PDZ domain-containing protein 8 (PDZD8) and similar proteins; PDZD8, also called Sarcoma antigen NY-SAR-84/NY-SAR-104, is a molecular tethering protein that connects endoplasmic reticulum (ER) and mitochondrial membranes. PDZD8-dependent ER-mitochondria membrane tethering is essential for ER-mitochondria Ca2+ transfer. In neurons, it is involved in the regulation of dendritic Ca2+ dynamics by regulating mitochondrial Ca2+ uptake. PDZD8 also plays an indirect role in the regulation of cell morphology and cytoskeletal organization. It contains a PDZ domain and a C1 domain. This model describes the C1 domain, a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410375  Cd Length: 55  Bit Score: 60.37  E-value: 2.55e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568955249 1636 HNGHVFASYQVNIPQSCEQCLSYIWLMDkALLCSVCKMTCHKKCVHKIQ--SYCSY 1689
Cdd:cd20825     1 EGKHDFVLTQFQNATYCDFCKKKIWLKE-AFQCRLCGMICHKKCLDKCQaeTLCTR 55
RA cd17043
Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA ...
19-99 8.97e-10

Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA domain-containing proteins function by interacting with Ras proteins directly or indirectly and are involved in various functions ranging from tumor suppression to being oncoproteins. Ras proteins are small GTPases that are involved in cellular signal transduction. The RA domain has the beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub); Ub is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. RA-containing proteins include RalGDS, AF6, RIN, RASSF1, SNX27, CYR1, STE50, and phospholipase C epsilon.


Pssm-ID: 340563  Cd Length: 87  Bit Score: 57.33  E-value: 8.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249   19 LHIYPQlSSAGSQTSCRVTATKDSTTSDVIQDVVASLHLDGS-KHYVLVEVKESGGEEWVLDASDSPVHRVLLWPRRAQD 97
Cdd:cd17043     2 LKVYDD-DLAPGSAYKSILVSSTTTAREVVQLLLEKYGLEEDpEDYSLYEVSEKQETERVLHDDECPLLIQLEWGPQGTE 80

                  ..
gi 568955249   98 EH 99
Cdd:cd17043    81 FR 82
C1_TNS2-like cd20826
protein kinase C conserved region 1 (C1 domain) found in tensin-2 like (TNS2-like) proteins; ...
1638-1688 1.54e-09

protein kinase C conserved region 1 (C1 domain) found in tensin-2 like (TNS2-like) proteins; The TNS2-like group includes TNS2, and variants of TNS1 and TNS3. Tensin-2 (TNS2), also called C1 domain-containing phosphatase and tensin (C1-TEN), or tensin-like C1 domain-containing phosphatase (TENC1), is an essential component for the maintenance of glomerular basement membrane (GBM) structures. It regulates cell motility and proliferation. It may have phosphatase activity. TNS2 reduces AKT1 phosphorylation, lowers AKT1 kinase activity and interferes with AKT1 signaling. Tensin-1 (TNS1) plays a role in fibrillar adhesion formation. It may be involved in cell migration, cartilage development and in linking signal transduction pathways to the cytoskeleton. Tensin-3 (TNS3), also called tensin-like SH2 domain-containing protein 1 (TENS1), or tumor endothelial marker 6 (TEM6), may play a role in actin remodeling. It is involved in the dissociation of the integrin-tensin-actin complex. Typical TNS1 and TNS3 do not contain C1 domains, but some isoforms/variants do. Members of this family contain an N-terminal region with a zinc finger (C1 domain), a protein tyrosine phosphatase (PTP)-like domain and a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains. This model corresponds to C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410376  Cd Length: 52  Bit Score: 55.47  E-value: 1.54e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568955249 1638 GHVFASYQVNIPQSCEQCLSYIWlmDKALLCSVCKMTCHKKCVHKIQSYCS 1688
Cdd:cd20826     2 SHSFKEKSFRKPRTCDVCKQIIW--NEGSSCRVCKYACHRKCEPKVTAACS 50
RhoGAP_OCRL1 cd04380
RhoGAP_OCRL1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
1717-1867 1.23e-08

RhoGAP_OCRL1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in OCRL1-like proteins. OCRL1 (oculocerebrorenal syndrome of Lowe 1)-like proteins contain two conserved domains: a central inositol polyphosphate 5-phosphatase domain and a C-terminal Rho GAP domain, this GAP domain lacks the catalytic residue and therefore maybe inactive. OCRL-like proteins are type II inositol polyphosphate 5-phosphatases that can hydrolyze lipid PI(4,5)P2 and PI(3,4,5)P3 and soluble Ins(1,4,5)P3 and Ins(1,3,4,5)P4, but their individual specificities vary. The functionality of the RhoGAP domain is still unclear. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239845  Cd Length: 220  Bit Score: 57.35  E-value: 1.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1717 SVPIVLEKLLEHVEMHGLYTEGLYRKSG----AANRTRELRQALQTDPAAVKLedFPIHAITGVLKQWLRELPEPLMTFA 1792
Cdd:cd04380    49 SIPKEIWRLVDYLYTRGLAQEGLFEEPGlpsePGELLAEIRDALDTGSPFNSP--GSAESVAEALLLFLESLPDPIIPYS 126
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568955249 1793 QYGDFLRAVELPEKQeqlsaIYAVLD-HLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRCPDNS 1867
Cdd:cd04380   127 LYERLLEAVANNEED-----KRQVIRiSLPPVHRNVFVYLCSFLRELLSESADRGLDENTLATIFGRVLLRDPPRA 197
C1_SpBZZ1-like cd20824
protein kinase C conserved region 1 (C1 domain) found in Schizosaccharomyces pombe protein ...
1639-1688 1.09e-07

protein kinase C conserved region 1 (C1 domain) found in Schizosaccharomyces pombe protein BZZ1 and similar proteins; BZZ1 is a syndapin-like F-BAR protein that plays a role in endocytosis and trafficking to the vacuole. It functions with type I myosins to restore polarity of the actin cytoskeleton after NaCl stress. BZZ1 contains an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs), a central coiled-coil, and two C-terminal SH3 domains. Schizosaccharomyces pombe BZZ1 also harbors a C1 domain, but Saccharomyces cerevisiae BZZ1 doesn't have any. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410374  Cd Length: 53  Bit Score: 50.01  E-value: 1.09e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568955249 1639 HVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYCS 1688
Cdd:cd20824     2 HNFKPHSFSIPTKCDYCGEKIWgLSKKGLSCKDCGFNCHIKCELKVPPECP 52
C1_DEF8 cd20819
protein kinase C conserved region 1 (C1 domain) found in differentially expressed in FDCP 8 ...
1637-1687 1.19e-07

protein kinase C conserved region 1 (C1 domain) found in differentially expressed in FDCP 8 (DEF-8) and similar proteins; DEF-8 positively regulates lysosome peripheral distribution and ruffled border formation in osteoclasts. It is involved in bone resorption. DEF-8 contains a protein kinase C conserved region 1 (C1) domain followed by a putative zinc-RING and/or ribbon. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410369  Cd Length: 62  Bit Score: 50.36  E-value: 1.19e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568955249 1637 NGHVFASYQVNIP--QSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYC 1687
Cdd:cd20819     4 LGHHFVLQKSKSSskQYCDKCCGIIWgLLQTWYRCTDCGYRCHSKCLNSITRTC 57
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
1639-1687 2.24e-07

Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the Protein kinase C conserved region 1 (C1) domain.


Pssm-ID: 395079  Cd Length: 53  Bit Score: 49.36  E-value: 2.24e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 568955249  1639 HVFASYQVNIPQSCEQCLSYIWLMDK-ALLCSVCKMTCHKKCVHKIQSYC 1687
Cdd:pfam00130    1 HHFVHRNFKQPTFCDHCGEFLWGLGKqGLKCSWCKLNVHKRCHEKVPPEC 50
C1_ARHGEF-like cd20832
protein kinase C conserved region 1 (C1 domain) found in uncharacterized Rho guanine ...
1638-1688 4.77e-07

protein kinase C conserved region 1 (C1 domain) found in uncharacterized Rho guanine nucleotide exchange factor (ARHGEF)-like proteins; The family includes a group of uncharacterized proteins that show high sequence similarity to vertebrate Rho guanine nucleotide exchange factors ARHGEF11 and ARHGEF12, which may play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13). Unlike typical ARHGEF11 and ARHGEF12, members of this family contain a C1 domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410382  Cd Length: 53  Bit Score: 48.14  E-value: 4.77e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568955249 1638 GHVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYCS 1688
Cdd:cd20832     1 GHQFVLQHYYQVTFCNHCSGLLWgIGYQGYQCSDCEFNIHKQCIEVIEESCP 52
C1_ScPKC1-like_rpt1 cd20822
first protein kinase C conserved region 1 (C1 domain) found in Saccharomyces cerevisiae ...
1637-1687 1.26e-06

first protein kinase C conserved region 1 (C1 domain) found in Saccharomyces cerevisiae protein kinase C-like 1 (ScPKC1) and similar proteins; ScPKC1 is required for cell growth and for the G2 to M transition of the cell division cycle. It mediates a protein kinase cascade, activating BCK1 which itself activates MKK1/MKK2. The family also includes Schizosaccharomyces pombe PKC1 and PKC2, which are involved in the control of cell shape and act as targets of the inhibitor staurosporine. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410372  Cd Length: 52  Bit Score: 46.90  E-value: 1.26e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568955249 1637 NGHVFAS---YQVNipqSCEQCLSYiwLMDKALLCSVCKMTCHKKCVHKIQSYC 1687
Cdd:cd20822     1 RGHKFVQkqfYQIM---RCAVCGEF--LVNAGYQCEDCKYTCHKKCYEKVVTKC 49
C1_RASSF1-like cd20820
protein kinase C conserved region 1 (C1 domain) found in the Ras association domain-containing ...
1638-1687 1.57e-06

protein kinase C conserved region 1 (C1 domain) found in the Ras association domain-containing protein 1 (RASSF1)-like family; The RASSF1-like family includes RASSF1 and RASSF5. RASSF1 and RASSF5 are members of a family of RAS effectors, of which there are currently 8 members (RASSF1-8), all containing a Ras-association (RA) domain of the Ral-GDS/AF6 type. RASSF1 has eight transcripts (A-H) arising from alternative splicing and differential promoter usage. RASSF1A and 1C are the most extensively studied RASSF1; both are localized to microtubules and involved in the regulation of growth and migration. RASSF1 is a potential tumor suppressor that is required for death receptor-dependent apoptosis. RASSF5, also called new ras effector 1 (NORE1), or regulator for cell adhesion and polarization enriched in lymphoid tissues (RAPL), is expressed as three transcripts (A-C) via differential promoter usage and alternative splicing. RASSF5A is a pro-apoptotic Ras effector and functions as a Ras regulated tumor suppressor. RASSF5C is regulated by Ras related protein and modulates cellular adhesion. RASSF5 is a potential tumor suppressor that seems to be involved in lymphocyte adhesion by linking RAP1A activation upon T-cell receptor or chemokine stimulation to integrin activation. RASSF1 and RASSF5 contain a C1 domain, which is descibed in this model. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410370  Cd Length: 52  Bit Score: 46.67  E-value: 1.57e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568955249 1638 GHVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYC 1687
Cdd:cd20820     1 GHRFVPLELEQPTWCDLCGSVILgLFRKCLRCANCKMTCHPRCRSLVCLTC 51
C1_RASSF1 cd20885
protein kinase C conserved region 1 (C1 domain) found in Ras association domain-containing ...
1636-1688 2.24e-06

protein kinase C conserved region 1 (C1 domain) found in Ras association domain-containing protein 1 (RASSF1) and similar proteins; RASSF1 is a member of a family of RAS effectors, of which there are currently 8 members (RASSF1-8), all containing a Ras-association (RA) domain of the Ral-GDS/AF6 type. RASSF1 has eight transcripts (A-H) arising from alternative splicing and differential promoter usage. RASSF1A and 1C are the most extensively studied RASSF1 with both localized to microtubules and involved in regulation of growth and migration. RASSF1 is a potential tumor suppressor that is required for death receptor-dependent apoptosis. It contains a C1 domain, which is descibed in this model. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410435  Cd Length: 54  Bit Score: 46.49  E-value: 2.24e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568955249 1636 HNGHVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYCS 1688
Cdd:cd20885     1 GEGHDFQPCSLTNPTWCDLCGDFIWgLYKQCLRCTHCKYTCHLRCRDLVTLDCS 54
C1_nPKC_theta-like_rpt1 cd20834
first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
1633-1691 3.85e-06

first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) theta, delta, and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domains. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410384  Cd Length: 61  Bit Score: 46.16  E-value: 3.85e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1633 VQEHNGHVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYCSYTG 1691
Cdd:cd20834     2 VHEVKGHEFIAKFFRQPTFCSVCKEFLWgFNKQGYQCRQCNAAVHKKCHDKILGKCPGSA 61
C1_DGKtheta_typeV_rpt1 cd20803
first protein kinase C conserved region 1 (C1 domain) found in type V diacylglycerol kinase, ...
1638-1688 5.30e-06

first protein kinase C conserved region 1 (C1 domain) found in type V diacylglycerol kinase, DAG kinase theta, and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase theta, also called diglyceride kinase theta (DGK-theta), is the only isoform classified as type V; it contains a pleckstrin homology (PH)-like domain and an additional C1 domain, compared to other DGKs. It may regulate the activity of protein kinase C by controlling the balance between the two signaling lipids, diacylglycerol and phosphatidic acid. DAG kinase theta contains three copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410353  Cd Length: 56  Bit Score: 45.38  E-value: 5.30e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568955249 1638 GHVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYCS 1688
Cdd:cd20803     1 GHSFRKKTFHKPTYCHHCTDLLWgLLNQGYQCEVCNFVSHERCLKTVVTPCS 52
C1_GMIP-like cd20816
protein kinase C conserved region 1 (C1 domain) found in the GEM-interacting protein (GMIP) ...
1637-1688 5.43e-06

protein kinase C conserved region 1 (C1 domain) found in the GEM-interacting protein (GMIP)-like family; The GMIP-like family includes GMIP, Rho GTPase-activating protein 29 (ARHGAP29) and Rho GTPase-activating protein 45 (ARHGAP45). GMIP is a RhoA-specific GTPase-activating protein that acts as a key factor in saltatory neuronal migration. It associates with the Rab27a effector JFC1 and modulates vesicular transport and exocytosis. ARHGAP29, also called PTPL1-associated RhoGAP protein 1 (PARG1) or Rho-type GTPase-activating protein 29, is a GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. It has strong activity toward RHOA, and weaker activity toward RAC1 and CDC42. ARHGAP29 may act as a specific effector of RAP2A to regulate Rho. In concert with RASIP1, ARHGAP29 suppresses RhoA signaling and dampens ROCK and MYH9 activities in endothelial cells and plays an essential role in blood vessel tubulogenesis. ARHGAP45, also called minor histocompatibility antigen HA-1 (mHag HA-1), is a Rac-GAP (GTPase-Activating Protein) in endothelial cells. It acts as a novel regulator of endothelial integrity. ARHGAP45 contains a GTPase activator for the Rho-type GTPases (RhoGAP) domain that would be able to negatively regulate the actin cytoskeleton as well as cell spreading. However, it also contains N-terminally a BAR-domin which can play an autoinhibitory effect on this RhoGAP activity. Members of this family contain a zinc-binding C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410366  Cd Length: 51  Bit Score: 45.33  E-value: 5.43e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568955249 1637 NGHVFAsyQVNIPQSCEQCLSYIWLmdKALLCSVCKMTCHKKCVHKIQSYCS 1688
Cdd:cd20816     1 QTHRFR--RLRTPSKCRECDSYVYF--NGAECEECGLACHKKCLETLAIQCG 48
C1_MgcRacGAP cd20821
protein kinase C conserved region 1 (C1 domain) found in male germ cell RacGap (MgcRacGAP) and ...
1639-1679 6.87e-06

protein kinase C conserved region 1 (C1 domain) found in male germ cell RacGap (MgcRacGAP) and similar proteins; MgcRacGAP, also called Rac GTPase-activating protein 1 (RACGAP1) or protein CYK4, plays an important dual role in cytokinesis: i) it is part of centralspindlin-complex, together with the mitotic kinesin MKLP1, which is critical for the structure of the central spindle by promoting microtuble bundling; and ii) after phosphorylation by aurora B, MgcRacGAP becomes an effective regulator of RhoA and plays an important role in the assembly of the contractile ring and the initiation of cytokinesis. MgcRacGAP-like proteins contain an N-terminal C1 domain, and a C-terminal RhoGAP domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410371  Cd Length: 55  Bit Score: 45.09  E-value: 6.87e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568955249 1639 HVFASYQVNIPQSCEQCLSYIWLMDKALLCSVCKMTCHKKC 1679
Cdd:cd20821     3 HRFVSKTVIKPETCVVCGKRIKFGKKALKCKDCRVVCHPDC 43
C1_nPKC_theta-like_rpt2 cd20837
second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
1639-1687 8.43e-06

second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) theta, delta, and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410387  Cd Length: 50  Bit Score: 44.73  E-value: 8.43e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 568955249 1639 HVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYC 1687
Cdd:cd20837     1 HRFKVYNYMSPTFCDHCGSLLWgLFRQGLKCEECGMNVHHKCQKKVANLC 50
C1_MTMR-like cd20828
protein kinase C conserved region 1 (C1 domain) found in uncharacterized proteins similar to ...
1639-1689 1.17e-05

protein kinase C conserved region 1 (C1 domain) found in uncharacterized proteins similar to myotubularin-related proteins; The family includes a group of uncharacterized proteins that show high sequence similarity to vertebrate myotubularin-related proteins (MTMRs), such as MTMR5 and MTMR13. MTMRs may function as guanine nucleotide exchange factors (GEFs). Vertebrate MTMR5 and MTMR13 contain an N-terminal DENN domain, a PH-GRAM domain, an inactive PTP domain, a SET interaction domain, a coiled-coil domain, and a C-terminal PH domain. Members of this family contain these domains and have an additional C1 domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410378  Cd Length: 57  Bit Score: 44.36  E-value: 1.17e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568955249 1639 HVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYCSY 1689
Cdd:cd20828     6 HNFEPHSFVTPTNCDYCLQILWgIVKKGMKCSECGYNCHEKCQPQVPKQCSK 57
C1_cPKC_nPKC_rpt1 cd20792
first protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) ...
1638-1688 1.75e-05

first protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) protein kinase C (cPKC), novel protein kinase C (nPKC), and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domains. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. nPKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs (aPKCs) only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. This family includes classical PKCs (cPKCs) and novel PKCs (nPKCs). There are four cPKC isoforms (named alpha, betaI, betaII, and gamma) and four nPKC isoforms (delta, epsilon, eta, and theta). Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410342  Cd Length: 53  Bit Score: 43.77  E-value: 1.75e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568955249 1638 GHVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYCS 1688
Cdd:cd20792     1 GHKFVATFFKQPTFCSHCKDFIWgLGKQGYQCQVCRFVVHKRCHEYVVFKCP 52
C1_dGM13116p-like cd20831
protein kinase C conserved region 1 (C1 domain) found in Drosophila melanogaster GM13116p and ...
1636-1688 2.14e-05

protein kinase C conserved region 1 (C1 domain) found in Drosophila melanogaster GM13116p and similar proteins; This group contains uncharacterized proteins including Drosophila melanogaster GM13116p and Caenorhabditis elegans hypothetical protein R11G1.4, both of which contain C2 (a calcium-binding domain) and C1 domains. This model describes the C1 domain, a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410381  Cd Length: 58  Bit Score: 43.87  E-value: 2.14e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568955249 1636 HNGHVFASYQVNIPQSCEQC-LSYIWLMDK-ALLCSVCKMTCHKKCVHKIQSYCS 1688
Cdd:cd20831     3 YNDHTFVATHFKGGPSCAVCnKLIPGRFGKqGYQCRDCGLICHKRCHVKVETHCP 57
C1_nPKC_epsilon-like_rpt1 cd20835
first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
1631-1687 3.71e-05

first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) epsilon, eta, and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domains. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. PKC-epsilon has been shown to behave as an oncoprotein. Its overexpression contributes to neoplastic transformation depending on the cell type. It contributes to oncogenesis by inducing disordered cell growth and inhibiting cell death. It also plays a role in tumor invasion and metastasis. PKC-epsilon has also been found to confer cardioprotection against ischemia and reperfusion-mediated damage. Other cellular functions include the regulation of gene expression, cell adhesion, and cell motility. PKC-eta is predominantly expressed in squamous epithelia, where it plays a crucial role in the signaling of cell-type specific differentiation. It is also expressed in pro-B cells and early-stage thymocytes, and acts as a key regulator in early B-cell development. PKC-eta increases glioblastoma multiforme (GBM) proliferation and resistance to radiation, and is being developed as a therapeutic target for the management of GBM. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410385  Cd Length: 64  Bit Score: 43.22  E-value: 3.71e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568955249 1631 RAVQEHNGHVFASYQVNIPQSCEQCLSYIW-LMDK-ALLCSVCKMTCHKKCVHKIQSYC 1687
Cdd:cd20835     2 RRVHQVNGHKFMATYLRQPTYCSHCKDFIWgVIGKqGYQCQVCTCVVHKRCHQLVVTKC 60
PHA02682 PHA02682
ORF080 virion core protein; Provisional
2027-2121 4.24e-05

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 47.55  E-value: 4.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 2027 PAPALPCPISPTLSPLPEAAAPPRGRPTSFVTVRVKTPRR-TPIMPMANIKLPPGLPLHLTSWAPALQEAVVPvKRREPP 2105
Cdd:PHA02682   96 PACAPAAPAPAVTCPAPAPACPPATAPTCPPPAVCPAPARpAPACPPSTRQCPPAPPLPTPKPAPAAKPIFLH-NQLPPP 174
                          90
                  ....*....|....*.
gi 568955249 2106 ARRQDQVHSVYIAPGA 2121
Cdd:PHA02682  175 DYPAASCPTIETAPAA 190
C1_aPKC cd20794
protein kinase C conserved region 1 (C1 domain) found in the atypical protein kinase C (aPKC) ...
1637-1688 6.38e-05

protein kinase C conserved region 1 (C1 domain) found in the atypical protein kinase C (aPKC) family; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. They contain a C2-like region, instead of a calcium-binding (C2) region found in classical PKCs, in their regulatory domain. There are two aPKC isoforms, zeta and iota. aPKCs are involved in many cellular functions including proliferation, migration, apoptosis, polarity maintenance and cytoskeletal regulation. They also play a critical role in the regulation of glucose metabolism and in the pathogenesis of type 2 diabetes. PKC-zeta plays a critical role in activating the glucose transport response. It is activated by glucose, insulin, and exercise through diverse pathways. PKC-zeta also plays a central role in maintaining cell polarity in yeast and mammalian cells. In addition, it affects actin remodeling in muscle cells. PKC-iota is directly implicated in carcinogenesis. It is critical to oncogenic signaling mediated by Ras and Bcr-Abl. The PKC-iota gene is the target of tumor-specific gene amplification in many human cancers, and has been identified as a human oncogene. In addition to its role in transformed growth, PKC-iota also promotes invasion, chemoresistance, and tumor cell survival. Expression profiling of PKC-iota is a prognostic marker of poor clinical outcome in several human cancers. PKC-iota also plays a role in establishing cell polarity, and has critical embryonic functions. Members of this family contain one C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410344  Cd Length: 55  Bit Score: 42.25  E-value: 6.38e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568955249 1637 NGHVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYCS 1688
Cdd:cd20794     1 NGHLFQAKRFNRRAVCAYCSDRIWgLGRQGYKCINCKLLVHKKCHKLVKVACG 53
C1_nPKC_epsilon-like_rpt2 cd20838
second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
1639-1687 8.79e-05

second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) epsilon, eta, and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. PKC-epsilon has been shown to behave as an oncoprotein. Its overexpression contributes to neoplastic transformation depending on the cell type. It contributes to oncogenesis by inducing disordered cell growth and inhibiting cell death. It also plays a role in tumor invasion and metastasis. PKC-epsilon has also been found to confer cardioprotection against ischemia and reperfusion-mediated damage. Other cellular functions include the regulation of gene expression, cell adhesion, and cell motility. PKC-eta is predominantly expressed in squamous epithelia, where it plays a crucial role in the signaling of cell-type specific differentiation. It is also expressed in pro-B cells and early-stage thymocytes, and acts as a key regulator in early B-cell development. PKC-eta increases glioblastoma multiforme (GBM) proliferation and resistance to radiation, and is being developed as a therapeutic target for the management of GBM. Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410388  Cd Length: 55  Bit Score: 41.87  E-value: 8.79e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 568955249 1639 HVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYC 1687
Cdd:cd20838     3 HRFSVHNYKRPTFCDHCGSLLYgLYKQGLQCKVCKMNVHKRCQKNVANNC 52
RhoGAP_fRGD2 cd04399
RhoGAP_fRGD2: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1704-1863 9.30e-05

RhoGAP_fRGD2: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal RGD2-like proteins. Yeast Rgd2 is a GAP protein for Cdc42 and Rho5. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239864  Cd Length: 212  Bit Score: 45.79  E-value: 9.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1704 FGVCVDSLT-SDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGA------ANRTRELRQALQT----DPAAVKLEDFPIHA 1772
Cdd:cd04399     1 FGVDLETRCrLDKKVVPLIVSAILSYLDQLYPDLINDEVRRNVwtdpvsLKETHQLRNLLNKpkkpDKEVIILKKFEPST 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955249 1773 ITGVLKQWLRELPEPLMTfAQYGDFLRAV-------ELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKvalLEDVN 1845
Cdd:cd04399    81 VASVLKLYLLELPDSLIP-HDIYDLIRSLysayppsQEDSDTARIQGLQSTLSQLPKSHIATLDAIITHFYR---LIEIT 156
                         170       180
                  ....*....|....*....|....
gi 568955249 1846 RMSPGA------LAIIFAPCLLRC 1863
Cdd:cd04399   157 KMGESEeeyadkLATSLSREILRP 180
C1_MRCKalpha cd20864
protein kinase C conserved region 1 (C1 domain) found in myotonic dystrophy kinase-related ...
1639-1687 9.81e-05

protein kinase C conserved region 1 (C1 domain) found in myotonic dystrophy kinase-related Cdc42-binding kinase alpha (MRCK alpha) and similar proteins; MRCK alpha, also called Cdc42-binding protein kinase alpha, DMPK-like alpha, or myotonic dystrophy protein kinase-like alpha, is a serine/threonine-protein kinase expressed ubiquitously in many tissues. It plays a role in the regulation of peripheral actin reorganization and neurite outgrowth. It may also play a role in the transferrin iron uptake pathway. MRCK alpha is an important downstream effector of Cdc42 and plays a role in the regulation of cytoskeleton reorganization and cell migration. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410414  Cd Length: 60  Bit Score: 41.93  E-value: 9.81e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 568955249 1639 HVFASYQVNIPQSCEQCLS-YIWLMDKALLCSVCKMTCHKKCVHKIQSYC 1687
Cdd:cd20864     3 HQFVVKSFTTPTKCNQCTSlMVGLIRQGCTCEVCGFSCHVTCADKAPSVC 52
C1_ROCK2 cd20875
protein kinase C conserved region 1 (C1 domain) found in Rho-associated coiled-coil containing ...
1636-1677 9.84e-05

protein kinase C conserved region 1 (C1 domain) found in Rho-associated coiled-coil containing protein kinase 2 (ROCK2) and similar proteins; ROCK2 is a serine/threonine kinase, catalyzing the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK2, also called Rho-associated protein kinase 2, Rho kinase 2, Rho-associated, coiled-coil-containing protein kinase II (ROCK-II), or p164 ROCK-2, was the first identified target of activated RhoA, and was found to play a role in stress fiber and focal adhesion formation. It is prominently expressed in the brain, heart, and skeletal muscles. It is implicated in vascular and neurological disorders, such as hypertension and vasospasm of the coronary and cerebral arteries. ROCK2 is also activated by caspase-2 cleavage, resulting in thrombin-induced microparticle generation in response to cell activation. Mice deficient in ROCK2 show intrauterine growth retardation and embryonic lethality because of placental dysfunction. ROCK proteins contain an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD), a pleckstrin homology (PH) domain and a C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410425  Cd Length: 71  Bit Score: 42.33  E-value: 9.84e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 568955249 1636 HNGHVFASYQVNIPQSCEQCLSYIWLMDK---ALLCSVCKMTCHK 1677
Cdd:cd20875     9 HKGHEFIPTLYHFPTNCEACMKPLWHMFKpppALECRRCHIKCHK 53
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
1036-1058 1.14e-04

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


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 40.77  E-value: 1.14e-04
                            10        20
                    ....*....|....*....|...
gi 568955249   1036 ERTQAAVYLQAAWRGYLQRQAYH 1058
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRYK 23
C1_RASSF5 cd20886
protein kinase C conserved region 1 (C1 domain) found in Ras association domain-containing ...
1638-1688 1.82e-04

protein kinase C conserved region 1 (C1 domain) found in Ras association domain-containing protein 5 (RASSF5) and similar proteins; RASSF5, also called new ras effector 1 (NORE1), or regulator for cell adhesion and polarization enriched in lymphoid tissues (RAPL), is a member of a family of RAS effectors, of which there are currently 8 members (RASSF1-8), all containing a Ras-association (RA) domain of the Ral-GDS/AF6 type. It is expressed as three transcripts (A-C) via differential promoter usage and alternative splicing. RASSF5A is a pro-apoptotic Ras effector and functions as a Ras regulated tumor suppressor. RASSF5C is regulated by Ras related protein and modulates cellular adhesion. RASSF5 is a potential tumor suppressor that seems to be involved in lymphocyte adhesion by linking RAP1A activation upon T-cell receptor or chemokine stimulation to integrin activation. It contains a C1 domain, which is descibed in this model. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410436  Cd Length: 50  Bit Score: 40.83  E-value: 1.82e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568955249 1638 GHVFASYQVnIPQSCEQCLSYIwlMDKALLCSVCKMTCHKKCVHKIQSYCS 1688
Cdd:cd20886     3 GHRFEPGAL-GPGWCDLCGRYI--LSQALRCTNCKYTCHSECRDLVQLDCN 50
C1_PKD_rpt2 cd20796
second protein kinase C conserved region 1 (C1 domain) found in the family of protein kinase D ...
1639-1687 1.84e-04

second protein kinase C conserved region 1 (C1 domain) found in the family of protein kinase D (PKD); PKDs are important regulators of many intracellular signaling pathways such as ERK and JNK, and cellular processes including the organization of the trans-Golgi network, membrane trafficking, cell proliferation, migration, and apoptosis. They are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs contain N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the second C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410346  Cd Length: 54  Bit Score: 41.12  E-value: 1.84e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 568955249 1639 HVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYC 1687
Cdd:cd20796     2 HTFVVHTYTKPTVCQHCKKLLKgLFRQGLQCKDCKFNCHKKCAEKVPKDC 51
C1_DGK_typeII_rpt1 cd20800
first protein kinase C conserved region 1 (C1 domain) found in type II diacylglycerol kinases; ...
1652-1690 1.88e-04

first protein kinase C conserved region 1 (C1 domain) found in type II diacylglycerol kinases; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. Type II DAG kinases (DGKs) contain pleckstrin homology (PH) and sterile alpha motifs (SAM) domains, in addition to C1 and catalytic domains that are present in all DGKs. The SAM domain mediates oligomerization of type II DGKs. Three DGK isozymes (delta, eta and kappa) are classified as type II. DAG kinase delta, also called 130 kDa DAG kinase, or diglyceride kinase delta (DGK-delta), is a residential lipid kinase in the endoplasmic reticulum. It promotes lipogenesis and is involved in triglyceride biosynthesis. DAG kinase eta, also called diglyceride kinase eta (DGK-eta), plays a key role in promoting cell growth. The DAG kinase eta gene, DGKH, is a replicated risk gene of bipolar disorder (BPD). DAG kinase kappa is also called diglyceride kinase kappa (DGK-kappa) or 142 kDa DAG kinase. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410350  Cd Length: 60  Bit Score: 41.15  E-value: 1.88e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 568955249 1652 CEQCLSYIwlMDKALLCSVCKMTCHKKCVHKIQSYCSYT 1690
Cdd:cd20800    21 CREALSGV--TSHGLSCEVCKFKAHKRCAVKAPNNCKWT 57
C1_DGKbeta_rpt1 cd20845
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase beta (DAG ...
1633-1690 2.64e-04

first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase beta (DAG kinase beta) and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase beta, also called 90 kDa diacylglycerol kinase, or diglyceride kinase beta (DGK-beta), exhibits high phosphorylation activity for long-chain diacylglycerols. It is classified as a type I DAG kinase (DGK), containing EF-hand structures that bind Ca(2+) and a recoverin homology domain, in addition to C1 and catalytic domains that are present in all DGKs. As a type I DGK, it is regulated by calcium binding. DAG kinase beta contains two copies of the C1 domain. This model corresponds to the first one. DGK-beta contains typical C1 domains that bind DAG and phorbol esters. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410395  Cd Length: 66  Bit Score: 40.99  E-value: 2.64e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568955249 1633 VQEHNGHVFASYQVNIPQSCEQCLSY-IWLMDKALLCSVCKMTCHKKCVHKIQSYCSYT 1690
Cdd:cd20845     2 VKDDGQHVWRLKHFNKPAYCNLCLNMlVGLGKQGLCCSFCKYTVHERCVQRAPASCIKT 60
C1_PKD_rpt1 cd20795
first protein kinase C conserved region 1 (C1 domain) found in the protein kinase D (PKD) ...
1636-1690 3.17e-04

first protein kinase C conserved region 1 (C1 domain) found in the protein kinase D (PKD) family; PKDs are important regulators of many intracellular signaling pathways such as ERK and JNK, and cellular processes including the organization of the trans-Golgi network, membrane trafficking, cell proliferation, migration, and apoptosis. They are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs contain N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the first C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410345  Cd Length: 56  Bit Score: 40.36  E-value: 3.17e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568955249 1636 HNGHVfASYQVniPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYCSYT 1690
Cdd:cd20795     4 HSLFV-HSYKS--PTFCDFCGEMLFgLVRQGLKCEGCGLNFHKRCAYKIPNNCTGS 56
C1_TNS3_v cd20889
protein kinase C conserved region 1 (C1 domain) found in tensin-3 (TNS3) variant and similar ...
1639-1687 4.19e-04

protein kinase C conserved region 1 (C1 domain) found in tensin-3 (TNS3) variant and similar proteins; Tensin-3 (TNS3), also called tensin-like SH2 domain-containing protein 1 (TENS1), or tumor endothelial marker 6 (TEM6), may play a role in actin remodeling. It is involved in the dissociation of the integrin-tensin-actin complex. This model corresponds to the C1 domain found in TNS3 variant. Typical TNS3 does not contain C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410439  Cd Length: 56  Bit Score: 40.26  E-value: 4.19e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 568955249 1639 HVFASYQVNIPQSCEQCLSYIwlMDKALLCSVCKMTCHKKCVHKIQSYC 1687
Cdd:cd20889     3 HTFKNKTFKKPKVCSICKQVI--DSQGISCRVCKYACHKKCEAKVVTPC 49
C1_TNS2 cd20887
protein kinase C conserved region 1 (C1 domain) found in tensin-2 and similar proteins; ...
1666-1688 7.40e-04

protein kinase C conserved region 1 (C1 domain) found in tensin-2 and similar proteins; Tensin-2 (TNS2), also called C1 domain-containing phosphatase and tensin (C1-TEN), or tensin-like C1 domain-containing phosphatase (TENC1), is an essential component for the maintenance of glomerular basement membrane (GBM) structures. It regulates cell motility and proliferation. It may have phosphatase activity. TNS2 reduces AKT1 phosphorylation, lowers AKT1 kinase activity, and interferes with AKT1 signaling. It contains an N-terminal region with a zinc finger (C1 domain), a protein tyrosine phosphatase (PTP)-like domain and a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410437  Cd Length: 53  Bit Score: 39.38  E-value: 7.40e-04
                          10        20
                  ....*....|....*....|...
gi 568955249 1666 LLCSVCKMTCHKKCVHKIQSYCS 1688
Cdd:cd20887    28 LVCRVCKVASHKKCEAKVTSACQ 50
C1_KSR cd20812
protein kinase C conserved region 1 (C1 domain) found in the kinase suppressor of Ras (KSR) ...
1639-1688 7.51e-04

protein kinase C conserved region 1 (C1 domain) found in the kinase suppressor of Ras (KSR) family; KSR is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases, but there is some debate in this designation as a few groups have reported detecting kinase catalytic activity for KSRs, specifically KSR1. Vertebrates contain two KSR proteins, KSR1 and KSR2. KSR proteins contain a SAM-like domain, a zinc finger cysteine-rich domain (C1), and a pseudokinase domain. This model describes the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410362  Cd Length: 48  Bit Score: 39.23  E-value: 7.51e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 568955249 1639 HVFASYQVnIPQSCEQCLSYIWLmdkALLCSVCKMTCHKKCVHKIQSYCS 1688
Cdd:cd20812     3 HRFSKKLF-MRQTCDYCHKQMFF---GLKCKDCKYKCHKKCAKKAPPSCG 48
C1_PKD1_rpt1 cd20839
first protein kinase C conserved region 1 (C1 domain) found in protein kinase D (PKD) and ...
1639-1694 8.91e-04

first protein kinase C conserved region 1 (C1 domain) found in protein kinase D (PKD) and similar proteins; PKD is also called PKD1, PRKD1, protein kinase C mu type (nPKC-mu), PRKCM, serine/threonine-protein kinase D1, or nPKC-D1. It is a serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of MAPK8/JNK1 and Ras signaling, Golgi membrane integrity and trafficking, cell survival through NF-kappa-B activation, cell migration, cell differentiation by mediating HDAC7 nuclear export, cell proliferation via MAPK1/3 (ERK1/2) signaling, and plays a role in cardiac hypertrophy, VEGFA-induced angiogenesis, genotoxic-induced apoptosis and flagellin-stimulated inflammatory response. PKD contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the first C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410389  Cd Length: 72  Bit Score: 39.62  E-value: 8.91e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568955249 1639 HVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYCSYTGRRK 1694
Cdd:cd20839     8 HALFVHSYRAPAFCDHCGEMLWgLVRQGLKCEGCGLNYHKRCAFKIPNNCSGVRKRR 64
C1_cPKC_nPKC_rpt2 cd20793
second protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) ...
1639-1687 9.55e-04

second protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) protein kinase C (cPKC), novel protein kinase C (nPKC), and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. nPKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs (aPKCs) only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. This family includes classical PKCs (cPKCs) and novel PKCs (nPKCs). There are four cPKC isoforms (named alpha, betaI, betaII, and gamma) and four nPKC isoforms (delta, epsilon, eta, and theta). Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410343  Cd Length: 50  Bit Score: 38.80  E-value: 9.55e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 568955249 1639 HVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYC 1687
Cdd:cd20793     1 HKFKVHTYYSPTFCDHCGSLLYgLVRQGLKCKDCGMNVHHRCKENVPHLC 50
C1_DGK_typeI_rpt1 cd20799
first protein kinase C conserved region 1 (C1 domain) found in type I diacylglycerol kinases; ...
1639-1690 9.63e-04

first protein kinase C conserved region 1 (C1 domain) found in type I diacylglycerol kinases; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. Type I DAG kinases (DGKs) contain EF-hand structures that bind Ca(2+) and recoverin homology domains, in addition to C1 and catalytic domains that are present in all DGKs. Type I DGKs, regulated by calcium binding, include three DGK isozymes (alpha, beta and gamma). DAG kinase alpha, also called 80 kDa DAG kinase, or diglyceride kinase alpha (DGK-alpha), is active upon cell stimulation, initiating the resynthesis of phosphatidylinositols and attenuating protein kinase C activity. DAG kinase beta, also called 90 kDa DAG kinase, or diglyceride kinase beta (DGK-beta), exhibits high phosphorylation activity for long-chain diacylglycerols. DAG kinase gamma, also called diglyceride kinase gamma (DGK-gamma), reverses the normal flow of glycerolipid biosynthesis by phosphorylating diacylglycerol back to phosphatidic acid. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. DGK-alpha contains atypical C1 domains, while DGK-beta and DGK-gamma contain typical C1 domains that bind DAG and phorbol esters. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410349  Cd Length: 62  Bit Score: 39.28  E-value: 9.63e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568955249 1639 HVFASYQVNIPQSCEQCLSYIWLMDK-ALLCSVCKMTCHKKCVHKIQSYCSYT 1690
Cdd:cd20799     6 HVWRLKHFNKPAYCNVCENMLVGLRKqGLCCTFCKYTVHERCVSRAPASCIRT 58
C1_Sbf-like cd20827
protein kinase C conserved region 1 (C1 domain) found in the myotubularin-related protein Sbf ...
1639-1688 1.08e-03

protein kinase C conserved region 1 (C1 domain) found in the myotubularin-related protein Sbf and similar proteins; This group includes Drosophila melanogaster SET domain binding factor (Sbf), the single homolog of human MTMR5/MTMR13, and similar proteins, that show high sequence similarity to vertebrate myotubularin-related proteins (MTMRs) which may function as guanine nucleotide exchange factors (GEFs). Sbf is a pseudophosphatase that coordinates both phosphatidylinositol 3-phosphate (PI(3)P) turnover and Rab21 GTPase activation in an endosomal pathway that controls macrophage remodeling. It also functions as a GEF that promotes Rab21 GTPase activation associated with PI(3)P endosomes. Vertebrate MTMR5 and MTMR13 contain an N-terminal DENN domain, a PH-GRAM domain, an inactive PTP domain, a SET interaction domain, a coiled-coil domain, and a C-terminal PH domain. Members of this family contain these domains and have an additional C1 domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410377  Cd Length: 53  Bit Score: 38.94  E-value: 1.08e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568955249 1639 HVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYCS 1688
Cdd:cd20827     2 HRFEKHNFTTPTYCDYCSSLLWgLVKTGMRCADCGYSCHEKCLEHVPKNCT 52
C1_MRCK cd20809
protein kinase C conserved region 1 (C1 domain) found in the Myotonic dystrophy kinase-related ...
1639-1689 1.32e-03

protein kinase C conserved region 1 (C1 domain) found in the Myotonic dystrophy kinase-related Cdc42-binding kinase (MRCK) family; MRCK is thought to be a coincidence detector of signaling by the small GTPase Cdc42 and phosphoinositides. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. MRCK has been shown to promote cytoskeletal reorganization, which affects many biological processes. Three isoforms of MRCK are known, named alpha, beta and gamma. MRCKgamma is expressed in heart and skeletal muscles, unlike MRCKalpha and MRCKbeta, which are expressed ubiquitously. MRCK consists of a serine/threonine kinase domain, a cysteine rich (C1) region, a PH domain and a p21 binding motif. This model corresponds to C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410359  Cd Length: 53  Bit Score: 38.41  E-value: 1.32e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568955249 1639 HVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYCSY 1689
Cdd:cd20809     1 HKFIVRTFSTPTKCNHCTSLMVgLVRQGLVCEVCGYACHVSCADKAPQVCPV 52
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
1038-1058 1.92e-03

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 425778  Cd Length: 21  Bit Score: 37.30  E-value: 1.92e-03
                           10        20
                   ....*....|....*....|.
gi 568955249  1038 TQAAVYLQAAWRGYLQRQAYH 1058
Cdd:pfam00612    1 RKAAIKIQAAWRGYLARKRYK 21
C1_betaCHN cd20857
protein kinase C conserved region 1 (C1 domain) found in beta-chimaerin and similar proteins; ...
1639-1693 2.09e-03

protein kinase C conserved region 1 (C1 domain) found in beta-chimaerin and similar proteins; Beta-chimaerin, also called beta-chimerin (BCH) or Rho GTPase-activating protein 3 (ARHGAP3), is a GTPase-activating protein (GAP) for p21-rac. Insufficient expression of beta-2 chimaerin is expected to lead to higher Rac activity and could therefore play a role in the progression from low-grade to high-grade tumors. Beta-chimaerin contains a functional SH2 domain that can bind to phosphotyrosine motifs within receptors, a GAP domain with specificity in vitro for Rac1 and a diacylglycerol (DAG)-binding C1 domain which allows them to translocate to membranes in response to DAG signaling and anchors them in close proximity to activated Rac. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410407  Cd Length: 61  Bit Score: 38.48  E-value: 2.09e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568955249 1639 HVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYCSYTGRR 1693
Cdd:cd20857     6 HNFKVHTFRGPHWCEYCANFMWgLIAQGVRCSDCGLNVHKQCSKHVPNDCQPDLKR 61
C1_ROCK1 cd20874
protein kinase C conserved region 1 (C1 domain) found in Rho-associated coiled-coil containing ...
1634-1682 2.56e-03

protein kinase C conserved region 1 (C1 domain) found in Rho-associated coiled-coil containing protein kinase 1 (ROCK1) and similar proteins; ROCK1 is a serine/threonine kinase, catalyzing the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK1, also called Rho-associated protein kinase 1, renal carcinoma antigen NY-REN-35, Rho-associated, coiled-coil-containing protein kinase I (ROCK-I), p160 ROCK-1, or p160ROCK, is preferentially expressed in the liver, lung, spleen, testes, and kidney. It mediates signaling from Rho to the actin cytoskeleton. It is implicated in the development of cardiac fibrosis, cardiomyocyte apoptosis, and hyperglycemia. Mice deficient with ROCK1 display eyelids open at birth (EOB) and omphalocele phenotypes due to the disorganization of actin filaments in the eyelids and the umbilical ring. ROCK proteins contain an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD), a pleckstrin homology (PH) domain and a C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410424  Cd Length: 69  Bit Score: 38.46  E-value: 2.56e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568955249 1634 QEHNGHVFASYQVNIPQSCEQCLSYIWLMDK---ALLCSVCKMTCHKKCVHK 1682
Cdd:cd20874     3 LPHKGHEFIPTLYHFPANCEACAKPLWHVFKpppALECRRCHVKCHKDHLDK 54
C1_TNS1_v cd20888
protein kinase C conserved region 1 (C1 domain) found in tensin-1 (TNS1) variant and similar ...
1637-1688 3.34e-03

protein kinase C conserved region 1 (C1 domain) found in tensin-1 (TNS1) variant and similar proteins; Tensin-1 (TNS1) plays a role in fibrillar adhesion formation. It may be involved in cell migration, cartilage development and in linking signal transduction pathways to the cytoskeleton. This model corresponds to the C1 domain found in TNS1 variant. Typical TNS1 does not contain C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410438  Cd Length: 57  Bit Score: 37.54  E-value: 3.34e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568955249 1637 NGHVFASYQVNIPQSCEQCLSYIwlMDKALLCSVCKMTCHKKCVHKIQSYCS 1688
Cdd:cd20888     4 HTHTFKVKTFKKVKSCGICKQAI--TREGSTCRVCKLSCHKKCEAKVATPCV 53
CRIK cd20814
protein kinase C conserved region 1 (C1 domain) found in citron Rho-interacting kinase (CRIK) ...
1639-1687 3.97e-03

protein kinase C conserved region 1 (C1 domain) found in citron Rho-interacting kinase (CRIK) and similar proteins; CRIK, also called serine/threonine-protein kinase 21, is an effector of the small GTPase Rho. It plays an important function during cytokinesis and affects its contractile process. CRIK-deficient mice show severe ataxia and epilepsy as a result of abnormal cytokinesis and massive apoptosis in neuronal precursors. A Down syndrome critical region protein TTC3 interacts with CRIK and inhibits CRIK-dependent neuronal differentiation and neurite extension. CRIK contains a catalytic domain, a central coiled-coil domain, and a C-terminal region containing a Rho-binding domain (RBD), a zinc finger (C1 domain), and a pleckstrin homology (PH) domain, in addition to other motifs. This model corresponds to C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410364  Cd Length: 56  Bit Score: 37.23  E-value: 3.97e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 568955249 1639 HVFASYQVNIPQSCEQCLSYIWLMDKALLCSVCKMTCHKKCVHKIQSYC 1687
Cdd:cd20814     5 HRFTTGLNMRATKCAVCLDGVPFGRQASKCSECGIVCHPKCSSSLPNTC 53
C1_AKAP13 cd20878
protein kinase C conserved region 1 (C1 domain) found in A-kinase anchor protein 13 (AKAP-13) ...
1637-1679 4.04e-03

protein kinase C conserved region 1 (C1 domain) found in A-kinase anchor protein 13 (AKAP-13) and similar proteins; AKAP-13, also called AKAP-Lbc, breast cancer nuclear receptor-binding auxiliary protein (Brx-1), guanine nucleotide exchange factor Lbc, human thyroid-anchoring protein 31, lymphoid blast crisis oncogene (LBC oncogene), non-oncogenic Rho GTPase-specific GTP exchange factor, protein kinase A-anchoring protein 13 (PRKA13), or p47, is a scaffold protein that plays an important role in assembling signaling complexes downstream of several types of G protein-coupled receptors (GPCRs). It activates RhoA in response to GPCR signaling via its function as a Rho guanine nucleotide exchange factor. It may also activate other Rho family members. AKAP-13 plays a role in cell growth, cell development and actin fiber formation. Its Rho-GEF activity is regulated by protein kinase A (PKA), through binding and phosphorylation. Alternative splicing of this gene in humans has at least 3 transcript variants encoding different isoforms (i.e. proto-/onco-Lymphoid blast crisis, Lbc and breast cancer nuclear receptor-binding auxiliary protein, and Brx) that contain a C1 domain followed by a dbl oncogene homology (DH) domain and a PH domain which are required for full transforming activity. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410428  Cd Length: 60  Bit Score: 37.32  E-value: 4.04e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 568955249 1637 NGHVFASYQVNIPQSCEQClSYIWLMDKALLCSVCKMTCHKKC 1679
Cdd:cd20878     6 NGHVFSPVSSVGPTQCYHC-SKPLNTKDAFLCANCNVQVHKGC 47
C1_aPKC_zeta cd21095
protein kinase C conserved region 1 (C1 domain) found in the atypical protein kinase C (aPKC) ...
1637-1679 4.75e-03

protein kinase C conserved region 1 (C1 domain) found in the atypical protein kinase C (aPKC) zeta type; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. They contain a C2-like region, instead of a calcium-binding (C2) region found in classical PKCs, in their regulatory domain. There are two aPKC isoforms, zeta and iota. aPKCs are involved in many cellular functions including proliferation, migration, apoptosis, polarity maintenance and cytoskeletal regulation. They also play a critical role in the regulation of glucose metabolism and in the pathogenesis of type 2 diabetes. PKC-zeta plays a critical role in activating the glucose transport response. It is activated by glucose, insulin, and exercise through diverse pathways. PKC-zeta also plays a central role in maintaining cell polarity in yeast and mammalian cells. In addition, it affects actin remodeling in muscle cells. Members of this family contain C1 domain found in aPKC isoform zeta. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410448  Cd Length: 55  Bit Score: 37.27  E-value: 4.75e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 568955249 1637 NGHVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKC 1679
Cdd:cd21095     1 NGHLFQAKRFNRRAYCGQCSERIWgLGRQGYKCINCKLLVHKRC 44
C1_PIK3R-like_rpt2 cd20830
second protein kinase C conserved region 1 (C1 domain) found in uncharacterized ...
1650-1681 4.91e-03

second protein kinase C conserved region 1 (C1 domain) found in uncharacterized phosphatidylinositol 3-kinase regulatory subunit-like proteins; The family includes a group of uncharacterized proteins that show high sequence similarity to vertebrate phosphatidylinositol 3-kinase regulatory subunits (PIK3Rs), which bind to activated (phosphorylated) protein-tyrosine kinases through its SH2 domain and regulate their kinase activity. Unlike typical PIK3Rs, members of this family have two C1 domains. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410380  Cd Length: 52  Bit Score: 36.84  E-value: 4.91e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 568955249 1650 QSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVH 1681
Cdd:cd20830    12 QWCDKCGKFLFgLVHQGLQCQDCGLVCHRTCAA 44
C1_PKD2_rpt2 cd20843
second protein kinase C conserved region 1 (C1 domain) found in protein kinase D2 (PKD2) and ...
1639-1687 5.08e-03

second protein kinase C conserved region 1 (C1 domain) found in protein kinase D2 (PKD2) and similar proteins; PKD2, also called PRKD2, HSPC187, or serine/threonine-protein kinase D2 (nPKC-D2), is a serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of cell proliferation via MAPK1/3 (ERK1/2) signaling, oxidative stress-induced NF-kappa-B activation, inhibition of HDAC7 transcriptional repression, signaling downstream of T-cell antigen receptor (TCR) and cytokine production, and plays a role in Golgi membrane trafficking, angiogenesis, secretory granule release and cell adhesion. PKD2 contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the second C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410393  Cd Length: 79  Bit Score: 37.65  E-value: 5.08e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 568955249 1639 HVFASYQVNIPQSCEQCLSYI-WLMDKALLCSVCKMTCHKKCVHKIQSYC 1687
Cdd:cd20843    12 HTFVIHSYTRPTVCQFCKKLLkGLFRQGLQCKDCKFNCHKRCATRVPNDC 61
C1_PKD1_rpt2 cd20842
second protein kinase C conserved region 1 (C1 domain) found in protein kinase D (PKD) and ...
1639-1687 5.13e-03

second protein kinase C conserved region 1 (C1 domain) found in protein kinase D (PKD) and similar proteins; PKD is also called PKD1, PRKD1, protein kinase C mu type (nPKC-mu), PRKCM, serine/threonine-protein kinase D1, or nPKC-D1. It is a serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of MAPK8/JNK1 and Ras signaling, Golgi membrane integrity and trafficking, cell survival through NF-kappa-B activation, cell migration, cell differentiation by mediating HDAC7 nuclear export, cell proliferation via MAPK1/3 (ERK1/2) signaling, and plays a role in cardiac hypertrophy, VEGFA-induced angiogenesis, genotoxic-induced apoptosis and flagellin-stimulated inflammatory response. PKD contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the second C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410392  Cd Length: 94  Bit Score: 38.07  E-value: 5.13e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 568955249 1639 HVFASYQVNIPQSCEQCLSYI-WLMDKALLCSVCKMTCHKKCVHKIQSYC 1687
Cdd:cd20842    35 HTFVIHSYTRPTVCQYCKKLLkGLFRQGLQCKDCKFNCHKRCAPKVPNNC 84
C1_ScPKC1-like_rpt2 cd20823
second protein kinase C conserved region 1 (C1 domain) found in Saccharomyces cerevisiae ...
1636-1687 5.37e-03

second protein kinase C conserved region 1 (C1 domain) found in Saccharomyces cerevisiae protein kinase C-like 1 (ScPKC1) and similar proteins; ScPKC1 is required for cell growth and for the G2 to M transition of the cell division cycle. It mediates a protein kinase cascade, activating BCK1 which itself activates MKK1/MKK2. The family also includes Schizosaccharomyces pombe PKC1 and PKC2, which are involved in the control of cell shape and act as targets of the inhibitor staurosporine. Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410373  Cd Length: 59  Bit Score: 36.90  E-value: 5.37e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568955249 1636 HNGHVFASYQVNIPQSCEQClSYI--WLMDKALLCSVCKMTCHKKCVHKIQSYC 1687
Cdd:cd20823     2 RIPHRFEPFTNLGANWCCHC-GQMlpLGRKQIRKCTECGKTAHAQCAHLVPNFC 54
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
1014-1035 5.49e-03

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


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 36.15  E-value: 5.49e-03
                            10        20
                    ....*....|....*....|..
gi 568955249   1014 QMKHAALTIQACWRSYRVRRAL 1035
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRY 22
C1_Stac cd20817
protein kinase C conserved region 1 (C1 domain) found in the SH3 and cysteine-rich ...
1639-1688 5.80e-03

protein kinase C conserved region 1 (C1 domain) found in the SH3 and cysteine-rich domain-containing protein (Stac) family; Stac proteins are putative adaptor proteins that are important for neuronal function. There are three mammalian members (Stac1, Stac2 and Stac3) of this family. Stac1 and Stac3 contain two SH3 domains while Stac2 contains a single SH3 domain at the C-terminus. Stac1 and Stac2 have been found to be expressed differently in mature dorsal root ganglia (DRG) neurons. Stac1 is mainly expressed in peptidergic neurons while Stac2 is found in a subset of nonpeptidergic and all trkB+ neurons. Stac proteins contain a cysteine-rich C1 domain and one or two SH3 domains at the C-terminus. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410367  Cd Length: 51  Bit Score: 36.92  E-value: 5.80e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568955249 1639 HVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIqSYCS 1688
Cdd:cd20817     1 HSFQEHTFKKPTFCDVCKELLVgLSKQGLRCKNCKMNVHHKCQEGV-PDCS 50
C1_PIK3R-like_rpt1 cd20829
first protein kinase C conserved region 1 (C1 domain) found in uncharacterized ...
1639-1680 6.64e-03

first protein kinase C conserved region 1 (C1 domain) found in uncharacterized phosphatidylinositol 3-kinase regulatory subunit-like proteins; The family includes a group of uncharacterized proteins that show high sequence similarity to vertebrate phosphatidylinositol 3-kinase regulatory subunits (PIK3Rs), which bind to activated (phosphorylated) protein-tyrosine kinases through its SH2 domain and regulate their kinase activity. Unlike typical PIK3Rs, members of this family have two C1 domains. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410379  Cd Length: 53  Bit Score: 36.56  E-value: 6.64e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 568955249 1639 HVFASYQVNIPQSCEQCLSYIWLMDKAL-LCSVCKMTCHKKCV 1680
Cdd:cd20829     1 HRLVDVYFVTPILCRHCKDYIWGKGKVGvRCEDCHACFHLVCA 43
C1_cPKC_rpt2 cd20836
second protein kinase C conserved region 1 (C1 domain) found in the classical (or conventional) ...
1639-1687 6.72e-03

second protein kinase C conserved region 1 (C1 domain) found in the classical (or conventional) protein kinase C (cPKC) family; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. cPKCs are potent kinases for histones, myelin basic protein, and protamine. They depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. PKC-alpha is expressed in many tissues and is associated with cell proliferation, apoptosis, and cell motility. It plays a role in the signaling of the growth factors PDGF, VEGF, EGF, and FGF. Abnormal levels of PKC-alpha have been detected in many transformed cell lines and several human tumors. In addition, PKC-alpha is required for HER2 dependent breast cancer invasion. The PKC beta isoforms (I and II), generated by alternative splicing of a single gene, are preferentially activated by hyperglycemia-induced DAG (1,2-diacylglycerol) in retinal tissues. This is implicated in diabetic microangiopathy such as ischemia, neovascularization, and abnormal vasodilator function. PKC-beta also plays an important role in VEGF signaling. In addition, glucose regulates proliferation in retinal endothelial cells via PKC-betaI. PKC-beta is also being explored as a therapeutic target in cancer. It contributes to tumor formation and is involved in the tumor host mechanisms of inflammation and angiogenesis. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia. Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410386  Cd Length: 54  Bit Score: 36.55  E-value: 6.72e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 568955249 1639 HVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYC 1687
Cdd:cd20836     1 HKFKVHTYSSPTFCDHCGSLLYgLIHQGMKCDTCDMNVHKRCVKNVPSLC 50
C1_PKD3_rpt2 cd20844
second protein kinase C conserved region 1 (C1 domain) found in protein kinase D3 (PKD3) and ...
1639-1687 8.89e-03

second protein kinase C conserved region 1 (C1 domain) found in protein kinase D3 (PKD3) and similar proteins; PKD3 is also called PRKD3, PRKCN, serine/threonine-protein kinase D3 (nPKC-D3), protein kinase C nu type (nPKC-nu), or protein kinase EPK2. It converts transient diacylglycerol (DAG) signals into prolonged physiological effects, downstream of PKC. It is involved in the regulation of the cell cycle by modulating microtubule nucleation and dynamics. PKD3 acts as a key mediator in several cancer development signaling pathways. PKD3 contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the second C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410394 [Multi-domain]  Cd Length: 69  Bit Score: 36.91  E-value: 8.89e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 568955249 1639 HVFASYQVNIPQSCEQCLSYI-WLMDKALLCSVCKMTCHKKCVHKIQSYC 1687
Cdd:cd20844     6 HTFAVHSYTRPTICQYCKRLLkGLFRQGMQCKDCRFNCHKRCASKVPRDC 55
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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