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Conserved domains on  [gi|568955272|ref|XP_006509643|]
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unconventional myosin-IXb isoform X18 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RhoGAP super family cl02570
RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like ...
 1127-1312 2.56e-128

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.


The actual alignment was detected with superfamily member cd04407:

Pssm-ID: 470621 [Multi-domain]  Cd Length: 186  Bit Score: 396.67  E-value: 2.56e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1127 FGVCVDSLTSDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKLEDFPIHAITGVLKQWLRE 1206
Cdd:cd04407     1 FGVRVGSLTSNKTSVPIVLEKLLEHVEMHGLYTEGIYRKSGSANRMKELHQLLQADPENVKLENYPIHAITGLLKQWLRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1207 LPEPLMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRC 1286
Cdd:cd04407    81 LPEPLMTFAQYNDFLRAVELPEKQEQLQAIYRVLEQLPTANHNTLERLIFHLVKVALEEDVNRMSPNALAIVFAPCLLRC 160

                         170       180
                  ....*....|....*....|....*.
gi 568955272 1287 PDNSDPLTSMKDVLKITTCVEMLIKE 1312
Cdd:cd04407   161 PDSSDPLTSMKDVAKTTTCVEMLIKE 186
Motor_domain super family cl22853
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
 20-398 3.66e-128

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.


The actual alignment was detected with superfamily member cd01385:

Pssm-ID: 473979 [Multi-domain]  Cd Length: 690  Bit Score: 416.01  E-value: 3.66e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272   20 FPHATSHTLLAKFKQQHEDNKYFLGTPVLEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLIGMD 99
Cdd:cd01385   439 FPGATNQTLLAKFKQQHKDNKYYEKPQVMEPAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVRELIGID 518

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  100 PVAVFRWAVLRAAIRAMAVLREAGRlraeraekaaagisspatrshmeelprgastpseklyrctgldfsferseeldvn 179
Cdd:cd01385   519 PVAVFRWAVLRAFFRAMAAFREAGR------------------------------------------------------- 543

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  180 afedimafyESRKARGQSdlhnqiikslkglpwqgedprrllqslslfqkprtsflkskgikqkqiipknlldskslrli 259
Cdd:cd01385   544 ---------RRAQRTAGH-------------------------------------------------------------- 552

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  260 iSMTLHDRTTKSLLHLHKKKKPPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETV 339
Cdd:cd01385   553 -SLTLHDRTTKSLLHLHKKKKPPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTGMLETV 631

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568955272  340 RIRRSGYSAKYTFQDFTEQFQVLLPKDVQPCREAIAALLEKLQVDRQNYQIGKTKVFLK 398
Cdd:cd01385   632 RIRRSGYSVRYTFQEFITQFQVLLPKGLISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
C1_Myosin-IXb cd20884
protein kinase C conserved region 1 (C1 domain) found in unconventional myosin-IXb and similar ...
 1057-1114 1.39e-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: 1.39e-36
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568955272 1057 QEHNGHVFASYQVNIPQSCEQCLSYIWLMDKALLCSVCKMTCHKKCVHKIQSYCSYTG 1114
Cdd:cd20884     1 EEYNGHVFTSYQVNIMQSCEQCSSYIWAMEKALLCSVCKMTCHKKCLSKIQSHCSSTC 58
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
 429-458 4.39e-05

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


:

Pssm-ID: 467745 [Multi-domain]  Cd Length: 37  Bit Score: 41.76  E-value: 4.39e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 568955272  429 ERKHFVQMKHAALTIQACWRSYRVRRALER 458
Cdd:cd23767     1 EEEELQRMNRAATLIQALWRGYKVRKELKK 30
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 457-479 1.15e-04

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


:

Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 40.39  E-value: 1.15e-04
                            10        20
                    ....*....|....*....|...
gi 568955272    457 ERTQAAVYLQAAWRGYLQRQAYH 479
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRYK 23
PHA02682 super family cl31817
ORF080 virion core protein; Provisional
 1450-1544 2.16e-04

ORF080 virion core protein; Provisional


The actual alignment was detected with superfamily member PHA02682:

Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 44.85  E-value: 2.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1450 PAPALPCPISPTLSPLPEAAAPPRGRPTSFVTVRVKTPRR-TPIMPMANIKLPPGLPLHLTSWAPALQEAVVPvKRREPP 1528
Cdd:PHA02682   96 PACAPAAPAPAVTCPAPAPACPPATAPTCPPPAVCPAPARpAPACPPSTRQCPPAPPLPTPKPAPAAKPIFLH-NQLPPP 174

                          90
                  ....*....|....*.
gi 568955272 1529 ARRQDQVHSVYIAPGA 1544
Cdd:PHA02682  175 DYPAASCPTIETAPAA 190
SepH super family cl48966
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ...
 1353-1494 9.08e-03

septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments.


The actual alignment was detected with superfamily member NF040712:

Pssm-ID: 468676 [Multi-domain]  Cd Length: 346  Bit Score: 40.14  E-value: 9.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1353 FSSPYEGVRIKSPRTPVVQDLELGALPEEAAGGDEDREKEI---LMERIQSIKEEKEDITYRLPELDPRGSDEENLDSET 1429
Cdd:NF040712  192 FGRPLRPLATVPRLAREPADARPEEVEPAPAAEGAPATDSDpaeAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAEPD 271

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568955272 1430 SASTESLLEERGVRGAVEGPPAPALPCPISPTLSPLPEAAAPPRGRPTsfVTVRVKTPRRTPIMP 1494
Cdd:NF040712  272 EATRDAGEPPAPGAAETPEAAEPPAPAPAAPAAPAAPEAEEPARPEPP--PAPKPKRRRRRASVP 334
 
Name Accession Description Interval E-value
RhoGAP_myosin_IXB cd04407
RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 1127-1312 2.56e-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: 396.67  E-value: 2.56e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1127 FGVCVDSLTSDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKLEDFPIHAITGVLKQWLRE 1206
Cdd:cd04407     1 FGVRVGSLTSNKTSVPIVLEKLLEHVEMHGLYTEGIYRKSGSANRMKELHQLLQADPENVKLENYPIHAITGLLKQWLRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1207 LPEPLMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRC 1286
Cdd:cd04407    81 LPEPLMTFAQYNDFLRAVELPEKQEQLQAIYRVLEQLPTANHNTLERLIFHLVKVALEEDVNRMSPNALAIVFAPCLLRC 160

                         170       180
                  ....*....|....*....|....*.
gi 568955272 1287 PDNSDPLTSMKDVLKITTCVEMLIKE 1312
Cdd:cd04407   161 PDSSDPLTSMKDVAKTTTCVEMLIKE 186
MYSc_Myo9 cd01385
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ...
 20-398 3.66e-128

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: 416.01  E-value: 3.66e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272   20 FPHATSHTLLAKFKQQHEDNKYFLGTPVLEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLIGMD 99
Cdd:cd01385   439 FPGATNQTLLAKFKQQHKDNKYYEKPQVMEPAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVRELIGID 518

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  100 PVAVFRWAVLRAAIRAMAVLREAGRlraeraekaaagisspatrshmeelprgastpseklyrctgldfsferseeldvn 179
Cdd:cd01385   519 PVAVFRWAVLRAFFRAMAAFREAGR------------------------------------------------------- 543

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  180 afedimafyESRKARGQSdlhnqiikslkglpwqgedprrllqslslfqkprtsflkskgikqkqiipknlldskslrli 259
Cdd:cd01385   544 ---------RRAQRTAGH-------------------------------------------------------------- 552

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  260 iSMTLHDRTTKSLLHLHKKKKPPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETV 339
Cdd:cd01385   553 -SLTLHDRTTKSLLHLHKKKKPPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTGMLETV 631

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568955272  340 RIRRSGYSAKYTFQDFTEQFQVLLPKDVQPCREAIAALLEKLQVDRQNYQIGKTKVFLK 398
Cdd:cd01385   632 RIRRSGYSVRYTFQEFITQFQVLLPKGLISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
 1140-1313 1.42e-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: 199.41  E-value: 1.42e-58
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272   1140 SVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVK-LEDFPIHAITGVLKQWLRELPEPLMTFAQYG 1218
Cdd:smart00324    2 PIPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDPDLdLSEYDVHDVAGLLKLFLRELPEPLITYELYE 81

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272   1219 DFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRCPDNSDPltSMKD 1298
Cdd:smart00324   82 EFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGEVA--SLKD 159

                           170
                    ....*....|....*
gi 568955272   1299 VLKITTCVEMLIKEQ 1313
Cdd:smart00324  160 IRHQNTVIEFLIENA 174
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
 1142-1288 3.30e-56

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 191.60  E-value: 3.30e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  1142 PIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPA-AVKLEDFPIHAITGVLKQWLRELPEPLMTFAQYGDF 1220
Cdd:pfam00620    1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGPDvDLDLEEEDVHVVASLLKLFLRELPEPLLTFELYEEF 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568955272  1221 LRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRCPD 1288
Cdd:pfam00620   81 IEAAKLPDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLLRPPD 148
MYSc smart00242
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...
 20-407 8.54e-54

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: 201.23  E-value: 8.54e-54
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272     20 FPHATSHTLLAKFKQQHEDNKYFLGTPVL-EPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLigm 98
Cdd:smart00242  454 FPKGTDQTFLEKLNQHHKKHPHFSKPKKKgRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASL--- 530

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272     99 dpvavfrwavlraairamavlreagrlraeraekaaagisspatrshmeelprgastpseklyrctgldfsferseeldv 178
Cdd:smart00242      --------------------------------------------------------------------------------

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272    179 naFEDimafYESRKargqsdlhnqiikslkglpwqgedprrllqslslfqkprtsflkskgikqkqiipknlldskslrl 258
Cdd:smart00242  531 --FPS----GVSNA------------------------------------------------------------------ 538

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272    259 iismtlhdrttksllhlHKKKKPPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLET 338
Cdd:smart00242  539 -----------------GSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLEN 601

                           330       340       350       360       370       380       390
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568955272    339 VRIRRSGYSAKYTFQDFTEQFQVLLPKDVQPC----REAIAALLEKLQVDRQNYQIGKTKVFLKETERQTLQE 407
Cdd:smart00242  602 IRIRRAGFPYRLPFDEFLQRYRVLLPDTWPPWggdaKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEE 674
C1_Myosin-IXb cd20884
protein kinase C conserved region 1 (C1 domain) found in unconventional myosin-IXb and similar ...
 1057-1114 1.39e-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: 1.39e-36
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568955272 1057 QEHNGHVFASYQVNIPQSCEQCLSYIWLMDKALLCSVCKMTCHKKCVHKIQSYCSYTG 1114
Cdd:cd20884     1 EEYNGHVFTSYQVNIMQSCEQCSSYIWAMEKALLCSVCKMTCHKKCLSKIQSHCSSTC 58
COG5022 COG5022
Myosin heavy chain [General function prediction only];
277-500 1.05e-35

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 148.69  E-value: 1.05e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  277 KKKKPPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFT 356
Cdd:COG5022   600 SKGRFPTLGSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFV 679

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  357 EQFQVLLP--------KDVQPCREAIAALLEKLQVDRQNYQIGKTKVFLKeTERQTLQEKLHGEVLRRIL-QLQSWFRMV 427
Cdd:COG5022   680 QRYRILSPskswtgeyTWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFK-AGVLAALEDMRDAKLDNIAtRIQRAIRGR 758

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568955272  428 LERKHFVQMKHAALTIQACWRSYRVRRALER---TQAAVYLQAAWRGYLQRQAYHHQRHSIIRLQSLCRGHLQRRS 500
Cdd:COG5022   759 YLRRRYLQALKRIKKIQVIQHGFRLRRLVDYelkWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIKREKKLRE 834
Myosin_head pfam00063
Myosin head (motor domain);
277-398 6.08e-32

Myosin head (motor domain);


Pssm-ID: 395017 [Multi-domain]  Cd Length: 674  Bit Score: 134.33  E-value: 6.08e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272   277 KKKKPPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFT 356
Cdd:pfam00063  549 KKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFV 628

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 568955272   357 EQFQVL----LPKDVQPCREAIAALLEKLQVDRQNYQIGKTKVFLK 398
Cdd:pfam00063  629 QRYRILapktWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
PTZ00014 PTZ00014
myosin-A; Provisional
 284-473 3.24e-21

myosin-A; Provisional


Pssm-ID: 240229 [Multi-domain]  Cd Length: 821  Bit Score: 100.87  E-value: 3.24e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  284 ISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL- 362
Cdd:PTZ00014  640 IGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLd 719

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  363 LP----KDVQPcREAIAALLEKLQVDRQNYQIGKTKVFLKETERQTLQEKLHgevlrriLQLQSWfrmvlerKHFVQMkh 438
Cdd:PTZ00014  720 LAvsndSSLDP-KEKAEKLLERSGLPKDSYAIGKTMVFLKKDAAKELTQIQR-------EKLAAW-------EPLVSV-- 782

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 568955272  439 aaltIQACWRSYRVRRAL-ERTQAAVYLQAAWRGYL 473
Cdd:PTZ00014  783 ----LEALILKIKKKRKVrKNIKSLVRIQAHLRRHL 814
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
 1062-1110 1.54e-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: 1.54e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 568955272   1062 HVFASYQVNIPQSCEQCLSYIWLMDK-ALLCSVCKMTCHKKCVHKIQSYC 1110
Cdd:smart00109    1 HKHVFRTFTKPTFCCVCRKSIWGSFKqGLRCSECKVKCHKKCADKVPKAC 50
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
 1062-1110 1.71e-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: 1.71e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 568955272  1062 HVFASYQVNIPQSCEQCLSYIWLMDK-ALLCSVCKMTCHKKCVHKIQSYC 1110
Cdd:pfam00130    1 HHFVHRNFKQPTFCDHCGEFLWGLGKqGLKCSWCKLNVHKRCHEKVPPEC 50
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
 429-458 4.39e-05

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


Pssm-ID: 467745 [Multi-domain]  Cd Length: 37  Bit Score: 41.76  E-value: 4.39e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 568955272  429 ERKHFVQMKHAALTIQACWRSYRVRRALER 458
Cdd:cd23767     1 EEEELQRMNRAATLIQALWRGYKVRKELKK 30
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 457-479 1.15e-04

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


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 40.39  E-value: 1.15e-04
                            10        20
                    ....*....|....*....|...
gi 568955272    457 ERTQAAVYLQAAWRGYLQRQAYH 479
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRYK 23
PHA02682 PHA02682
ORF080 virion core protein; Provisional
 1450-1544 2.16e-04

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 44.85  E-value: 2.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1450 PAPALPCPISPTLSPLPEAAAPPRGRPTSFVTVRVKTPRR-TPIMPMANIKLPPGLPLHLTSWAPALQEAVVPvKRREPP 1528
Cdd:PHA02682   96 PACAPAAPAPAVTCPAPAPACPPATAPTCPPPAVCPAPARpAPACPPSTRQCPPAPPLPTPKPAPAAKPIFLH-NQLPPP 174

                          90
                  ....*....|....*.
gi 568955272 1529 ARRQDQVHSVYIAPGA 1544
Cdd:PHA02682  175 DYPAASCPTIETAPAA 190
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
 459-479 1.84e-03

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 459869  Cd Length: 21  Bit Score: 36.91  E-value: 1.84e-03
                           10        20
                   ....*....|....*....|.
gi 568955272   459 TQAAVYLQAAWRGYLQRQAYH 479
Cdd:pfam00612    1 RKAAIKIQAAWRGYLARKRYK 21
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 435-456 5.38e-03

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


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 35.76  E-value: 5.38e-03
                            10        20
                    ....*....|....*....|..
gi 568955272    435 QMKHAALTIQACWRSYRVRRAL 456
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRY 22
SepH NF040712
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ...
 1353-1494 9.08e-03

septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments.


Pssm-ID: 468676 [Multi-domain]  Cd Length: 346  Bit Score: 40.14  E-value: 9.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1353 FSSPYEGVRIKSPRTPVVQDLELGALPEEAAGGDEDREKEI---LMERIQSIKEEKEDITYRLPELDPRGSDEENLDSET 1429
Cdd:NF040712  192 FGRPLRPLATVPRLAREPADARPEEVEPAPAAEGAPATDSDpaeAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAEPD 271

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568955272 1430 SASTESLLEERGVRGAVEGPPAPALPCPISPTLSPLPEAAAPPRGRPTsfVTVRVKTPRRTPIMP 1494
Cdd:NF040712  272 EATRDAGEPPAPGAAETPEAAEPPAPAPAAPAAPAAPEAEEPARPEPP--PAPKPKRRRRRASVP 334
 
Name Accession Description Interval E-value
RhoGAP_myosin_IXB cd04407
RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 1127-1312 2.56e-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: 396.67  E-value: 2.56e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1127 FGVCVDSLTSDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKLEDFPIHAITGVLKQWLRE 1206
Cdd:cd04407     1 FGVRVGSLTSNKTSVPIVLEKLLEHVEMHGLYTEGIYRKSGSANRMKELHQLLQADPENVKLENYPIHAITGLLKQWLRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1207 LPEPLMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRC 1286
Cdd:cd04407    81 LPEPLMTFAQYNDFLRAVELPEKQEQLQAIYRVLEQLPTANHNTLERLIFHLVKVALEEDVNRMSPNALAIVFAPCLLRC 160

                         170       180
                  ....*....|....*....|....*.
gi 568955272 1287 PDNSDPLTSMKDVLKITTCVEMLIKE 1312
Cdd:cd04407   161 PDSSDPLTSMKDVAKTTTCVEMLIKE 186
MYSc_Myo9 cd01385
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ...
 20-398 3.66e-128

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: 416.01  E-value: 3.66e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272   20 FPHATSHTLLAKFKQQHEDNKYFLGTPVLEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLIGMD 99
Cdd:cd01385   439 FPGATNQTLLAKFKQQHKDNKYYEKPQVMEPAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVRELIGID 518

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  100 PVAVFRWAVLRAAIRAMAVLREAGRlraeraekaaagisspatrshmeelprgastpseklyrctgldfsferseeldvn 179
Cdd:cd01385   519 PVAVFRWAVLRAFFRAMAAFREAGR------------------------------------------------------- 543

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  180 afedimafyESRKARGQSdlhnqiikslkglpwqgedprrllqslslfqkprtsflkskgikqkqiipknlldskslrli 259
Cdd:cd01385   544 ---------RRAQRTAGH-------------------------------------------------------------- 552

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  260 iSMTLHDRTTKSLLHLHKKKKPPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETV 339
Cdd:cd01385   553 -SLTLHDRTTKSLLHLHKKKKPPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTGMLETV 631

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568955272  340 RIRRSGYSAKYTFQDFTEQFQVLLPKDVQPCREAIAALLEKLQVDRQNYQIGKTKVFLK 398
Cdd:cd01385   632 RIRRSGYSVRYTFQEFITQFQVLLPKGLISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
RhoGAP_myosin_IX cd04377
RhoGAP_myosin_IX: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 1127-1312 1.08e-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: 353.67  E-value: 1.08e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1127 FGVCVDSLTSDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKLEDFPIHAITGVLKQWLRE 1206
Cdd:cd04377     1 FGVSLSSLTSEDRSVPLVLEKLLEHIEMHGLYTEGIYRKSGSANKIKELRQGLDTDPDSVNLEDYPIHVITSVLKQWLRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1207 LPEPLMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRC 1286
Cdd:cd04377    81 LPEPLMTFELYENFLRAMELEEKQERVRALYSVLEQLPRANLNTLERLIFHLVRVALQEEVNRMSANALAIVFAPCILRC 160

                         170       180
                  ....*....|....*....|....*.
gi 568955272 1287 PDNSDPLTSMKDVLKITTCVEMLIKE 1312
Cdd:cd04377   161 PDTADPLQSLQDVSKTTTCVETLIKE 186
RhoGAP_myosin_IXA cd04406
RhoGAP_myosin_IXA: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 1127-1312 5.62e-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: 5.62e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1127 FGVCVDSLTSDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKLEDFPIHAITGVLKQWLRE 1206
Cdd:cd04406     1 FGVELSRLTSEDRSVPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDANSVNLDDYNIHVIASVFKQWLRD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1207 LPEPLMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRC 1286
Cdd:cd04406    81 LPNPLMTFELYEEFLRAMGLQERRETVRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEETNRMSANALAIVFAPCILRC 160

                         170       180
                  ....*....|....*....|....*.
gi 568955272 1287 PDNSDPLTSMKDVLKITTCVEMLIKE 1312
Cdd:cd04406   161 PDTTDPLQSVQDISKTTTCVELIVCE 186
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
 1140-1313 1.42e-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: 199.41  E-value: 1.42e-58
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272   1140 SVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVK-LEDFPIHAITGVLKQWLRELPEPLMTFAQYG 1218
Cdd:smart00324    2 PIPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDPDLdLSEYDVHDVAGLLKLFLRELPEPLITYELYE 81

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272   1219 DFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRCPDNSDPltSMKD 1298
Cdd:smart00324   82 EFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGEVA--SLKD 159

                           170
                    ....*....|....*
gi 568955272   1299 VLKITTCVEMLIKEQ 1313
Cdd:smart00324  160 IRHQNTVIEFLIENA 174
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
 1142-1288 3.30e-56

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 191.60  E-value: 3.30e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  1142 PIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPA-AVKLEDFPIHAITGVLKQWLRELPEPLMTFAQYGDF 1220
Cdd:pfam00620    1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGPDvDLDLEEEDVHVVASLLKLFLRELPEPLLTFELYEEF 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568955272  1221 LRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRCPD 1288
Cdd:pfam00620   81 IEAAKLPDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLLRPPD 148
RhoGAP cd00159
RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like ...
 1142-1312 3.75e-54

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 [Multi-domain]  Cd Length: 169  Bit Score: 186.74  E-value: 3.75e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1142 PIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKLEDFPIHAITGVLKQWLRELPEPLMTFAQYGDFL 1221
Cdd:cd00159     1 PLIIEKCIEYLEKNGLNTEGIFRVSGSASKIEELKKKFDRGEDIDDLEDYDVHDVASLLKLYLRELPEPLIPFELYDEFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1222 RAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRCPDNSDplTSMKDVLK 1301
Cdd:cd00159    81 ELAKIEDEEERIEALKELLKSLPPENRDLLKYLLKLLHKISQNSEVNKMTASNLAIVFAPTLLRPPDSDD--ELLEDIKK 158

                         170
                  ....*....|.
gi 568955272 1302 ITTCVEMLIKE 1312
Cdd:cd00159   159 LNEIVEFLIEN 169
MYSc smart00242
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...
 20-407 8.54e-54

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: 201.23  E-value: 8.54e-54
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272     20 FPHATSHTLLAKFKQQHEDNKYFLGTPVL-EPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLigm 98
Cdd:smart00242  454 FPKGTDQTFLEKLNQHHKKHPHFSKPKKKgRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASL--- 530

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272     99 dpvavfrwavlraairamavlreagrlraeraekaaagisspatrshmeelprgastpseklyrctgldfsferseeldv 178
Cdd:smart00242      --------------------------------------------------------------------------------

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272    179 naFEDimafYESRKargqsdlhnqiikslkglpwqgedprrllqslslfqkprtsflkskgikqkqiipknlldskslrl 258
Cdd:smart00242  531 --FPS----GVSNA------------------------------------------------------------------ 538

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272    259 iismtlhdrttksllhlHKKKKPPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLET 338
Cdd:smart00242  539 -----------------GSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLEN 601

                           330       340       350       360       370       380       390
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568955272    339 VRIRRSGYSAKYTFQDFTEQFQVLLPKDVQPC----REAIAALLEKLQVDRQNYQIGKTKVFLKETERQTLQE 407
Cdd:smart00242  602 IRIRRAGFPYRLPFDEFLQRYRVLLPDTWPPWggdaKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEE 674
MYSc cd00124
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ...
 285-398 1.09e-39

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


Pssm-ID: 276950 [Multi-domain]  Cd Length: 633  Bit Score: 157.75  E-value: 1.09e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  285 SAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLP 364
Cdd:cd00124   516 GSQFRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAP 595

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 568955272  365 KDVQPCR----EAIAALLEKLQVDRQNYQIGKTKVFLK 398
Cdd:cd00124   596 GATEKASdskkAAVLALLLLLKLDSSGYQLGKTKVFLR 633
MYSc_Myo7 cd01381
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ...
 248-398 6.07e-39

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: 155.87  E-value: 6.07e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  248 KNLLDSKSLRLIISMTLHDRTTKSllhlHKKKKPPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVL 327
Cdd:cd01381   498 LQLVQSSKNKFLKQLFNEDISMGS----ETRKKSPTLSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCV 573

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568955272  328 QQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPkDVQP-----CREAIAALLEKLQVDRQNYQIGKTKVFLK 398
Cdd:cd01381   574 RQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVP-GIPPahktdCRAATRKICCAVLGGDADYQLGKTKIFLK 648
RhoGAP_ARAP cd04385
RhoGAP_ARAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
 1134-1284 1.31e-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: 142.83  E-value: 1.31e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1134 LTSDkaSVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKL---EDFPiHAITGVLKQWLRELPEP 1210
Cdd:cd04385    10 LTDN--DIPVIVDKCIDFITQHGLMSEGIYRKNGKNSSVKKLLEAFRKDARSVQLregEYTV-HDVADVLKRFLRDLPDP 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568955272 1211 LMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLL 1284
Cdd:cd04385    87 LLTSELHAEWIEAAELENKDERIARYKELIRRLPPINRATLKVLIGHLYRVQKHSDENQMSVHNLALVFGPTLF 160
C1_Myosin-IXb cd20884
protein kinase C conserved region 1 (C1 domain) found in unconventional myosin-IXb and similar ...
 1057-1114 1.39e-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: 1.39e-36
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568955272 1057 QEHNGHVFASYQVNIPQSCEQCLSYIWLMDKALLCSVCKMTCHKKCVHKIQSYCSYTG 1114
Cdd:cd20884     1 EEYNGHVFTSYQVNIMQSCEQCSSYIWAMEKALLCSVCKMTCHKKCLSKIQSHCSSTC 58
COG5022 COG5022
Myosin heavy chain [General function prediction only];
277-500 1.05e-35

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 148.69  E-value: 1.05e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  277 KKKKPPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFT 356
Cdd:COG5022   600 SKGRFPTLGSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFV 679

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  357 EQFQVLLP--------KDVQPCREAIAALLEKLQVDRQNYQIGKTKVFLKeTERQTLQEKLHGEVLRRIL-QLQSWFRMV 427
Cdd:COG5022   680 QRYRILSPskswtgeyTWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFK-AGVLAALEDMRDAKLDNIAtRIQRAIRGR 758

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568955272  428 LERKHFVQMKHAALTIQACWRSYRVRRALER---TQAAVYLQAAWRGYLQRQAYHHQRHSIIRLQSLCRGHLQRRS 500
Cdd:COG5022   759 YLRRRYLQALKRIKKIQVIQHGFRLRRLVDYelkWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIKREKKLRE 834
RhoGAP_nadrin cd04386
RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1127-1312 1.46e-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: 134.89  E-value: 1.46e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1127 FGVCV-DSLTSDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKLEDF---PiHAITGVLKQ 1202
Cdd:cd04386     5 FGTPLeEHLKRTGREIALPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKAALDAGTFSLPLDEFysdP-HAVASALKS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1203 WLRELPEPLMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPC 1282
Cdd:cd04386    84 YLRELPDPLLTYNLYEDWVQAANKPDEDERLQAIWRILNKLPRENRDNLRYLIKFLSKLAQKSDENKMSPSNIAIVLAPN 163

                         170       180       190
                  ....*....|....*....|....*....|.
gi 568955272 1283 LLRCP-DNSDPLTSMKDVLKITTCVEMLIKE 1312
Cdd:cd04386   164 LLWAKnEGSLAEMAAGTSVHVVAIVELIISH 194
RhoGAP_fRGD1 cd04398
RhoGAP_fRGD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1127-1296 1.80e-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: 1.80e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1127 FGVCVDSLTS-DKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKL---EDF--PIHAITGVL 1200
Cdd:cd04398     1 FGVPLEDLILrEGDNVPNIVYQCIQAIENFGLNLEGIYRLSGNVSRVNKLKELFDKDPLNVLLispEDYesDIHSVASLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1201 KQWLRELPEPLMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFA 1280
Cdd:cd04398    81 KLFFRELPEPLLTKALSREFIEAAKIEDESRRRDALHGLINDLPDANYATLRALMFHLARIKEHESVNRMSVNNLAIIWG 160

                         170
                  ....*....|....*.
gi 568955272 1281 PCLLrcPDNSDPLTSM 1296
Cdd:cd04398   161 PTLM--NAAPDNAADM 174
MYSc_Myo10 cd14873
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ...
 249-398 1.80e-34

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: 142.24  E-value: 1.80e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  249 NLLDSKSLRLIISMTLHD--RTTKSLLHLHKKKKPPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELV 326
Cdd:cd14873   498 NLLRESRFDFIYDLFEHVssRNNQDTLKCGSKHRRPTVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVV 577

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568955272  327 LQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLP--KDVQPCREAIAALLEKLQVDRQNYQIGKTKVFLK 398
Cdd:cd14873   578 LNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRnlALPEDVRGKCTSLLQLYDASNSEWQLGKTKVFLR 651
RhoGAP_ARHGAP27_15_12_9 cd04403
RhoGAP_ARHGAP27_15_12_9: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 1127-1296 2.25e-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: 2.25e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1127 FGVCVDSLTS-DKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAA----VKLEDfpIHAITGVLK 1201
Cdd:cd04403     1 FGCHLEALCQrENSTVPKFVRLCIEAVEKRGLDVDGIYRVSGNLAVIQKLRFAVDHDEKLdlddSKWED--IHVITGALK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1202 QWLRELPEPLMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAP 1281
Cdd:cd04403    79 LFFRELPEPLFPYSLFNDFVAAIKLSDYEQRVSAVKDLIKSLPKPNHDTLKMLFRHLCRVIEHGEKNRMTTQNLAIVFGP 158

                         170
                  ....*....|....*..
gi 568955272 1282 CLLRcP--DNSDPLTSM 1296
Cdd:cd04403   159 TLLR-PeqETGNIAVHM 174
RhoGAP_chimaerin cd04372
RhoGAP_chimaerin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1134-1311 4.20e-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 [Multi-domain]  Cd Length: 194  Bit Score: 127.25  E-value: 4.20e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1134 LTSDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTD--PAAVKLEDFP-IHAITGVLKQWLRELPEP 1210
Cdd:cd04372     9 VKAHNTQRPMVVDMCIREIEARGLQSEGLYRVSGFAEEIEDVKMAFDRDgeKADISATVYPdINVITGALKLYFRDLPIP 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1211 LMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRCPDnS 1290
Cdd:cd04372    89 VITYDTYPKFIDAAKISNPDERLEAVHEALMLLPPAHYETLRYLMEHLKRVTLHEKDNKMNAENLGIVFGPTLMRPPE-D 167

                         170       180
                  ....*....|....*....|.
gi 568955272 1291 DPLTSMKDVLKITTCVEMLIK 1311
Cdd:cd04372   168 SALTTLNDMRYQILIVQLLIT 188
Myosin_head pfam00063
Myosin head (motor domain);
277-398 6.08e-32

Myosin head (motor domain);


Pssm-ID: 395017 [Multi-domain]  Cd Length: 674  Bit Score: 134.33  E-value: 6.08e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272   277 KKKKPPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFT 356
Cdd:pfam00063  549 KKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFV 628

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 568955272   357 EQFQVL----LPKDVQPCREAIAALLEKLQVDRQNYQIGKTKVFLK 398
Cdd:pfam00063  629 QRYRILapktWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
MYSc_Myo3 cd01379
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ...
 284-398 1.53e-30

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: 129.70  E-value: 1.53e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  284 ISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL- 362
Cdd:cd01379   518 VATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYYFLa 597

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 568955272  363 --LPKDVQPCREAIAALLEKLQVDrqNYQIGKTKVFLK 398
Cdd:cd01379   598 fkWNEEVVANRENCRLILERLKLD--NWALGKTKVFLK 633
RhoGAP_SYD1 cd04379
RhoGAP_SYD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
 1127-1294 1.86e-30

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: 120.26  E-value: 1.86e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1127 FGVCVDSLT---SDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKL--EDFP-IHAITGVL 1200
Cdd:cd04379     1 FGVPLSRLVereGESRDVPIVLQKCVQEIERRGLDVIGLYRLCGSAAKKKELRDAFERNSAAVELseELYPdINVITGVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1201 KQWLRELPEPLMTFAQYGDFLRA--VELP-EKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAI 1277
Cdd:cd04379    81 KDYLRELPEPLITPQLYEMVLEAlaVALPnDVQTNTHLTLSIIDCLPLSAKATLLLLLDHLSLVLSNSERNKMTPQNLAV 160

                         170
                  ....*....|....*..
gi 568955272 1278 IFAPCLLRCPDNSDPLT 1294
Cdd:cd04379   161 CFGPVLMFCSQEFSRYG 177
RhoGAP_ARHGAP20 cd04402
RhoGAP_ARHGAP20: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1127-1310 9.42e-30

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: 9.42e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1127 FGVCVDSLTSDkASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDpAAVKLEDFPIHAITGVLKQWLRE 1206
Cdd:cd04402     2 FGQPLSNICED-DNLPKPILDMLSLLYQKGPSTEGIFRRSANAKACKELKEKLNSG-VEVDLKAEPVLLLASVLKDFLRN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1207 LPEPLMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRC 1286
Cdd:cd04402    80 IPGSLLSSDLYEEWMSALDQENEEEKIAELQRLLDKLPRPNVLLLKHLICVLHNISQNSETNKMDAFNLAVCIAPSLLWP 159

                         170       180
                  ....*....|....*....|....
gi 568955272 1287 PDNSDPLtsMKDVLKITTCVEMLI 1310
Cdd:cd04402   160 PASSELQ--NEDLKKVTSLVQFLI 181
RhoGAP_ARHGAP21 cd04395
RhoGAP_ARHGAP21: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1127-1310 1.30e-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: 1.30e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1127 FGVCVDS--LTSDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKLED---FPIHAITGVLK 1201
Cdd:cd04395     2 FGVPLDDcpPSSENPYVPLIVEVCCNIVEARGLETVGIYRVPGNNAAISALQEELNRGGFDIDLQDprwRDVNVVSSLLK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1202 QWLRELPEPLMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAP 1281
Cdd:cd04395    82 SFFRKLPEPLFTNELYPDFIEANRIEDPVERLKELRRLIHSLPDHHYETLKHLIRHLKTVADNSEVNKMEPRNLAIVFGP 161

                         170       180       190
                  ....*....|....*....|....*....|.
gi 568955272 1282 CLLRCPDNS--DPLTSMKDVLKIttcVEMLI 1310
Cdd:cd04395   162 TLVRTSDDNmeTMVTHMPDQCKI---VETLI 189
MYSc_Myo22 cd14883
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ...
 277-398 1.56e-29

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: 126.67  E-value: 1.56e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  277 KKKKPPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFT 356
Cdd:cd14883   536 TSKGKPTVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFV 615

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 568955272  357 EQFQVLLPK--DVQPCREAIA--ALLEKLQVDRQNYQIGKTKVFLK 398
Cdd:cd14883   616 DRYLCLDPRarSADHKETCGAvrALMGLGGLPEDEWQVGKTKVFLR 661
RhoGAP_GMIP_PARG1 cd04378
RhoGAP_GMIP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 1140-1311 6.72e-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: 6.72e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1140 SVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKLEDFPIHAITGVLKQWLRELPEPLMTFAQYGD 1219
Cdd:cd04378    15 EVPFIIKKCTSEIENRALGVQGIYRVSGSKARVEKLCQAFENGKDLVELSELSPHDISSVLKLFLRQLPEPLILFRLYND 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1220 FL----RAVELPEKQEQL-------SAIYAV---LDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLR 1285
Cdd:cd04378    95 FIalakEIQRDTEEDKAPntpievnRIIRKLkdlLRQLPASNYNTLQHLIAHLYRVAEQFEENKMSPNNLGIVFGPTLIR 174

                         170       180
                  ....*....|....*....|....*...
gi 568955272 1286 CPDNSDP--LTSMKDVLKITTCVEMLIK 1311
Cdd:cd04378   175 PRPGDADvsLSSLVDYGYQARLVEFLIT 202
C1_Myosin-IX cd20818
protein kinase C conserved region 1 (C1 domain) found in the unconventional myosin-IX family; ...
 1059-1114 1.29e-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: 1.29e-28
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568955272 1059 HNGHVFASYQVNIPQSCEQCLSYIWLMDKALLCSVCKMTCHKKCVHKIQSYCSYTG 1114
Cdd:cd20818     1 HNGHKFATVQFNIPTYCEVCNSFIWLMEKGLVCQVCKFTCHKKCYSKITAPCKGNS 56
RhoGAP-p50rhoGAP cd04404
RhoGAP-p50rhoGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1127-1314 2.62e-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 [Multi-domain]  Cd Length: 195  Bit Score: 113.59  E-value: 2.62e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1127 FGVCVDSLTS---DKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQAL-QTDPaaVKLEDFP-IHAITGVLK 1201
Cdd:cd04404     6 FGVSLQFLKEknpEQEPIPPVVRETVEYLQAHALTTEGIFRRSANTQVVKEVQQKYnMGEP--VDFDQYEdVHLPAVILK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1202 QWLRELPEPLMTFAQYGDFLRAVELPeKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAP 1281
Cdd:cd04404    84 TFLRELPEPLLTFDLYDDIVGFLNVD-KEERVERVKQLLQTLPEENYQVLKYLIKFLVQVSAHSDQNKMTNSNLAVVFGP 162

                         170       180       190
                  ....*....|....*....|....*....|...
gi 568955272 1282 CLLRCPDNSDPLTSMKdvlKITTCVEMLIKEQM 1314
Cdd:cd04404   163 NLLWAKDASMSLSAIN---PINTFTKFLLDHQD 192
MYSc_Myo1 cd01378
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ...
 248-398 3.86e-28

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: 122.27  E-value: 3.86e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  248 KNLLDSKSLRLIISMTLHDRTTKSllhlhkKKKPPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVL 327
Cdd:cd01378   504 KELMQSSSNPFLRSLFPEGVDLDS------KKRPPTAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVL 577

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568955272  328 QQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPK-------DVQpcrEAIAALLEKLQVDRQNYQIGKTKVFLK 398
Cdd:cd01378   578 HQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPKtwpawdgTWQ---GGVESILKDLNIPPEEYQMGKTKIFIR 652
MYSc_Myo15 cd01387
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ...
 250-398 4.67e-28

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: 122.17  E-value: 4.67e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  250 LLDSKSLRLIISMT--LHDRTTKSLLHLHK------KKKPPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCF 321
Cdd:cd01387   497 LLVSSRTRVVAHLFssHRAQTDKAPPRLGKgrfvtmKPRTPTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLF 576

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  322 DDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLL------PKDVQPCREAIAALLEklQVDRQNYQIGKTKV 395
Cdd:cd01387   577 DMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLValklprPAPGDMCVSLLSRLCT--VTPKDMYRLGATKV 654


                  ...
gi 568955272  396 FLK 398
Cdd:cd01387   655 FLR 657
MYSc_Myo8 cd01383
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ...
 260-398 5.42e-28

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: 121.65  E-value: 5.42e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  260 ISMTLHDRTTKSLLHLHKKKKPP-SISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLET 338
Cdd:cd01383   505 SKMLDASRKALPLTKASGSDSQKqSVATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEV 584

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568955272  339 VRIRRSGYSAKYTFQDFTEQFQVLLPKDVQPCREAIA---ALLEKLQVDRQNYQIGKTKVFLK 398
Cdd:cd01383   585 VRISRSGYPTRMTHQEFARRYGFLLPEDVSASQDPLStsvAILQQFNILPEMYQVGYTKLFFR 647
RhoGAP_MgcRacGAP cd04382
RhoGAP_MgcRacGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 1128-1299 2.68e-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: 110.46  E-value: 2.68e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1128 GVCVDSLTSDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKLEDFPIHAITGVLKQWLREL 1207
Cdd:cd04382     4 GELADFDPSTSPMIPALIVHCVNEIEARGLTEEGLYRVSGSEREVKALKEKFLRGKTVPNLSKVDIHVICGCLKDFLRSL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1208 PEPLMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDvNRMSPGALAIIFAPCLLRCP 1287
Cdd:cd04382    84 KEPLITFALWKEFMEAAEILDEDNSRAALYQAISELPQPNRDTLAFLILHLQRVAQSPE-CKMDINNLARVFGPTIVGYS 162

                         170
                  ....*....|...
gi 568955272 1288 D-NSDPLTSMKDV 1299
Cdd:cd04382   163 VpNPDPMTILQDT 175
MYSc_Myo5 cd01380
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ...
 278-398 3.76e-27

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: 119.18  E-value: 3.76e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  278 KKKPPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTE 357
Cdd:cd01380   506 KNRKKTVGSQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFS 585

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 568955272  358 QFQVLLPKDV---QPCREAIAALLEKLQVDRQNYQIGKTKVFLK 398
Cdd:cd01380   586 RYRVLLPSKEwlrDDKKKTCENILENLILDPDKYQFGKTKIFFR 629
RhoGAP_GMIP cd04408
RhoGAP_GMIP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP ...
 1127-1310 5.65e-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: 109.91  E-value: 5.65e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1127 FGVCVDSLTSD-KASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKLEDFPIHAITGVLKQWLR 1205
Cdd:cd04408     1 FGVDFSQLPRDfPEEVPFVVVRCTAEIENRALGVQGIYRISGSKARVEKLCQAFENGRDLVDLSGHSPHDITSVLKHFLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1206 ELPEPLMTFAQYGDFL-----------RAVELPE-KQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPG 1273
Cdd:cd04408    81 ELPEPVLPFQLYDDFIalakelqrdseKAAESPSiVENIIRSLKELLGRLPVSNYNTLRHLMAHLYRVAERFEDNKMSPN 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 568955272 1274 ALAIIFAPCLLRCPDNSD-PLTSMKDVLKITTCVEMLI 1310
Cdd:cd04408   161 NLGIVFGPTLLRPLVGGDvSMICLLDTGYQAQLVEFLI 198
RhoGAP_Graf cd04374
RhoGAP_Graf: GTPase-activator protein (GAP) domain for Rho-like GTPases found in GRAF (GTPase ...
 1137-1310 1.14e-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: 109.02  E-value: 1.14e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1137 DKASVPIVlEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQAL----QTDPAAVKLE--DFPIHAITGVLKQWLRELPEP 1210
Cdd:cd04374    25 DDIGFKFV-RKCIEAVETRGINEQGLYRVVGVNSKVQKLLSLGldpkTSTPGDVDLDnsEWEIKTITSALKTYLRNLPEP 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1211 LMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRCPDNS 1290
Cdd:cd04374   104 LMTYELHNDFINAAKSENLESRVNAIHSLVHKLPEKNREMLELLIKHLTNVSDHSKKNLMTVSNLGVVFGPTLLRPQEET 183

                         170       180
                  ....*....|....*....|
gi 568955272 1291 dpLTSMKDVLKITTCVEMLI 1310
Cdd:cd04374   184 --VAAIMDIKFQNIVVEILI 201
RhoGAP_p190 cd04373
RhoGAP_p190: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1127-1310 1.89e-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: 1.89e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1127 FGVCVDSLTSDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTREL-RQALQTDPAAVKLEDFPIHAITGVLKQWLR 1205
Cdd:cd04373     1 FGVPLANVVTSEKPIPIFLEKCVEFIEATGLETEGIYRVSGNKTHLDSLqKQFDQDHNLDLVSKDFTVNAVAGALKSFFS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1206 ELPEPLMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLR 1285
Cdd:cd04373    81 ELPDPLIPYSMHLELVEAAKINDREQRLHALKELLKKFPPENFDVFKYVITHLNKVSQNSKVNLMTSENLSICFWPTLMR 160

                         170       180
                  ....*....|....*....|....*..
gi 568955272 1286 cPD--NSDPLTSMKDVlkiTTCVEMLI 1310
Cdd:cd04373   161 -PDftSMEALSATRIY---QTIIETFI 183
RhoGAP_Bcr cd04387
RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr ...
 1127-1298 3.35e-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: 107.71  E-value: 3.35e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1127 FGVCVDSLTSDKAS-VPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTD--PAAVKLEDFPIHAITGVLKQW 1203
Cdd:cd04387     1 FGVKISTVTKRERSkVPYIVRQCVEEVERRGMEEVGIYRISGVATDIQALKAAFDTNnkDVSVMLSEMDVNAIAGTLKLY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1204 LRELPEPLMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCL 1283
Cdd:cd04387    81 FRELPEPLFTDELYPNFAEGIALSDPVAKESCMLNLLLSLPDPNLVTFLFLLHHLKRVAEREEVNKMSLHNLATVFGPTL 160

                         170
                  ....*....|....*..
gi 568955272 1284 LRCP--DNSDPLTSMKD 1298
Cdd:cd04387   161 LRPSekESKIPTNTMTD 177
MYSc_Myo29 cd14890
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ...
 283-398 3.92e-25

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: 112.95  E-value: 3.92e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  283 SISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL 362
Cdd:cd14890   548 SVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQIRQQGFALREEHDSFFYDFQVL 627

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 568955272  363 LPkDVQPCREAIAALLEKLQVDRQNYQIGKTKVFLK 398
Cdd:cd14890   628 LP-TAENIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662
MYSc_Myo11 cd01384
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ...
 277-398 5.89e-25

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: 112.38  E-value: 5.89e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  277 KKKKPPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFT 356
Cdd:cd01384   525 SSSKFSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFL 604

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 568955272  357 EQFQVLLP---KDVQPCREAIAALLEKLQVdrQNYQIGKTKVFLK 398
Cdd:cd01384   605 DRFGLLAPevlKGSDDEKAACKKILEKAGL--KGYQIGKTKVFLR 647
RhoGAP_CdGAP cd04384
RhoGAP_CdGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1141-1287 1.73e-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: 1.73e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1141 VPIVLEKLLEHVEMHGLYTeGLYRKSGAANRTRELRQALQTDpAAVKLEDFP----IHAITGVLKQWLRELPEPLMTFAQ 1216
Cdd:cd04384    18 VPQVLKSCTEFIEKHGIVD-GIYRLSGIASNIQRLRHEFDSE-QIPDLTKDVyiqdIHSVSSLCKLYFRELPNPLLTYQL 95

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568955272 1217 YGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRCP 1287
Cdd:cd04384    96 YEKFSEAVSAASDEERLEKIHDVIQQLPPPHYRTLEFLMRHLSRLAKYCSITNMHAKNLAIVWAPNLLRSK 166
RhoGAP_ARHGAP18 cd04391
RhoGAP_ARHGAP18: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1127-1313 3.38e-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: 3.38e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1127 FGVCVDSL------TSDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTD--PAAVKLEDFPIHAITG 1198
Cdd:cd04391     2 FGVPLSTLlerdqkKVPGSKVPLIFQKLINKLEERGLETEGILRIPGSAQRVKFLCQELEAKfyEGTFLWDQVKQHDAAS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1199 VLKQWLRELPEPLMTfAQYGDFLRAVE-LPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAI 1277
Cdd:cd04391    82 LLKLFIRELPQPLLT-VEYLPAFYSVQgLPSKKDQLQALNLLVLLLPEANRDTLKALLEFLQKVVDHEEKNKMNLWNVAM 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 568955272 1278 IFAPCLLRC--PDNSDPLTSMKDVLKITTC---VEMLIKEQ 1313
Cdd:cd04391   161 IMAPNLFPPrgKHSKDNESLQEEVNMAAGCaniMRLLIRYQ 201
RhoGAP-ARHGAP11A cd04394
RhoGAP-ARHGAP11A: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1127-1310 2.13e-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: 2.13e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1127 FGVCVDSLT----SDKASVPIVLEKLLEHVEMHgLYTEGLYRKSGAANRTRELRqaLQTDPAAVKLEDFPIHAITGVLKQ 1202
Cdd:cd04394     2 FGVPLHSLPhstvPEYGNVPKFLVDACTFLLDH-LSTEGLFRKSGSVVRQKELK--AKLEGGEACLSSALPCDVAGLLKQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1203 WLRELPEPLMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPC 1282
Cdd:cd04394    79 FFRELPEPLLPYDLHEALLKAQELPTDEERKSATLLLTCLLPDEHVNTLRYFFSFLYDVAQRCSENKMDSSNLAVIFAPN 158

                         170       180       190
                  ....*....|....*....|....*....|
gi 568955272 1283 LLRCPDNSDPLTS--MKDVLKITTCVEMLI 1310
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 ...
 1141-1312 2.49e-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: 2.49e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1141 VPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKLEDFPIHAITGVLKQWLRELPEPLMTFAQYGDF 1220
Cdd:cd04390    22 VPILVEQCVDFIREHGLKEEGLFRLPGQANLVKQLQDAFDAGERPSFDSDTDVHTVASLLKLYLRELPEPVIPWAQYEDF 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1221 LRAVELPEKQEQ--LSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRcPDNSDPLTSMKD 1298
Cdd:cd04390   102 LSCAQLLSKDEEkgLGELMKQVSILPKVNYNLLSYICRFLDEVQSNSSVNKMSVQNLATVFGPNILR-PKVEDPATIMEG 180

                         170
                  ....*....|....
gi 568955272 1299 VLKITTCVEMLIKE 1312
Cdd:cd04390   181 TPQIQQLMTVMISK 194
MYSc_class_II cd01377
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ...
 277-398 2.54e-23

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: 107.16  E-value: 2.54e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  277 KKKKppsiSAQFQT-------SLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAK 349
Cdd:cd01377   534 KKKK----GGSFRTvsqlhkeQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNR 609

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568955272  350 YTFQDFTEQFQVLLPKDVQPC----REAIAALLEKLQVDRQNYQIGKTKVFLK 398
Cdd:cd01377   610 IIFAEFKQRYSILAPNAIPKGfddgKAACEKILKALQLDPELYRIGNTKVFFK 662
MYSc_Myo28 cd14889
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ...
 278-398 4.97e-23

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: 106.14  E-value: 4.97e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  278 KKKPPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTE 357
Cdd:cd14889   540 STRKQSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAE 619

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 568955272  358 QFQVLLPK-DVQPCREAIAALLEKLQVdrQNYQIGKTKVFLK 398
Cdd:cd14889   620 RYKILLCEpALPGTKQSCLRILKATKL--VGWKCGKTRLFFK 659
RhoGAP_PARG1 cd04409
RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1141-1311 3.18e-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: 96.42  E-value: 3.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1141 VPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKLEDFPIHAITGVLKQWLRELPEPLMTFAQYGDF 1220
Cdd:cd04409    16 IPFIIKKCTSEIESRALCLKGIYRVNGAKSRVEKLCQAFENGKDLVELSELSPHDISNVLKLYLRQLPEPLILFRLYNEF 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1221 L-------------RAVELPEKQEQ---------LSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAII 1278
Cdd:cd04409    96 IglakesqhvnetqEAKKNSDKKWPnmctelnriLLKSKDLLRQLPAPNYNTLQFLIVHLHRVSEQAEENKMSASNLGII 175

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 568955272 1279 FAPCLLRcPDNSDP---LTSMKDVLKITTCVEMLIK 1311
Cdd:cd04409   176 FGPTLIR-PRPTDAtvsLSSLVDYPHQARLVELLIT 210
MYSc_Myo36 cd14897
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ...
 288-398 3.58e-22

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: 103.23  E-value: 3.58e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  288 FQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPKdv 367
Cdd:cd14897   524 FKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRYKEICDF-- 601

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 568955272  368 qpCREAIAALLEKLQV-----DRQNYQIGKTKVFLK 398
Cdd:cd14897   602 --SNKVRSDDLGKCQKilktaGIKGYQFGKTKVFLK 635
MYSc_Myo31 cd14892
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ...
 285-398 7.88e-22

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: 102.15  E-value: 7.88e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  285 SAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLL- 363
Cdd:cd14892   533 SSKFRTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREGFPIRRQFEEFYEKFWPLAr 612

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 568955272  364 ----------PKDVQPCREAIAALLEKlQVDRQNYQIGKTKVFLK 398
Cdd:cd14892   613 nkagvaaspdACDATTARKKCEEIVAR-ALERENFQLGRTKVFLR 656
RhoGAP_ARHGAP6 cd04376
RhoGAP_ARHGAP6: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1140-1310 1.19e-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: 1.19e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1140 SVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKLEDFPIHAITGVLKQWLRELPEPLMTFAQYGD 1219
Cdd:cd04376     8 QVPRLVESCCQHLEKHGLQTVGIFRVGSSKKRVRQLREEFDRGIDVVLDENHSVHDVAALLKEFFRDMPDPLLPRELYTA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1220 FLRAVELpEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVAL-LEDV----------NRMSPGALAIIFAPCLLRCPD 1288
Cdd:cd04376    88 FIGTALL-EPDEQLEALQLLIYLLPPCNCDTLHRLLKFLHTVAEhAADSidedgqevsgNKMTSLNLATIFGPNLLHKQK 166

                         170       180
                  ....*....|....*....|....*..
gi 568955272 1289 NSDPLTS-----MKDVLKITTCVEMLI 1310
Cdd:cd04376   167 SGEREFVqaslrIEESTAIINVVQTMI 193
MYSc_Myo4 cd14872
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ...
 241-395 1.96e-21

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: 101.01  E-value: 1.96e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  241 KQKQIIPKNLLD---SKSLRLIISMtlhdrttKSLLHLHKKKKPPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKK 317
Cdd:cd14872   487 KNKDTLQKDLYVllsSSKNKLIAVL-------FPPSEGDQKTSKVTLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKR 559

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  318 ELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLL-------PKDVqpcREAIAALLEKLQVDRQNYQI 390
Cdd:cd14872   560 ARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFLVktiakrvGPDD---RQRCDLLLKSLKQDFSKVQV 636


                  ....*
gi 568955272  391 GKTKV 395
Cdd:cd14872   637 GKTRV 641
RhoGAP_FAM13A1a cd04393
RhoGAP_FAM13A1a: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1127-1303 2.05e-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: 93.68  E-value: 2.05e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1127 FGVCVDSLTSD---KASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKLEDFPIHAITGVLKQW 1203
Cdd:cd04393     3 FGVPLQELQQAgqpENGVPAVVRHIVEYLEQHGLEQEGLFRVNGNAETVEWLRQRLDSGEEVDLSKEADVCSAASLLRLF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1204 LRELPEPLMTFAQYGDFLRAV-ELPEKQEQLSAIYAVLDHLPEANHtSLERLIFH-LVKVALLEDVNRMSPGALAIIFAP 1281
Cdd:cd04393    83 LQELPEGLIPASLQIRLMQLYqDYNGEDEFGRKLRDLLQQLPPVNY-SLLKFLCHfLSNVASQHHENRMTAENLAAVFGP 161

                         170       180
                  ....*....|....*....|..
gi 568955272 1282 CLLRCPDNSDPLTSMKDVLKIT 1303
Cdd:cd04393   162 DVFHVYTDVEDMKEQEICSRIM 183
PTZ00014 PTZ00014
myosin-A; Provisional
 284-473 3.24e-21

myosin-A; Provisional


Pssm-ID: 240229 [Multi-domain]  Cd Length: 821  Bit Score: 100.87  E-value: 3.24e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  284 ISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL- 362
Cdd:PTZ00014  640 IGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLd 719

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  363 LP----KDVQPcREAIAALLEKLQVDRQNYQIGKTKVFLKETERQTLQEKLHgevlrriLQLQSWfrmvlerKHFVQMkh 438
Cdd:PTZ00014  720 LAvsndSSLDP-KEKAEKLLERSGLPKDSYAIGKTMVFLKKDAAKELTQIQR-------EKLAAW-------EPLVSV-- 782

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 568955272  439 aaltIQACWRSYRVRRAL-ERTQAAVYLQAAWRGYL 473
Cdd:PTZ00014  783 ----LEALILKIKKKRKVrKNIKSLVRIQAHLRRHL 814
RhoGAP_ARHGAP19 cd04392
RhoGAP_ARHGAP19: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1147-1318 3.92e-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: 3.92e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1147 KLLEHVEMHgLYTEGLYRKSGAANRTRELRQALQTD-PAAVKLEDFPIHAITGVLKQWLRELPEPLMTFAQYGDFLRAVE 1225
Cdd:cd04392    15 QLIEYLEKN-LRVEGLFRKPGNSARQQELRDLLNSGtDLDLESGGFHAHDCATVLKGFLGELPEPLLTHAHYPAHLQIAD 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1226 L------------PEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLrCPDNSDPL 1293
Cdd:cd04392    94 LcqfdekgnktsaPDKERLLEALQLLLLLLPEENRNLLKLILDLLYQTAKHEDKNKMSADNLALLFTPHLI-CPRNLTPE 172

                         170       180
                  ....*....|....*....|....*
gi 568955272 1294 TSMKDVLKITTCVEMLIKEQMRKYK 1318
Cdd:cd04392   173 DLHENAQKLNSIVTFMIKHSQKLFK 197
MYSc_Myh15_mammals cd14929
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ...
 236-398 1.30e-20

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: 98.51  E-value: 1.30e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  236 KSKGIKQKQIIPknLLDSKSLRLIISMTLHDRTTKSLLHLHKKKKPPSISAQFQTSL-----NKLLEALGKAEPFFIRCI 310
Cdd:cd14929   492 KNKDLLNETVVA--VFQKSSNRLLASLFENYISTDSAIQFGEKKRKKGASFQTVASLhkenlNKLMTNLKSTAPHFVRCI 569

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  311 RSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPK-----DVQPCREAIAALLEKLQVDR 385
Cdd:cd14929   570 NPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRtfpksKFVSSRKAAEELLGSLEIDH 649

                         170
                  ....*....|...
gi 568955272  386 QNYQIGKTKVFLK 398
Cdd:cd14929   650 TQYRFGITKVFFK 662
RhoGAP_fBEM3 cd04400
RhoGAP_fBEM3: RhoGAP (GTPase-activator [GAP] protein for Rho-like small GTPases) domain of ...
 1140-1283 1.49e-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: 91.27  E-value: 1.49e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1140 SVPIVLEKLLEHVEMHG-LYTEGLYRKSGAANRTRELRQALQTDPAAVKLED---FPIHAITGVLKQWLRELPEPLMTFA 1215
Cdd:cd04400    21 DLPSVVYRCIEYLDKNRaIYEEGIFRLSGSASVIKQLKERFNTEYDVDLFSSslyPDVHTVAGLLKLYLRELPTLILGGE 100

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568955272 1216 QYGDFLRAVELPEKQEQLSAIYAVL-DHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCL 1283
Cdd:cd04400   101 LHNDFKRLVEENHDRSQRALELKDLvSQLPQANYDLLYVLFSFLRKIIEHSDVNKMNLRNVCIVFSPTL 169
MYSc_Myo14 cd14876
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ...
 284-398 1.49e-20

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: 98.14  E-value: 1.49e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  284 ISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLL 363
Cdd:cd14876   531 IGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFLD 610

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 568955272  364 P-----KDVQPcREAIAALLEKLQVDRQNYQIGKTKVFLK 398
Cdd:cd14876   611 LgiandKSLDP-KVAALKLLESSGLSEDEYAIGKTMVFLK 649
MYSc_Myo40 cd14901
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ...
 281-397 1.24e-19

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: 95.24  E-value: 1.24e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  281 PPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQ 360
Cdd:cd14901   529 SSTVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHTYS 608

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 568955272  361 VLLP---KDVQPCREAIAALLEKLQV------DRQNYQIGKTKVFL 397
Cdd:cd14901   609 CLAPdgaSDTWKVNELAERLMSQLQHselnieHLPPFQVGKTKVFL 654
MYSc_Myo27 cd14888
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ...
 277-398 1.80e-19

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: 94.76  E-value: 1.80e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  277 KKKKPPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFT 356
Cdd:cd14888   560 KKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGVLQAVQVSRAGYPVRLSHAEFY 639

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 568955272  357 EQFQVLLPKDvqpcreaiaallEKLQVdrQNYQIGKTKVFLK 398
Cdd:cd14888   640 NDYRILLNGE------------GKKQL--SIWAVGKTLCFFK 667
RhoGAP_KIAA1688 cd04389
RhoGAP_KIAA1688: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
 1141-1311 1.81e-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: 1.81e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1141 VPIVLEKLLEHV-EMHGLYTEGLYRKSGAANRTRELRqaLQTDPAAV---KLEDfpIHAITGVLKQWLRELPEPLMTFAQ 1216
Cdd:cd04389    21 LPWILTFLSEKVlALGGFQTEGIFRVPGDIDEVNELK--LRVDQWDYplsGLED--PHVPASLLKLWLRELEEPLIPDAL 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1217 YGDFLRAVELPEKqeqlsaIYAVLDHLPEANHTSLERLIfHLVKVALLEDV---NRMSPGALAIIFAPCLLRCpDNSDPL 1293
Cdd:cd04389    97 YQQCISASEDPDK------AVEIVQKLPIINRLVLCYLI-NFLQVFAQPENvahTKMDVSNLAMVFAPNILRC-TSDDPR 168

                         170
                  ....*....|....*...
gi 568955272 1294 TSMKDVLKITTCVEMLIK 1311
Cdd:cd04389   169 VIFENTRKEMSFLRTLIE 186
C1_Myosin-IXa cd20883
protein kinase C conserved region 1 (C1 domain) found in unconventional myosin-IXa and similar ...
 1057-1111 1.87e-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: 1.87e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568955272 1057 QEHNGHVFASYQVNIPQSCEQCLSYIWLMDKALLCSVCKMTCHKKCVHKIQSYCS 1111
Cdd:cd20883     1 EEHNGHIFKSTQYSIPTYCEYCSSLIWMMDRAYVCKLCRYACHKKCCLKTTTKCS 55
RhoGap_RalBP1 cd04381
RhoGap_RalBP1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 1127-1283 6.47e-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: 6.47e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1127 FGVCVD-----SLTSDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRqALQTDPAAVKLEDFPIHAITGVLK 1201
Cdd:cd04381     1 FGASLSlaverSRCHDGIDLPLVFRECIDYVEKHGMKCEGIYKVSGIKSKVDELK-AAYNRRESPNLEEYEPPTVASLLK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1202 QWLRELPEPLMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAP 1281
Cdd:cd04381    80 QYLRELPEPLLTKELMPRFEEACGRPTEAEREQELQRLLKELPECNRLLLAWLIVHMDHVIAQELETKMNIQNISIVLSP 159


                  ..
gi 568955272 1282 CL 1283
Cdd:cd04381   160 TV 161
RhoGAP_DLC1 cd04375
RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1127-1283 1.97e-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: 1.97e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1127 FGVCVD-SLTSDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKLEDFPIHAITGVLKQWLR 1205
Cdd:cd04375     5 FGVPLLvNLQRTGQPLPRSIQQAMRWLRNNALDQVGLFRKSGVKSRIQKLRSMIESSTDNVNYDGQQAYDVADMLKQYFR 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568955272 1206 ELPEPLMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCL 1283
Cdd:cd04375    85 DLPEPLLTNKLSETFIAIFQYVPKEQRLEAVQCAILLLPDENREVLQTLLYFLSDVAANSQENQMTATNLAVCLAPSL 162
MYSc_Myo41 cd14902
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ...
 282-373 2.26e-18

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: 91.49  E-value: 2.26e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  282 PSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQV 361
Cdd:cd14902   559 PSVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRIARHGYSVRLAHASFIELFSG 638

                          90
                  ....*....|..
gi 568955272  362 LLPKDVQPCREA 373
Cdd:cd14902   639 FKCFLSTRDRAA 650
MYSc_Myh7b cd14927
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ...
 276-398 3.39e-18

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: 90.78  E-value: 3.39e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  276 HKKKKppsiSAQFQT-------SLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSA 348
Cdd:cd14927   546 EKRKK----AASFQTvsqlhkeNLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPN 621

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568955272  349 KYTFQDFTEQFQVLLPKDVQP-----CREAIAALLEKLQVDRQNYQIGKTKVFLK 398
Cdd:cd14927   622 RILYADFKQRYRILNPSAIPDdkfvdSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
MYSc_Myh3 cd14913
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ...
 277-398 4.11e-18

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: 90.50  E-value: 4.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  277 KKKKPPS---ISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQ 353
Cdd:cd14913   539 AKKKGSSfqtVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYG 618

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 568955272  354 DFTEQFQVLLPKDVQP-----CREAIAALLEKLQVDRQNYQIGKTKVFLK 398
Cdd:cd14913   619 DFKQRYRVLNASAIPEgqfidSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
MYSc_Myh10 cd14920
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ...
 277-398 9.99e-18

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: 89.30  E-value: 9.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  277 KKKKPPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFT 356
Cdd:cd14920   548 KKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFR 627

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 568955272  357 EQFQVL----LPKDVQPCREAIAALLEKLQVDRQNYQIGKTKVFLK 398
Cdd:cd14920   628 QRYEILtpnaIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
MYSc_Myo35 cd14896
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ...
 276-398 1.07e-17

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: 89.07  E-value: 1.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  276 HKKKKPPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDF 355
Cdd:cd14896   519 GLGQGKPTLASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAF 598

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 568955272  356 TEQFQVLLpKDVQPC---REAIAALLEK-LQVDRQNYQIGKTKVFLK 398
Cdd:cd14896   599 LARFGALG-SERQEAlsdRERCGAILSQvLGAESPLYHLGATKVLLK 644
MYSc_Myo46 cd14907
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ...
 236-398 1.57e-17

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: 88.55  E-value: 1.57e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  236 KSKGIKQKQIIpkNLLDSKSLRLIISMTLHD---RTTKSLLHLHKKKKPPSISAQFQTSLNKLLEALGKAEPFFIRCIRS 312
Cdd:cd14907   528 KNKDEISQSII--NCIQNSKNRIISSIFSGEdgsQQQNQSKQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKP 605

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  313 NAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLlpkdvqpcreaiaalleklqvdRQNYQIGK 392
Cdd:cd14907   606 NEEKKADLFIQGYVLNQIRYLGVLESIRVRKQGYPYRKSYEDFYKQYSLL----------------------KKNVLFGK 663


                  ....*.
gi 568955272  393 TKVFLK 398
Cdd:cd14907   664 TKIFMK 669
RhoGAP_p85 cd04388
RhoGAP_p85: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
 1142-1292 2.04e-17

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: 82.23  E-value: 2.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1142 PIVLEKLLEHVEMHGLYTEGLYRKSGAANRTrELRQALQTDPAAVKLEDFPIHAITGVLKQWLRELPEPLMTFAQYGDFL 1221
Cdd:cd04388    16 PPLLIKLVEAIEKKGLESSTLYRTQSSSSLT-ELRQILDCDAASVDLEQFDVAALADALKRYLLDLPNPVIPAPVYSEMI 94

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568955272 1222 RA---VELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRCPDNSDP 1292
Cdd:cd04388    95 SRaqeVQSSDEYAQLLRKLIRSPNLPHQYWLTLQYLLKHFFRLCQSSSKNLLSARALAEIFSPLLFRFQPASSD 168
RhoGAP_srGAP cd04383
RhoGAP_srGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 1141-1292 4.28e-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: 4.28e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1141 VPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQ--TDPAAVKLEDFPIHAITGVLKQWLRELPEPLMTFAQYG 1218
Cdd:cd04383    18 IPLVVESCIRFINLYGLQHQGIFRVSGSQVEVNDIKNAFErgEDPLADDQNDHDINSVAGVLKLYFRGLENPLFPKERFE 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568955272 1219 DFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRCPDNSDP 1292
Cdd:cd04383    98 DLMSCVKLENPTERVHQIREILSTLPRSVIIVMRYLFAFLNHLSQFSDENMMDPYNLAICFGPTLMPVPEGQDQ 171
MYSc_Myo43 cd14904
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ...
 277-398 4.49e-17

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: 86.92  E-value: 4.49e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  277 KKKKPPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFT 356
Cdd:cd14904   529 GTKAPKSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELA 608

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 568955272  357 EQFQVLLP-----KDV-QPCREAIAALLEKLQVDrqnYQIGKTKVFLK 398
Cdd:cd14904   609 TRYAIMFPpsmhsKDVrRTCSVFMTAIGRKSPLE---YQIGKSLIYFK 653
MYSc_Myo42 cd14903
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ...
 287-398 4.67e-17

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: 87.14  E-value: 4.67e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  287 QFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLP-- 364
Cdd:cd14903   543 QFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFLPeg 622

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 568955272  365 -KDVQPCREAIAALLEKLQVDR-QNYQIGKTKVFLK 398
Cdd:cd14903   623 rNTDVPVAERCEALMKKLKLESpEQYQMGLTRIYFQ 658
MYSc_Myh2_insects_mollusks cd14911
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ...
 283-398 1.72e-16

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: 85.42  E-value: 1.72e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  283 SISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL 362
Cdd:cd14911   555 TVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELL 634

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 568955272  363 ----LPKDVQPCREAIAALLEKLQVDRQNYQIGKTKVFLK 398
Cdd:cd14911   635 tpnvIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
MYSc_Myh1_mammals cd14910
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ...
 278-398 1.97e-16

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: 85.17  E-value: 1.97e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  278 KKKPPS---ISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQD 354
Cdd:cd14910   543 KKKGSSfqtVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYAD 622

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 568955272  355 FTEQFQVL----LPK-DVQPCREAIAALLEKLQVDRQNYQIGKTKVFLK 398
Cdd:cd14910   623 FKQRYKVLnasaIPEgQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
MYSc_Myh2_mammals cd14912
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ...
 278-398 2.57e-16

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: 84.78  E-value: 2.57e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  278 KKKPPS---ISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQD 354
Cdd:cd14912   545 KKKGSSfqtVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYAD 624

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 568955272  355 FTEQFQVL----LPK-DVQPCREAIAALLEKLQVDRQNYQIGKTKVFLK 398
Cdd:cd14912   625 FKQRYKVLnasaIPEgQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
MYSc_Myh9 cd14919
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ...
 283-398 2.61e-16

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: 84.76  E-value: 2.61e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  283 SISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL 362
Cdd:cd14919   551 TVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEIL 630

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 568955272  363 ----LPKDVQPCREAIAALLEKLQVDRQNYQIGKTKVFLK 398
Cdd:cd14919   631 tpnsIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
MYSc_Myh8 cd14918
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ...
 278-398 3.41e-16

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: 84.40  E-value: 3.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  278 KKKPPS---ISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQD 354
Cdd:cd14918   540 KKKGSSfqtVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGD 619

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 568955272  355 FTEQFQVL----LPK-DVQPCREAIAALLEKLQVDRQNYQIGKTKVFLK 398
Cdd:cd14918   620 FKQRYKVLnasaIPEgQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
MYSc_Myh7 cd14917
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ...
 283-398 4.03e-16

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: 84.00  E-value: 4.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  283 SISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL 362
Cdd:cd14917   548 TVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRIL 627

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 568955272  363 LPKDVQP-----CREAIAALLEKLQVDRQNYQIGKTKVFLK 398
Cdd:cd14917   628 NPAAIPEgqfidSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
MYSc_Myh4 cd14915
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ...
 278-398 4.65e-16

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: 84.01  E-value: 4.65e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  278 KKKPPS---ISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQD 354
Cdd:cd14915   543 KKKGSSfqtVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYAD 622

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 568955272  355 FTEQFQVL----LPK-DVQPCREAIAALLEKLQVDRQNYQIGKTKVFLK 398
Cdd:cd14915   623 FKQRYKVLnasaIPEgQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
MYSc_Myh18 cd14932
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ...
 283-398 4.89e-16

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: 83.92  E-value: 4.89e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  283 SISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL 362
Cdd:cd14932   557 TVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 636

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 568955272  363 ----LPKDVQPCREAIAALLEKLQVDRQNYQIGKTKVFLK 398
Cdd:cd14932   637 tpnaIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
MYSc_Myh19 cd15896
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ...
 283-398 6.26e-16

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: 83.58  E-value: 6.26e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  283 SISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL 362
Cdd:cd15896   556 TVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 635

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 568955272  363 ----LPKDVQPCREAIAALLEKLQVDRQNYQIGKTKVFLK 398
Cdd:cd15896   636 tpnaIPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
MYSc_Myo34 cd14895
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ...
 284-398 6.39e-16

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: 83.46  E-value: 6.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  284 ISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLL 363
Cdd:cd14895   593 IGSQFKQQLASLLDVVQQTQTHYIRCIKPNDESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLV 672

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 568955272  364 PKDVQPCREAiAALLEKLQVDrqNYQIGKTKVFLK 398
Cdd:cd14895   673 AAKNASDATA-SALIETLKVD--HAELGKTRVFLR 704
MYSc_Myh11 cd14921
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ...
 268-398 7.34e-16

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: 83.14  E-value: 7.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  268 TTKSLLHLHKKKKP--PSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSG 345
Cdd:cd14921   537 TESSLPSASKTKKGmfRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQG 616

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568955272  346 YSAKYTFQDFTEQFQVL----LPKDVQPCREAIAALLEKLQVDRQNYQIGKTKVFLK 398
Cdd:cd14921   617 FPNRIVFQEFRQRYEILaanaIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
MYSc_Myh13 cd14923
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ...
 283-398 8.51e-16

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: 82.81  E-value: 8.51e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  283 SISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL 362
Cdd:cd14923   551 TVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRIL 630

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 568955272  363 LPKDVQP-----CREAIAALLEKLQVDRQNYQIGKTKVFLK 398
Cdd:cd14923   631 NASAIPEgqfidSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
MYSc_Myo26 cd14887
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ...
 260-398 1.12e-15

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: 82.77  E-value: 1.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  260 ISMTLHDRttKSLLHLHKKKKPpSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETV 339
Cdd:cd14887   587 TRLVGSKK--NSGVRAISSRRS-TLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLL 663

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568955272  340 RIRRSGYSAKYTFQDFTEQFQVLLPKDVQ---PCREAIAALLEKLQVDRQNYQIGKTKVFLK 398
Cdd:cd14887   664 RVMADGFPCRLPYVELWRRYETKLPMALRealTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
MYSc_Myh14_mammals cd14930
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ...
 283-398 1.36e-15

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: 82.45  E-value: 1.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  283 SISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL 362
Cdd:cd14930   551 TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIL 630

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 568955272  363 ----LPKDVQPCREAIAALLEKLQVDRQNYQIGKTKVFLK 398
Cdd:cd14930   631 tpnaIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
MYSc_Myh6 cd14916
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ...
 278-398 3.71e-15

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: 80.87  E-value: 3.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  278 KKKPPS---ISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQD 354
Cdd:cd14916   542 KKKGSSfqtVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGD 621

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 568955272  355 FTEQFQVLLPKDVQP-----CREAIAALLEKLQVDRQNYQIGKTKVFLK 398
Cdd:cd14916   622 FRQRYRILNPAAIPEgqfidSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
MYSc_Myo12 cd14874
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ...
 283-398 1.23e-14

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: 79.14  E-value: 1.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  283 SISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL 362
Cdd:cd14874   509 SQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCL 588

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 568955272  363 LPKDVQPC---REAIAALLEKLQVDRQN-YQIGKTKVFLK 398
Cdd:cd14874   589 LPGDIAMCqneKEIIQDILQGQGVKYENdFKIGTEYVFLR 628
MYSc_Myh16 cd14934
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ...
 277-398 1.32e-14

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: 78.92  E-value: 1.32e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  277 KKKKPPS----ISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTF 352
Cdd:cd14934   530 KKQKRGSsfmtVSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQY 609

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 568955272  353 QDFTEQFQVL----LPKDVQPCREAIAALLEKLQVDRQNYQIGKTKVFLK 398
Cdd:cd14934   610 PEFKQRYQVLnpnvIPQGFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
MYSc_Myo16 cd14878
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ...
 252-398 2.98e-14

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: 77.93  E-value: 2.98e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  252 DSKSLRLIISMtlhdRTTKSLL--HLHKKKKPpSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQ 329
Cdd:cd14878   510 DSLSQNLLFVM----KTSENVVinHLFQSKLV-TIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQ 584

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568955272  330 LRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLpkDVQPCREAIAALLEK-----LQVDRQNYQIGKTKVFLK 398
Cdd:cd14878   585 LQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLA--DTLLGEKKKQSAEERcrlvlQQCKLQGWQMGVRKVFLK 656
RhoGAP_fLRG1 cd04397
RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1118-1310 1.28e-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: 1.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1118 SELGAEPGHFgvcvdsltsdkaSVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVK--LEDFPIHa 1195
Cdd:cd04397    16 STLGVGPGKL------------RIPALIDDIISAMRQMDMSVEGVFRKNGNIRRLKELTEEIDKNPTEVPdlSKENPVQ- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1196 ITGVLKQWLRELPEPLMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDV-----NRM 1270
Cdd:cd04397    83 LAALLKKFLRELPDPLLTFKLYRLWISSQKIEDEEERKRVLHLVYCLLPKYHRDTMEVLFSFLKWVSSFSHIdeetgSKM 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 568955272 1271 SPGALAIIFAPCLLRcPDNSDPLTSMKDVLKITTcVEMLI 1310
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 ...
 1140-1288 3.08e-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: 70.90  E-value: 3.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1140 SVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDP---AAVKLEDFPIHAITGVLKQWLRELPEPLMTFAQ 1216
Cdd:cd04396    31 YIPVVVAKCGVYLKENATEVEGIFRVAGSSKRIRELQLIFSTPPdygKSFDWDGYTVHDAASVLRRYLNNLPEPLVPLDL 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1217 YGDFLRAVE----------------LPEKQEQLSAIY-AVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIF 1279
Cdd:cd04396   111 YEEFRNPLRkrprilqymkgrinepLNTDIDQAIKEYrDLITRLPNLNRQLLLYLLDLLAVFARNSDKNLMTASNLAAIF 190


                  ....*....
gi 568955272 1280 APCLLRCPD 1288
Cdd:cd04396   191 QPGILSHPD 199
MYSc_Myo25 cd14886
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ...
 284-398 3.32e-13

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: 74.54  E-value: 3.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  284 ISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLL 363
Cdd:cd14886   530 LGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILI 609

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 568955272  364 ---------PKDVqpcREAIAALLEKLQVDRQNYQIGKTKVFLK 398
Cdd:cd14886   610 shnsssqnaGEDL---VEAVKSILENLGIPCSDYRIGKTKVFLR 650
MYSc_Myo13 cd14875
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ...
 283-398 3.82e-13

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: 74.46  E-value: 3.82e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  283 SISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL 362
Cdd:cd14875   539 TVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFCRYFYLI 618

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 568955272  363 LPKDV------QPCREAIAALLEKLQV----DRQNYQIGKTKVFLK 398
Cdd:cd14875   619 MPRSTaslfkqEKYSEAAKDFLAYYQRlygwAKPNYAVGKTKVFLR 664
MYSc_Myo19 cd14880
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ...
 283-397 5.60e-13

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: 73.73  E-value: 5.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  283 SISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL 362
Cdd:cd14880   545 TVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYKLL 624

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 568955272  363 LPKdvQPCREAIAALLEKLQVDRQNYQIGKTKVFL 397
Cdd:cd14880   625 RRL--RPHTSSGPHSPYPAKGLSEPVHCGRTKVFM 657
MYSc_Myo21 cd14882
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ...
 283-398 7.20e-13

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: 73.62  E-value: 7.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  283 SISAQFQTSLNKLLEAL----GKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQ 358
Cdd:cd14882   522 TLAATFRATSLELLKMLsigaNSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQEFLRR 601

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 568955272  359 FQVL---LPKDVQPCREAIAALLEKLQVdrQNYQIGKTKVFLK 398
Cdd:cd14882   602 YQFLafdFDETVEMTKDNCRLLLIRLKM--EGWAIGKTKVFLK 642
MYSc_Myo47 cd14908
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ...
 285-398 8.44e-13

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: 73.40  E-value: 8.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  285 SAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLP 364
Cdd:cd14908   545 GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLLP 624

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568955272  365 ---KDVQP----------------CREAIAALLEKLQVDRQNY-----QIGKTKVFLK 398
Cdd:cd14908   625 lipEVVLSwsmerldpqklcvkkmCKDLVKGVLSPAMVSMKNIpedtmQLGKSKVFMR 682
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
 1062-1110 1.54e-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: 1.54e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 568955272   1062 HVFASYQVNIPQSCEQCLSYIWLMDK-ALLCSVCKMTCHKKCVHKIQSYC 1110
Cdd:smart00109    1 HKHVFRTFTKPTFCCVCRKSIWGSFKqGLRCSECKVKCHKKCADKVPKAC 50
MYSc_Myo6 cd01382
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ...
 283-398 1.75e-12

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: 72.28  E-value: 1.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  283 SISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL 362
Cdd:cd01382   532 SVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSFHDLYNMYKKY 611

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 568955272  363 LPKDV---QP---CReaiaALLEKLQVDRQNYQIGKTKVFLK 398
Cdd:cd01382   612 LPPKLarlDPrlfCK----ALFKALGLNENDFKFGLTKVFFR 649
MYSc_Myo45 cd14906
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ...
 277-397 2.97e-12

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: 71.55  E-value: 2.97e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  277 KKKKPPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFT 356
Cdd:cd14906   566 KQTQSNTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLNTIKVRKMGYSYRRDFNQFF 645

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568955272  357 EQFQVLL----------PKD-VQPCREAIAALLEKLQV-----------------DRQNYQIGKTKVFL 397
Cdd:cd14906   646 SRYKCIVdmynrknnnnPKLaSQLILQNIQSKLKTMGIsnnkkknnsnsnsnttnDKPLFQIGKTKIFI 714
MYSc_Myo30 cd14891
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ...
 285-398 4.46e-12

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: 70.84  E-value: 4.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  285 SAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLP 364
Cdd:cd14891   527 SAKFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRVTYAELVDVYKPVLP 606

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 568955272  365 KDVQPCREA-----IAALLEKLQVDRQNYQIGKTKVFLK 398
Cdd:cd14891   607 PSVTRLFAEndrtlTQAILWAFRVPSDAYRLGRTRVFFR 645
C1 cd00029
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ...
 1062-1110 6.08e-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: 6.08e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 568955272 1062 HVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYC 1110
Cdd:cd00029     1 HRFVPTTFSSPTFCDVCGKLIWgLFKQGLKCSDCGLVCHKKCLDKAPSPC 50
MYSc_Myo37 cd14898
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ...
 288-398 1.65e-11

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: 68.77  E-value: 1.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  288 FQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLlpkdv 367
Cdd:cd14898   484 FKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRIL----- 558

                          90       100       110
                  ....*....|....*....|....*....|.
gi 568955272  368 QPCREaiaalleklqvDRQNYQIGKTKVFLK 398
Cdd:cd14898   559 GITLF-----------EVVDYRKGRTRYFMK 578
C1_PDZD8 cd20825
protein kinase C conserved region 1 (C1 domain) found in PDZ domain-containing protein 8 ...
 1059-1112 1.95e-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: 1.95e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568955272 1059 HNGHVFASYQVNIPQSCEQCLSYIWLMDkALLCSVCKMTCHKKCVHKIQ--SYCSY 1112
Cdd:cd20825     1 EGKHDFVLTQFQNATYCDFCKKKIWLKE-AFQCRLCGMICHKKCLDKCQaeTLCTR 55
MYSc_Myo18 cd01386
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ...
 266-398 2.39e-11

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: 68.49  E-value: 2.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  266 DRTTKSLLHLHKKK----KPPSISAQFQTSLNKLLEALGKAEPFFIRCI--RSNAEKKE----LCFDDELVLQ------Q 329
Cdd:cd01386   532 AQNATQLLQESQKEtaavKRKSPCLQIKFQVDALIDTLRRTGLHFVHCLlpQHNAGKDErstsSPAAGDELLDvpllrsQ 611

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568955272  330 LRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPKDVQPC---------REAIAALLEKLQVDRQNYQIGKTKVFLK 398
Cdd:cd01386   612 LRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLglnsevadeRKAVEELLEELDLEKSSYRIGLSQVFFR 689
MYSc_Myo20 cd14881
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ...
 288-397 4.04e-11

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: 67.83  E-value: 4.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  288 FQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLP--- 364
Cdd:cd14881   510 FHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKAFNARYRLLAPfrl 589

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 568955272  365 ------KDVQPCR----EAIAALLEKLQVDRQNYQIGKTKVFL 397
Cdd:cd14881   590 lrrveeKALEDCAlilqFLEAQPPSKLSSVSTSWALGKRHIFL 632
MYSc_Myo17 cd14879
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ...
 285-397 4.65e-10

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: 64.49  E-value: 4.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  285 SAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLP 364
Cdd:cd14879   527 ATQLNAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELAARLRVEYVVSLEHAEFCERYKSTLR 606

                          90       100       110
                  ....*....|....*....|....*....|...
gi 568955272  365 KDVQPcrEAIAALLEKLQVDRQNYQIGKTKVFL 397
Cdd:cd14879   607 GSAAE--RIRQCARANGWWEGRDYVLGNTKVFL 637
MYSc_Myo24A cd14937
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ...
 241-398 5.89e-10

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: 63.88  E-value: 5.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  241 KQKQIIPKN---LLDSKSLRLIISMTLHDRTTKSLlhlhkkKKPPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKK 317
Cdd:cd14937   481 KNKDILPSNivrLLKVSNNKLVRSLYEDVEVSESL------GRKNLITFKYLKNLNNIISYLKSTNIYFIKCIKPNENKE 554

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  318 ELCFDDELVLQQLRYTGMLETVRIRRSgYSAKYTFQDFTEQFQVL---LPKDVQPC-REAIAALLEKlQVDRQNYQIGKT 393
Cdd:cd14937   555 KNNFNQKKVFPQLFSLSIIETLNISFF-FQYKYTFDVFLSYFEYLdysTSKDSSLTdKEKVSMILQN-TVDPDLYKVGKT 632


                  ....*
gi 568955272  394 KVFLK 398
Cdd:cd14937   633 MVFLK 637
C1_TNS2-like cd20826
protein kinase C conserved region 1 (C1 domain) found in tensin-2 like (TNS2-like) proteins; ...
 1061-1111 1.79e-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: 54.70  E-value: 1.79e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568955272 1061 GHVFASYQVNIPQSCEQCLSYIWlmDKALLCSVCKMTCHKKCVHKIQSYCS 1111
Cdd:cd20826     2 SHSFKEKSFRKPRTCDVCKQIIW--NEGSSCRVCKYACHRKCEPKVTAACS 50
MYSc_Myo39 cd14900
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ...
 287-362 4.55e-09

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: 61.09  E-value: 4.55e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568955272  287 QFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL 362
Cdd:cd14900   515 QFKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVARAGFPIRLLHDEFVARYFSL 590
RhoGAP_OCRL1 cd04380
RhoGAP_OCRL1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
 1140-1290 9.55e-09

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: 9.55e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1140 SVPIVLEKLLEHVEMHGLYTEGLYRKSG----AANRTRELRQALQTDPAAVKLedFPIHAITGVLKQWLRELPEPLMTFA 1215
Cdd:cd04380    49 SIPKEIWRLVDYLYTRGLAQEGLFEEPGlpsePGELLAEIRDALDTGSPFNSP--GSAESVAEALLLFLESLPDPIIPYS 126

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568955272 1216 QYGDFLRAVELPEKQeqlsaIYAVLD-HLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRCPDNS 1290
Cdd:cd04380   127 LYERLLEAVANNEED-----KRQVIRiSLPPVHRNVFVYLCSFLRELLSESADRGLDENTLATIFGRVLLRDPPRA 197
MYSc_Myo44 cd14905
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ...
 306-398 4.88e-08

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: 57.79  E-value: 4.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  306 FIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPKdvqpcREAIAALLEKLQVDR 385
Cdd:cd14905   578 FIRCIKPNSKKTHLTFDVKSVNEQIKSLCLLETTRIQRFGYTIHYNNKIFFDRFSFFFQN-----QRNFQNLFEKLKEND 652

                          90       100
                  ....*....|....*....|.
gi 568955272  386 QN--------YQIGKTKVFLK 398
Cdd:cd14905   653 INidsilpppIQVGNTKIFLR 673
C1_SpBZZ1-like cd20824
protein kinase C conserved region 1 (C1 domain) found in Schizosaccharomyces pombe protein ...
 1062-1111 8.29e-08

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: 8.29e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568955272 1062 HVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYCS 1111
Cdd:cd20824     2 HNFKPHSFSIPTKCDYCGEKIWgLSKKGLSCKDCGFNCHIKCELKVPPECP 52
MYSc_Myo17 cd14879
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ...
 20-87 8.41e-08

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: 57.17  E-value: 8.41e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568955272   20 FPHATSHTLLAKFKQQHEDNKYF-----LGTPVLEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGS 87
Cdd:cd14879   455 MPKKTDEQMLEALRKRFGNHSSFiavgnFATRSGSASFTVNHYAGEVTYSVEGFLERNGDVLSPDFVNLLRGA 527
C1_DEF8 cd20819
protein kinase C conserved region 1 (C1 domain) found in differentially expressed in FDCP 8 ...
 1060-1110 9.11e-08

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: 9.11e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568955272 1060 NGHVFASYQVNIP--QSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYC 1110
Cdd:cd20819     4 LGHHFVLQKSKSSskQYCDKCCGIIWgLLQTWYRCTDCGYRCHSKCLNSITRTC 57
MYSc_Myo20 cd14881
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ...
 21-85 1.15e-07

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: 56.66  E-value: 1.15e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568955272   21 PHATSHTLLAKFKQQHEDNKYFLGT-PVLEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLR 85
Cdd:cd14881   430 PRGTAESYVAKIKVQHRQNPRLFEAkPQDDRMFGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFY 495
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
 1062-1110 1.71e-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: 1.71e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 568955272  1062 HVFASYQVNIPQSCEQCLSYIWLMDK-ALLCSVCKMTCHKKCVHKIQSYC 1110
Cdd:pfam00130    1 HHFVHRNFKQPTFCDHCGEFLWGLGKqGLKCSWCKLNVHKRCHEKVPPEC 50
MYSc_Myo24B cd14938
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ...
 270-397 2.82e-07

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: 55.23  E-value: 2.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  270 KSLLHLHKKKKPPSisAQFQTSL--NKLLEALGKAEP---FFIRCIRSNAEKKELC-FDDELVLQQLRYTGMLETVRIRR 343
Cdd:cd14938   585 QSALKLFKRRYDTK--NQMAVSLlrNNLTELEKLQETtfcHFIVCMKPNESKRELCsFDANIVLRQVRNFSIVEASQLKV 662

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568955272  344 SGYSAKYTFQDFTEQFQVLlpkdvQPC-REAIAALLEKLQVDRQNYQIGKTKVFL 397
Cdd:cd14938   663 GYYPHKFTLNEFLSIFDIK-----NEDlKEKVEALIKSYQISNYEWMIGNNMIFL 712
MYSc_Myo38 cd14899
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ...
 283-363 3.38e-07

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: 55.10  E-value: 3.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  283 SISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL 362
Cdd:cd14899   608 SVGTQFKIQLNELLSTVRATTPRYVRCIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRYRRV 687


                  .
gi 568955272  363 L 363
Cdd:cd14899   688 L 688
C1_ARHGEF-like cd20832
protein kinase C conserved region 1 (C1 domain) found in uncharacterized Rho guanine ...
 1061-1111 3.65e-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: 3.65e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568955272 1061 GHVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYCS 1111
Cdd:cd20832     1 GHQFVLQHYYQVTFCNHCSGLLWgIGYQGYQCSDCEFNIHKQCIEVIEESCP 52
C1_ScPKC1-like_rpt1 cd20822
first protein kinase C conserved region 1 (C1 domain) found in Saccharomyces cerevisiae ...
 1060-1110 9.65e-07

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: 9.65e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568955272 1060 NGHVFAS---YQVNipqSCEQCLSYiwLMDKALLCSVCKMTCHKKCVHKIQSYC 1110
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 ...
 1061-1110 1.20e-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: 1.20e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568955272 1061 GHVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYC 1110
Cdd:cd20820     1 GHRFVPLELEQPTWCDLCGSVILgLFRKCLRCANCKMTCHPRCRSLVCLTC 51
C1_RASSF1 cd20885
protein kinase C conserved region 1 (C1 domain) found in Ras association domain-containing ...
 1059-1111 1.71e-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: 1.71e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568955272 1059 HNGHVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYCS 1111
Cdd:cd20885     1 GEGHDFQPCSLTNPTWCDLCGDFIWgLYKQCLRCTHCKYTCHLRCRDLVTLDCS 54
MYSc_Myo32 cd14893
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ...
 283-397 1.81e-06

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: 52.67  E-value: 1.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272  283 SISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFqvl 362
Cdd:cd14893   627 SAATDVYNQADALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRY--- 703

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 568955272  363 lpKDVQPCREAIAALLEKLQ----VDRQNYQIGKTKVFL 397
Cdd:cd14893   704 --KNVCGHRGTLESLLRSLSaigvLEEEKFVVGKTKVYL 740
C1_nPKC_theta-like_rpt1 cd20834
first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
 1056-1114 2.93e-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: 2.93e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1056 VQEHNGHVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYCSYTG 1114
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, ...
 1061-1111 4.05e-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: 4.05e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568955272 1061 GHVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYCS 1111
Cdd:cd20803     1 GHSFRKKTFHKPTYCHHCTDLLWgLLNQGYQCEVCNFVSHERCLKTVVTPCS 52
C1_GMIP-like cd20816
protein kinase C conserved region 1 (C1 domain) found in the GEM-interacting protein (GMIP) ...
 1060-1111 4.76e-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: 44.94  E-value: 4.76e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568955272 1060 NGHVFAsyQVNIPQSCEQCLSYIWLmdKALLCSVCKMTCHKKCVHKIQSYCS 1111
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 ...
 1062-1102 5.24e-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: 5.24e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568955272 1062 HVFASYQVNIPQSCEQCLSYIWLMDKALLCSVCKMTCHKKC 1102
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) ...
 1062-1110 6.44e-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: 6.44e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 568955272 1062 HVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYC 1110
Cdd:cd20837     1 HRFKVYNYMSPTFCDHCGSLLWgLFRQGLKCEECGMNVHHKCQKKVANLC 50
C1_MTMR-like cd20828
protein kinase C conserved region 1 (C1 domain) found in uncharacterized proteins similar to ...
 1062-1112 8.96e-06

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: 8.96e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568955272 1062 HVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYCSY 1112
Cdd:cd20828     6 HNFEPHSFVTPTNCDYCLQILWgIVKKGMKCSECGYNCHEKCQPQVPKQCSK 57
C1_cPKC_nPKC_rpt1 cd20792
first protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) ...
 1061-1111 1.33e-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: 1.33e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568955272 1061 GHVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYCS 1111
Cdd:cd20792     1 GHKFVATFFKQPTFCSHCKDFIWgLGKQGYQCQVCRFVVHKRCHEYVVFKCP 52
C1_dGM13116p-like cd20831
protein kinase C conserved region 1 (C1 domain) found in Drosophila melanogaster GM13116p and ...
 1059-1111 1.63e-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: 1.63e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568955272 1059 HNGHVFASYQVNIPQSCEQC-LSYIWLMDK-ALLCSVCKMTCHKKCVHKIQSYCS 1111
Cdd:cd20831     3 YNDHTFVATHFKGGPSCAVCnKLIPGRFGKqGYQCRDCGLICHKRCHVKVETHCP 57
MYSc_Myo30 cd14891
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ...
 23-87 1.75e-05

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: 49.66  E-value: 1.75e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568955272   23 ATSHTLLAK---FKQQHEDNKYFLgtpvlepaFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGS 87
Cdd:cd14891   468 ETLHKTHKRhpcFPRPHPKDMREM--------FIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASS 527
C1_nPKC_epsilon-like_rpt1 cd20835
first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
 1054-1110 2.83e-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: 2.83e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568955272 1054 RAVQEHNGHVFASYQVNIPQSCEQCLSYIW-LMDK-ALLCSVCKMTCHKKCVHKIQSYC 1110
Cdd:cd20835     2 RRVHQVNGHKFMATYLRQPTYCSHCKDFIWgVIGKqGYQCQVCTCVVHKRCHQLVVTKC 60
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
 429-458 4.39e-05

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


Pssm-ID: 467745 [Multi-domain]  Cd Length: 37  Bit Score: 41.76  E-value: 4.39e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 568955272  429 ERKHFVQMKHAALTIQACWRSYRVRRALER 458
Cdd:cd23767     1 EEEELQRMNRAATLIQALWRGYKVRKELKK 30
C1_aPKC cd20794
protein kinase C conserved region 1 (C1 domain) found in the atypical protein kinase C (aPKC) ...
 1060-1111 4.87e-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: 4.87e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568955272 1060 NGHVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYCS 1111
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) ...
 1062-1110 6.71e-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: 6.71e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 568955272 1062 HVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYC 1110
Cdd:cd20838     3 HRFSVHNYKRPTFCDHCGSLLYgLYKQGLQCKVCKMNVHKRCQKNVANNC 52
RhoGAP_fRGD2 cd04399
RhoGAP_fRGD2: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
 1127-1286 7.09e-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: 7.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1127 FGVCVDSLT-SDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGA------ANRTRELRQALQT----DPAAVKLEDFPIHA 1195
Cdd:cd04399     1 FGVDLETRCrLDKKVVPLIVSAILSYLDQLYPDLINDEVRRNVwtdpvsLKETHQLRNLLNKpkkpDKEVIILKKFEPST 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1196 ITGVLKQWLRELPEPLMTfAQYGDFLRAV-------ELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKvalLEDVN 1268
Cdd:cd04399    81 VASVLKLYLLELPDSLIP-HDIYDLIRSLysayppsQEDSDTARIQGLQSTLSQLPKSHIATLDAIITHFYR---LIEIT 156

                         170       180
                  ....*....|....*....|....
gi 568955272 1269 RMSPGA------LAIIFAPCLLRC 1286
Cdd:cd04399   157 KMGESEeeyadkLATSLSREILRP 180
C1_MRCKalpha cd20864
protein kinase C conserved region 1 (C1 domain) found in myotonic dystrophy kinase-related ...
 1062-1110 7.48e-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: 7.48e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 568955272 1062 HVFASYQVNIPQSCEQCLS-YIWLMDKALLCSVCKMTCHKKCVHKIQSYC 1110
Cdd:cd20864     3 HQFVVKSFTTPTKCNQCTSlMVGLIRQGCTCEVCGFSCHVTCADKAPSVC 52
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 457-479 1.15e-04

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


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 40.39  E-value: 1.15e-04
                            10        20
                    ....*....|....*....|...
gi 568955272    457 ERTQAAVYLQAAWRGYLQRQAYH 479
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRYK 23
C1_ROCK2 cd20875
protein kinase C conserved region 1 (C1 domain) found in Rho-associated coiled-coil containing ...
 1059-1100 1.20e-04

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: 41.94  E-value: 1.20e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 568955272 1059 HNGHVFASYQVNIPQSCEQCLSYIWLMDK---ALLCSVCKMTCHK 1100
Cdd:cd20875     9 HKGHEFIPTLYHFPTNCEACMKPLWHMFKpppALECRRCHIKCHK 53
C1_RASSF5 cd20886
protein kinase C conserved region 1 (C1 domain) found in Ras association domain-containing ...
 1061-1111 1.39e-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: 1.39e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568955272 1061 GHVFASYQVnIPQSCEQCLSYIwlMDKALLCSVCKMTCHKKCVHKIQSYCS 1111
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 ...
 1062-1110 1.40e-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: 1.40e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 568955272 1062 HVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYC 1110
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; ...
 1075-1113 1.44e-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: 1.44e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 568955272 1075 CEQCLSYIwlMDKALLCSVCKMTCHKKCVHKIQSYCSYT 1113
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 ...
 1056-1113 2.01e-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: 2.01e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568955272 1056 VQEHNGHVFASYQVNIPQSCEQCLSY-IWLMDKALLCSVCKMTCHKKCVHKIQSYCSYT 1113
Cdd:cd20845     2 VKDDGQHVWRLKHFNKPAYCNLCLNMlVGLGKQGLCCSFCKYTVHERCVQRAPASCIKT 60
PHA02682 PHA02682
ORF080 virion core protein; Provisional
 1450-1544 2.16e-04

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 44.85  E-value: 2.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1450 PAPALPCPISPTLSPLPEAAAPPRGRPTSFVTVRVKTPRR-TPIMPMANIKLPPGLPLHLTSWAPALQEAVVPvKRREPP 1528
Cdd:PHA02682   96 PACAPAAPAPAVTCPAPAPACPPATAPTCPPPAVCPAPARpAPACPPSTRQCPPAPPLPTPKPAPAAKPIFLH-NQLPPP 174

                          90
                  ....*....|....*.
gi 568955272 1529 ARRQDQVHSVYIAPGA 1544
Cdd:PHA02682  175 DYPAASCPTIETAPAA 190
C1_PKD_rpt1 cd20795
first protein kinase C conserved region 1 (C1 domain) found in the protein kinase D (PKD) ...
 1059-1113 2.42e-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: 2.42e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568955272 1059 HNGHVfASYQVniPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYCSYT 1113
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 ...
 1062-1110 4.74e-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: 39.49  E-value: 4.74e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 568955272 1062 HVFASYQVNIPQSCEQCLSYIwlMDKALLCSVCKMTCHKKCVHKIQSYC 1110
Cdd:cd20889     3 HTFKNKTFKKPKVCSICKQVI--DSQGISCRVCKYACHKKCEAKVVTPC 49
C1_KSR cd20812
protein kinase C conserved region 1 (C1 domain) found in the kinase suppressor of Ras (KSR) ...
 1062-1111 5.74e-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: 5.74e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 568955272 1062 HVFASYQVnIPQSCEQCLSYIWLmdkALLCSVCKMTCHKKCVHKIQSYCS 1111
Cdd:cd20812     3 HRFSKKLF-MRQTCDYCHKQMFF---GLKCKDCKYKCHKKCAKKAPPSCG 48
C1_cPKC_nPKC_rpt2 cd20793
second protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) ...
 1062-1110 7.29e-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: 7.29e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 568955272 1062 HVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYC 1110
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; ...
 1062-1113 7.34e-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: 7.34e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568955272 1062 HVFASYQVNIPQSCEQCLSYIWLMDK-ALLCSVCKMTCHKKCVHKIQSYCSYT 1113
Cdd:cd20799     6 HVWRLKHFNKPAYCNVCENMLVGLRKqGLCCTFCKYTVHERCVSRAPASCIRT 58
C1_PKD1_rpt1 cd20839
first protein kinase C conserved region 1 (C1 domain) found in protein kinase D (PKD) and ...
 1062-1117 8.02e-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: 8.02e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568955272 1062 HVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYCSYTGRRK 1117
Cdd:cd20839     8 HALFVHSYRAPAFCDHCGEMLWgLVRQGLKCEGCGLNYHKRCAFKIPNNCSGVRKRR 64
C1_Sbf-like cd20827
protein kinase C conserved region 1 (C1 domain) found in the myotubularin-related protein Sbf ...
 1062-1111 8.21e-04

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: 8.21e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568955272 1062 HVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYCS 1111
Cdd:cd20827     2 HRFEKHNFTTPTYCDYCSSLLWgLVKTGMRCADCGYSCHEKCLEHVPKNCT 52
C1_MRCK cd20809
protein kinase C conserved region 1 (C1 domain) found in the Myotonic dystrophy kinase-related ...
 1062-1112 1.24e-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: 1.24e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568955272 1062 HVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYCSY 1112
Cdd:cd20809     1 HKFIVRTFSTPTKCNHCTSLMVgLVRQGLVCEVCGYACHVSCADKAPQVCPV 52
C1_TNS2 cd20887
protein kinase C conserved region 1 (C1 domain) found in tensin-2 and similar proteins; ...
 1089-1111 1.45e-03

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: 38.22  E-value: 1.45e-03
                          10        20
                  ....*....|....*....|...
gi 568955272 1089 LLCSVCKMTCHKKCVHKIQSYCS 1111
Cdd:cd20887    28 LVCRVCKVASHKKCEAKVTSACQ 50
C1_betaCHN cd20857
protein kinase C conserved region 1 (C1 domain) found in beta-chimaerin and similar proteins; ...
 1062-1116 1.68e-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: 1.68e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568955272 1062 HVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYCSYTGRR 1116
Cdd:cd20857     6 HNFKVHTFRGPHWCEYCANFMWgLIAQGVRCSDCGLNVHKQCSKHVPNDCQPDLKR 61
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
 459-479 1.84e-03

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 459869  Cd Length: 21  Bit Score: 36.91  E-value: 1.84e-03
                           10        20
                   ....*....|....*....|.
gi 568955272   459 TQAAVYLQAAWRGYLQRQAYH 479
Cdd:pfam00612    1 RKAAIKIQAAWRGYLARKRYK 21
C1_ROCK1 cd20874
protein kinase C conserved region 1 (C1 domain) found in Rho-associated coiled-coil containing ...
 1057-1105 1.95e-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: 1.95e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568955272 1057 QEHNGHVFASYQVNIPQSCEQCLSYIWLMDK---ALLCSVCKMTCHKKCVHK 1105
Cdd:cd20874     3 LPHKGHEFIPTLYHFPANCEACAKPLWHVFKpppALECRRCHVKCHKDHLDK 54
MYSc_Myo33 cd14894
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ...
 283-348 2.23e-03

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: 42.81  E-value: 2.23e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568955272  283 SISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRR---SGYSA 348
Cdd:cd14894   735 SFVGQFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQMEICRnssSSYSA 803
C1_AKAP13 cd20878
protein kinase C conserved region 1 (C1 domain) found in A-kinase anchor protein 13 (AKAP-13) ...
 1060-1102 3.08e-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: 3.08e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 568955272 1060 NGHVFASYQVNIPQSCEQClSYIWLMDKALLCSVCKMTCHKKC 1102
Cdd:cd20878     6 NGHVFSPVSSVGPTQCYHC-SKPLNTKDAFLCANCNVQVHKGC 47
CRIK cd20814
protein kinase C conserved region 1 (C1 domain) found in citron Rho-interacting kinase (CRIK) ...
 1062-1110 3.18e-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: 3.18e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 568955272 1062 HVFASYQVNIPQSCEQCLSYIWLMDKALLCSVCKMTCHKKCVHKIQSYC 1110
Cdd:cd20814     5 HRFTTGLNMRATKCAVCLDGVPFGRQASKCSECGIVCHPKCSSSLPNTC 53
C1_aPKC_zeta cd21095
protein kinase C conserved region 1 (C1 domain) found in the atypical protein kinase C (aPKC) ...
 1060-1102 3.69e-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: 3.69e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 568955272 1060 NGHVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKC 1102
Cdd:cd21095     1 NGHLFQAKRFNRRAYCGQCSERIWgLGRQGYKCINCKLLVHKRC 44
C1_PIK3R-like_rpt2 cd20830
second protein kinase C conserved region 1 (C1 domain) found in uncharacterized ...
 1073-1104 3.75e-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: 3.75e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 568955272 1073 QSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVH 1104
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 ...
 1062-1110 3.87e-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: 3.87e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 568955272 1062 HVFASYQVNIPQSCEQCLSYI-WLMDKALLCSVCKMTCHKKCVHKIQSYC 1110
Cdd:cd20843    12 HTFVIHSYTRPTVCQFCKKLLkGLFRQGLQCKDCKFNCHKRCATRVPNDC 61
C1_ScPKC1-like_rpt2 cd20823
second protein kinase C conserved region 1 (C1 domain) found in Saccharomyces cerevisiae ...
 1059-1110 4.10e-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: 4.10e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568955272 1059 HNGHVFASYQVNIPQSCEQClSYI--WLMDKALLCSVCKMTCHKKCVHKIQSYC 1110
Cdd:cd20823     2 RIPHRFEPFTNLGANWCCHC-GQMlpLGRKQIRKCTECGKTAHAQCAHLVPNFC 54
C1_Stac cd20817
protein kinase C conserved region 1 (C1 domain) found in the SH3 and cysteine-rich ...
 1062-1111 4.43e-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: 4.43e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568955272 1062 HVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIqSYCS 1111
Cdd:cd20817     1 HSFQEHTFKKPTFCDVCKELLVgLSKQGLRCKNCKMNVHHKCQEGV-PDCS 50
C1_PKD1_rpt2 cd20842
second protein kinase C conserved region 1 (C1 domain) found in protein kinase D (PKD) and ...
 1062-1110 4.64e-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: 4.64e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 568955272 1062 HVFASYQVNIPQSCEQCLSYI-WLMDKALLCSVCKMTCHKKCVHKIQSYC 1110
Cdd:cd20842    35 HTFVIHSYTRPTVCQYCKKLLkGLFRQGLQCKDCKFNCHKRCAPKVPNNC 84
C1_TNS1_v cd20888
protein kinase C conserved region 1 (C1 domain) found in tensin-1 (TNS1) variant and similar ...
 1060-1111 5.02e-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: 36.77  E-value: 5.02e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568955272 1060 NGHVFASYQVNIPQSCEQCLSYIwlMDKALLCSVCKMTCHKKCVHKIQSYCS 1111
Cdd:cd20888     4 HTHTFKVKTFKKVKSCGICKQAI--TREGSTCRVCKLSCHKKCEAKVATPCV 53
C1_PIK3R-like_rpt1 cd20829
first protein kinase C conserved region 1 (C1 domain) found in uncharacterized ...
 1062-1103 5.07e-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: 5.07e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 568955272 1062 HVFASYQVNIPQSCEQCLSYIWLMDKAL-LCSVCKMTCHKKCV 1103
Cdd:cd20829     1 HRLVDVYFVTPILCRHCKDYIWGKGKVGvRCEDCHACFHLVCA 43
C1_cPKC_rpt2 cd20836
second protein kinase C conserved region 1 (C1 domain) found in the classical (or conventional) ...
 1062-1110 5.13e-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: 5.13e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 568955272 1062 HVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYC 1110
Cdd:cd20836     1 HKFKVHTYSSPTFCDHCGSLLYgLIHQGMKCDTCDMNVHKRCVKNVPSLC 50
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
 435-456 5.38e-03

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


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 35.76  E-value: 5.38e-03
                            10        20
                    ....*....|....*....|..
gi 568955272    435 QMKHAALTIQACWRSYRVRRAL 456
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRY 22
C1_aPKC_iota cd21094
protein kinase C conserved region 1 (C1 domain) found in the atypical protein kinase C (aPKC) ...
 1060-1106 7.96e-03

protein kinase C conserved region 1 (C1 domain) found in the atypical protein kinase C (aPKC) iota 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-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 C1 domain found in aPKC isoform iota. 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: 410447  Cd Length: 55  Bit Score: 36.13  E-value: 7.96e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 568955272 1060 NGHVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCvHKI 1106
Cdd:cd21094     1 NGHTFQAKRFNRRAHCAICTDRIWgLGRQGYKCINCKLLVHKKC-HKL 47
C1_DGKgamma_rpt1 cd20846
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase gamma ...
 1053-1113 7.99e-03

first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase gamma (DAG kinase gamma) and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase gamma, also called diglyceride kinase gamma (DGK-gamma), reverses the normal flow of glycerolipid biosynthesis by phosphorylating diacylglycerol back to phosphatidic acid. 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. DGK-gamma contains two copies of the C1 domain. This model corresponds to the first one. DGK-gamma 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: 410396  Cd Length: 73  Bit Score: 36.83  E-value: 7.99e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568955272 1053 ERAVQEHNGHVFASYQVNIPQSCEQCLSYIWLMDK-ALLCSVCKMTCHKKCVHKIQSYCSYT 1113
Cdd:cd20846     8 ETNVKDDGQHAWRLKHFKKPAYCNFCHTMLLGVRKqGLCCSFCKYTVHERCVSKDIASCIST 69
SepH NF040712
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ...
 1353-1494 9.08e-03

septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments.


Pssm-ID: 468676 [Multi-domain]  Cd Length: 346  Bit Score: 40.14  E-value: 9.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568955272 1353 FSSPYEGVRIKSPRTPVVQDLELGALPEEAAGGDEDREKEI---LMERIQSIKEEKEDITYRLPELDPRGSDEENLDSET 1429
Cdd:NF040712  192 FGRPLRPLATVPRLAREPADARPEEVEPAPAAEGAPATDSDpaeAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAEPD 271

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568955272 1430 SASTESLLEERGVRGAVEGPPAPALPCPISPTLSPLPEAAAPPRGRPTsfVTVRVKTPRRTPIMP 1494
Cdd:NF040712  272 EATRDAGEPPAPGAAETPEAAEPPAPAPAAPAAPAAPEAEEPARPEPP--PAPKPKRRRRRASVP 334
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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