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Conserved domains on  [gi|1907198218|ref|XP_036010926|]
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unconventional myosin-IXa isoform X9 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MYSc_Myo9 cd01385
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ...
160-986 0e+00

class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play a role in signalling. It has a N-terminal RA domain, an IQ domain, a C1_1 domain, and a RhoGAP domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


:

Pssm-ID: 276836 [Multi-domain]  Cd Length: 690  Bit Score: 1315.06  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  160 KTLLENLRNRFKHEKIYTYVGSILIAINPFKFLPIYNPKYVKMYDNHQLGKLEPHIYAVADVAYHAMLQRKKNQCIVISG 239
Cdd:cd01385      1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  240 ESGSGKTQSTNFLIHHLTALSQKGFASGVEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQETGTVLGAYVEKYL 319
Cdd:cd01385     81 ESGSGKTESTNFLLHHLTALSQKGYGSGVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVEKYL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  320 LEKSRLVYQEHNERNYHVFYYLLAGASEEERLAFHLKQPEEYHFLNQ-DCFTVEGEDLRHDFERLQLAMEMVGFLPKTRR 398
Cdd:cd01385    161 LEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNQsDCYTLEGEDEKYEFERLKQAMEMVGFLPETQR 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  399 QIFSLLSAILHLGNISYKKKTY-RDDSIDICNPEVLPIVSELLEVKEEMLFEALVTRKTVTVGEKLILPYKLAEAVTVRN 477
Cdd:cd01385    241 QIFSVLSAVLHLGNIEYKKKAYhRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLILPYKLPEAIATRD 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  478 SMAKSLYSALFDWIVFRINHALLNSKDLEQDtKTLSIGVLDIFGFEDYENNSFEQFCINFANERLQHYFNQHIFKLEQEE 557
Cdd:cd01385    321 AMAKCLYSALFDWIVLRINHALLNKKDLEEA-KGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIFKLEQEE 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  558 YRTEGISWHNIDYIDNTCCINLISKKPTGLLHLLDEESNFPQATNQTLLDKFKHQHEENSYIEFPAVMEPAFIIKHYAGK 637
Cdd:cd01385    400 YKKEGISWHNIEYTDNTGCLQLISKKPTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNKYYEKPQVMEPAFIIAHYAGK 479
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  638 VKYGVKDFREKNTDHMRPDIVALLRSSRNAFVSGMTGIDPVAVFRWAVLRAFFRAVVAFREAGKRHIQRKSGHddttpca 717
Cdd:cd01385    480 VKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVRELIGIDPVAVFRWAVLRAFFRAMAAFREAGRRRAQRTAGH------- 552
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  718 ilksmdsfsflqhpvhqrsleilqrckeekysitrknprtplsdlqgmntlneknqhdtfdiawnvrtgirqsrlpasnt 797
Cdd:cd01385        --------------------------------------------------------------------------------
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  798 slldkdgifahsasskllerahgiltrnknfrskpvlpkhllevnslkhltRLTLQDRITKSLLHLHKKKKPPSISAQFQ 877
Cdd:cd01385    553 ---------------------------------------------------SLTLHDRTTKSLLHLHKKKKPPSVSAQFQ 581
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  878 ASLSKLMETLGQAEPYFVKCIRSNAEKLPLRFSDALVLRQLRYTGMLETVRIRQSGYSSKYSFQDFVSHFHVLLPQHIIP 957
Cdd:cd01385    582 TSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVLLPKGLIS 661
                          810       820
                   ....*....|....*....|....*....
gi 1907198218  958 SKFNIQDFFRKININSDNYQVGKTMVFLK 986
Cdd:cd01385    662 SKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
RhoGAP_myosin_IX cd04377
RhoGAP_myosin_IX: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
2115-2300 2.68e-114

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: 360.21  E-value: 2.68e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2115 FGVELSRLTSEDRAVPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDAESVNLDDYNIHVIASVFKQWLRD 2194
Cdd:cd04377      1 FGVSLSSLTSEDRSVPLVLEKLLEHIEMHGLYTEGIYRKSGSANKIKELRQGLDTDPDSVNLEDYPIHVITSVLKQWLRE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2195 LPNPLMTFELYEEFLRAMGLQERKETIRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEDTNRMSANALAIVFAPCILRC 2274
Cdd:cd04377     81 LPEPLMTFELYENFLRAMELEEKQERVRALYSVLEQLPRANLNTLERLIFHLVRVALQEEVNRMSANALAIVFAPCILRC 160
                          170       180
                   ....*....|....*....|....*.
gi 1907198218 2275 PDTTDPLQSVQDISKTTTCVELIVVE 2300
Cdd:cd04377    161 PDTADPLQSLQDVSKTTTCVETLIKE 186
RA_Myosin-IXa cd17216
Ras-associating (RA) domain found in Myosin-IXa; Myosin-IXa, also termed myosin-9a (Myo9a), is ...
15-110 2.90e-68

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


:

Pssm-ID: 340736  Cd Length: 96  Bit Score: 224.81  E-value: 2.90e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218   15 EHTLRIYPGTISEGTIYCPIPARKNSTAAEVIDSLINRLHLDKTKCYVLAEVKEFGGEEWILNPTDCPVQRMMLWPRMAL 94
Cdd:cd17216      1 EFTLRIYPGNIAEGTIYCPVPARKNTTAAEVIESLINKLQLDKTKCYVLAEVKEFGGEEWILNPTDCPVQRMMLWPRMAL 80
                           90
                   ....*....|....*.
gi 1907198218   95 ENRLSGEDYRFLLREK 110
Cdd:cd17216     81 ENRFSGEDYRFLLREK 96
C1_Myosin-IXa cd20883
protein kinase C conserved region 1 (C1 domain) found in unconventional myosin-IXa and similar ...
2049-2106 4.64e-40

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: 142.80  E-value: 4.64e-40
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907198218 2049 EEHNGHIFKATQYSIPTYCEYCSSLIWIMDRASVCKLCKYACHKKCCLKTTAKCSKKY 2106
Cdd:cd20883      1 EEHNGHIFKSTQYSIPTYCEYCSSLIWMMDRAYVCKLCRYACHKKCCLKTTTKCSKKY 58
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
1097-1118 2.28e-06

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


:

Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 45.78  E-value: 2.28e-06
                            10        20
                    ....*....|....*....|..
gi 1907198218  1097 RHKAATCIQSRWRGYRQRKKYK 1118
Cdd:smart00015    2 LTRAAIIIQAAWRGYLARKRYK 23
 
Name Accession Description Interval E-value
MYSc_Myo9 cd01385
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ...
160-986 0e+00

class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play a role in signalling. It has a N-terminal RA domain, an IQ domain, a C1_1 domain, and a RhoGAP domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276836 [Multi-domain]  Cd Length: 690  Bit Score: 1315.06  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  160 KTLLENLRNRFKHEKIYTYVGSILIAINPFKFLPIYNPKYVKMYDNHQLGKLEPHIYAVADVAYHAMLQRKKNQCIVISG 239
Cdd:cd01385      1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  240 ESGSGKTQSTNFLIHHLTALSQKGFASGVEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQETGTVLGAYVEKYL 319
Cdd:cd01385     81 ESGSGKTESTNFLLHHLTALSQKGYGSGVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVEKYL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  320 LEKSRLVYQEHNERNYHVFYYLLAGASEEERLAFHLKQPEEYHFLNQ-DCFTVEGEDLRHDFERLQLAMEMVGFLPKTRR 398
Cdd:cd01385    161 LEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNQsDCYTLEGEDEKYEFERLKQAMEMVGFLPETQR 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  399 QIFSLLSAILHLGNISYKKKTY-RDDSIDICNPEVLPIVSELLEVKEEMLFEALVTRKTVTVGEKLILPYKLAEAVTVRN 477
Cdd:cd01385    241 QIFSVLSAVLHLGNIEYKKKAYhRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLILPYKLPEAIATRD 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  478 SMAKSLYSALFDWIVFRINHALLNSKDLEQDtKTLSIGVLDIFGFEDYENNSFEQFCINFANERLQHYFNQHIFKLEQEE 557
Cdd:cd01385    321 AMAKCLYSALFDWIVLRINHALLNKKDLEEA-KGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIFKLEQEE 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  558 YRTEGISWHNIDYIDNTCCINLISKKPTGLLHLLDEESNFPQATNQTLLDKFKHQHEENSYIEFPAVMEPAFIIKHYAGK 637
Cdd:cd01385    400 YKKEGISWHNIEYTDNTGCLQLISKKPTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNKYYEKPQVMEPAFIIAHYAGK 479
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  638 VKYGVKDFREKNTDHMRPDIVALLRSSRNAFVSGMTGIDPVAVFRWAVLRAFFRAVVAFREAGKRHIQRKSGHddttpca 717
Cdd:cd01385    480 VKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVRELIGIDPVAVFRWAVLRAFFRAMAAFREAGRRRAQRTAGH------- 552
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  718 ilksmdsfsflqhpvhqrsleilqrckeekysitrknprtplsdlqgmntlneknqhdtfdiawnvrtgirqsrlpasnt 797
Cdd:cd01385        --------------------------------------------------------------------------------
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  798 slldkdgifahsasskllerahgiltrnknfrskpvlpkhllevnslkhltRLTLQDRITKSLLHLHKKKKPPSISAQFQ 877
Cdd:cd01385    553 ---------------------------------------------------SLTLHDRTTKSLLHLHKKKKPPSVSAQFQ 581
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  878 ASLSKLMETLGQAEPYFVKCIRSNAEKLPLRFSDALVLRQLRYTGMLETVRIRQSGYSSKYSFQDFVSHFHVLLPQHIIP 957
Cdd:cd01385    582 TSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVLLPKGLIS 661
                          810       820
                   ....*....|....*....|....*....
gi 1907198218  958 SKFNIQDFFRKININSDNYQVGKTMVFLK 986
Cdd:cd01385    662 SKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
MYSc smart00242
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...
143-996 0e+00

Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical interaction between myosin and actin. The core of the myosin structure is similar in fold to that of kinesin.


Pssm-ID: 214580 [Multi-domain]  Cd Length: 677  Bit Score: 846.06  E-value: 0e+00
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218   143 PQQKDFDDLCSLPDLNEKTLLENLRNRFKHEKIYTYVGSILIAINPFKFLPIYNPKYVKMYDNHQLGKLEPHIYAVADVA 222
Cdd:smart00242    3 PKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIADNA 82
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218   223 YHAMLQRKKNQCIVISGESGSGKTQSTNFLIHHLTALS-QKGFASGVEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQ 301
Cdd:smart00242   83 YRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSgSNTEVGSVEDQILESNPILEAFGNAKTLRNNNSSRFGKFIE 162
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218   302 VNYQETGTVLGAYVEKYLLEKSRLVYQEHNERNYHVFYYLLAGASEEERLAFHLKQPEEYHFLNQ-DCFTVEGEDLRHDF 380
Cdd:smart00242  163 IHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQgGCLTVDGIDDAEEF 242
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218   381 ERLQLAMEMVGFLPKTRRQIFSLLSAILHLGNISYKKKTYRDDSIDICNPEVLPIVSELLEVKEEMLFEALVTRKTVTVG 460
Cdd:smart00242  243 KETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKEELSNAAELLGVDPEELEKALTKRKIKTGG 322
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218   461 EKLILPYKLAEAVTVRNSMAKSLYSALFDWIVFRINHALLNskdleQDTKTLSIGVLDIFGFEDYENNSFEQFCINFANE 540
Cdd:smart00242  323 EVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSF-----KDGSTYFIGVLDIYGFEIFEVNSFEQLCINYANE 397
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218   541 RLQHYFNQHIFKLEQEEYRTEGISWHNIDYIDNTCCINLISKKPTGLLHLLDEESNFPQATNQTLLDKFKHQHEENSYIE 620
Cdd:smart00242  398 KLQQFFNQHVFKLEQEEYEREGIDWTFIDFFDNQDCIDLIEKKPPGILSLLDEECRFPKGTDQTFLEKLNQHHKKHPHFS 477
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218   621 FPAVM-EPAFIIKHYAGKVKYGVKDFREKNTDHMRPDIVALLRSSRNAFVSGMtgidpvavfrwavlraffravvafrea 699
Cdd:smart00242  478 KPKKKgRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASL--------------------------- 530
                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218   700 gkrhiqrksghddttpcailksmdsfsflqhpvhqrsleilqrckeekysitrknprtplsdlqgmntlneknqhdtfdi 779
Cdd:smart00242      --------------------------------------------------------------------------------
                           650       660       670       680       690       700       710       720
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218   780 awnvrtgirqsrlpasntslldkdgiFAHSASSKllerahgiltrnknfrskpvlpkhllevnslkhltrltlqdritks 859
Cdd:smart00242  531 --------------------------FPSGVSNA---------------------------------------------- 538
                           730       740       750       760       770       780       790       800
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218   860 llhlHKKKKPPSISAQFQASLSKLMETLGQAEPYFVKCIRSNAEKLPLRFSDALVLRQLRYTGMLETVRIRQSGYSSKYS 939
Cdd:smart00242  539 ----GSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLP 614
                           810       820       830       840       850       860
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907198218   940 FQDFVSHFHVLLPQHIIP----SKFNIQDFFRKININSDNYQVGKTMVFLKEHERQHLQDL 996
Cdd:smart00242  615 FDEFLQRYRVLLPDTWPPwggdAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEEL 675
Myosin_head pfam00063
Myosin head (motor domain);
149-986 0e+00

Myosin head (motor domain);


Pssm-ID: 395017 [Multi-domain]  Cd Length: 674  Bit Score: 665.52  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  149 DDLCSLPDLNEKTLLENLRNRFKHEKIYTYVGSILIAINPFKFLPIYNPKYVKMYDNHQLGKLEPHIYAVADVAYHAMLQ 228
Cdd:pfam00063    2 EDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSMLQ 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  229 RKKNQCIVISGESGSGKTQSTNFLIHHLTALSQKGFASG---VEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQ 305
Cdd:pfam00063   82 DKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGNvgrLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQFD 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  306 ETGTVLGAYVEKYLLEKSRLVYQEHNERNYHVFYYLLAGASEEERLAFHLKQPEEYHFLNQD-CFTVEGEDLRHDFERLQ 384
Cdd:pfam00063  162 AKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQSgCYTIDGIDDSEEFKITD 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  385 LAMEMVGFLPKTRRQIFSLLSAILHLGNISYKKKTYRDDSIDICNpEVLPIVSELLEVKEEMLFEALVTRKTVTVGEKLI 464
Cdd:pfam00063  242 KAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDT-ENLQKAASLLGIDSTELEKALCKRRIKTGRETVS 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  465 LPYKLAEAVTVRNSMAKSLYSALFDWIVFRINHALlnskDLEQDTKTLSIGVLDIFGFEDYENNSFEQFCINFANERLQH 544
Cdd:pfam00063  321 KPQNVEQANYARDALAKAIYSRLFDWLVDRINKSL----DVKTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQ 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  545 YFNQHIFKLEQEEYRTEGISWHNIDYIDNTCCINLISKKPTGLLHLLDEESNFPQATNQTLLDKFKHQHEENSYIEFPAV 624
Cdd:pfam00063  397 FFNHHMFKLEQEEYVREGIEWTFIDFGDNQPCIDLIEKKPLGILSLLDEECLFPKATDQTFLDKLYSTFSKHPHFQKPRL 476
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  625 M-EPAFIIKHYAGKVKYGVKDFREKNTDHMRPDIVALLRSSRNAFVSGMtgidpvavfrwavlraffravvaFREAGKrh 703
Cdd:pfam00063  477 QgETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAEL-----------------------FPDYET-- 531
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  704 iqrksghddttpcailksmdsfsflqhpvhqrsleilqrckeekysitrknprtplsdlQGMNTLNEKNQHDTFDIawnv 783
Cdd:pfam00063  532 -----------------------------------------------------------AESAAANESGKSTPKRT---- 548
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  784 rtgirqsrlpasntslldkdgifahsasskllerahgiltrnknfrskpvlpkhllevnslkhltrltlqdritksllhl 863
Cdd:pfam00063      --------------------------------------------------------------------------------
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  864 hKKKKPPSISAQFQASLSKLMETLGQAEPYFVKCIRSNAEKLPLRFSDALVLRQLRYTGMLETVRIRQSGYSSKYSFQDF 943
Cdd:pfam00063  549 -KKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEF 627
                          810       820       830       840
                   ....*....|....*....|....*....|....*....|....*..
gi 1907198218  944 VSHFHVLLPQHI----IPSKFNIQDFFRKININSDNYQVGKTMVFLK 986
Cdd:pfam00063  628 VQRYRILAPKTWpkwkGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
COG5022 COG5022
Myosin heavy chain [General function prediction only];
143-1261 0e+00

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 646.75  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  143 PQQKDFDDLCSLPDLNEKTLLENLRNRFKHEKIYTYVGSILIAINPFKFLPIYNPKYVKMYDNHQLGKLEPHIYAVADVA 222
Cdd:COG5022     63 PKFDGVDDLTELSYLNEPAVLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEA 142
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  223 YHAMLQRKKNQCIVISGESGSGKTQSTNFLIHHLTAL--SQKGFASGVEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFI 300
Cdd:COG5022    143 YRNLLSEKENQTIIISGESGAGKTENAKRIMQYLASVtsSSTVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYI 222
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  301 QVNYQETGTVLGAYVEKYLLEKSRLVYQEHNERNYHVFYYLLAGASEEERLAFHLKQPEEYHFLNQ-DCFTVEGEDLRHD 379
Cdd:COG5022    223 KIEFDENGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQgGCDKIDGIDDAKE 302
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  380 FERLQLAMEMVGFLPKTRRQIFSLLSAILHLGNISYKKKtyRDDSIDICNPEVLPIVSELLEVKEEMLFEALVTRKTVTV 459
Cdd:COG5022    303 FKITLDALKTIGIDEEEQDQIFKILAAILHIGNIEFKED--RNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTG 380
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  460 GEKLILPYKLAEAVTVRNSMAKSLYSALFDWIVFRINHALLNSKDLEQdtktlSIGVLDIFGFEDYENNSFEQFCINFAN 539
Cdd:COG5022    381 GEWIVVPLNLEQALAIRDSLAKALYSNLFDWIVDRINKSLDHSAAASN-----FIGVLDIYGFEIFEKNSFEQLCINYTN 455
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  540 ERLQHYFNQHIFKLEQEEYRTEGISWHNIDYIDNTCCINLISKK-PTGLLHLLDEESNFPQATNQTLLDKFKHQ--HEEN 616
Cdd:COG5022    456 EKLQQFFNQHMFKLEQEEYVKEGIEWSFIDYFDNQPCIDLIEKKnPLGILSLLDEECVMPHATDESFTSKLAQRlnKNSN 535
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  617 SYIEFPAVMEPAFIIKHYAGKVKYGVKDFREKNTDHMRPDIVALLRSSRNAFVSgmtgidpvavfrwavlraffravvaf 696
Cdd:COG5022    536 PKFKKSRFRDNKFVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVS-------------------------- 589
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  697 reagkrhiqrksghddttpcailksmdsfsflqhpvhqrsleilqrckeekysitrknprtplsdlqgmntlneknqhdt 776
Cdd:COG5022        --------------------------------------------------------------------------------
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  777 fdiawnvrtgirqsrlpasntSLLDKdgifahsasskllerahgilTRNKNfrskpvlpkhllevnslkhltrltlqdri 856
Cdd:COG5022    590 ---------------------TLFDD--------------------EENIE----------------------------- 599
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  857 tksllhlhKKKKPPSISAQFQASLSKLMETLGQAEPYFVKCIRSNAEKLPLRFSDALVLRQLRYTGMLETVRIRQSGYSS 936
Cdd:COG5022    600 --------SKGRFPTLGSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPS 671
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  937 KYSFQDFVSHFHVLLPQHI--------IPSKFNIQDFFRKININSDNYQVGKTMVFLKEHERQHLQDLLHQEVLRRIVLL 1008
Cdd:COG5022    672 RWTFDEFVQRYRILSPSKSwtgeytwkEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRI 751
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 1009 QRWFRVLLSRQQFLHLRQasiiIQRFWRNYLNQKQVRNaavEKDAFIMASAASLLQASWRAHLERQRYLELRAAAVIIQQ 1088
Cdd:COG5022    752 QRAIRGRYLRRRYLQALK----RIKKIQVIQHGFRLRR---LVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQK 824
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 1089 R-WRELYRC-------RHKAATCIQSRWRGYRQRKKYKEQRNKIILLQSIYRGFRARQRcnaLKEEKLREAKLEHglvhv 1160
Cdd:COG5022    825 TiKREKKLReteevefSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQ---LQELKIDVKSISS----- 896
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 1161 kacgpLEIQGSDpSEWEDRSFDNRVKAIEECKYVIESNRISRE----SSMDFsKESPDKQQERgRRQSGTDLQEDVIVRQ 1236
Cdd:COG5022    897 -----LKLVNLE-LESEIIELKKSLSSDLIENLEFKTELIARLkkllNNIDL-EEGPSIEYVK-LPELNKLHEVESKLKE 968
                         1130      1140
                   ....*....|....*....|....*
gi 1907198218 1237 RPKSLEDLHqKKVGRAKRESRRMRE 1261
Cdd:COG5022    969 TSEEYEDLL-KKSTILVREGNKANS 992
PTZ00014 PTZ00014
myosin-A; Provisional
148-1046 2.86e-122

myosin-A; Provisional


Pssm-ID: 240229 [Multi-domain]  Cd Length: 821  Bit Score: 408.26  E-value: 2.86e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  148 FDDLCSLPDLNEKTLLENLRNRFKHEKIYTYVGSILIAINPFKFLPIYNPKYVKMY-DNHQLGKLEPHIYAVADVAYHAM 226
Cdd:PTZ00014    98 YGDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYrDAKDSDKLPPHVFTTARRALENL 177
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  227 LQRKKNQCIVISGESGSGKTQSTNFLIHHLTALSQKGFASGVEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQE 306
Cdd:PTZ00014   178 HGVKKSQTIIVSGESGAGKTEATKQIMRYFASSKSGNMDLKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGE 257
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  307 TGTVLGAYVEKYLLEKSRLVYQEHNERNYHVFYYLLAGASEEERLAFHLKQPEEYHFLNQDCFTVEGEDLRHDFERLQLA 386
Cdd:PTZ00014   258 EGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPKCLDVPGIDDVKDFEEVMES 337
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  387 MEMVGFLPKTRRQIFSLLSAILHLGNISYKKKTyrDDSIDIC------NPEVLPIVSELLEVKEEMLFEALVTRKTVTVG 460
Cdd:PTZ00014   338 FDSMGLSESQIEDIFSILSGVLLLGNVEIEGKE--EGGLTDAaaisdeSLEVFNEACELLFLDYESLKKELTVKVTYAGN 415
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  461 EKLILPYKLAEAVTVRNSMAKSLYSALFDWIVFRINHALLNSKDLEqdtktLSIGVLDIFGFEDYENNSFEQFCINFANE 540
Cdd:PTZ00014   416 QKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFK-----VFIGMLDIFGFEVFKNNSLEQLFINITNE 490
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  541 RLQHYFNQHIFKLEQEEYRTEGISWHNIDYIDNTCCINLISKKPTGLLHLLDEESNFPQATNQTLLDKFKHQHEENS-YI 619
Cdd:PTZ00014   491 MLQKNFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGKSVLSILEDQCLAPGGTDEKFVSSCNTNLKNNPkYK 570
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  620 EFPAVMEPAFIIKHYAGKVKYGVKDFREKNTDHMRPDIVALLRSSRNAFVSGMtgidpvavfrwavlrafFRAVVAfrEA 699
Cdd:PTZ00014   571 PAKVDSNKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDL-----------------FEGVEV--EK 631
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  700 GKrhiqrksghddttpcailksmdsfsflqhpvhqrsleilqrckeekysitrknprtplsdlqgmntlneknqhdtfdi 779
Cdd:PTZ00014   632 GK------------------------------------------------------------------------------ 633
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  780 awnvrtgirqsrlpasntslldkdgifahsasskllerahgiltrnknfrskpvlpkhllevnslkhltrltlqdrITKS 859
Cdd:PTZ00014   634 ----------------------------------------------------------------------------LAKG 637
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  860 LLhlhkkkkppsISAQFQASLSKLMETLGQAEPYFVKCIRSNAEKLPLRFSDALVLRQLRYTGMLETVRIRQSGYSSKYS 939
Cdd:PTZ00014   638 QL----------IGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRT 707
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  940 FQDFVSHFHVL-LPQHIIPS---KFNIQDFFRKININSDNYQVGKTMVFLKEHERQHLQDLLhQEVLRR----IVLLQRW 1011
Cdd:PTZ00014   708 FAEFLSQFKYLdLAVSNDSSldpKEKAEKLLERSGLPKDSYAIGKTMVFLKKDAAKELTQIQ-REKLAAweplVSVLEAL 786
                          890       900       910
                   ....*....|....*....|....*....|....*
gi 1907198218 1012 FRVLLSRQQFLHLRQASIIIQRFWRNYLNQKQVRN 1046
Cdd:PTZ00014   787 ILKIKKKRKVRKNIKSLVRIQAHLRRHLVIAEIKP 821
RhoGAP_myosin_IX cd04377
RhoGAP_myosin_IX: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
2115-2300 2.68e-114

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: 360.21  E-value: 2.68e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2115 FGVELSRLTSEDRAVPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDAESVNLDDYNIHVIASVFKQWLRD 2194
Cdd:cd04377      1 FGVSLSSLTSEDRSVPLVLEKLLEHIEMHGLYTEGIYRKSGSANKIKELRQGLDTDPDSVNLEDYPIHVITSVLKQWLRE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2195 LPNPLMTFELYEEFLRAMGLQERKETIRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEDTNRMSANALAIVFAPCILRC 2274
Cdd:cd04377     81 LPEPLMTFELYENFLRAMELEEKQERVRALYSVLEQLPRANLNTLERLIFHLVRVALQEEVNRMSANALAIVFAPCILRC 160
                          170       180
                   ....*....|....*....|....*.
gi 1907198218 2275 PDTTDPLQSVQDISKTTTCVELIVVE 2300
Cdd:cd04377    161 PDTADPLQSLQDVSKTTTCVETLIKE 186
RA_Myosin-IXa cd17216
Ras-associating (RA) domain found in Myosin-IXa; Myosin-IXa, also termed myosin-9a (Myo9a), is ...
15-110 2.90e-68

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


Pssm-ID: 340736  Cd Length: 96  Bit Score: 224.81  E-value: 2.90e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218   15 EHTLRIYPGTISEGTIYCPIPARKNSTAAEVIDSLINRLHLDKTKCYVLAEVKEFGGEEWILNPTDCPVQRMMLWPRMAL 94
Cdd:cd17216      1 EFTLRIYPGNIAEGTIYCPVPARKNTTAAEVIESLINKLQLDKTKCYVLAEVKEFGGEEWILNPTDCPVQRMMLWPRMAL 80
                           90
                   ....*....|....*.
gi 1907198218   95 ENRLSGEDYRFLLREK 110
Cdd:cd17216     81 ENRFSGEDYRFLLREK 96
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
2129-2301 4.97e-62

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: 210.20  E-value: 4.97e-62
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  2129 VPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDAE-SVNLDDYNIHVIASVFKQWLRDLPNPLMTFELYEE 2207
Cdd:smart00324    3 IPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDpDLDLSEYDVHDVAGLLKLFLRELPEPLITYELYEE 82
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  2208 FLRAMGLQERKETIRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEDTNRMSANALAIVFAPCILRCPDTTDPlqSVQDI 2287
Cdd:smart00324   83 FIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGEVA--SLKDI 160
                           170
                    ....*....|....
gi 1907198218  2288 SKTTTCVELIVVEQ 2301
Cdd:smart00324  161 RHQNTVIEFLIENA 174
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
2130-2276 5.24e-59

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 200.46  E-value: 5.24e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2130 PLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDAESV-NLDDYNIHVIASVFKQWLRDLPNPLMTFELYEEF 2208
Cdd:pfam00620    1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGPDVDlDLEEEDVHVVASLLKLFLRELPEPLLTFELYEEF 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907198218 2209 LRAMGLQERKETIRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEDTNRMSANALAIVFAPCILRCPD 2276
Cdd:pfam00620   81 IEAAKLPDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLLRPPD 148
C1_Myosin-IXa cd20883
protein kinase C conserved region 1 (C1 domain) found in unconventional myosin-IXa and similar ...
2049-2106 4.64e-40

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: 142.80  E-value: 4.64e-40
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907198218 2049 EEHNGHIFKATQYSIPTYCEYCSSLIWIMDRASVCKLCKYACHKKCCLKTTAKCSKKY 2106
Cdd:cd20883      1 EEHNGHIFKSTQYSIPTYCEYCSSLIWMMDRAYVCKLCRYACHKKCCLKTTTKCSKKY 58
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
16-111 3.39e-21

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


Pssm-ID: 425871  Cd Length: 93  Bit Score: 90.08  E-value: 3.39e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218   16 HTLRIYPGTISEGTIYCPIPARKNSTAAEVIDSLINRLHL-DKTKCYVLAEVKEFGGEEWILNPTDCPVQRMMLWPRmal 94
Cdd:pfam00788    3 GVLKVYTEDGKPGTTYKTILVSSSTTAEEVIEALLEKFGLeDDPRDYVLVEVLERGGGERRLPDDECPLQIQLQWPR--- 79
                           90
                   ....*....|....*..
gi 1907198218   95 enrlSGEDYRFLLREKN 111
Cdd:pfam00788   80 ----DASDSRFLLRKRD 92
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
15-111 2.91e-18

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


Pssm-ID: 214612  Cd Length: 90  Bit Score: 81.58  E-value: 2.91e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218    15 EHTLRIYPGTISEGTiYCPIPARKNSTAAEVIDSLINRLHLDKT-KCYVLAEVKEfGGEEWILNPTDCPVQRMMLWPRma 93
Cdd:smart00314    2 TFVLRVYVDDLPGGT-YKTLRVSSRTTARDVIQQLLEKFHLTDDpEEYVLVEVLP-DGKERVLPDDENPLQLQKLWPR-- 77
                            90
                    ....*....|....*...
gi 1907198218    94 lenrlSGEDYRFLLREKN 111
Cdd:smart00314   78 -----RGPNLRFVLRKRD 90
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
2054-2102 2.22e-12

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


Pssm-ID: 197519  Cd Length: 50  Bit Score: 63.64  E-value: 2.22e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 1907198218  2054 HIFKATQYSIPTYCEYCSSLIWIMDRASV-CKLCKYACHKKCCLKTTAKC 2102
Cdd:smart00109    1 HKHVFRTFTKPTFCCVCRKSIWGSFKQGLrCSECKVKCHKKCADKVPKAC 50
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
2054-2102 8.93e-10

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: 56.30  E-value: 8.93e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2054 HIFKATQYSIPTYCEYCSSLIWIMDRASV-CKLCKYACHKKCCLKTTAKC 2102
Cdd:pfam00130    1 HHFVHRNFKQPTFCDHCGEFLWGLGKQGLkCSWCKLNVHKRCHEKVPPEC 50
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
1097-1118 2.28e-06

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


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 45.78  E-value: 2.28e-06
                            10        20
                    ....*....|....*....|..
gi 1907198218  1097 RHKAATCIQSRWRGYRQRKKYK 1118
Cdd:smart00015    2 LTRAAIIIQAAWRGYLARKRYK 23
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
1098-1118 3.41e-05

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 459869  Cd Length: 21  Bit Score: 42.69  E-value: 3.41e-05
                           10        20
                   ....*....|....*....|.
gi 1907198218 1098 HKAATCIQSRWRGYRQRKKYK 1118
Cdd:pfam00612    1 RKAAIKIQAAWRGYLARKRYK 21
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
1097-1123 9.13e-04

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


Pssm-ID: 467745 [Multi-domain]  Cd Length: 37  Bit Score: 38.68  E-value: 9.13e-04
                           10        20
                   ....*....|....*....|....*..
gi 1907198218 1097 RHKAATCIQSRWRGYRQRKKYKEQRNK 1123
Cdd:cd23767      8 MNRAATLIQALWRGYKVRKELKKKKKK 34
 
Name Accession Description Interval E-value
MYSc_Myo9 cd01385
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ...
160-986 0e+00

class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play a role in signalling. It has a N-terminal RA domain, an IQ domain, a C1_1 domain, and a RhoGAP domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276836 [Multi-domain]  Cd Length: 690  Bit Score: 1315.06  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  160 KTLLENLRNRFKHEKIYTYVGSILIAINPFKFLPIYNPKYVKMYDNHQLGKLEPHIYAVADVAYHAMLQRKKNQCIVISG 239
Cdd:cd01385      1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  240 ESGSGKTQSTNFLIHHLTALSQKGFASGVEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQETGTVLGAYVEKYL 319
Cdd:cd01385     81 ESGSGKTESTNFLLHHLTALSQKGYGSGVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVEKYL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  320 LEKSRLVYQEHNERNYHVFYYLLAGASEEERLAFHLKQPEEYHFLNQ-DCFTVEGEDLRHDFERLQLAMEMVGFLPKTRR 398
Cdd:cd01385    161 LEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNQsDCYTLEGEDEKYEFERLKQAMEMVGFLPETQR 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  399 QIFSLLSAILHLGNISYKKKTY-RDDSIDICNPEVLPIVSELLEVKEEMLFEALVTRKTVTVGEKLILPYKLAEAVTVRN 477
Cdd:cd01385    241 QIFSVLSAVLHLGNIEYKKKAYhRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLILPYKLPEAIATRD 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  478 SMAKSLYSALFDWIVFRINHALLNSKDLEQDtKTLSIGVLDIFGFEDYENNSFEQFCINFANERLQHYFNQHIFKLEQEE 557
Cdd:cd01385    321 AMAKCLYSALFDWIVLRINHALLNKKDLEEA-KGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIFKLEQEE 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  558 YRTEGISWHNIDYIDNTCCINLISKKPTGLLHLLDEESNFPQATNQTLLDKFKHQHEENSYIEFPAVMEPAFIIKHYAGK 637
Cdd:cd01385    400 YKKEGISWHNIEYTDNTGCLQLISKKPTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNKYYEKPQVMEPAFIIAHYAGK 479
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  638 VKYGVKDFREKNTDHMRPDIVALLRSSRNAFVSGMTGIDPVAVFRWAVLRAFFRAVVAFREAGKRHIQRKSGHddttpca 717
Cdd:cd01385    480 VKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVRELIGIDPVAVFRWAVLRAFFRAMAAFREAGRRRAQRTAGH------- 552
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  718 ilksmdsfsflqhpvhqrsleilqrckeekysitrknprtplsdlqgmntlneknqhdtfdiawnvrtgirqsrlpasnt 797
Cdd:cd01385        --------------------------------------------------------------------------------
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  798 slldkdgifahsasskllerahgiltrnknfrskpvlpkhllevnslkhltRLTLQDRITKSLLHLHKKKKPPSISAQFQ 877
Cdd:cd01385    553 ---------------------------------------------------SLTLHDRTTKSLLHLHKKKKPPSVSAQFQ 581
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  878 ASLSKLMETLGQAEPYFVKCIRSNAEKLPLRFSDALVLRQLRYTGMLETVRIRQSGYSSKYSFQDFVSHFHVLLPQHIIP 957
Cdd:cd01385    582 TSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVLLPKGLIS 661
                          810       820
                   ....*....|....*....|....*....
gi 1907198218  958 SKFNIQDFFRKININSDNYQVGKTMVFLK 986
Cdd:cd01385    662 SKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
MYSc smart00242
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...
143-996 0e+00

Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical interaction between myosin and actin. The core of the myosin structure is similar in fold to that of kinesin.


Pssm-ID: 214580 [Multi-domain]  Cd Length: 677  Bit Score: 846.06  E-value: 0e+00
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218   143 PQQKDFDDLCSLPDLNEKTLLENLRNRFKHEKIYTYVGSILIAINPFKFLPIYNPKYVKMYDNHQLGKLEPHIYAVADVA 222
Cdd:smart00242    3 PKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIADNA 82
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218   223 YHAMLQRKKNQCIVISGESGSGKTQSTNFLIHHLTALS-QKGFASGVEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQ 301
Cdd:smart00242   83 YRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSgSNTEVGSVEDQILESNPILEAFGNAKTLRNNNSSRFGKFIE 162
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218   302 VNYQETGTVLGAYVEKYLLEKSRLVYQEHNERNYHVFYYLLAGASEEERLAFHLKQPEEYHFLNQ-DCFTVEGEDLRHDF 380
Cdd:smart00242  163 IHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQgGCLTVDGIDDAEEF 242
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218   381 ERLQLAMEMVGFLPKTRRQIFSLLSAILHLGNISYKKKTYRDDSIDICNPEVLPIVSELLEVKEEMLFEALVTRKTVTVG 460
Cdd:smart00242  243 KETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKEELSNAAELLGVDPEELEKALTKRKIKTGG 322
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218   461 EKLILPYKLAEAVTVRNSMAKSLYSALFDWIVFRINHALLNskdleQDTKTLSIGVLDIFGFEDYENNSFEQFCINFANE 540
Cdd:smart00242  323 EVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSF-----KDGSTYFIGVLDIYGFEIFEVNSFEQLCINYANE 397
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218   541 RLQHYFNQHIFKLEQEEYRTEGISWHNIDYIDNTCCINLISKKPTGLLHLLDEESNFPQATNQTLLDKFKHQHEENSYIE 620
Cdd:smart00242  398 KLQQFFNQHVFKLEQEEYEREGIDWTFIDFFDNQDCIDLIEKKPPGILSLLDEECRFPKGTDQTFLEKLNQHHKKHPHFS 477
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218   621 FPAVM-EPAFIIKHYAGKVKYGVKDFREKNTDHMRPDIVALLRSSRNAFVSGMtgidpvavfrwavlraffravvafrea 699
Cdd:smart00242  478 KPKKKgRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASL--------------------------- 530
                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218   700 gkrhiqrksghddttpcailksmdsfsflqhpvhqrsleilqrckeekysitrknprtplsdlqgmntlneknqhdtfdi 779
Cdd:smart00242      --------------------------------------------------------------------------------
                           650       660       670       680       690       700       710       720
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218   780 awnvrtgirqsrlpasntslldkdgiFAHSASSKllerahgiltrnknfrskpvlpkhllevnslkhltrltlqdritks 859
Cdd:smart00242  531 --------------------------FPSGVSNA---------------------------------------------- 538
                           730       740       750       760       770       780       790       800
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218   860 llhlHKKKKPPSISAQFQASLSKLMETLGQAEPYFVKCIRSNAEKLPLRFSDALVLRQLRYTGMLETVRIRQSGYSSKYS 939
Cdd:smart00242  539 ----GSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLP 614
                           810       820       830       840       850       860
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907198218   940 FQDFVSHFHVLLPQHIIP----SKFNIQDFFRKININSDNYQVGKTMVFLKEHERQHLQDL 996
Cdd:smart00242  615 FDEFLQRYRVLLPDTWPPwggdAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEEL 675
MYSc cd00124
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ...
161-986 0e+00

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


Pssm-ID: 276950 [Multi-domain]  Cd Length: 633  Bit Score: 744.03  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  161 TLLENLRNRFKHEKIYTYVGSILIAINPFKFLPIYNPKYVKMYDNHQLGK-LEPHIYAVADVAYHAMLQRKKNQCIVISG 239
Cdd:cd00124      2 AILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSAdLPPHVFAVADAAYRAMLRDGQNQSILISG 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  240 ESGSGKTQSTNFLIHHLTALSQKGF------ASGVEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQETGTVLGA 313
Cdd:cd00124     82 ESGAGKTETTKLVLKYLAALSGSGSskssssASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLVGA 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  314 YVEKYLLEKSRLVYQEHNERNYHVFYYLLA----GASEEERLAFHLKQPEEYHFLNQ-DCFTVEGEDLRHDFERLQLAME 388
Cdd:cd00124    162 SIETYLLEKSRVVSQAPGERNFHIFYQLLAglsdGAREELKLELLLSYYYLNDYLNSsGCDRIDGVDDAEEFQELLDALD 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  389 MVGFLPKTRRQIFSLLSAILHLGNISY-KKKTYRDDSIDICNPEVLPIVSELLEVKEEMLFEALVTRKTVTVGEKLILPY 467
Cdd:cd00124    242 VLGFSDEEQDSIFRILAAILHLGNIEFeEDEEDEDSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETITKPL 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  468 KLAEAVTVRNSMAKSLYSALFDWIVFRINHALLNSKDleqDTKTLSIGVLDIFGFEDYENNSFEQFCINFANERLQHYFN 547
Cdd:cd00124    322 TVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDA---AESTSFIGILDIFGFENFEVNSFEQLCINYANEKLQQFFN 398
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  548 QHIFKLEQEEYRTEGISWHNIDYIDNTCCINLISKKPTGLLHLLDEESNFPQATNQTLLDKFKHQHEEN-SYIEFPAVME 626
Cdd:cd00124    399 QHVFKLEQEEYEEEGIDWSFIDFPDNQDCLDLIEGKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHpRFFSKKRKAK 478
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  627 PAFIIKHYAGKVKYGVKDFREKNTDHMRPDIVALLRSSrnafvsgmtgidpvavfrwavlrAFFRavvafreagkrhiqr 706
Cdd:cd00124    479 LEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSG-----------------------SQFR--------------- 520
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  707 ksghddttpcailksmdsfsflqhpvhqRSLEILqrckeekysitrknprtplsdlqgMNTLNeknqhdtfdiawnvrtg 786
Cdd:cd00124    521 ----------------------------SQLDAL------------------------MDTLN----------------- 531
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  787 irqsrlpasntslldkdgifahsasskllerahgiltrnknfrskpvlpkhllevnslkhltrltlqdritksllhlhkk 866
Cdd:cd00124        --------------------------------------------------------------------------------
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  867 kkppsisaqfqaslsklmetlgQAEPYFVKCIRSNAEKLPLRFSDALVLRQLRYTGMLETVRIRQSGYSSKYSFQDFVSH 946
Cdd:cd00124    532 ----------------------STQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKR 589
                          810       820       830       840
                   ....*....|....*....|....*....|....*....|....
gi 1907198218  947 FHVLLPQHIIPSKFNIQDFF----RKININSDNYQVGKTMVFLK 986
Cdd:cd00124    590 YRILAPGATEKASDSKKAAVlallLLLKLDSSGYQLGKTKVFLR 633
MYSc_Myo7 cd01381
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ...
161-986 0e+00

class VII myosin, motor domain; These monomeric myosins have been associated with functions in sensory systems such as vision and hearing. Mammalian myosin VII has a tail with 2 MyTH4 domains, 2 FERM domains, and a SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276832  Cd Length: 648  Bit Score: 679.75  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  161 TLLENLRNRFKHEKIYTYVGSILIAINPFKFLPIYNPKYVKMYDNHQLGKLEPHIYAVADVAYHAMLQRKKNQCIVISGE 240
Cdd:cd01381      2 GILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISGE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  241 SGSGKTQSTNFLIHHLTALSqkGFASGVEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQETGTVLGAYVEKYLL 320
Cdd:cd01381     82 SGAGKTESTKLILQYLAAIS--GQHSWIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKIEQYLL 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  321 EKSRLVYQEHNERNYHVFYYLLAGASEEERLAFHLKQPEEYHFLNQ-DCFTVEGEDLRHDFERLQLAMEMVGFLPKTRRQ 399
Cdd:cd01381    160 EKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQgNCLTCEGRDDAAEFADIRSAMKVLMFTDEEIWD 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  400 IFSLLSAILHLGNISYKKKTYRD-DSIDICNPEVLPIVSELLEVKEEMLFEALVTRKTVTVGEKLILPYKLAEAVTVRNS 478
Cdd:cd01381    240 IFKLLAAILHLGNIKFEATVVDNlDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAEQALDVRDA 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  479 MAKSLYSALFDWIVFRINHALlnSKDLEQDTKTLSIGVLDIFGFEDYENNSFEQFCINFANERLQHYFNQHIFKLEQEEY 558
Cdd:cd01381    320 FVKGIYGRLFIWIVNKINSAI--YKPRGTDSSRTSIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFKLEQEEY 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  559 RTEGISWHNIDYIDNTCCINLISKKPTGLLHLLDEESNFPQATNQTLLDKFKHQHEENS-YIEFPAVMEPAFIIKHYAGK 637
Cdd:cd01381    398 DKEGINWQHIEFVDNQDVLDLIALKPMNIMSLIDEESKFPKGTDQTMLEKLHSTHGNNKnYLKPKSDLNTSFGINHFAGV 477
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  638 VKYGVKDFREKNTDHMRPDIVALLRSSRNAFVsgmtgidpvavfrwavlraffravvafreagkrhiqrksghddttpca 717
Cdd:cd01381    478 VFYDTRGFLEKNRDTFSADLLQLVQSSKNKFL------------------------------------------------ 509
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  718 ilksmdsfsflqhpvhqrsleilqrckeekysitrknprtplsdlqgmntlneknqhdtfdiawnvrtgirqsrlpasnt 797
Cdd:cd01381        --------------------------------------------------------------------------------
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  798 slldkDGIFAHsasskllERAHGILTRnknfrskpvlpkhllevnslkhltrltlqdritksllhlhkkKKPPSISAQFQ 877
Cdd:cd01381    510 -----KQLFNE-------DISMGSETR------------------------------------------KKSPTLSSQFR 535
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  878 ASLSKLMETLGQAEPYFVKCIRSNAEKLPLRFSDALVLRQLRYTGMLETVRIRQSGYSSKYSFQDFVSHFHVLLPQHIIP 957
Cdd:cd01381    536 KSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVPGIPPA 615
                          810       820       830
                   ....*....|....*....|....*....|...
gi 1907198218  958 SKFNIQDFFRKIN----INSDNYQVGKTMVFLK 986
Cdd:cd01381    616 HKTDCRAATRKICcavlGGDADYQLGKTKIFLK 648
Myosin_head pfam00063
Myosin head (motor domain);
149-986 0e+00

Myosin head (motor domain);


Pssm-ID: 395017 [Multi-domain]  Cd Length: 674  Bit Score: 665.52  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  149 DDLCSLPDLNEKTLLENLRNRFKHEKIYTYVGSILIAINPFKFLPIYNPKYVKMYDNHQLGKLEPHIYAVADVAYHAMLQ 228
Cdd:pfam00063    2 EDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSMLQ 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  229 RKKNQCIVISGESGSGKTQSTNFLIHHLTALSQKGFASG---VEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQ 305
Cdd:pfam00063   82 DKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGNvgrLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQFD 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  306 ETGTVLGAYVEKYLLEKSRLVYQEHNERNYHVFYYLLAGASEEERLAFHLKQPEEYHFLNQD-CFTVEGEDLRHDFERLQ 384
Cdd:pfam00063  162 AKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQSgCYTIDGIDDSEEFKITD 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  385 LAMEMVGFLPKTRRQIFSLLSAILHLGNISYKKKTYRDDSIDICNpEVLPIVSELLEVKEEMLFEALVTRKTVTVGEKLI 464
Cdd:pfam00063  242 KAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDT-ENLQKAASLLGIDSTELEKALCKRRIKTGRETVS 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  465 LPYKLAEAVTVRNSMAKSLYSALFDWIVFRINHALlnskDLEQDTKTLSIGVLDIFGFEDYENNSFEQFCINFANERLQH 544
Cdd:pfam00063  321 KPQNVEQANYARDALAKAIYSRLFDWLVDRINKSL----DVKTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQ 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  545 YFNQHIFKLEQEEYRTEGISWHNIDYIDNTCCINLISKKPTGLLHLLDEESNFPQATNQTLLDKFKHQHEENSYIEFPAV 624
Cdd:pfam00063  397 FFNHHMFKLEQEEYVREGIEWTFIDFGDNQPCIDLIEKKPLGILSLLDEECLFPKATDQTFLDKLYSTFSKHPHFQKPRL 476
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  625 M-EPAFIIKHYAGKVKYGVKDFREKNTDHMRPDIVALLRSSRNAFVSGMtgidpvavfrwavlraffravvaFREAGKrh 703
Cdd:pfam00063  477 QgETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAEL-----------------------FPDYET-- 531
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  704 iqrksghddttpcailksmdsfsflqhpvhqrsleilqrckeekysitrknprtplsdlQGMNTLNEKNQHDTFDIawnv 783
Cdd:pfam00063  532 -----------------------------------------------------------AESAAANESGKSTPKRT---- 548
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  784 rtgirqsrlpasntslldkdgifahsasskllerahgiltrnknfrskpvlpkhllevnslkhltrltlqdritksllhl 863
Cdd:pfam00063      --------------------------------------------------------------------------------
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  864 hKKKKPPSISAQFQASLSKLMETLGQAEPYFVKCIRSNAEKLPLRFSDALVLRQLRYTGMLETVRIRQSGYSSKYSFQDF 943
Cdd:pfam00063  549 -KKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEF 627
                          810       820       830       840
                   ....*....|....*....|....*....|....*....|....*..
gi 1907198218  944 VSHFHVLLPQHI----IPSKFNIQDFFRKININSDNYQVGKTMVFLK 986
Cdd:pfam00063  628 VQRYRILAPKTWpkwkGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
COG5022 COG5022
Myosin heavy chain [General function prediction only];
143-1261 0e+00

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 646.75  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  143 PQQKDFDDLCSLPDLNEKTLLENLRNRFKHEKIYTYVGSILIAINPFKFLPIYNPKYVKMYDNHQLGKLEPHIYAVADVA 222
Cdd:COG5022     63 PKFDGVDDLTELSYLNEPAVLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEA 142
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  223 YHAMLQRKKNQCIVISGESGSGKTQSTNFLIHHLTAL--SQKGFASGVEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFI 300
Cdd:COG5022    143 YRNLLSEKENQTIIISGESGAGKTENAKRIMQYLASVtsSSTVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYI 222
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  301 QVNYQETGTVLGAYVEKYLLEKSRLVYQEHNERNYHVFYYLLAGASEEERLAFHLKQPEEYHFLNQ-DCFTVEGEDLRHD 379
Cdd:COG5022    223 KIEFDENGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQgGCDKIDGIDDAKE 302
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  380 FERLQLAMEMVGFLPKTRRQIFSLLSAILHLGNISYKKKtyRDDSIDICNPEVLPIVSELLEVKEEMLFEALVTRKTVTV 459
Cdd:COG5022    303 FKITLDALKTIGIDEEEQDQIFKILAAILHIGNIEFKED--RNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTG 380
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  460 GEKLILPYKLAEAVTVRNSMAKSLYSALFDWIVFRINHALLNSKDLEQdtktlSIGVLDIFGFEDYENNSFEQFCINFAN 539
Cdd:COG5022    381 GEWIVVPLNLEQALAIRDSLAKALYSNLFDWIVDRINKSLDHSAAASN-----FIGVLDIYGFEIFEKNSFEQLCINYTN 455
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  540 ERLQHYFNQHIFKLEQEEYRTEGISWHNIDYIDNTCCINLISKK-PTGLLHLLDEESNFPQATNQTLLDKFKHQ--HEEN 616
Cdd:COG5022    456 EKLQQFFNQHMFKLEQEEYVKEGIEWSFIDYFDNQPCIDLIEKKnPLGILSLLDEECVMPHATDESFTSKLAQRlnKNSN 535
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  617 SYIEFPAVMEPAFIIKHYAGKVKYGVKDFREKNTDHMRPDIVALLRSSRNAFVSgmtgidpvavfrwavlraffravvaf 696
Cdd:COG5022    536 PKFKKSRFRDNKFVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVS-------------------------- 589
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  697 reagkrhiqrksghddttpcailksmdsfsflqhpvhqrsleilqrckeekysitrknprtplsdlqgmntlneknqhdt 776
Cdd:COG5022        --------------------------------------------------------------------------------
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  777 fdiawnvrtgirqsrlpasntSLLDKdgifahsasskllerahgilTRNKNfrskpvlpkhllevnslkhltrltlqdri 856
Cdd:COG5022    590 ---------------------TLFDD--------------------EENIE----------------------------- 599
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  857 tksllhlhKKKKPPSISAQFQASLSKLMETLGQAEPYFVKCIRSNAEKLPLRFSDALVLRQLRYTGMLETVRIRQSGYSS 936
Cdd:COG5022    600 --------SKGRFPTLGSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPS 671
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  937 KYSFQDFVSHFHVLLPQHI--------IPSKFNIQDFFRKININSDNYQVGKTMVFLKEHERQHLQDLLHQEVLRRIVLL 1008
Cdd:COG5022    672 RWTFDEFVQRYRILSPSKSwtgeytwkEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRI 751
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 1009 QRWFRVLLSRQQFLHLRQasiiIQRFWRNYLNQKQVRNaavEKDAFIMASAASLLQASWRAHLERQRYLELRAAAVIIQQ 1088
Cdd:COG5022    752 QRAIRGRYLRRRYLQALK----RIKKIQVIQHGFRLRR---LVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQK 824
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 1089 R-WRELYRC-------RHKAATCIQSRWRGYRQRKKYKEQRNKIILLQSIYRGFRARQRcnaLKEEKLREAKLEHglvhv 1160
Cdd:COG5022    825 TiKREKKLReteevefSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQ---LQELKIDVKSISS----- 896
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 1161 kacgpLEIQGSDpSEWEDRSFDNRVKAIEECKYVIESNRISRE----SSMDFsKESPDKQQERgRRQSGTDLQEDVIVRQ 1236
Cdd:COG5022    897 -----LKLVNLE-LESEIIELKKSLSSDLIENLEFKTELIARLkkllNNIDL-EEGPSIEYVK-LPELNKLHEVESKLKE 968
                         1130      1140
                   ....*....|....*....|....*
gi 1907198218 1237 RPKSLEDLHqKKVGRAKRESRRMRE 1261
Cdd:COG5022    969 TSEEYEDLL-KKSTILVREGNKANS 992
MYSc_Myo22 cd14883
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ...
161-986 0e+00

class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ motifs such as found in class V, VIII, XI, and XIII myosins. These myosins are defined by two tandem MyTH4 and FERM domains. The apicomplexan, but not diatom myosins contain 4-6 WD40 repeats near the end of the C-terminal tail which suggests a possible function of these myosins in signal transduction and transcriptional regulation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276849 [Multi-domain]  Cd Length: 661  Bit Score: 641.30  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  161 TLLENLRNRFKHEKIYTYVGSILIAINPFKFLPIYNPKYVKMYDNHQLGKLEPHIYAVADVAYHAMLQRKKNQCIVISGE 240
Cdd:cd14883      2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  241 SGSGKTQSTNFLIHHLTALSQKgfASGVEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQETGTVLGAYVEKYLL 320
Cdd:cd14883     82 SGAGKTETTKLILQYLCAVTNN--HSWVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGAIIQDYLL 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  321 EKSRLVYQEHNERNYHVFYYLLAGA--SEEERLAFHLKQPEEYHFLNQD-CFTVEGEDLRHDFERLQLAMEMVGFLPKTR 397
Cdd:cd14883    160 EQSRITFQAPGERNYHVFYQLLAGAkhSKELKEKLKLGEPEDYHYLNQSgCIRIDNINDKKDFDHLRLAMNVLGIPEEMQ 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  398 RQIFSLLSAILHLGNISYKK--KTYRDDSIDicNPEVLPIVSELLEVKEEMLFEALVTRKTVTVGEKLILPYKLAEAVTV 475
Cdd:cd14883    240 EGIFSVLSAILHLGNLTFEDidGETGALTVE--DKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQEARDN 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  476 RNSMAKSLYSALFDWIVFRINhallNSKDLEQDTKTLsIGVLDIFGFEDYENNSFEQFCINFANERLQHYFNQHIFKLEQ 555
Cdd:cd14883    318 RDAMAKALYSRTFAWLVNHIN----SCTNPGQKNSRF-IGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKLEQ 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  556 EEYRTEGISWHNIDYIDNTCCINLISKKPTGLLHLLDEESNFPQATNQTLLDKFKHQHEENSYIEFPAV--MEPAFIIKH 633
Cdd:cd14883    393 EEYEKEGINWSHIVFTDNQECLDLIEKPPLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEKPDRrrWKTEFGVKH 472
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  634 YAGKVKYGVKDFREKNTDHMRPDIVALLRSSRNAFVsgmtgidpvavfrwavlRAFFRavvafreagkrhiqrksghddt 713
Cdd:cd14883    473 YAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFV-----------------KELFT---------------------- 513
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  714 tpcailksmdsfsflqhpvhqrsleilqrckeekysitrknprtplsdlqgmntlneknqhdtfdiawnvrtgirqsrlp 793
Cdd:cd14883        --------------------------------------------------------------------------------
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  794 asntslldkdgifahsasskllerahgiltrnknfrskpvlPKHLLEVNSLKHLTRLTLQDRITksllhlhkKKKPPSIS 873
Cdd:cd14883    514 -----------------------------------------YPDLLALTGLSISLGGDTTSRGT--------SKGKPTVG 544
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  874 AQFQASLSKLMETLGQAEPYFVKCIRSNAEKLPLRFSDALVLRQLRYTGMLETVRIRQSGYSSKYSFQDFVSHFHVLLPQ 953
Cdd:cd14883    545 DTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPR 624
                          810       820       830
                   ....*....|....*....|....*....|....*..
gi 1907198218  954 HIIPS----KFNIQDFFRKININSDNYQVGKTMVFLK 986
Cdd:cd14883    625 ARSADhketCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
MYSc_Myo15 cd01387
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ...
161-986 0e+00

class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, myosin XV appears to be expressed in sensory tissue and play a role in hearing. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are 2 MyTH4 domain, a FERM domain, and a SH3 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276838 [Multi-domain]  Cd Length: 657  Bit Score: 621.39  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  161 TLLENLRNRFKHEKIYTYVGSILIAINPFKFLPIYNPKYVKMYDNHQLGKLEPHIYAVADVAYHAMLQRKKNQCIVISGE 240
Cdd:cd01387      2 TVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISGE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  241 SGSGKTQSTNFLIHHLTALSQKGFASGVEQIiLGAGPVLEAFGNAKTAHNNNSSRFGKFIQVnYQETGTVLGAYVEKYLL 320
Cdd:cd01387     82 SGSGKTEATKLIMQYLAAVNQRRNNLVTEQI-LEATPLLEAFGNAKTVRNDNSSRFGKYLEV-FFEGGVIVGAITSQYLL 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  321 EKSRLVYQEHNERNYHVFYYLLAGASEEERLAFHLKQPEEYHFLNQ---DCftVEGEDLRHDFERLQLAMEMVGFLPKTR 397
Cdd:cd01387    160 EKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQggnCE--IAGKSDADDFRRLLAAMQVLGFSSEEQ 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  398 RQIFSLLSAILHLGNISYKKKTYRD--DSIDICNPEVLPIVSELLEVKEEMLFEALVTRKTVTVGEKLILPYKLAEAVTV 475
Cdd:cd01387    238 DSIFRILASVLHLGNVYFHKRQLRHgqEGVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRERIFTPLTIDQALDA 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  476 RNSMAKSLYSALFDWIVFRINHALLNSKDleqdtKTLSIGVLDIFGFEDYENNSFEQFCINFANERLQHYFNQHIFKLEQ 555
Cdd:cd01387    318 RDAIAKALYALLFSWLVTRVNAIVYSGTQ-----DTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVFKLEQ 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  556 EEYRTEGISWHNIDYIDNTCCINLISKKPTGLLHLLDEESNFPQATNQTLLDKFKHQHEENSYIEFPAVMEPAFIIKHYA 635
Cdd:cd01387    393 EEYIREQIDWTEIAFADNQPVINLISKKPVGILHILDDECNFPQATDHSFLEKCHYHHALNELYSKPRMPLPEFTIKHYA 472
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  636 GKVKYGVKDFREKNTDHMRPDIVALLRSSRNAFVSGMTgidpvavfrwavlraffravvafreagKRHIQRksgHDDTTP 715
Cdd:cd01387    473 GQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLF---------------------------SSHRAQ---TDKAPP 522
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  716 caiLKSMDSFsflqhpvhqrsleilqrckeekysITRKnPRTplsdlqgmntlneknqhdtfdiawnvrtgirqsrlpas 795
Cdd:cd01387    523 ---RLGKGRF------------------------VTMK-PRT-------------------------------------- 536
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  796 ntslldkdgifahsasskllerahgiltrnknfrskpvlpkhllevnslkhltrltlqdritksllhlhkkkkpPSISAQ 875
Cdd:cd01387    537 --------------------------------------------------------------------------PTVAAR 542
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  876 FQASLSKLMETLGQAEPYFVKCIRSNAEKLPLRFSDALVLRQLRYTGMLETVRIRQSGYSSKYSFQDFVSHFHVLLP-QH 954
Cdd:cd01387    543 FQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVAlKL 622
                          810       820       830
                   ....*....|....*....|....*....|....*
gi 1907198218  955 IIPSKFNIQDFFRKI---NINSDNYQVGKTMVFLK 986
Cdd:cd01387    623 PRPAPGDMCVSLLSRlctVTPKDMYRLGATKVFLR 657
MYSc_Myo3 cd01379
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ...
161-986 0e+00

class III myosin, motor domain; Myosin III has been shown to play a role in the vision process in insects and in hearing in mammals. Myosin III, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They are characterized by an N-terminal protein kinase domain and several IQ domains. Some members also contain WW, SH2, PH, and Y-phosphatase domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276830 [Multi-domain]  Cd Length: 633  Bit Score: 608.12  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  161 TLLENLRNRFKHEKIYTYVGSILIAINPFKFLPIYNPKYVKMYDNHQLGKLEPHIYAVADVAYHAMLQRKKNQCIVISGE 240
Cdd:cd01379      2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  241 SGSGKTQSTNFLIHHLTALSqKGFASGVEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQETGTVLGAYVEKYLL 320
Cdd:cd01379     82 SGAGKTESANLLVQQLTVLG-KANNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEYLL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  321 EKSRLVYQEHNERNYHVFYYLLAGASEEERLA-FHL---KQPEEYHFLNQDCFTVEGEDL-RHDFERLQLAMEMVGFLPK 395
Cdd:cd01379    161 EKSRVVHQAIGERNFHIFYYIYAGLAEDKKLAkYKLpenKPPRYLQNDGLTVQDIVNNSGnREKFEEIEQCFKVIGFTKE 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  396 TRRQIFSLLSAILHLGNISYK---KKTYRDDSIDICNPEVLPIVSELLEVKEEMLFEALVTRKTVTVGEKLILPYKLAEA 472
Cdd:cd01379    241 EVDSVYSILAAILHIGDIEFTeveSNHQTDKSSRISNPEALNNVAKLLGIEADELQEALTSHSVVTRGETIIRNNTVEEA 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  473 VTVRNSMAKSLYSALFDWIVFRINHALLNSKDLEQDTktLSIGVLDIFGFEDYENNSFEQFCINFANERLQHYFNQHIFK 552
Cdd:cd01379    321 TDARDAMAKALYGRLFSWIVNRINSLLKPDRSASDEP--LSIGILDIFGFENFQKNSFEQLCINIANEQIQYYFNQHIFA 398
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  553 LEQEEYRTEGISWHNIDYIDNTCCINLISKKPTGLLHLLDEESNFPQATNQTLLDKFkHQHEENSYIEFPAVMEPAFIIK 632
Cdd:cd01379    399 WEQQEYLNEGIDVDLIEYEDNRPLLDMFLQKPMGLLALLDEESRFPKATDQTLVEKF-HNNIKSKYYWRPKSNALSFGIH 477
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  633 HYAGKVKYGVKDFREKNTDHMRPDIVALLRSSrnafvsgmtgidpvavfrwavlraffravvafreagkrhiqrksghdd 712
Cdd:cd01379    478 HYAGKVLYDASGFLEKNRDTLPPDVVQLLRSS------------------------------------------------ 509
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  713 ttpcailksmdsfsflQHPVhqrsleilqrckeekysitrknprtplsdlqgmntlneknqhdtfdiawnvrtgIRQsrl 792
Cdd:cd01379    510 ----------------ENPL------------------------------------------------------VRQ--- 516
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  793 pasntslldkdgifahsasskllerahgilTRNKNFRskpvlpkhllevNSLKHLtrltlqdritksllhlhkkkkppsi 872
Cdd:cd01379    517 ------------------------------TVATYFR------------YSLMDL------------------------- 529
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  873 saqfqasLSKLMetlgQAEPYFVKCIRSNAEKLPLRFSDALVLRQLRYTGMLETVRIRQSGYSSKYSFQDFVSHFHVL-- 950
Cdd:cd01379    530 -------LSKMV----VGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYYFLaf 598
                          810       820       830
                   ....*....|....*....|....*....|....*..
gi 1907198218  951 -LPQHIIPSKFNIQDFFRKINInsDNYQVGKTMVFLK 986
Cdd:cd01379    599 kWNEEVVANRENCRLILERLKL--DNWALGKTKVFLK 633
MYSc_Myo5 cd01380
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ...
163-986 0e+00

class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins that transport a variety of intracellular cargo processively along actin filaments, such as melanosomes, synaptic vesicles, vacuoles, and mRNA. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains a IQ domain and a globular DIL domain. Myosin V is a class of actin-based motor proteins involved in cytoplasmic vesicle transport and anchorage, spindle-pole alignment and mRNA translocation. The protein encoded by this gene is abundant in melanocytes and nerve cells. Mutations in this gene cause Griscelli syndrome type-1 (GS1), Griscelli syndrome type-3 (GS3) and neuroectodermal melanolysosomal disease, or Elejalde disease. Multiple alternatively spliced transcript variants encoding different isoforms have been reported, but the full-length nature of some variants has not been determined. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Note that the Dictyostelium myoVs are not contained in this child group. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276831 [Multi-domain]  Cd Length: 629  Bit Score: 604.53  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  163 LENLRNRF-KHEKIYTYVGSILIAINPFKFLPIYNPKYVKMYDNHQLGKLEPHIYAVADVAYHAMLQRKKNQCIVISGES 241
Cdd:cd01380      4 LHNLKVRFcQRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSGES 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  242 GSGKTQSTNFLIHHLTALSQKGFA-SGVEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQETGTVLGAYVEKYLL 320
Cdd:cd01380     84 GAGKTVSAKYAMRYFATVGGSSSGeTQVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANMRTYLL 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  321 EKSRLVYQEHNERNYHVFYYLLAGASEEERLAFHLKQPEEYHFLNQ-DCFTVEGEDLRHDFERLQLAMEMVGFLPKTRRQ 399
Cdd:cd01380    164 EKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQgGSPVIDGVDDAAEFEETRKALTLLGISEEEQME 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  400 IFSLLSAILHLGNISYKKKTYRDDSIDICNPEvLPIVSELLEVKEEMLFEALVTRKTVTVGEKLILPYKLAEAVTVRNSM 479
Cdd:cd01380    244 IFRILAAILHLGNVEIKATRNDSASISPDDEH-LQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQAIVARDAL 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  480 AKSLYSALFDWIVFRINHALLNSKDLEQDTktlSIGVLDIFGFEDYENNSFEQFCINFANERLQHYFNQHIFKLEQEEYR 559
Cdd:cd01380    323 AKHIYAQLFDWIVDRINKALASPVKEKQHS---FIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQEEYV 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  560 TEGISWHNIDYIDNTCCINLISKKPtGLLHLLDEESNFPQATNQTLLDKFKHQHE--ENSYIEFPAVMEPAFIIKHYAGK 637
Cdd:cd01380    400 KEEIEWSFIDFYDNQPCIDLIEGKL-GILDLLDEECRLPKGSDENWAQKLYNQHLkkPNKHFKKPRFSNTAFIVKHFADD 478
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  638 VKYGVKDfrekntdhmrpdivallrssrnafvsgmtgidpvavfrwavlraffravvafreagkrhiqrksghddttpca 717
Cdd:cd01380    479 VEYQVEG------------------------------------------------------------------------- 485
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  718 ilksmdsfsFLqhpvhqrsleilqrckeekysitrknprtplsdlqgmntlnEKNQhDTfdiawnvrtgirqsrlpasnt 797
Cdd:cd01380    486 ---------FL-----------------------------------------EKNR-DT--------------------- 493
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  798 slldkdgifahsasskllerahgiltrnknfrskpVLPKHLlevnslkhltrltlqdritkSLLHLHKKKKPpSISAQFQ 877
Cdd:cd01380    494 -----------------------------------VSEEHL--------------------NVLKASKNRKK-TVGSQFR 517
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  878 ASLSKLMETLGQAEPYFVKCIRSNAEKLPLRFSDALVLRQLRYTGMLETVRIRQSGYSSKYSFQDFVSHFHVLLP-QHII 956
Cdd:cd01380    518 DSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPsKEWL 597
                          810       820       830
                   ....*....|....*....|....*....|....
gi 1907198218  957 PSkfNIQDFFRKININ----SDNYQVGKTMVFLK 986
Cdd:cd01380    598 RD--DKKKTCENILENlildPDKYQFGKTKIFFR 629
MYSc_Myo10 cd14873
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ...
161-986 0e+00

class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a monomer. In mammalian cells, the motor is found to localize to filopodia. Myosin X walks towards the barbed ends of filaments and is thought to walk on bundles of actin, rather than single filaments, a unique behavior. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are a variable number of IQ domains, 2 PH domains, a MyTH4 domain, and a FERM domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276840 [Multi-domain]  Cd Length: 651  Bit Score: 597.55  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  161 TLLENLRNRFKHEKIYTYVGSILIAINPFKFLP-IYNPKYVKMYDNHQLGKLEPHIYAVADVAYHAMLQRKKNQCIVISG 239
Cdd:cd14873      2 SIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILISG 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  240 ESGSGKTQSTNFLIHHLTALSQ-------KGFASGVEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQETGTVLG 312
Cdd:cd14873     82 ESGAGKTESTKLILKFLSVISQqslelslKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQG 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  313 AYVEKYLLEKSRLVYQEHNERNYHVFYYLLAGASEEERLAFHLKQPEEYHFLNQD-CFTVEGEDLRHDFERLQLAMEMVG 391
Cdd:cd14873    162 GRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNQSgCVEDKTISDQESFREVITAMEVMQ 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  392 FLPKTRRQIFSLLSAILHLGNISYKKKTyrddSIDICNPEVLPIVSELLEVKEEMLFEALVTRKTVTVGEKLILPYKLAE 471
Cdd:cd14873    242 FSKEEVREVSRLLAGILHLGNIEFITAG----GAQVSFKTALGRSAELLGLDPTQLTDALTQRSMFLRGEEILTPLNVQQ 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  472 AVTVRNSMAKSLYSALFDWIVFRINHALLNSKDLEqdtktlSIGVLDIFGFEDYENNSFEQFCINFANERLQHYFNQHIF 551
Cdd:cd14873    318 AVDSRDSLAMALYARCFEWVIKKINSRIKGKEDFK------SIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIF 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  552 KLEQEEYRTEGISWHNIDYIDNTCCINLISKKpTGLLHLLDEESNFPQATNQTLLDKFKHQHEENSYIEFPAVMEPAFII 631
Cdd:cd14873    392 SLEQLEYSREGLVWEDIDWIDNGECLDLIEKK-LGLLALINEESHFPQATDSTLLEKLHSQHANNHFYVKPRVAVNNFGV 470
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  632 KHYAGKVKYGVKDFREKNTDHMRPDIVALLRSSRNAFVsgmtgidpvavfrwavlraffravvafreagkrhiqrksghd 711
Cdd:cd14873    471 KHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFI------------------------------------------ 508
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  712 dttpcailksmdsfsflqhpvhqrsleilqrckeekysitrknprtplsdlqgmntlneknqHDTFDiawnvrtgirqsr 791
Cdd:cd14873    509 --------------------------------------------------------------YDLFE------------- 513
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  792 lpasntslldkdgifaHSASskllerahgiltrnknfrskpvlpkhllevnslkhltrltlqdRITKSLLHLHKKKKPPS 871
Cdd:cd14873    514 ----------------HVSS-------------------------------------------RNNQDTLKCGSKHRRPT 534
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  872 ISAQFQASLSKLMETLGQAEPYFVKCIRSNAEKLPLRFSDALVLRQLRYTGMLETVRIRQSGYSSKYSFQDFVSHFHVLL 951
Cdd:cd14873    535 VSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLM 614
                          810       820       830
                   ....*....|....*....|....*....|....*..
gi 1907198218  952 PQHIIPSKFNIQ--DFFRKININSDNYQVGKTMVFLK 986
Cdd:cd14873    615 RNLALPEDVRGKctSLLQLYDASNSEWQLGKTKVFLR 651
MYSc_Myo8 cd01383
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ...
162-986 0e+00

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


Pssm-ID: 276834  Cd Length: 647  Bit Score: 594.29  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  162 LLENLRNRFKHEKIYTYVGSILIAINPFKFLPIYNPKYVKMYDNHQLgkLEPHIYAVADVAYHAMLQRKKNQCIVISGES 241
Cdd:cd01383      3 VLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYRQKLL--DSPHVYAVADTAYREMMRDEINQSIIISGES 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  242 GSGKTQSTNFLIHHLTALSqkGFASGVEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQETGTVLGAYVEKYLLE 321
Cdd:cd01383     81 GAGKTETAKIAMQYLAALG--GGSSGIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQTYLLE 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  322 KSRLVYQEHNERNYHVFYYLLAGASEEERLAFHLKQPEEYHFLNQ-DCFTVEGEDLRHDFERLQLAMEMVGFLPKTRRQI 400
Cdd:cd01383    159 KSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNQsNCLTIDGVDDAKKFHELKEALDTVGISKEDQEHI 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  401 FSLLSAILHLGNISYKKkTYRDDSIDICNPEVLPIVSELLEVKEEMLFEALVTRKTVTVGEKLILPYKLAEAVTVRNSMA 480
Cdd:cd01383    239 FQMLAAVLWLGNISFQV-IDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAIDARDALA 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  481 KSLYSALFDWIVFRINHALLNSKdlEQDTKTLSIgvLDIFGFEDYENNSFEQFCINFANERLQHYFNQHIFKLEQEEYRT 560
Cdd:cd01383    318 KAIYASLFDWLVEQINKSLEVGK--RRTGRSISI--LDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEEYEL 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  561 EGISWHNIDYIDNTCCINLISKKPTGLLHLLDEESNFPQATNQTLLDKFKHQHEENSYieFPAVMEPAFIIKHYAGKVKY 640
Cdd:cd01383    394 DGIDWTKVDFEDNQECLDLIEKKPLGLISLLDEESNFPKATDLTFANKLKQHLKSNSC--FKGERGGAFTIRHYAGEVTY 471
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  641 GVKDFREKNTDHMRPDIVALLRSSR----NAFVSGMTGidpvavfrwavlraffravvafreagkrhiqrksGHDDTTPC 716
Cdd:cd01383    472 DTSGFLEKNRDLLHSDLIQLLSSCScqlpQLFASKMLD----------------------------------ASRKALPL 517
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  717 AILKSMDSfsflqhpvhQRSleilqrckeekysitrknprtplsdlqgmntlneknqhdtfdiawnvrtgirqsrlpasn 796
Cdd:cd01383    518 TKASGSDS---------QKQ------------------------------------------------------------ 528
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  797 tslldkdgifahsasskllerahgiltrnknfrskpvlpkhllevnslkhltrltlqdritksllhlhkkkkppSISAQF 876
Cdd:cd01383    529 --------------------------------------------------------------------------SVATKF 534
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  877 QASLSKLMETLGQAEPYFVKCIRSNAEKLPLRFSDALVLRQLRYTGMLETVRIRQSGYSSKYSFQDFVSHFHVLLPQHII 956
Cdd:cd01383    535 KGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDVS 614
                          810       820       830
                   ....*....|....*....|....*....|....*..
gi 1907198218  957 PSkfniQD-------FFRKININSDNYQVGKTMVFLK 986
Cdd:cd01383    615 AS----QDplstsvaILQQFNILPEMYQVGYTKLFFR 647
MYSc_Myo1 cd01378
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ...
162-986 0e+00

class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, and class I myosins have been implicated in phagocytosis and vesicle transport. Myosin I, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. There are 5 myosin subclasses with subclasses c/h, d/g, and a/b have an IQ domain and a TH1 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276829  Cd Length: 652  Bit Score: 587.59  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  162 LLENLRNRFKHEKIYTYVGSILIAINPFKFLPIYNPKYVKMYDNHQLGKLEPHIYAVADVAYHAMLQRKKNQCIVISGES 241
Cdd:cd01378      3 INENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGES 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  242 GSGKTQSTNFLIHHLTALSQKGfASGVEQI---ILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQETGTVLGAYVEKY 318
Cdd:cd01378     83 GAGKTEASKRIMQYIAAVSGGS-ESEVERVkdmLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGHITNY 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  319 LLEKSRLVYQEHNERNYHVFYYLLAGASEEERLAFHLKQPEEYHFLNQ-DCFTVEGEDLRHDFERLQLAMEMVGFLPKTR 397
Cdd:cd01378    162 LLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKsGCFDVDGIDDAADFKEVLNAMKVIGFTEEEQ 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  398 RQIFSLLSAILHLGNISYKKKTyrDDSIDICNPEVLPIVSELLEVKEEMLFEALVTRKTVTVGEK---LILPYKLAEAVT 474
Cdd:cd01378    242 DSIFRILAAILHLGNIQFAEDE--EGNAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvYEVPLNVEQAAY 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  475 VRNSMAKSLYSALFDWIVFRINHALLNSkdleQDTKTLSIGVLDIFGFEDYENNSFEQFCINFANERLQHYFNQHIFKLE 554
Cdd:cd01378    320 ARDALAKAIYSRLFDWIVERINKSLAAK----SGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELTLKAE 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  555 QEEYRTEGISWHNIDYIDNTCCINLISKKPTGLLHLLDEESNFP-QATNQTLLDKF-----KHQHEENSYIEFpAVMEPA 628
Cdd:cd01378    396 QEEYVREGIEWTPIKYFNNKIICDLIEEKPPGIFAILDDACLTAgDATDQTFLQKLnqlfsNHPHFECPSGHF-ELRRGE 474
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  629 FIIKHYAGKVKYGVKDFREKNTDHMRPDIVALLRSSRNAFVSGMtgidpvavfrwavlraffravvafreagkrhiqrks 708
Cdd:cd01378    475 FRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSL------------------------------------ 518
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  709 ghddttpcailksmdsfsflqhpvhqrsleilqrckeekysitrknprtplsdlqgmntLNEKNQHDtfdiawnvrtgir 788
Cdd:cd01378    519 -----------------------------------------------------------FPEGVDLD------------- 526
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  789 qsrlpasntslldkdgifahsasskllerahgiltrnknfrskpvlpkhllevnslkhltrltlqdritksllhlhKKKK 868
Cdd:cd01378    527 ----------------------------------------------------------------------------SKKR 530
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  869 PPSISAQFQASLSKLMETLGQAEPYFVKCIRSNAEKLPLRFSDALVLRQLRYTGMLETVRIRQSGYSSKYSFQDFVSHFH 948
Cdd:cd01378    531 PPTAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYK 610
                          810       820       830       840
                   ....*....|....*....|....*....|....*....|..
gi 1907198218  949 VLLPQ----HIIPSKFNIQDFFRKININSDNYQVGKTMVFLK 986
Cdd:cd01378    611 LLSPKtwpaWDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
MYSc_Myo11 cd01384
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ...
163-986 0e+00

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


Pssm-ID: 276835  Cd Length: 647  Bit Score: 586.95  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  163 LENLRNRFKHEKIYTYVGSILIAINPFKFLP-IYNPKYVKMYDNHQLGKLEPHIYAVADVAYHAMLQRKKNQCIVISGES 241
Cdd:cd01384      4 LHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVSGES 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  242 GSGKTQSTNFLIHHLTALSQKGFASG--VEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQETGTVLGAYVEKYL 319
Cdd:cd01384     84 GAGKTETTKMLMQYLAYMGGRAVTEGrsVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAAIRTYL 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  320 LEKSRLVYQEHNERNYHVFYYLLAGASEEERLAFHLKQPEEYHFLNQ-DCFTVEGEDLRHDFERLQLAMEMVGFLPKTRR 398
Cdd:cd01384    164 LERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNQsKCFELDGVDDAEEYRATRRAMDVVGISEEEQD 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  399 QIFSLLSAILHLGNISYKKKTyRDDSIDICNPEV---LPIVSELLEVKEEMLFEALVTRKTVTVGEKLILPYKLAEAVTV 475
Cdd:cd01384    244 AIFRVVAAILHLGNIEFSKGE-EDDSSVPKDEKSefhLKAAAELLMCDEKALEDALCKRVIVTPDGIITKPLDPDAATLS 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  476 RNSMAKSLYSALFDWIVFRINhallnsKDLEQD-TKTLSIGVLDIFGFEDYENNSFEQFCINFANERLQHYFNQHIFKLE 554
Cdd:cd01384    323 RDALAKTIYSRLFDWLVDKIN------RSIGQDpNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQHVFKME 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  555 QEEYRTEGISWHNIDYIDNTCCINLISKKPTGLLHLLDEESNFPQATNQTLLDKFKHQHEENSYIEFPAVMEPAFIIKHY 634
Cdd:cd01384    397 QEEYTKEEIDWSYIEFVDNQDVLDLIEKKPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHKRFSKPKLSRTDFTIDHY 476
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  635 AGKVKYGVKDFREKNTDHMRPDIVALLRSSRNAFVSGMtgidpvavfrwavlraffravvaFREAGKRHIQRKSghddtt 714
Cdd:cd01384    477 AGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGL-----------------------FPPLPREGTSSSS------ 527
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  715 pcailksmdsfsflqhpvhqrsleilqrckeeKYSitrknprtplsdlqgmntlneknqhdtfdiawnvrtgirqsrlpa 794
Cdd:cd01384    528 --------------------------------KFS--------------------------------------------- 530
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  795 sntslldkdgifahsasskllerahgiltrnknfrskpvlpkhllevnslkhltrltlqdritksllhlhkkkkppSISA 874
Cdd:cd01384    531 ----------------------------------------------------------------------------SIGS 534
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  875 QFQASLSKLMETLGQAEPYFVKCIRSNAEKLPLRFSDALVLRQLRYTGMLETVRIRQSGYSSKYSFQDFVSHFHVLLPQH 954
Cdd:cd01384    535 RFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPEV 614
                          810       820       830
                   ....*....|....*....|....*....|....*
gi 1907198218  955 II---PSKFNIQDFFRKININsdNYQVGKTMVFLK 986
Cdd:cd01384    615 LKgsdDEKAACKKILEKAGLK--GYQIGKTKVFLR 647
MYSc_class_II cd01377
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ...
163-986 0e+00

class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. Thus, myosin II has two heads. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276951 [Multi-domain]  Cd Length: 662  Bit Score: 580.96  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  163 LENLRNRFKHEKIYTYVGSILIAINPFKFLPIYNPKYVKMYDNHQLGKLEPHIYAVADVAYHAMLQRKKNQCIVISGESG 242
Cdd:cd01377      4 LHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITGESG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  243 SGKTQSTNFLIHHLT---ALSQKGFASG-----VEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQETGTVLGAY 314
Cdd:cd01377     84 AGKTENTKKVIQYLAsvaASSKKKKESGkkkgtLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKIAGAD 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  315 VEKYLLEKSRLVYQEHNERNYHVFYYLLAGASEEERLAFHLKQ-PEEYHFLNQDCFTVEGEDLRHDFERLQLAMEMVGFL 393
Cdd:cd01377    164 IETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGdPSYYFFLSQGELTIDGVDDAEEFKLTDEAFDILGFS 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  394 PKTRRQIFSLLSAILHLGNISYKKKTyRDDSIDICNPEVLPIVSELLEVKEEMLFEALVT------RKTVTVGeklilpY 467
Cdd:cd01377    244 EEEKMSIFKIVAAILHLGNIKFKQRR-REEQAELDGTEEADKAAHLLGVNSSDLLKALLKprikvgREWVTKG------Q 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  468 KLAEAVTVRNSMAKSLYSALFDWIVFRINHALlnskDLEQDTKTlSIGVLDIFGFEDYENNSFEQFCINFANERLQHYFN 547
Cdd:cd01377    317 NKEQVVFSVGALAKALYERLFLWLVKRINKTL----DTKSKRQY-FIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFN 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  548 QHIFKLEQEEYRTEGISWHNIDY-IDNTCCINLISKKPTGLLHLLDEESNFPQATNQTLLDKFKHQHEENS--YIEFPAV 624
Cdd:cd01377    392 HHMFVLEQEEYKKEGIEWTFIDFgLDLQPTIDLIEKPNMGILSILDEECVFPKATDKTFVEKLYSNHLGKSknFKKPKPK 471
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  625 -MEPAFIIKHYAGKVKYGVKDFREKNTDHMRPDIVALLRSSRNAFVSGMtgidpvavfrwavlrafFRAVVAFREAGKRH 703
Cdd:cd01377    472 kSEAHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASL-----------------FKDYEESGGGGGKK 534
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  704 IQRKSghddttpcailksmdSFsflqhpvhqrsleilqrckeekysitrknpRTplsdlqgmntlneknqhdtfdiawnv 783
Cdd:cd01377    535 KKKGG---------------SF------------------------------RT-------------------------- 543
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  784 rtgirqsrlpasntslldkdgifahsasskllerahgiltrnknfrskpvlpkhllevnslkhltrltlqdritksllhl 863
Cdd:cd01377        --------------------------------------------------------------------------------
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  864 hkkkkppsISAQFQASLSKLMETLGQAEPYFVKCIRSNAEKLPLRFSDALVLRQLRYTGMLETVRIRQSGYSSKYSFQDF 943
Cdd:cd01377    544 --------VSQLHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEF 615
                          810       820       830       840
                   ....*....|....*....|....*....|....*....|....*...
gi 1907198218  944 VSHFHVLLPqHIIPSKFNIQDFF-----RKININSDNYQVGKTMVFLK 986
Cdd:cd01377    616 KQRYSILAP-NAIPKGFDDGKAAcekilKALQLDPELYRIGNTKVFFK 662
MYSc_Myo36 cd14897
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ...
160-986 5.11e-161

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: 513.47  E-value: 5.11e-161
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  160 KTLLENLRNRFKHEKIYTYVGSILIAINPFKFLPIYNPKYVKMYDNHQL-GKLEPHIYAVADVAYHAMLQRKKNQCIVIS 238
Cdd:cd14897      1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSVrSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  239 GESGSGKTQSTNFLIHHLTALSQKGFASGVEQIIlGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQETGTVLGAYVEKY 318
Cdd:cd14897     81 GESGAGKTESTKYMIKHLMKLSPSDDSDLLDKIV-QINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAKIDDY 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  319 LLEKSRLVYQEHNERNYHVFYYLLAGASEEERLAFHLKQPEEYHFL-----NQDCFTVEGEDLRHD--FERLQLAMEMVG 391
Cdd:cd14897    160 LLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILrddnrNRPVFNDSEELEYYRqmFHDLTNIMKLIG 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  392 FLPKTRRQIFSLLSAILHLGNISYKKKTyRDDSIDICNPEVLPIVSELLEVKEEMLFEALVTRKTVTVGEKLILPYKLAE 471
Cdd:cd14897    240 FSEEDISVIFTILAAILHLTNIVFIPDE-DTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNTIRGERIQSWKSLRQ 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  472 AVTVRNSMAKSLYSALFDWIVFRINHALLNSKDLEQDTKTLSIGVLDIFGFEDYENNSFEQFCINFANERLQHYFNQHIF 551
Cdd:cd14897    319 ANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDFQIMTRGPSIGILDMSGFENFKINSFDQLCINLSNERLQQYFNDYVF 398
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  552 KLEQEEYRTEGISWHNIDYIDNTCCINLISKKPTGLLHLLDEESNFPQATNQTLLDKF-KHQHEENSYIEFPAvMEPAFI 630
Cdd:cd14897    399 PRERSEYEIEGIEWRDIEYHDNDDVLELFFKKPLGILPLLDEESTFPQSTDSSLVQKLnKYCGESPRYVASPG-NRVAFG 477
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  631 IKHYAGKVKYGVKDFREKNTDHMRPDIVALLRSSRNAFVSGMtgidpvavfrwavlraffravvafreagkrhiqrksgh 710
Cdd:cd14897    478 IRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDL-------------------------------------- 519
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  711 ddttpcailksmdsfsFLQHpvHQRSLeilqrckeekysitrknprtplsdlqgmntlneknqhdtfdiawnvrtgirqs 790
Cdd:cd14897    520 ----------------FTSY--FKRSL----------------------------------------------------- 528
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  791 rlpasntslldkdgifahsasskllerahgiltrnknfrskpvlpkhllevnslkhltrltlqdritksllhlhkkkkpp 870
Cdd:cd14897        --------------------------------------------------------------------------------
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  871 sisaqfqaslSKLMETLGQAEPYFVKCIRSNAEKLPLRFSDALVLRQLRYTGMLETVRIRQSGYSSKYSFQDFVSHFHVL 950
Cdd:cd14897    529 ----------SDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRYKEI 598
                          810       820       830       840
                   ....*....|....*....|....*....|....*....|.
gi 1907198218  951 LPQhiiPSKFNIQDFFR-----KININSDnYQVGKTMVFLK 986
Cdd:cd14897    599 CDF---SNKVRSDDLGKcqkilKTAGIKG-YQFGKTKVFLK 635
MYSc_Myo4 cd14872
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ...
162-983 1.03e-158

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: 507.39  E-value: 1.03e-158
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  162 LLENLRNRFKHEKIYTYVGSILIAINPFKFLPIYNPKYVKMYDNHQLGKLEPHIYAVADVAYHAMLQRKKNQCIVISGES 241
Cdd:cd14872      3 IVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISGES 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  242 GSGKTQSTNFLIHHLTALSqkGFASGVEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQETGTVLGAYVEKYLLE 321
Cdd:cd14872     83 GAGKTEATKQCLSFFAEVA--GSTNGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGASTENYLLE 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  322 KSRLVYQEHNERNYHVFYYLLAGASEEERLAFHLKQPeeYHFLNQ-DCFTVEGEDLRHDFERLQLAMEMVGFLPKTRRQI 400
Cdd:cd14872    161 KSRVVYQIKGERNFHIFYQLLASPDPASRGGWGSSAA--YGYLSLsGCIEVEGVDDVADFEEVVLAMEQLGFDDADINNV 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  401 FSLLSAILHLGNISYKKKTYRDD--SIDICNPEVLPIVSELLEVKEEMLFEALVTRK-TVTVGEKLILPYKLAEAVTVRN 477
Cdd:cd14872    239 MSLIAAILKLGNIEFASGGGKSLvsGSTVANRDVLKEVATLLGVDAATLEEALTSRLmEIKGCDPTRIPLTPAQATDACD 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  478 SMAKSLYSALFDWIVFRINHALLNSKDleqdTKTLSIGVLDIFGFEDYENNSFEQFCINFANERLQHYFNQHIFKLEQEE 557
Cdd:cd14872    319 ALAKAAYSRLFDWLVKKINESMRPQKG----AKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTFKLEEAL 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  558 YRTEGISWHNIDYIDNTCCINLISKKPTGLLHLLDEESNFPQATNQTLLDKFKHQHEENSYI--EFPAVMEPAFIIKHYA 635
Cdd:cd14872    395 YQSEGVKFEHIDFIDNQPVLDLIEKKQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKSTFvyAEVRTSRTEFIVKHYA 474
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  636 GKVKYGVKDFREKNTDHMRPDIVALLRSSRNAFVSGMtgidpvavfrwavlraffravvafreagkrhiqrksghddttp 715
Cdd:cd14872    475 GDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVL------------------------------------------- 511
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  716 cailksmdsfsflqhpvhqrsleilqrckeekysitrknprtplsdlqgmntlneknqhdtfdiawnvrtgirqsrlpas 795
Cdd:cd14872        --------------------------------------------------------------------------------
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  796 ntslldkdgifahsasskllerahgiltrnknfrskpvlpkhllevnslkhltrltlqdritKSLLHLHKKKKPPSISAQ 875
Cdd:cd14872    512 --------------------------------------------------------------FPPSEGDQKTSKVTLGGQ 529
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  876 FQASLSKLMETLGQAEPYFVKCIRSNAEKLPLRFSDALVLRQLRYTGMLETVRIRQSGYSSKYSFQDFVSHFHVLLPQHI 955
Cdd:cd14872    530 FRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFLVKTIA 609
                          810       820       830
                   ....*....|....*....|....*....|..
gi 1907198218  956 I----PSKFNIQDFFRKININSDNYQVGKTMV 983
Cdd:cd14872    610 KrvgpDDRQRCDLLLKSLKQDFSKVQVGKTRV 641
MYSc_Myo28 cd14889
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ...
160-986 1.33e-157

class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The tail regions of these class-XXVIII myosins consist of an IQ motif, a short coiled-coil region, and an SH2 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276854  Cd Length: 659  Bit Score: 504.83  E-value: 1.33e-157
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  160 KTLLENLRNRFKHEKIYTYVGSILIAINPFKFLPIYNPKYVKMYDNHQLGKLEPHIYAVADVAYHAMLQR----KKNQCI 235
Cdd:cd14889      1 KVLLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLGRlargPKNQCI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  236 VISGESGSGKTQSTNFLIHHLTALSQKGfaSGVEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQEtGTVLGAYV 315
Cdd:cd14889     81 VISGESGAGKTESTKLLLRQIMELCRGN--SQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRFRN-GHVKGAKI 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  316 EKYLLEKSRLVYQEHNERNYHVFYYLLAGASEEERLAFHLKQPEEYHFLNQ--DCfTVEGEDLRHDFERLQLAMEMVGFL 393
Cdd:cd14889    158 NEYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLLDPGKYRYLNNgaGC-KREVQYWKKKYDEVCNAMDMVGFT 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  394 PKTRRQIFSLLSAILHLGNISYKkkTYRDDSIDICNPEVLPI--VSELLEVKEEMLFEALVTRKTVTVGEKLILPYKLAE 471
Cdd:cd14889    237 EQEEVDMFTILAGILSLGNITFE--MDDDEALKVENDSNGWLkaAAGQFGVSEEDLLKTLTCTVTFTRGEQIQRHHTKQQ 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  472 AVTVRNSMAKSLYSALFDWIVFRINHALLNSKDLEQDTKtlSIGVLDIFGFEDYENNSFEQFCINFANERLQHYFNQHIF 551
Cdd:cd14889    315 AEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSVELR--EIGILDIFGFENFAVNRFEQACINLANEQLQYFFNHHIF 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  552 KLEQEEYRTEGISWHNIDYIDNTCCINLISKKPTGLLHLLDEESNFPQATNQTLLDKFKHQHEENSYIEFPAVMEPAFII 631
Cdd:cd14889    393 LMEQKEYKKEGIDWKEITYKDNKPILDLFLNKPIGILSLLDEQSHFPQATDESFVDKLNIHFKGNSYYGKSRSKSPKFTV 472
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  632 KHYAGKVKYGVKDFREKNTDHMRPDIVALlrssrnaFVSGMTgidpvavfrwAVLRAFFRAvvafreagkrhiqrksghd 711
Cdd:cd14889    473 NHYAGKVTYNASGFLEKNRDTIPASIRTL-------FINSAT----------PLLSVLFTA------------------- 516
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  712 dttpcailksmdsfsflqhpvhqrsleilqrckeekySITRKNPRTPlsdlqgmntlneknqhdtfdiawnvrtgiRQSR 791
Cdd:cd14889    517 -------------------------------------TRSRTGTLMP-----------------------------RAKL 530
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  792 LPASntslldkdgifahsasskllerahgiltrNKNFRSkpvlpkhllevnslkhltrltlqdritksllhlhkkKKPPS 871
Cdd:cd14889    531 PQAG-----------------------------SDNFNS------------------------------------TRKQS 545
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  872 ISAQFQASLSKLMETLGQAEPYFVKCIRSNAEKLPLRFSDALVLRQLRYTGMLETVRIRQSGYSSKYSFQDFVSHFHVLL 951
Cdd:cd14889    546 VGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAERYKILL 625
                          810       820       830
                   ....*....|....*....|....*....|....*.
gi 1907198218  952 PQHIIPskFNIQDFFRKININS-DNYQVGKTMVFLK 986
Cdd:cd14889    626 CEPALP--GTKQSCLRILKATKlVGWKCGKTRLFFK 659
MYSc_Myo6 cd01382
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ...
161-672 1.73e-154

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: 495.23  E-value: 1.73e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  161 TLLENLRNRFKHEKIYTYVGSILIAINPFKFLP-IYNPKYVKMYDNHQLGKLEPHIYAVADVAYHAMLQRKKNQCIVISG 239
Cdd:cd01382      2 TLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVSG 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  240 ESGSGKTQSTNFLIHHLTAlSQKGFASGVEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQETGTVLGAYVEKYL 319
Cdd:cd01382     82 ESGAGKTESTKYILRYLTE-SWGSGAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  320 LEKSRLVYQEHNERNYHVFYYLLAGASEEERLAFhLKQPeeyhFLNqdcftvegeDLRhDFERLQLAMEMVGFLPKTRRQ 399
Cdd:cd01382    161 LEKSRICVQSKEERNYHIFYRLCAGAPEDLREKL-LKDP----LLD---------DVG-DFIRMDKAMKKIGLSDEEKLD 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  400 IFSLLSAILHLGNISYKKKTyrDDSIDICN-----PEVLPIVSELLEVKEEMLFEALVTRKTVTVGE----KLIL-PYKL 469
Cdd:cd01382    226 IFRVVAAVLHLGNIEFEENG--SDSGGGCNvkpksEQSLEYAAELLGLDQDELRVSLTTRVMQTTRGgakgTVIKvPLKV 303
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  470 AEAVTVRNSMAKSLYSALFDWIVFRINhallnsKDLEQDTKTLSIGVLDIFGFEDYENNSFEQFCINFANERLQHYFNQH 549
Cdd:cd01382    304 EEANNARDALAKAIYSKLFDHIVNRIN------QCIPFETSSYFIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQFFNER 377
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  550 IFKLEQEEYRTEGISWHNIDYIDNTCCINLISKKPTGLLHLLDEESNFPQATNQTLLDKFKHQHEENSYIEFPAVM---- 625
Cdd:cd01382    378 ILKEEQELYEKEGLGVKEVEYVDNQDCIDLIEAKLVGILDLLDEESKLPKPSDQHFTSAVHQKHKNHFRLSIPRKSklki 457
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907198218  626 ------EPAFIIKHYAGKVKYGVKDFREKNTDHMRPDIVALLRSSRNAFVSGM 672
Cdd:cd01382    458 hrnlrdDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSL 510
MYSc_Myo46 cd14907
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ...
161-986 3.51e-152

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: 489.54  E-value: 3.51e-152
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  161 TLLENLRNRFKHEKIYTYVGSILIAINPFKFLP-IYNPKYVKMYDNH--------QLGKLEPHIYAVADVAYHAMLQRKK 231
Cdd:cd14907      2 ELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQiiqngeyfDIKKEPPHIYAIAALAFKQLFENNK 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  232 NQCIVISGESGSGKTQSTNFLIHHLTALSQKGFAS------------------GVEQIILGAGPVLEAFGNAKTAHNNNS 293
Cdd:cd14907     82 KQAIVISGESGAGKTENAKYAMKFLTQLSQQEQNSeevltltssiratskstkSIEQKILSCNPILEAFGNAKTVRNDNS 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  294 SRFGKF--IQVNYQETgTVLGAYVEKYLLEKSRLVYQEHNERNYHVFYYLLAGASEEERLAFHLKQP---EEYHFLNQ-D 367
Cdd:cd14907    162 SRFGKYvsILVDKKKR-KILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNQlsgDRYDYLKKsN 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  368 CFTVEGEDLRHDFERLQLAMEMVGFLPKTRRQIFSLLSAILHLGNISYKKKTYRDDSI-DICNPEVLPIVSELLEVKEEM 446
Cdd:cd14907    241 CYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTLDDNSPcCVKNKETLQIIAKLLGIDEEE 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  447 LFEALVTRKTVTVGEKLILPYKLAEAVTVRNSMAKSLYSALFDWIVFRINHALLNSKDLEQDT---KTLSIGVLDIFGFE 523
Cdd:cd14907    321 LKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTIMPKDEKDQQLfqnKYLSIGLLDIFGFE 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  524 DYENNSFEQFCINFANERLQHYFNQHIFKLEQEEYRTEGISWH--NIDYIDNTCCINLISKKPTGLLHLLDEESNFPQAT 601
Cdd:cd14907    401 VFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYlnQLSYTDNQDVIDLLDKPPIGIFNLLDDSCKLATGT 480
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  602 NQTLLDKFKHQHEENSYIEFPA-VMEPAFIIKHYAGKVKYGVKDFREKNTDHMRPDIVALLRSSRNAFVSGMtgidpvav 680
Cdd:cd14907    481 DEKLLNKIKKQHKNNSKLIFPNkINKDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSI-------- 552
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  681 frwavlraffravvafreagkrhiqrksghddttpcailksmdsFSFLQHPVHQRSLEILQRCKEEKYsitrknprtpls 760
Cdd:cd14907    553 --------------------------------------------FSGEDGSQQQNQSKQKKSQKKDKF------------ 576
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  761 dlqgmntlneknqhdtfdiawnvrtgirqsrlpasntslldkdgifahsasskllerahgiltrnknfrskpvlpkhlle 840
Cdd:cd14907        --------------------------------------------------------------------------------
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  841 vnslkhltrltlqdritksllhlhkkkkppsISAQFQASLSKLMETLGQAEPYFVKCIRSNAEKLPLRFSDALVLRQLRY 920
Cdd:cd14907    577 -------------------------------LGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRY 625
                          810       820       830       840       850       860
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907198218  921 TGMLETVRIRQSGYsskysfqdfvshfhvllpqhiiPSKFNIQDFFRKININSDNYQVGKTMVFLK 986
Cdd:cd14907    626 LGVLESIRVRKQGY----------------------PYRKSYEDFYKQYSLLKKNVLFGKTKIFMK 669
MYSc_Myo29 cd14890
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ...
162-986 8.98e-151

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: 485.05  E-value: 8.98e-151
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  162 LLENLRNRFKHEKIYTYVGSILIAINPFKFLP-IYNPKYVKMYDNHQLGKLEPHIYAVADVAYHAMLQ----RKKNQCIV 236
Cdd:cd14890      3 LLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQSII 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  237 ISGESGSGKTQSTNFLIHHLTALSqKGFASG------------------VEQIILGAGPVLEAFGNAKTAHNNNSSRFGK 298
Cdd:cd14890     83 ISGESGAGKTEATKIIMQYLARIT-SGFAQGasgegeaaseaieqtlgsLEDRVLSSNPLLESFGNAKTLRNDNSSRFGK 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  299 FIQVNYQETGTVLGAYVEKYLLEKSRLVYQEHNERNYHVFYYLLAGASEEERLAFHLKQPEEYHFLNQDCFTVEGEDLRH 378
Cdd:cd14890    162 FIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLRGECSSIPSCDDAK 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  379 DFERLQLAMEMVGFLPKTRRQIFSLLSAILHLGNISYKKKTYRDDSIDICNPEVLPIVSELLEVKEEMLFEALVTRKTVT 458
Cdd:cd14890    242 AFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLEDATTLQSLKLAAELLGVNEDALEKALLTRQLFV 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  459 VGEKLILPYKLAEAVTVRNSMAKSLYSALFDWIVFRINHALLnskdlEQDTKTLSIGVLDIFGFEDYENNSFEQFCINFA 538
Cdd:cd14890    322 GGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTIS-----SPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYA 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  539 NERLQHYFNQHIFKLEQEEYRTEGISWHNIDYIDNTCCINLISKKPTG---LLHLLD-------EESN----------FP 598
Cdd:cd14890    397 NEKLQRHFNQHMFEVEQVEYSNEGIDWQYITFNDNQACLELIEGKVNGkpgIFITLDdcwrfkgEEANkkfvsqlhasFG 476
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  599 QATNQTLLDKFKHQHEenSYIEfPAV-MEPAFIIKHYAGKVKYGVKDFREKNtdhmrpdivallrssrnafvsgmtgidp 677
Cdd:cd14890    477 RKSGSGGTRRGSSQHP--HFVH-PKFdADKQFGIKHYAGDVIYDASGFNEKN---------------------------- 525
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  678 vavfrwavlraffravvafreagkrhiqrksghddttpcailksmdsfsflqhpvhqrsleilqrckeekysitrknprt 757
Cdd:cd14890        --------------------------------------------------------------------------------
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  758 plsdlqgMNTLNEknqhdtfdiawNVRTGIRQSRlpasntslldkdgifahsasskllerahgiltrnKNFRSKpvlpkh 837
Cdd:cd14890    526 -------NETLNA-----------EMKELIKQSR----------------------------------RSIREV------ 547
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  838 llevnslkhltrltlqdritksllhlhkkkkppSISAQFQASLSKLMETLGQAEPYFVKCIRSNAEKLPLRFSDALVLRQ 917
Cdd:cd14890    548 ---------------------------------SVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQ 594
                          810       820       830       840       850       860       870
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907198218  918 LRYTGMLETVRIRQSGYSSKYSFQDFVSHFHVLLPQhiipsKFNIQDFFRKI----NINSDNYQVGKTMVFLK 986
Cdd:cd14890    595 LKYSGMMEAIQIRQQGFALREEHDSFFYDFQVLLPT-----AENIEQLVAVLskmlGLGKADWQIGSSKIFLK 662
MYSc_Myo27 cd14888
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ...
162-986 7.75e-149

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: 479.96  E-value: 7.75e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  162 LLENLRNRFKHEKIYTYVGSILIAINPFKFLPiynpkyvKMYDNHQLGKL-------EPHIYAVADVAYHAMLQRKKNQC 234
Cdd:cd14888      3 ILHSLNLRFDIDEIYTFTGPILIAVNPFKTIP-------GLYSDEMLLKFiqpsiskSPHVFSTASSAYQGMCNNKKSQT 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  235 IVISGESGSGKTQSTNFLIHHLT-ALSQ-KGFASGVEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQET----- 307
Cdd:cd14888     76 ILISGESGAGKTESTKYVMKFLAcAGSEdIKKRSLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSKLkskrm 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  308 ----GTVLGAYVEKYLLEKSRLVYQEHNERNYHVFYYLLAGASEEERLAFHLKQPEEYHFLNQD---------------- 367
Cdd:cd14888    156 sgdrGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYEENDEKLAKGADakpisidmssfephlk 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  368 --------CFTVEGEDLRHDFERLQLAMEMVGFLPKTRRQIFSLLSAILHLGNISYKKKTYRDDS--IDICNPEVLPIVS 437
Cdd:cd14888    236 fryltkssCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGavVSASCTDDLEKVA 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  438 ELLEVKEEMLFEALVTRKTVTVGEKLILPYKLAEAVTVRNSMAKSLYSALFDWIVFRINhallNSKDLEQDTKTLSIGVL 517
Cdd:cd14888    316 SLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTN----ESIGYSKDNSLLFCGVL 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  518 DIFGFEDYENNSFEQFCINFANERLQHYFNQHIFKLEQEEYRTEGISWHNIDYIDNTCCINLISKKPTGLLHLLDEESNF 597
Cdd:cd14888    392 DIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFPDNQDCVDLLQEKPLGIFCMLDEECFV 471
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  598 PQATNQTLLDKFKHQHEENSYIEFPAVMEPAFIIKHYAGKVKYGVKDFREKNTDHMRPDIVALLRSSRNAFVSgmtgidp 677
Cdd:cd14888    472 PGGKDQGLCNKLCQKHKGHKRFDVVKTDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFIS------- 544
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  678 vAVFrwavlraffravvafreagkrhiqrksghddttpcailksmdsfsflqhpvhqrsleilqrckeEKYsitrknprt 757
Cdd:cd14888    545 -NLF----------------------------------------------------------------SAY--------- 550
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  758 pLSDLQGMNTlneknqhdtfdiawnvrtgirqsrlpasntslldkdgifahsasskllerahgiltrnknfrskpvlpkh 837
Cdd:cd14888    551 -LRRGTDGNT---------------------------------------------------------------------- 559
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  838 llevnslkhltrltlqdritksllhlhKKKKPPSISAQFQASLSKLMETLGQAEPYFVKCIRSNAEKLPLRFSDALVLRQ 917
Cdd:cd14888    560 ---------------------------KKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQ 612
                          810       820       830       840       850       860
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907198218  918 LRYTGMLETVRIRQSGYSSKYSFQDFVSHFHVLLPQHIipskfniqdffrKININSdnYQVGKTMVFLK 986
Cdd:cd14888    613 LKYGGVLQAVQVSRAGYPVRLSHAEFYNDYRILLNGEG------------KKQLSI--WAVGKTLCFFK 667
MYSc_Myo31 cd14892
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ...
162-665 7.35e-147

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: 473.86  E-value: 7.35e-147
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  162 LLENLRNRFKHEKIYTYVGSILIAINPFKFLP-IYNpkyVKMYDnhQLGKLE-------PHIYAVADVAYHAMLQRKKN- 232
Cdd:cd14892      3 LLDVLRRRYERDAIYTFTADILISINPYKSIPlLYD---VPGFD--SQRKEEatassppPHVFSIAERAYRAMKGVGKGq 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  233 ---QCIVISGESGSGKTQSTNFLIHHLTALSQ-----------KGFASGVEQIILGAGPVLEAFGNAKTAHNNNSSRFGK 298
Cdd:cd14892     78 gtpQSIVVSGESGAGKTEASKYIMKYLATASKlakgastskgaANAHESIEECVLLSNLILEAFGNAKTIRNDNSSRFGK 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  299 FIQVNYQETGTVLGAYVEKYLLEKSRLVYQEHNERNYHVFYYLLAGASEEERLAFHLKQPEEYHFLNQ-DCFTVEGEDLR 377
Cdd:cd14892    158 YIQIHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQgNCVEVDGVDDA 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  378 HDFERLQLAMEMVGFLPKTRRQIFSLLSAILHLGNISYKKKTYRDDSIDICN-PEVLPIVSELLEVKEEMLFEALVTRKT 456
Cdd:cd14892    238 TEFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDVFAQSAdGVNVAKAAGLLGVDAAELMFKLVTQTT 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  457 VTV-GEKLILPYKLAEAVTVRNSMAKSLYSALFDWIVFRIN-----HALLNSKDLEQDTKTLSIGVLDIFGFEDYENNSF 530
Cdd:cd14892    318 STArGSVLEIKLTAREAKNALDALCKYLYGELFDWLISRINachkqQTSGVTGGAASPTFSPFIGILDIFGFEIMPTNSF 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  531 EQFCINFANERLQHYFNQHIFKLEQEEYRTEGISWHNIDYIDNTCCINLISKKPTGLLHLLDEESNFP-QATNQTLLDKF 609
Cdd:cd14892    398 EQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQDNQDCLDLIQKKPLGLLPLLEEQMLLKrKTTDKQLLTIY 477
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907198218  610 KHQHEE--NSYIEfPAVMEPAFIIKHYAGKVKYGVKDFREKNTDHMRPDIVALLRSSR 665
Cdd:cd14892    478 HQTHLDkhPHYAK-PRFECDEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSS 534
MYSc_Myo30 cd14891
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ...
162-675 5.14e-144

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: 464.90  E-value: 5.14e-144
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  162 LLENLRNRFKHE--KIYTYVGSILIAINPFKFLPiyNPKyVKMYDNHQLGKLEPHIYAVADVAYHAML---QRKKNQCIV 236
Cdd:cd14891      3 ILHNLEERSKLDnqRPYTFMANVLIAVNPLRRLP--EPD-KSDYINTPLDPCPPHPYAIAEMAYQQMClgsGRMQNQSIV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  237 ISGESGSGKTQSTNFLIHHLT-----------------ALSQKGFASGVEQIILGAGPVLEAFGNAKTAHNNNSSRFGKF 299
Cdd:cd14891     80 ISGESGAGKTETSKIILRFLTtravggkkasgqdieqsSKKRKLSVTSLDERLMDTNPILESFGNAKTLRNHNSSRFGKF 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  300 IQVNYQETGTVL-GAYVEKYLLEKSRLVYQEHNERNYHVFYYLLAGASEEERLAFHLKQPEEYHFLNQ-DCFTVEGEDLR 377
Cdd:cd14891    160 MKLQFTKDKFKLaGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNQsGCVSDDNIDDA 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  378 HDFERLQLAMEMVGFLPKTRRQIFSLLSAILHLGNISYKKKTYRDDSIDICNPEVLPIV---SELLEVKEEMLFEALVTR 454
Cdd:cd14891    240 ANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEGEAEIASESDKEALataAELLGVDEEALEKVITQR 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  455 KTVTVGEKLILPYKLAEAVTVRNSMAKSLYSALFDWIVFRINHALlnskdlEQDTKTLS-IGVLDIFGFEDYE-NNSFEQ 532
Cdd:cd14891    320 EIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSL------GHDPDPLPyIGVLDIFGFESFEtKNDFEQ 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  533 FCINFANERLQHYFNQHIFKLEQEEYRTEGISWHNIDYIDNTCCINLISKKPTGLLHLLDEESNFPQATNQTLLDKFKHQ 612
Cdd:cd14891    394 LLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWPDNRECLDLIASKPNGILPLLDNEARNPNPSDAKLNETLHKT 473
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907198218  613 HEENSYieFPAV----MEPAFIIKHYAGKVKYGVKDFREKNTDHMRPDIVALLRSSrNAFVSGMTGI 675
Cdd:cd14891    474 HKRHPC--FPRPhpkdMREMFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASS-AKFSDQMQEL 537
MYSc_Myo40 cd14901
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ...
161-670 4.22e-143

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


Pssm-ID: 276866 [Multi-domain]  Cd Length: 655  Bit Score: 462.72  E-value: 4.22e-143
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  161 TLLENLRNRFKHEKIYTYVGSILIAINPFKFLPIYNPKYVKMY------DNHQLGKLEPHIYAVADVAYHAMLQ----RK 230
Cdd:cd14901      2 SILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFasrgQK 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  231 KNQCIVISGESGSGKTQSTNFLIHHLTALSQKGFASG-------VEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVN 303
Cdd:cd14901     82 CDQSILVSGESGAGKTETTKIIMNYLASVSSATTHGQnaterenVRDRVLESNPILEAFGNARTNRNNNSSRFGKFIRLG 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  304 YQETGTVLGAYVEKYLLEKSRLVYQEHNERNYHVFYYLLAGASEEERLAFHLKQPEEYHFLNQ-DCFT-VEGEDLRHDFE 381
Cdd:cd14901    162 FASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLNSsQCYDrRDGVDDSVQYA 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  382 RLQLAMEMVGFLPKTRRQIFSLLSAILHLGNISYKKKTYRDDSIDICNPEVLPIVSELLEVKEEMLFEALVTRKTVTVGE 461
Cdd:cd14901    242 KTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGGTFSMSSLANVRAACDLLGLDMDVLEKTLCTREIRAGGE 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  462 KLILPYKLAEAVTVRNSMAKSLYSALFDWIVFRINHALLNSkdlEQDTKTLSIGVLDIFGFEDYENNSFEQFCINFANER 541
Cdd:cd14901    322 YITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYS---ESTGASRFIGIVDIFGFEIFATNSLEQLCINFANEK 398
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  542 LQHYFNQHIFKLEQEEYRTEGISWHNIDYIDNTCCINLISKKPTGLLHLLDEESNFPQATNQTLLDKF-----KHQHEEN 616
Cdd:cd14901    399 LQQLFGKFVFEMEQDEYVAEAIPWTFVEYPNNDACVAMFEARPTGLFSLLDEQCLLPRGNDEKLANKYydllaKHASFSV 478
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907198218  617 SYIEfpaVMEPAFIIKHYAGKVKYGVKDFREKNTDHMRPDIVALLRSSRNAFVS 670
Cdd:cd14901    479 SKLQ---QGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLS 529
MYSc_Myo42 cd14903
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ...
162-986 9.95e-141

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: 456.16  E-value: 9.95e-141
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  162 LLENLRNRFKHEKIYTYVGSILIAINPFKFLP-IYNPKYVKMYDNHQLGKLEPHIYAVADVAYHAMLQRKKNQCIVISGE 240
Cdd:cd14903      3 ILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVSGE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  241 SGSGKTQSTNFLIHHLTALSQKGFASGVEQIIlGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQETGTVLGAYVEKYLL 320
Cdd:cd14903     83 SGAGKTETTKILMNHLATIAGGLNDSTIKKII-EVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLVGAKCRTYLL 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  321 EKSRLVYQEHNERNYHVFYYLLAGASEEERLAFHLKQPEEYHFLNqDCFTVEGEDLRHDFERLQLAMEMVGFLPKTRRQI 400
Cdd:cd14903    162 EKTRVISHERPERNYHIFYQLLASPDVEERLFLDSANECAYTGAN-KTIKIEGMSDRKHFARTKEALSLIGVSEEKQEVL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  401 FSLLSAILHLGNISYKKKTyRDDSIDICNP--EVLPIVSELLEVKEEMLFEALVTRKTVTVGEKLILPYKLAEAVTVRNS 478
Cdd:cd14903    241 FEVLAGILHLGQLQIQSKP-NDDEKSAIAPgdQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKKDQAEDCRDA 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  479 MAKSLYSALFDWIVFRINHALLNSKDLEQdtktlSIGVLDIFGFEDYENNSFEQFCINFANERLQHYFNQHIFKLEQEEY 558
Cdd:cd14903    320 LAKAIYSNVFDWLVATINASLGNDAKMAN-----HIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFKTVQIEY 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  559 RTEGISWHNIDYIDNTCCINLISKKpTGLLHLLDEESNFPQATNQTLLDKFKHQHE-ENSYIEFPAVMEPAFIIKHYAGK 637
Cdd:cd14903    395 EEEGIRWAHIDFADNQDVLAVIEDR-LGIISLLNDEVMRPKGNEESFVSKLSSIHKdEQDVIEFPRTSRTQFTIKHYAGP 473
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  638 VKYGVKDFREKNTDHMRPDIVALLRSSRNAFvsgmtgidpvavfrwavLRAFFRAVVAFREAGKrhiqrksghddttpca 717
Cdd:cd14903    474 VTYESLGFLEKHKDALLPDLSDLMRGSSKPF-----------------LRMLFKEKVESPAAAS---------------- 520
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  718 ilksmdsfsflqhpvhqrsleilqrckeekysitrknprtplsdlqgmntlneknqhdtfdiawnvrTGIRQSRLPASNT 797
Cdd:cd14903    521 -------------------------------------------------------------------TSLARGARRRRGG 533
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  798 SLLDKdgifahsasskllerahgiltrnknfrskpvlpkhllevnslkhltrltlqdritksllhlhkkkkppSISAQFQ 877
Cdd:cd14903    534 ALTTT--------------------------------------------------------------------TVGTQFK 545
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  878 ASLSKLMETLGQAEPYFVKCIRSNAEKLPLRFSDALVLRQLRYTGMLETVRIRQSGYSSKYSFQDFVSHFHVLLPQH--- 954
Cdd:cd14903    546 DSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFLPEGrnt 625
                          810       820       830
                   ....*....|....*....|....*....|...
gi 1907198218  955 IIPSKFNIQDFFRKININS-DNYQVGKTMVFLK 986
Cdd:cd14903    626 DVPVAERCEALMKKLKLESpEQYQMGLTRIYFQ 658
MYSc_Myo35 cd14896
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ...
161-986 3.61e-134

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: 436.52  E-value: 3.61e-134
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  161 TLLENLRNRFKHEKIYTYVGSILIAINPFKFLPIYNPKYVKMYDNHQLGKLEPHIYAVADVAYHAMLQRKKNQCIVISGE 240
Cdd:cd14896      2 SVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSGH 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  241 SGSGKTQSTNFLIHHLTALSQKGFASGVEQIiLGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQEtGTVLGAYVEKYLL 320
Cdd:cd14896     82 SGSGKTEAAKKIVQFLSSLYQDQTEDRLRQP-EDVLPILESFGHAKTILNANASRFGQVLRLHLQH-GVIVGASVSHYLL 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  321 EKSRLVYQEHNERNYHVFYYLLAGASEEERLAFHLKQPEEYHFLNQD--CfTVEGEDLRHDFERLQLAMEMVGFLPKTRR 398
Cdd:cd14896    160 ETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGgaC-RLQGKEDAQDFEGLLKALQGLGLCAEELT 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  399 QIFSLLSAILHLGNI---SYKKKTYrdDSIDICNPEVLPIVSELLEVKEEMLFEALVTRKTVTVGEKLILPYKLAEAVTV 475
Cdd:cd14896    239 AIWAVLAAILQLGNIcfsSSERESQ--EVAAVSSWAEIHTAARLLQVPPERLEGAVTHRVTETPYGRVSRPLPVEGAIDA 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  476 RNSMAKSLYSALFDWIVFRINHALLNSKDLEQDTktlSIGVLDIFGFEDYENNSFEQFCINFANERLQHYFNQHIFKLEQ 555
Cdd:cd14896    317 RDALAKTLYSRLFTWLLKRINAWLAPPGEAESDA---TIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLLAQEE 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  556 EEYRTEGISWHNIDYIDNTCCINLISKKPTGLLHLLDEESNFPQATNQTLLDKFKHQHEENSYIEFPAVMEPAFIIKHYA 635
Cdd:cd14896    394 EECQRELLPWVPIPQPPRESCLDLLVDQPHSLLSILDDQTWLSQATDHTFLQKCHYHHGDHPSYAKPQLPLPVFTVRHYA 473
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  636 GKVKYGVKDFREKNTDHMRPDIVALLRSSRNAFVSGMtgidpvavfrwavlraffravvaFREAgkrhiqrksghddttp 715
Cdd:cd14896    474 GTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSL-----------------------FQEA---------------- 514
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  716 cailksmdsfsflqhpvhqrsleilqrckEEKYsitrknprtplsdlqgmntlneknqhdtfdiawnvrtgirqsrlpas 795
Cdd:cd14896    515 -----------------------------EPQY----------------------------------------------- 518
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  796 ntslldkdgifahsasskllerahgiltrnknfrskpvlpkhllevnslkhltrltlqdritksllhlHKKKKPPSISAQ 875
Cdd:cd14896    519 --------------------------------------------------------------------GLGQGKPTLASR 530
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  876 FQASLSKLMETLGQAEPYFVKCIRSNAEKLPLRFSDALVLRQLRYTGMLETVRIRQSGYSSKYSFQDFVSHFHVLLP--Q 953
Cdd:cd14896    531 FQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALGSerQ 610
                          810       820       830
                   ....*....|....*....|....*....|....
gi 1907198218  954 HIIPSKFNIQDFFRKININ-SDNYQVGKTMVFLK 986
Cdd:cd14896    611 EALSDRERCGAILSQVLGAeSPLYHLGATKVLLK 644
MYSc_Myo17 cd14879
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ...
157-686 8.64e-131

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: 426.97  E-value: 8.64e-131
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  157 LNEKTLLENLRNRFKHEKIYTYVGS-ILIAINPFKFLPIYNPKYVKMYDN-------HQLGKLEPHIYAVADVAYHAMLQ 228
Cdd:cd14879      1 PSDDAITSHLASRFRSDLPYTRLGSsALVAVNPYKYLSSNSDASLGEYGSeyydttsGSKEPLPPHAYDLAARAYLRMRR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  229 RKKNQCIVISGESGSGKTQSTNFLIHHLTALSQKGFASG--VEQIILgAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQE 306
Cdd:cd14879     81 RSEDQAVVFLGETGSGKSESRRLLLRQLLRLSSHSKKGTklSSQISA-AEFVLDSFGNAKTLTNPNASRFGRYTELQFNE 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  307 TGTVLGAYVEKYLLEKSRLVYQEHNERNYHVFYYLLAGASEEERLAFHLKQPEEYHFL-NQDCF----TVEGEDlRHDFE 381
Cdd:cd14879    160 RGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLaSYGCHplplGPGSDD-AEGFQ 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  382 RLQLAMEMVGFLPKTRRQIFSLLSAILHLGNISYkkkTY----RDDSIDICNPEVLPIVSELLEVKEEMLFEALvTRKTV 457
Cdd:cd14879    239 ELKTALKTLGFKRKHVAQICQLLAAILHLGNLEF---TYdhegGEESAVVKNTDVLDIVAAFLGVSPEDLETSL-TYKTK 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  458 TVGEklilpyklaEAVTV----------RNSMAKSLYSALFDWIVFRINHALLNSKDLEQDTktlsIGVLDIFGFEDY-- 525
Cdd:cd14879    315 LVRK---------ELCTVfldpegaaaqRDELARTLYSLLFAWVVETINQKLCAPEDDFATF----ISLLDFPGFQNRss 381
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  526 -ENNSFEQFCINFANERLQHYFNQHIFKLEQEEYRTEGISWHNIDYIDNTCCINLISKKPTGLLHLLDEE-SNFPQATNQ 603
Cdd:cd14879    382 tGGNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSYFDNSDCVRLLRGKPGGLLGILDDQtRRMPKKTDE 461
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  604 TLLDKFKHQHE-ENSYIEFPAVM----EPAFIIKHYAGKVKYGVKDFREKNTDHMRPDIVALLRSSRNAFVSGMTGIDPV 678
Cdd:cd14879    462 QMLEALRKRFGnHSSFIAVGNFAtrsgSASFTVNHYAGEVTYSVEGFLERNGDVLSPDFVNLLRGATQLNAALSELLDTL 541

                   ....*....
gi 1907198218  679 AVFR-WAVL 686
Cdd:cd14879    542 DRTRlWSVF 550
MYSc_Myo43 cd14904
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ...
161-986 1.05e-130

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: 427.05  E-value: 1.05e-130
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  161 TLLENLRNRFKHEKIYTYVGSILIAINPFKFLP-IYNPKYVKMYDNHQLGKLEPHIYAVADVAYHAMLQRKKNQCIVISG 239
Cdd:cd14904      2 SILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVSG 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  240 ESGSGKTQSTNFLIHHLTALSQKGFASGVEQIIlGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQETGTVLGAYVEKYL 319
Cdd:cd14904     82 ESGAGKTETTKIVMNHLASVAGGRKDKTIAKVI-DVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAKCETYL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  320 LEKSRLVYQEHNERNYHVFYYLLAGASEEERLAFHLKQPEEYHFLNQ--DCFTVEGEDLRHDFERLQLAMEMVGFLPKTR 397
Cdd:cd14904    161 LEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLGDslAQMQIPGLDDAKLFASTQKSLSLIGLDNDAQ 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  398 RQIFSLLSAILHLGNISYKKktYRDDSIDICNPEVLPIVSELLEVKEEMLFEALVTRKTVTVGEKLILPYKLAEAVTVRN 477
Cdd:cd14904    241 RTLFKILSGVLHLGEVMFDK--SDENGSRISNGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLAPVEAEENRD 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  478 SMAKSLYSALFDWIVFRINHALlnskDLEQDTKTLSIGVLDIFGFEDYENNSFEQFCINFANERLQHYFNQHIFKLEQEE 557
Cdd:cd14904    319 ALAKAIYSKLFDWMVVKINAAI----STDDDRIKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKTVEEE 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  558 YRTEGISWHNIDYIDNTCCINLISKKpTGLLHLLDEESNFPQATNQTLLDKFKHQHEE---NSYIEFPAVMEPAFIIKHY 634
Cdd:cd14904    395 YIREGLQWDHIEYQDNQGIVEVIDGK-MGIIALMNDHLRQPRGTEEALVNKIRTNHQTkkdNESIDFPKVKRTQFIINHY 473
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  635 AGKVKYGVKDFREKNTDHMRPDIVALLRSSrnafvsgmtgidpvavfRWAVLRAFFRAVVAFREAgkrhiqrksghddtt 714
Cdd:cd14904    474 AGPVTYETVGFMEKHRDTLQNDLLDLVLLS-----------------SLDLLTELFGSSEAPSET--------------- 521
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  715 pcailksmdsfsflqhpvhqrsleilqrckeeKYSITRKnprtplsdlqgmntlneknqhdtfdiawnvrtgirqsrlpa 794
Cdd:cd14904    522 --------------------------------KEGKSGK----------------------------------------- 528
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  795 sntslldkdgifahsasskllerahgiltrnknfrskpvlpkhllevnslkhltrltlqdritksllhlhKKKKPPSISA 874
Cdd:cd14904    529 ----------------------------------------------------------------------GTKAPKSLGS 538
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  875 QFQASLSKLMETLGQAEPYFVKCIRSNAEKLPLRFSDALVLRQLRYTGMLETVRIRQSGYSSKYSFQDFVSHFHVLLPqh 954
Cdd:cd14904    539 QFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFP-- 616
                          810       820       830
                   ....*....|....*....|....*....|....*....
gi 1907198218  955 iiPSKFN------IQDFFRKININSD-NYQVGKTMVFLK 986
Cdd:cd14904    617 --PSMHSkdvrrtCSVFMTAIGRKSPlEYQIGKSLIYFK 653
MYSc_Myh10 cd14920
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ...
161-986 6.50e-128

class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy chain 10 (also called NMMHCB). Mutations in this gene have been associated with May-Hegglin anomaly and developmental defects in brain and heart. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276952 [Multi-domain]  Cd Length: 673  Bit Score: 419.80  E-value: 6.50e-128
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  161 TLLENLRNRFKHEKIYTYVGSILIAINPFKFLPIYNPKYVKMYDNHQLGKLEPHIYAVADVAYHAMLQRKKNQCIVISGE 240
Cdd:cd14920      2 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  241 SGSGKTQSTNFLIHHLT--ALSQKG-----FASGVEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQETGTVLGA 313
Cdd:cd14920     82 SGAGKTENTKKVIQYLAhvASSHKGrkdhnIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  314 YVEKYLLEKSRLVYQEHNERNYHVFYYLLAGASEEERLAFHLKQPEEYHFLNQDCFTVEGEDLRHDFERLQLAMEMVGFL 393
Cdd:cd14920    162 NIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMHIMGFS 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  394 PKTRRQIFSLLSAILHLGNISYKKKTYRDDSiDICNPEVLPIVSELLEVKEEMLFEALVTRKtVTVGEKLILPYKLAE-A 472
Cdd:cd14920    242 HEEILSMLKVVSSVLQFGNISFKKERNTDQA-SMPENTVAQKLCHLLGMNVMEFTRAILTPR-IKVGRDYVQKAQTKEqA 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  473 VTVRNSMAKSLYSALFDWIVFRINHALlnskDLEQDTKTLSIGVLDIFGFEDYENNSFEQFCINFANERLQHYFNQHIFK 552
Cdd:cd14920    320 DFAVEALAKATYERLFRWLVHRINKAL----DRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  553 LEQEEYRTEGISWHNIDY-IDNTCCINLISK--KPTGLLHLLDEESNFPQATNQTLLDKFkhQHEENSYIEFPAVMEPA- 628
Cdd:cd14920    396 LEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKL--VQEQGSHSKFQKPRQLKd 473
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  629 ---FIIKHYAGKVKYGVKDFREKNTDHMRPDIVALLRSSRNAFVSGMtgidpvavfrWavlraffravvafreagkRHIQ 705
Cdd:cd14920    474 kadFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAEL----------W------------------KDVD 525
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  706 RKSGHDDTTpcailkSMDSFSFlqhpvhqrsleilqrckeekysitrknprtplsdlqgmntlneknqhdtfdiawnvrt 785
Cdd:cd14920    526 RIVGLDQVT------GMTETAF---------------------------------------------------------- 541
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  786 girqsrlpasntslldkdgifahsasskllerAHGILTRNKNFRskpvlpkhllevnslkhltrltlqdritksllhlhk 865
Cdd:cd14920    542 --------------------------------GSAYKTKKGMFR------------------------------------ 553
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  866 kkkppSISAQFQASLSKLMETLGQAEPYFVKCIRSNAEKLPLRFSDALVLRQLRYTGMLETVRIRQSGYSSKYSFQDFVS 945
Cdd:cd14920    554 -----TVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 628
                          810       820       830       840
                   ....*....|....*....|....*....|....*....|....*.
gi 1907198218  946 HFHVLLPqHIIPSKF-----NIQDFFRKININSDNYQVGKTMVFLK 986
Cdd:cd14920    629 RYEILTP-NAIPKGFmdgkqACERMIRALELDPNLYRIGQSKIFFR 673
MYSc_Myo41 cd14902
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ...
162-674 9.02e-124

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: 409.28  E-value: 9.02e-124
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  162 LLENLRNRFKHEKIYTYVGSILIAINPFKFLP-IYNPKYVKMYD--------NHQLGKLEPHIYAVADVAYHAMLQ-RKK 231
Cdd:cd14902      3 LLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKpERR 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  232 NQCIVISGESGSGKTQSTNFLIHHLTAL--------SQKGFASGVEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVN 303
Cdd:cd14902     83 NQSILVSGESGSGKTESTKFLMQFLTSVgrdqssteQEGSDAVEIGKRILQTNPILESFGNAQTIRNDNSSRFGKFIKIQ 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  304 YQETGTVLGAYVEKYLLEKSRLVYQEHNERNYHVFYYLLAGASEEERLAFHLKQPEEYHFLNQ-DCFTVEGEDLRHDFER 382
Cdd:cd14902    163 FGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELLNSyGPSFARKRAVADKYAQ 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  383 LQL----AMEMVGFLPKTRRQIFSLLSAILHLGNISYKKKTYRDDSIDIC--NPEVLPIVSELLEVKEEMLFEALVTRKT 456
Cdd:cd14902    243 LYVetvrAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAVTaaSRFHLAKCAELMGVDVDKLETLLSSREI 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  457 VTVGEKLILPYKLAEAVTVRNSMAKSLYSALFDWIVFR----INHALLNSKDLEQDTKTLSIGVLDIFGFEDYENNSFEQ 532
Cdd:cd14902    323 KAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRlsdeINYFDSAVSISDEDEELATIGILDIFGFESLNRNGFEQ 402
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  533 FCINFANERLQHYFNQHIFKLEQEEYRTEGISWHNIDYIDNTCCINLISKKPTGLLHLLDEESNFPQATNQTLLDKFKHQ 612
Cdd:cd14902    403 LCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYPSNAACLALFDDKSNGLFSLLDQECLMPKGSNQALSTKFYRY 482
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907198218  613 HeensyiefpaVMEPAFIIKHYAGKVKYGVKDFREKNTDHMRPDIVALLRSSRNAFVSGMTG 674
Cdd:cd14902    483 H----------GGLGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGA 534
MYSc_Myh2_insects_mollusks cd14911
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ...
161-986 5.81e-123

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: 405.52  E-value: 5.81e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  161 TLLENLRNRFKHEKIYTYVGSILIAINPFKFLPIYNPKYVKMYDNHQLGKLEPHIYAVADVAYHAMLQRKKNQCIVISGE 240
Cdd:cd14911      2 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  241 SGSGKTQSTNFLIHHL----------------TALSQKGFASGVEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNY 304
Cdd:cd14911     82 SGAGKTENTKKVIQFLayvaaskpkgsgavphPAVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  305 QETGTVLGAYVEKYLLEKSRLVYQEHNERNYHVFYYLLAGASEEERLAFHLKQPEEYHFLNQDCFTVEGEDLRHDFERLQ 384
Cdd:cd14911    162 DASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAEFQATV 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  385 LAMEMVGFLPKTRRQIFSLLSAILHLGNISYKKKTyRDDSIDICNPEVLPIVSELLEVKEEMLFEALVTRKtVTVGEKLI 464
Cdd:cd14911    242 KSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQER-NNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPR-IKVGRDFV 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  465 LPYKLAEAVTVR-NSMAKSLYSALFDWIVFRINHALlnskDLEQDTKTLSIGVLDIFGFEDYENNSFEQFCINFANERLQ 543
Cdd:cd14911    320 TKAQTKEQVEFAvEAIAKACYERMFKWLVNRINRSL----DRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQ 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  544 HYFNQHIFKLEQEEYRTEGISWHNIDY-IDNTCCINLIsKKPTGLLHLLDEESNFPQATNQTLLDKFKHQHEENSYI--- 619
Cdd:cd14911    396 QLFNHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLI-DKPGGIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFmkt 474
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  620 EFPAVMEpaFIIKHYAGKVKYGVKDFREKNTDHMRPDIVALLRSSRnafvsgmtgiDPVAVFRWavlraffravvafrea 699
Cdd:cd14911    475 DFRGVAD--FAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQ----------DPFVVNIW---------------- 526
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  700 gkrhiqrksghddttpcailksmdsfsflqhpvhqrsleilqrckeekysitrknprtplsdlqgmntlneknqhdtfdi 779
Cdd:cd14911        --------------------------------------------------------------------------------
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  780 awnvrtgirqsrlpasntslldKDGIFAHSASSKLLERAHGILTRNKNFRskpvlpkhllevnslkhltrltlqdritks 859
Cdd:cd14911    527 ----------------------KDAEIVGMAQQALTDTQFGARTRKGMFR------------------------------ 554
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  860 llhlhkkkkppSISAQFQASLSKLMETLGQAEPYFVKCIRSNAEKLPLRFSDALVLRQLRYTGMLETVRIRQSGYSSKYS 939
Cdd:cd14911    555 -----------TVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIP 623
                          810       820       830       840       850
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907198218  940 FQDFVSHFHVLLPqHIIPSKF-----NIQDFFRKININSDNYQVGKTMVFLK 986
Cdd:cd14911    624 FQEFRQRYELLTP-NVIPKGFmdgkkACEKMIQALELDSNLYRVGQSKIFFR 674
MYSc_Myh15_mammals cd14929
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ...
161-986 7.45e-123

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: 404.74  E-value: 7.45e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  161 TLLENLRNRFKHEKIYTYVGSILIAINPFKFLPIYNPKYVKMYDNHQLGKLEPHIYAVADVAYHAMLQRKKNQCIVISGE 240
Cdd:cd14929      2 SVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTGE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  241 SGSGKTQSTNFLIHHLTALS----QKGFASGVEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQETGTVLGAYVE 316
Cdd:cd14929     82 SGAGKTVNTKHIIQYFATIAamieSKKKLGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSADID 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  317 KYLLEKSRLVYQEHNERNYHVFYYLLAGASEEERLAFHLKQPEEYHFLNQDCFTVEGEDLRHDFERLQLAMEMVGFLPKT 396
Cdd:cd14929    162 IYLLEKSRVIFQQPGERNYHIFYQILSGKKELRDLLLVSANPSDFHFCSCGAVAVESLDDAEELLATEQAMDILGFLPDE 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  397 RRQIFSLLSAILHLGNISYKKKTyRDDSIDICNPEVLPIVSELLEVKEEMLFEALVTRKtVTVGEKLILPYKLAEAVTVR 476
Cdd:cd14929    242 KYGCYKLTGAIMHFGNMKFKQKP-REEQLEADGTENADKAAFLMGINSSELVKGLIHPR-IKVGNEYVTRSQNIEQVTYA 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  477 -NSMAKSLYSALFDWIVFRINHALlnskdleqDTKTLS---IGVLDIFGFEDYENNSFEQFCINFANERLQHYFNQHIFK 552
Cdd:cd14929    320 vGALSKSIYERMFKWLVARINRVL--------DAKLSRqffIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFV 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  553 LEQEEYRTEGISWHNIDY-IDNTCCINLIsKKPTGLLHLLDEESNFPQATNQTLLDK-FKHQHEENSYIEFPAV----ME 626
Cdd:cd14929    392 LEQEEYRKEGIDWVSIDFgLDLQACIDLI-EKPMGIFSILEEECMFPKATDLTFKTKlFDNHFGKSVHFQKPKPdkkkFE 470
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  627 PAFIIKHYAGKVKYGVKDFREKNTDHMRPDIVALLRSSRNafvsgmtgidpvavfrwAVLRAFFravvafreagkrhiqr 706
Cdd:cd14929    471 AHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSN-----------------RLLASLF---------------- 517
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  707 ksghddttpcailksmdsfsflqhpvhqrsleilqrckeEKYSITRknprtplSDLQgmntLNEKNQhdtfdiawnvrtg 786
Cdd:cd14929    518 ---------------------------------------ENYISTD-------SAIQ----FGEKKR------------- 534
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  787 irqsrlpasntslldKDGIFAHSASSkllerahgiltrnknfrskpvlpkhllevnslkhltrltlqdritksllhLHKK 866
Cdd:cd14929    535 ---------------KKGASFQTVAS--------------------------------------------------LHKE 549
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  867 kkppsisaqfqaSLSKLMETLGQAEPYFVKCIRSNAEKLPLRFSDALVLRQLRYTGMLETVRIRQSGYSSKYSFQDFVSH 946
Cdd:cd14929    550 ------------NLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQR 617
                          810       820       830       840
                   ....*....|....*....|....*....|....*....|....*
gi 1907198218  947 FHVLLPQHIIPSKF-----NIQDFFRKININSDNYQVGKTMVFLK 986
Cdd:cd14929    618 YCILNPRTFPKSKFvssrkAAEELLGSLEIDHTQYRFGITKVFFK 662
PTZ00014 PTZ00014
myosin-A; Provisional
148-1046 2.86e-122

myosin-A; Provisional


Pssm-ID: 240229 [Multi-domain]  Cd Length: 821  Bit Score: 408.26  E-value: 2.86e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  148 FDDLCSLPDLNEKTLLENLRNRFKHEKIYTYVGSILIAINPFKFLPIYNPKYVKMY-DNHQLGKLEPHIYAVADVAYHAM 226
Cdd:PTZ00014    98 YGDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYrDAKDSDKLPPHVFTTARRALENL 177
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  227 LQRKKNQCIVISGESGSGKTQSTNFLIHHLTALSQKGFASGVEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQE 306
Cdd:PTZ00014   178 HGVKKSQTIIVSGESGAGKTEATKQIMRYFASSKSGNMDLKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGE 257
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  307 TGTVLGAYVEKYLLEKSRLVYQEHNERNYHVFYYLLAGASEEERLAFHLKQPEEYHFLNQDCFTVEGEDLRHDFERLQLA 386
Cdd:PTZ00014   258 EGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPKCLDVPGIDDVKDFEEVMES 337
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  387 MEMVGFLPKTRRQIFSLLSAILHLGNISYKKKTyrDDSIDIC------NPEVLPIVSELLEVKEEMLFEALVTRKTVTVG 460
Cdd:PTZ00014   338 FDSMGLSESQIEDIFSILSGVLLLGNVEIEGKE--EGGLTDAaaisdeSLEVFNEACELLFLDYESLKKELTVKVTYAGN 415
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  461 EKLILPYKLAEAVTVRNSMAKSLYSALFDWIVFRINHALLNSKDLEqdtktLSIGVLDIFGFEDYENNSFEQFCINFANE 540
Cdd:PTZ00014   416 QKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFK-----VFIGMLDIFGFEVFKNNSLEQLFINITNE 490
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  541 RLQHYFNQHIFKLEQEEYRTEGISWHNIDYIDNTCCINLISKKPTGLLHLLDEESNFPQATNQTLLDKFKHQHEENS-YI 619
Cdd:PTZ00014   491 MLQKNFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGKSVLSILEDQCLAPGGTDEKFVSSCNTNLKNNPkYK 570
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  620 EFPAVMEPAFIIKHYAGKVKYGVKDFREKNTDHMRPDIVALLRSSRNAFVSGMtgidpvavfrwavlrafFRAVVAfrEA 699
Cdd:PTZ00014   571 PAKVDSNKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDL-----------------FEGVEV--EK 631
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  700 GKrhiqrksghddttpcailksmdsfsflqhpvhqrsleilqrckeekysitrknprtplsdlqgmntlneknqhdtfdi 779
Cdd:PTZ00014   632 GK------------------------------------------------------------------------------ 633
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  780 awnvrtgirqsrlpasntslldkdgifahsasskllerahgiltrnknfrskpvlpkhllevnslkhltrltlqdrITKS 859
Cdd:PTZ00014   634 ----------------------------------------------------------------------------LAKG 637
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  860 LLhlhkkkkppsISAQFQASLSKLMETLGQAEPYFVKCIRSNAEKLPLRFSDALVLRQLRYTGMLETVRIRQSGYSSKYS 939
Cdd:PTZ00014   638 QL----------IGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRT 707
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  940 FQDFVSHFHVL-LPQHIIPS---KFNIQDFFRKININSDNYQVGKTMVFLKEHERQHLQDLLhQEVLRR----IVLLQRW 1011
Cdd:PTZ00014   708 FAEFLSQFKYLdLAVSNDSSldpKEKAEKLLERSGLPKDSYAIGKTMVFLKKDAAKELTQIQ-REKLAAweplVSVLEAL 786
                          890       900       910
                   ....*....|....*....|....*....|....*
gi 1907198218 1012 FRVLLSRQQFLHLRQASIIIQRFWRNYLNQKQVRN 1046
Cdd:PTZ00014   787 ILKIKKKRKVRKNIKSLVRIQAHLRRHLVIAEIKP 821
MYSc_Myo39 cd14900
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ...
161-661 1.99e-121

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


Pssm-ID: 276865  Cd Length: 627  Bit Score: 399.30  E-value: 1.99e-121
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  161 TLLENLRNRFKHEKIYTYVGSILIAINPFKFLP-IYNPKYVKMY-------DNHQLGK----LEPHIYAVADVAYHAM-- 226
Cdd:cd14900      2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearSSSTRNKgsdpMPPHIYQVAGEAYKAMml 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  227 --LQRKKNQCIVISGESGSGKTQSTNFLIHHLT---------ALSQKGFASGVEQIILGAGPVLEAFGNAKTAHNNNSSR 295
Cdd:cd14900     82 glNGVMSDQSILVSGESGSGKTESTKFLMEYLAqagdnnlaaSVSMGKSTSGIAAKVLQTNILLESFGNARTLRNDNSSR 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  296 FGKFIQVNYQETGTVLGAYVEKYLLEKSRLVYQEHNERNYHVFYYLLAGASEEERLafhlkqpeeyhflnqdcftveged 375
Cdd:cd14900    162 FGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARK------------------------ 217
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  376 lRHDFERLQLAMEMVGFLPKTRRQIFSLLSAILHLGNISYKKKTyRDDSIDICNPEVLP-------IVSELLEVKEEMLF 448
Cdd:cd14900    218 -RDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDE-NSDRLGQLKSDLAPssiwsrdAAATLLSVDATKLE 295
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  449 EALVTRKTVTVGEKLILPYKLAEAVTVRNSMAKSLYSALFDWIVFRINHALLNSKDLEQDTKTLSIGVLDIFGFEDYENN 528
Cdd:cd14900    296 KALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLKMDDSSKSHGGLHFIGILDIFGFEVFPKN 375
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  529 SFEQFCINFANERLQHYFNQHIFKLEQEEYRTEGISWHNIDYIDNTCCINLISKKPTGLLHLLDEESNFPQATNQTLLDK 608
Cdd:cd14900    376 SFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFCDNQDCVNLISQRPTGILSLIDEECVMPKGSDTTLASK 455
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907198218  609 FKHQHEenSYIEFPAVM----EPAFIIKHYAGKVKYGVKDFREKNTDHMRPDIVALL 661
Cdd:cd14900    456 LYRACG--SHPRFSASRiqraRGLFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDLF 510
MYSc_Myo47 cd14908
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ...
162-653 1.45e-119

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: 395.82  E-value: 1.45e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  162 LLENLRNRFKHEKIYTYVGSILIAINPFKFLPIYNPKYVKMYDNHQL---------GKLEPHIYAVADVAYHAML-QRKK 231
Cdd:cd14908      3 ILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRQEGLlrsqgiespQALGPHVFAIADRSYRQMMsEIRA 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  232 NQCIVISGESGSGKTQSTNFLIHHLTAL-------SQKGFASG---VEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQ 301
Cdd:cd14908     83 SQSILISGESGAGKTESTKIVMLYLTTLgngeegaPNEGEELGklsIMDRVLQSNPILEAFGNARTLRNDNSSRFGKFIE 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  302 VNYQETGTVLGAYVEKYLLEKSRLVYQEHNERNYHVFYYLLAGASEEER--------LAFHLKQPEEYHFLNQ-DCF--- 369
Cdd:cd14908    163 LGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHekyefhdgITGGLQLPNEFHYTGQgGAPdlr 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  370 TVEGEDlrhDFERLQLAMEMVGFLPKTRRQIFSLLSAILHLGNISYKKKTYRD--DSIDICNPEVLPIVSELLEVKEEML 447
Cdd:cd14908    243 EFTDED---GLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGaaEIAEEGNEKCLARVAKLLGVDVDKL 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  448 FEALVTRKTVTVGEKLILPYKLAEAVTVRNSMAKSLYSALFDWIVFRINHALlnSKDLEQDTKTlSIGVLDIFGFEDYEN 527
Cdd:cd14908    320 LRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSI--NWENDKDIRS-SVGVLDIFGFECFAH 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  528 NSFEQFCINFANERLQHYFNQHIFKLEQEEYRTEGISWHNIDYIDNTCCINLISKKPTGLLHLLDEE---------SNFP 598
Cdd:cd14908    397 NSFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFPDNQDCLDTIQAKKKGILTMLDDEcrlgirgsdANYA 476
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907198218  599 QATNQTLLDKFKHQHEENSYIEFPAVMEPA--FIIKHYAGKVKYGVKD-FREKNTDHM 653
Cdd:cd14908    477 SRLYETYLPEKNQTHSENTRFEATSIQKTKliFAVRHFAGQVQYTVETtFCEKNKDEI 534
MYSc_Myh3 cd14913
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ...
162-986 8.33e-118

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: 390.18  E-value: 8.33e-118
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  162 LLENLRNRFKHEKIYTYVGSILIAINPFKFLPIYNPKYVKMYDNHQLGKLEPHIYAVADVAYHAMLQRKKNQCIVISGES 241
Cdd:cd14913      3 VLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  242 GSGKTQSTNFLIHHLTALSQKG---------FASGVEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQETGTVLG 312
Cdd:cd14913     83 GAGKTVNTKRVIQYFATIAATGdlakkkdskMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  313 AYVEKYLLEKSRLVYQEHNERNYHVFYYLLAGASEEE-RLAFHLKQPEEYHFLNQDCFTVEGEDLRHDFERLQLAMEMVG 391
Cdd:cd14913    163 ADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELiELLLITTNPYDYPFISQGEILVASIDDAEELLATDSAIDILG 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  392 FLPKTRRQIFSLLSAILHLGNISYKKKTyRDDSIDICNPEVLPIVSELLEVKEEMLFEALVTRKtVTVGEKLILPYKLAE 471
Cdd:cd14913    243 FTPEEKSGLYKLTGAVMHYGNMKFKQKQ-REEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPR-VKVGNEYVTKGQTVD 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  472 AV-TVRNSMAKSLYSALFDWIVFRINHALlnskdleqDTKTLS---IGVLDIFGFEDYENNSFEQFCINFANERLQHYFN 547
Cdd:cd14913    321 QVhHAVNALSKSVYEKLFLWMVTRINQQL--------DTKLPRqhfIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFN 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  548 QHIFKLEQEEYRTEGISWHNIDY-IDNTCCINLIsKKPTGLLHLLDEESNFPQATNQTLLDKFKHQH-EENSYIEFPAVM 625
Cdd:cd14913    393 HHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYDQHlGKSNNFQKPKVV 471
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  626 ----EPAFIIKHYAGKVKYGVKDFREKNTDHMRPDIVALLRSSRNAFVsgmtgidpvavfrwAVLRAFFRAVVAfrEAGK 701
Cdd:cd14913    472 kgraEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLL--------------AHLYATFATADA--DSGK 535
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  702 RHIQRKSGhddttpcailksmDSFSflqhpvhqrsleilqrckeekysitrknprtplsdlqgmntlneknqhdtfdiaw 781
Cdd:cd14913    536 KKVAKKKG-------------SSFQ------------------------------------------------------- 547
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  782 nvrtgirqsrlpasntslldkdgifahsasskllerahgiltrnknfrskpvlpkhllevnslkhltrltlqdritksll 861
Cdd:cd14913        --------------------------------------------------------------------------------
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  862 hlhkkkkppSISAQFQASLSKLMETLGQAEPYFVKCIRSNAEKLPLRFSDALVLRQLRYTGMLETVRIRQSGYSSKYSFQ 941
Cdd:cd14913    548 ---------TVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYG 618
                          810       820       830       840       850
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907198218  942 DFVSHFHVLLPQHI-----IPSKFNIQDFFRKININSDNYQVGKTMVFLK 986
Cdd:cd14913    619 DFKQRYRVLNASAIpegqfIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
MYSc_Myo14 cd14876
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ...
163-986 1.47e-117

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: 388.58  E-value: 1.47e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  163 LENLRNRFKHEKIYTYVGSILIAINPFKFLPIYNPKYVKMY-DNHQLGKLEPHIYAVADVAYHAMLQRKKNQCIVISGES 241
Cdd:cd14876      4 LDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYrDAPDLTKLPPHVFYTARRALENLHGVNKSQTIIVSGES 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  242 GSGKTQSTNFLIHHLtALSQKGFASG-VEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQETGTVLGAYVEKYLL 320
Cdd:cd14876     84 GAGKTEATKQIMRYF-ASAKSGNMDLrIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIRYGSVVAFLL 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  321 EKSRLVYQEHNERNYHVFYYLLAGASEEERLAFHLKQPEEYHFLNQDCFTVEGEDLRHDFERLQLAMEMVGFLPKTRRQI 400
Cdd:cd14876    163 EKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLNPKCLDVPGIDDVADFEEVLESLKSMGLTEEQIDTV 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  401 FSLLSAILHLGNISYKKKTYR--DDS--IDICNPEVLPIVSELLEVKEEMLFEALVTRKTVTVGEKLILPYKLAEAVTVR 476
Cdd:cd14876    243 FSIVSGVLLLGNVKITGKTEQgvDDAaaISNESLEVFKEACSLLFLDPEALKRELTVKVTKAGGQEIEGRWTKDDAEMLK 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  477 NSMAKSLYSALFDWIVFRINHALlnskDLEQDTKTLsIGVLDIFGFEDYENNSFEQFCINFANERLQHYFNQHIFKLEQE 556
Cdd:cd14876    323 LSLAKAMYDKLFLWIIRNLNSTI----EPPGGFKNF-MGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFIDIVFERESK 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  557 EYRTEGISWHNIDYIDNTCCINLISKKPTGLLHLLDEESNFPQATNQTLLDKFKHQHEENSYIEfPAVMEP--AFIIKHY 634
Cdd:cd14876    398 LYKDEGIPTAELEYTSNAEVIDVLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSKLKSNGKFK-PAKVDSniNFIVVHT 476
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  635 AGKVKYGVKDFREKNTDHMRPDIVALLRSSRNAFVSGMtgidpvavfrwavlrafFRAVVAfrEAGKrhiqrksghddtt 714
Cdd:cd14876    477 IGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKAL-----------------FEGVVV--EKGK------------- 524
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  715 pcailksmdsfsflqhpvhqrsleilqrckeekysitrknprtplsdlqgmntlneknqhdtfdiawnvrtgirqsrlpa 794
Cdd:cd14876        --------------------------------------------------------------------------------
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  795 sntslldkdgifahsasskllerahgiltrnknfrskpvlpkhllevnslkhltrltlqdrITKSLLhlhkkkkppsISA 874
Cdd:cd14876    525 -------------------------------------------------------------IAKGSL----------IGS 533
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  875 QFQASLSKLMETLGQAEPYFVKCIRSNAEKLPLRFSDALVLRQLRYTGMLETVRIRQSGYSSKYSFQDFVSHFHVLLPQ- 953
Cdd:cd14876    534 QFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFLDLGi 613
                          810       820       830
                   ....*....|....*....|....*....|....*.
gi 1907198218  954 ---HIIPSKFNIQDFFRKININSDNYQVGKTMVFLK 986
Cdd:cd14876    614 andKSLDPKVAALKLLESSGLSEDEYAIGKTMVFLK 649
MYSc_Myo34 cd14895
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ...
166-986 1.54e-117

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: 390.47  E-value: 1.54e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  166 LRNRFKHEKIYTYVGSILIAINPFKFLPiynpkyvKMYDNHQLGK-------LEPHIYAVADVAYHAMLQR-------KK 231
Cdd:cd14895      7 LAQRYGVDQVYCRSGAVLIAVNPFKHIP-------GLYDLHKYREempgwtaLPPHVFSIAEGAYRSLRRRlhepgasKK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  232 NQCIVISGESGSGKTQSTNFLIHHLTALSQKGFA----------SGVEqiILGAGPVLEAFGNAKTAHNNNSSRFGKFIQ 301
Cdd:cd14895     80 NQTILVSGESGAGKTETTKFIMNYLAESSKHTTAtssskrrraiSGSE--LLSANPILESFGNARTLRNDNSSRFGKFVR 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  302 VNYQ-----ETGTVLGAYVEKYLLEKSRLVYQEHNERNYHVFYYLLAGASEE--ERLAFHLKQPEEYHFLN-QDCFtVEG 373
Cdd:cd14895    158 MFFEgheldTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDmkLELQLELLSAQEFQYISgGQCY-QRN 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  374 EDLRHD--FERLQLAMEMVGFLPKTRRQIFSLLSAILHLGNISY---KKKTYRDDSIDICNP--------------EVLP 434
Cdd:cd14895    237 DGVRDDkqFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFvasSEDEGEEDNGAASAPcrlasaspssltvqQHLD 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  435 IVSELLEVKEEMLFEALVTRKTVTVGEKLILPYKLAEAVTVRNSMAKSLYSALFDWIVFRIN-------HALLNSKDLEQ 507
Cdd:cd14895    317 IVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNsaspqrqFALNPNKAANK 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  508 DTkTLSIGVLDIFGFEDYENNSFEQFCINFANERLQHYFNQHIFKLEQEEYRTEGISWHNIDYIDNTCCINLISKKPTGL 587
Cdd:cd14895    397 DT-TPCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDNSVCLEMLEQRPSGI 475
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  588 LHLLDEESNFPQATNQTLLDKFKHQHEENSYieFPAV----MEPAFIIKHYAGKVKYGVKDFREKNTDHMRPDIVALLRS 663
Cdd:cd14895    476 FSLLDEECVVPKGSDAGFARKLYQRLQEHSN--FSASrtdqADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAELFSVLGK 553
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  664 SRNAFvsgmtgidpvavfrwavLRAFFRAVVAFREAgkrhiqrksghddttpcailksmdSFSFLQHPVHQRSleilqrc 743
Cdd:cd14895    554 TSDAH-----------------LRELFEFFKASESA------------------------ELSLGQPKLRRRS------- 585
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  744 keekysitrknprtplSDLQGMntlneknqhdtfdiawnvrtgirqsrlpasntslldkdgifahsasskllerahgilt 823
Cdd:cd14895    586 ----------------SVLSSV---------------------------------------------------------- 591
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  824 rnknfrskpvlpkhllevnslkhltrltlqdritksllhlhkkkkppSISAQFQASLSKLMETLGQAEPYFVKCIRSNAE 903
Cdd:cd14895    592 -----------------------------------------------GIGSQFKQQLASLLDVVQQTQTHYIRCIKPNDE 624
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  904 KLPLRFSDALVLRQLRYTGMLETVRIRQSGYSSKYSFQDFVSHFHVLLPQHiIPSKFNIQDFFRKINInsDNYQVGKTMV 983
Cdd:cd14895    625 SASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAK-NASDATASALIETLKV--DHAELGKTRV 701

                   ...
gi 1907198218  984 FLK 986
Cdd:cd14895    702 FLR 704
MYSc_Myh16 cd14934
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ...
161-664 1.87e-117

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: 389.00  E-value: 1.87e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  161 TLLENLRNRFKHEKIYTYVGSILIAINPFKFLPIYNPKYVKMYDNHQLGKLEPHIYAVADVAYHAMLQRKKNQCIVISGE 240
Cdd:cd14934      2 SVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITGE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  241 SGSGKTQSTNFLIHHLTALSQKGFAS-----GVEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQETGTVLGAYV 315
Cdd:cd14934     82 SGAGKTENTKKVIQYFANIGGTGKQSsdgkgSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGADI 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  316 EKYLLEKSRLVYQEHNERNYHVFYYLLAGASEE--ERLAFhLKQPEEYHFLNQDCFTVEGEDlrhDFERLQL---AMEMV 390
Cdd:cd14934    162 ESYLLEKSRVISQQAAERGYHIFYQILSNKKPEliESLLL-VPNPKEYHWVSQGVTVVDNMD---DGEELQItdvAFDVL 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  391 GFLPKTRRQIFSLLSAILHLGNISYKKKTyRDDSIDICNPEVLPIVSELLEVKEEMLFEAlVTRKTVTVGEKLILP-YKL 469
Cdd:cd14934    238 GFSAEEKIGVYKLTGGIMHFGNMKFKQKP-REEQAEVDTTEVADKVAHLMGLNSGELQKG-ITRPRVKVGNEFVQKgQNM 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  470 AEAVTVRNSMAKSLYSALFDWIVFRINHALlnskdleqDTK---TLSIGVLDIFGFEDYENNSFEQFCINFANERLQHYF 546
Cdd:cd14934    316 EQCNNSIGALGKAVYDKMFKWLVVRINKTL--------DTKmqrQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFF 387
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  547 NQHIFKLEQEEYRTEGISWHNIDY-IDNTCCINLIsKKPTGLLHLLDEESNFPQATNQTlldkFKHQHEENSYIEFPAVM 625
Cdd:cd14934    388 NHHMFVLEQEEYKREGIEWVFIDFgLDLQACIDLL-EKPMGIFSILEEQCVFPKATDAT----FKAALYDNHLGKSSNFL 462
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 1907198218  626 EPA----------FIIKHYAGKVKYGVKDFREKNTDHMRPDIVALLRSS 664
Cdd:cd14934    463 KPKggkgkgpeahFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKS 511
MYSc_Myh7b cd14927
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ...
161-986 7.69e-117

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: 387.77  E-value: 7.69e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  161 TLLENLRNRFKHEKIYTYVGSILIAINPFKFLPIYNPKYVKMYDNHQLGKLEPHIYAVADVAYHAMLQRKKNQCIVISGE 240
Cdd:cd14927      2 SVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITGE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  241 SGSGKTQSTNFLIHHLTALSQKGFASG-------------VEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQET 307
Cdd:cd14927     82 SGAGKTVNTKRVIQYFAIVAALGDGPGkkaqflatktggtLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  308 GTVLGAYVEKYLLEKSRLVYQEHNERNYHVFYYLLAGASEE-ERLAFHLKQPEEYHFLNQDCFTVEGEDlrhDFERLQL- 385
Cdd:cd14927    162 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPElQDMLLVSMNPYDYHFCSQGVTTVDNMD---DGEELMAt 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  386 --AMEMVGFLPKTRRQIFSLLSAILHLGNISYKKKTyRDDSIDICNPEVLPIVSELLEVKEEMLFEALVTRKtVTVGEKL 463
Cdd:cd14927    239 dhAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQ-REEQAEADGTESADKAAYLMGVSSADLLKGLLHPR-VKVGNEY 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  464 ILPYKLAEAVTVR-NSMAKSLYSALFDWIVFRINHALLNSKdleqdTKTLSIGVLDIFGFEDYENNSFEQFCINFANERL 542
Cdd:cd14927    317 VTKGQSVEQVVYAvGALAKATYDRMFKWLVSRINQTLDTKL-----PRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKL 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  543 QHYFNQHIFKLEQEEYRTEGISWHNIDY-IDNTCCINLIsKKPTGLLHLLDEESNFPQATNQTLLDKFKHQHEENSyief 621
Cdd:cd14927    392 QQFFNHHMFILEQEEYKREGIEWVFIDFgLDLQACIDLI-EKPLGILSILEEECMFPKASDASFKAKLYDNHLGKS---- 466
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  622 PAVMEPA----------FIIKHYAGKVKYGVKDFREKNTDHMRPDIVALLRSSRNAFVSGMTgidpvavfrwavlraffr 691
Cdd:cd14927    467 PNFQKPRpdkkrkyeahFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLY------------------ 528
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  692 avvafreagkrhiqrksghddttpcailksmdsfsflqhpvhqrsleilqrckeEKYSITrknprtplsdlqgmntlnek 771
Cdd:cd14927    529 ------------------------------------------------------ENYVGS-------------------- 534
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  772 nqhdtfDIAWNVRTGIRQSRLPASNtslldkdgifahsasskllerahgiltrnknfrskpvlpkhllevnslkhltrlt 851
Cdd:cd14927    535 ------DSTEDPKSGVKEKRKKAAS------------------------------------------------------- 553
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  852 lqdriTKSLLHLHKKkkppsisaqfqaSLSKLMETLGQAEPYFVKCIRSNAEKLPLRFSDALVLRQLRYTGMLETVRIRQ 931
Cdd:cd14927    554 -----FQTVSQLHKE------------NLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICR 616
                          810       820       830       840       850       860
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  932 SGYSSKYSFQDFVSHFHVLLPQHIIPSKF-----NIQDFFRKININSDNYQVGKTMVFLK 986
Cdd:cd14927    617 KGFPNRILYADFKQRYRILNPSAIPDDKFvdsrkATEKLLGSLDIDHTQYQFGHTKVFFK 676
RhoGAP_myosin_IX cd04377
RhoGAP_myosin_IX: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
2115-2300 2.68e-114

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: 360.21  E-value: 2.68e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2115 FGVELSRLTSEDRAVPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDAESVNLDDYNIHVIASVFKQWLRD 2194
Cdd:cd04377      1 FGVSLSSLTSEDRSVPLVLEKLLEHIEMHGLYTEGIYRKSGSANKIKELRQGLDTDPDSVNLEDYPIHVITSVLKQWLRE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2195 LPNPLMTFELYEEFLRAMGLQERKETIRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEDTNRMSANALAIVFAPCILRC 2274
Cdd:cd04377     81 LPEPLMTFELYENFLRAMELEEKQERVRALYSVLEQLPRANLNTLERLIFHLVRVALQEEVNRMSANALAIVFAPCILRC 160
                          170       180
                   ....*....|....*....|....*.
gi 1907198218 2275 PDTTDPLQSVQDISKTTTCVELIVVE 2300
Cdd:cd04377    161 PDTADPLQSLQDVSKTTTCVETLIKE 186
MYSc_Myh18 cd14932
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ...
161-701 4.81e-114

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: 379.37  E-value: 4.81e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  161 TLLENLRNRFKHEKIYTYVGSILIAINPFKFLPIYNPKYVKMYDNHQLGKLEPHIYAVADVAYHAMLQRKKNQCIVISGE 240
Cdd:cd14932      2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  241 SGSGKTQSTNFLIHHLTAL-----SQKGFASGV------EQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQETGT 309
Cdd:cd14932     82 SGAGKTENTKKVIQYLAYVassfkTKKDQSSIAlshgelEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  310 VLGAYVEKYLLEKSRLVYQEHNERNYHVFYYLLAGASEEERLAFHLKQPEEYHFLNQDCFTVEGEDLRHDFERLQLAMEM 389
Cdd:cd14932    162 IVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQDKELFAETMEAFRI 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  390 VGFLPKTRRQIFSLLSAILHLGNISYKKKTYRDDSiDICNPEVLPIVSELLEVKEEMLFEALVTRKtVTVGEKLILPYKL 469
Cdd:cd14932    242 MSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQA-SMPDDTAAQKVCHLLGMNVTDFTRAILSPR-IKVGRDYVQKAQT 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  470 AE-AVTVRNSMAKSLYSALFDWIVFRINHALlnskDLEQDTKTLSIGVLDIFGFEDYENNSFEQFCINFANERLQHYFNQ 548
Cdd:cd14932    320 QEqAEFAVEALAKASYERMFRWLVMRINKAL----DKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  549 HIFKLEQEEYRTEGISWHNIDY-IDNTCCINLISKK--PTGLLHLLDEESNFPQATNQTLLDKFKHQHEENSYIEFPAVM 625
Cdd:cd14932    396 TMFILEQEEYQREGIEWSFIDFgLDLQPCIELIEKPngPPGILALLDEECWFPKATDKSFVEKVVQEQGNNPKFQKPKKL 475
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  626 --EPAFIIKHYAGKVKYGVKDFREKNTDHMRPDIVALLRSSRNAFVSGM-------TGIDPVAVFRWAVLRAFFRAVVAF 696
Cdd:cd14932    476 kdDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELwkdvdriVGLDKVAGMGESLHGAFKTRKGMF 555

                   ....*
gi 1907198218  697 REAGK 701
Cdd:cd14932    556 RTVGQ 560
MYSc_Myo45 cd14906
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ...
162-670 4.91e-114

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: 380.86  E-value: 4.91e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  162 LLENLRNRFKHEKIYTYVGSILIAINPFKFLP-IYNPKYVKMY-DNHQLGKLEPHIYAVADVAYHAMLQRKKNQCIVISG 239
Cdd:cd14906      3 ILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYkDINQNKSPIPHIYAVALRAYQSMVSEKKNQSIIISG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  240 ESGSGKTQSTNFLIHHLTALSQKGFASG---------VEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQET-GT 309
Cdd:cd14906     83 ESGSGKTEASKTILQYLINTSSSNQQQNnnnnnnnnsIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSdGK 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  310 VLGAYVEKYLLEKSRLVYQ-EHNERNYHVFYYLLAGASEEERLAFHLKQ-PEEYHFLNQDCFTVE--------------- 372
Cdd:cd14906    163 IDGASIETYLLEKSRISHRpDNINLSYHIFYYLVYGASKDERSKWGLNNdPSKYRYLDARDDVISsfksqssnknsnhnn 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  373 GEDLRHDFERLQLAMEMVGFLPKTRRQIFSLLSAILHLGNISYKKKTYRDDSIDICNP--EVLPIVSELLEVKEEMLFEA 450
Cdd:cd14906    243 KTESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAYQKDKvtASLESVSKLLGYIESVFKQA 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  451 LVTRKTVTVGEKLIL--PYKLAEAVTVRNSMAKSLYSALFDWIVFRINHALLN---SKDLEQDTK---TLSIGVLDIFGF 522
Cdd:cd14906    323 LLNRNLKAGGRGSVYcrPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQntqSNDLAGGSNkknNLFIGVLDIFGF 402
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  523 EDYENNSFEQFCINFANERLQHYFNQHIFKLEQEEYRTEGISWHNIDYIDNTCCINLISKKPTGLLHLLDEESNFPQATN 602
Cdd:cd14906    403 ENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNFIDNKECIELIEKKSDGILSLLDDECIMPKGSE 482
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907198218  603 QTLLDKFKHQ-HEENSYIEfPAVMEPAFIIKHYAGKVKYGVKDFREKNTDHMRPDIVALLRSSRNAFVS 670
Cdd:cd14906    483 QSLLEKYNKQyHNTNQYYQ-RTLAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKK 550
RhoGAP_myosin_IXA cd04406
RhoGAP_myosin_IXA: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
2115-2300 8.70e-114

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: 358.93  E-value: 8.70e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2115 FGVELSRLTSEDRAVPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDAESVNLDDYNIHVIASVFKQWLRD 2194
Cdd:cd04406      1 FGVELSRLTSEDRSVPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDANSVNLDDYNIHVIASVFKQWLRD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2195 LPNPLMTFELYEEFLRAMGLQERKETIRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEDTNRMSANALAIVFAPCILRC 2274
Cdd:cd04406     81 LPNPLMTFELYEEFLRAMGLQERRETVRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEETNRMSANALAIVFAPCILRC 160
                          170       180
                   ....*....|....*....|....*.
gi 1907198218 2275 PDTTDPLQSVQDISKTTTCVELIVVE 2300
Cdd:cd04406    161 PDTTDPLQSVQDISKTTTCVELIVCE 186
MYSc_Myh9 cd14919
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ...
161-986 8.76e-110

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: 367.11  E-value: 8.76e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  161 TLLENLRNRFKHEKIYTYVGSILIAINPFKFLPIYNPKYVKMYDNHQLGKLEPHIYAVADVAYHAMLQRKKNQCIVISGE 240
Cdd:cd14919      2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  241 SGSGKTQSTNFLIHHLTALSQ----KGFASGVEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQETGTVLGAYVE 316
Cdd:cd14919     82 SGAGKTENTKKVIQYLAHVASshksKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIE 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  317 KYLLEKSRLVYQEHNERNYHVFYYLLAGASEEERLAFHLKQPEEYHFLNQDCFTVEGEDLRHDFERLQLAMEMVGFLPKT 396
Cdd:cd14919    162 TYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIPEEE 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  397 RRQIFSLLSAILHLGNISYKKKTYRDDSiDICNPEVLPIVSELLEVKEEMLFEALVTRKtVTVGEKLILPYKLAEAVTVR 476
Cdd:cd14919    242 QMGLLRVISGVLQLGNIVFKKERNTDQA-SMPDNTAAQKVSHLLGINVTDFTRGILTPR-IKVGRDYVQKAQTKEQADFA 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  477 -NSMAKSLYSALFDWIVFRINHALlnskDLEQDTKTLSIGVLDIFGFEDYENNSFEQFCINFANERLQHYFNQHIFKLEQ 555
Cdd:cd14919    320 iEALAKATYERMFRWLVLRINKAL----DKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQ 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  556 EEYRTEGISWHNIDY-IDNTCCINLISKK--PTGLLHLLDEESNFPQATNQTLLDKFKHQHEENSYIEFPAVMEPA--FI 630
Cdd:cd14919    396 EEYQREGIEWNFIDFgLDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDKadFC 475
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  631 IKHYAGKVKYGVKDFREKNTDHMRPDIVALLRSSRNAFVSGMtgidpvavfrWavlraffravvafreagkRHIQRKSGH 710
Cdd:cd14919    476 IIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSEL----------W------------------KDVDRIIGL 527
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  711 DDTtpcailksmdsfsflqhpvhqrsleilqrckeekysitrknprtplsdlqgmntlneknqhdtfdiawnvrTGIRQS 790
Cdd:cd14919    528 DQV-----------------------------------------------------------------------AGMSET 536
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  791 RLPasntslldkdGIFAhsasskllerahgilTRNKNFRskpvlpkhllevnslkhltrltlqdritksllhlhkkkkpp 870
Cdd:cd14919    537 ALP----------GAFK---------------TRKGMFR----------------------------------------- 550
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  871 SISAQFQASLSKLMETLGQAEPYFVKCIRSNAEKLPLRFSDALVLRQLRYTGMLETVRIRQSGYSSKYSFQDFVSHFHVL 950
Cdd:cd14919    551 TVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEIL 630
                          810       820       830       840
                   ....*....|....*....|....*....|....*....|
gi 1907198218  951 LPQHI----IPSKFNIQDFFRKININSDNYQVGKTMVFLK 986
Cdd:cd14919    631 TPNSIpkgfMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
MYSc_Myh11 cd14921
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ...
161-986 1.99e-109

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: 365.88  E-value: 1.99e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  161 TLLENLRNRFKHEKIYTYVGSILIAINPFKFLPIYNPKYVKMYDNHQLGKLEPHIYAVADVAYHAMLQRKKNQCIVISGE 240
Cdd:cd14921      2 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  241 SGSGKTQSTNFLIHHLT--ALSQKG-----FASGVEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQETGTVLGA 313
Cdd:cd14921     82 SGAGKTENTKKVIQYLAvvASSHKGkkdtsITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  314 YVEKYLLEKSRLVYQEHNERNYHVFYYLLAGASEEERLAFHLKQPEEYHFLNQDCFTVEGEDLRHDFERLQLAMEMVGFL 393
Cdd:cd14921    162 NIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETLEAMSIMGFS 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  394 PKTRRQIFSLLSAILHLGNISYKKKTYRDDSiDICNPEVLPIVSELLEVKEEMLFEALVTRKtVTVGEKLILPYKLAE-A 472
Cdd:cd14921    242 EEEQLSILKVVSSVLQLGNIVFKKERNTDQA-SMPDNTAAQKVCHLMGINVTDFTRSILTPR-IKVGRDVVQKAQTKEqA 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  473 VTVRNSMAKSLYSALFDWIVFRINHALLNSKdlEQDTKTLsiGVLDIFGFEDYENNSFEQFCINFANERLQHYFNQHIFK 552
Cdd:cd14921    320 DFAIEALAKATYERLFRWILTRVNKALDKTH--RQGASFL--GILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFI 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  553 LEQEEYRTEGISWHNIDY-IDNTCCINLISK--KPTGLLHLLDEESNFPQATNQTLLDKFKHQHEENSYIEFPAVM--EP 627
Cdd:cd14921    396 LEQEEYQREGIEWNFIDFgLDLQPCIELIERpnNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKPKQLkdKT 475
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  628 AFIIKHYAGKVKYGVKDFREKNTDHMRPDIVALLRSSRNAFVSGMtgidpvavfrWavlraffravvafreagkRHIQRK 707
Cdd:cd14921    476 EFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADL----------W------------------KDVDRI 527
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  708 SGHDDttpcailksmdsfsflqhpvhqrsleilqrckeekysitrknprtplsdlqgMNTLNEknqhdtfdiawnvrtgi 787
Cdd:cd14921    528 VGLDQ----------------------------------------------------MAKMTE----------------- 538
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  788 rqSRLPASNTSlldKDGIFahsasskllerahgiltrnknfrskpvlpkhllevnslkhltrltlqdritKSLLHLHKKK 867
Cdd:cd14921    539 --SSLPSASKT---KKGMF---------------------------------------------------RTVGQLYKEQ 562
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  868 kppsisaqfqasLSKLMETLGQAEPYFVKCIRSNAEKLPLRFSDALVLRQLRYTGMLETVRIRQSGYSSKYSFQDFVSHF 947
Cdd:cd14921    563 ------------LGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 630
                          810       820       830       840
                   ....*....|....*....|....*....|....*....|...
gi 1907198218  948 HVL----LPQHIIPSKFNIQDFFRKININSDNYQVGKTMVFLK 986
Cdd:cd14921    631 EILaanaIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
MYSc_Myh1_insects_crustaceans cd14909
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ...
161-669 8.07e-109

class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in insects and crustaceans. Myh1 is a type I skeletal muscle myosin that in Humans is encoded by the MYH1 gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276874  Cd Length: 666  Bit Score: 363.77  E-value: 8.07e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  161 TLLENLRNRFKHEKIYTYVGSILIAINPFKFLPIYNPKYVKMYDNHQLGKLEPHIYAVADVAYHAMLQRKKNQCIVISGE 240
Cdd:cd14909      2 SVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITGE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  241 SGSGKTQSTNFLIHHLTAL--SQKGFASG-----VEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQETGTVLGA 313
Cdd:cd14909     82 SGAGKTENTKKVIAYFATVgaSKKTDEAAkskgsLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAGA 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  314 YVEKYLLEKSRLVYQEHNERNYHVFYYLLAGASEE-ERLAFHLKQPEEYHFLNQDCFTVEGEDLRHDFERLQLAMEMVGF 392
Cdd:cd14909    162 DIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGvKEMCLLSDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQAFDILGF 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  393 LPKTRRQIFSLLSAILHLGNISYKKKTyRDDSIDICNPEVLPIVSELLEVKEEMLFEALVtRKTVTVGEKLILPYKLAEA 472
Cdd:cd14909    242 TKQEKEDVYRITAAVMHMGGMKFKQRG-REEQAEQDGEEEGGRVSKLFGCDTAELYKNLL-KPRIKVGNEFVTQGRNVQQ 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  473 VTVR-NSMAKSLYSALFDWIVFRINHALlnskDLEQDTKTLsIGVLDIFGFEDYENNSFEQFCINFANERLQHYFNQHIF 551
Cdd:cd14909    320 VTNSiGALCKGVFDRLFKWLVKKCNETL----DTQQKRQHF-IGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMF 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  552 KLEQEEYRTEGISWHNIDY-IDNTCCINLIsKKPTGLLHLLDEESNFPQATNQTLLDKFKHQHEENSyiefPAVMEPA-- 628
Cdd:cd14909    395 VLEQEEYKREGIDWAFIDFgMDLLACIDLI-EKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKS----APFQKPKpp 469
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 1907198218  629 --------FIIKHYAGKVKYGVKDFREKNTDHMRPDIVALLRSSRNAFV 669
Cdd:cd14909    470 kpgqqaahFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLL 518
MYSc_Myo13 cd14875
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ...
161-698 1.15e-106

class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain binding domain, and a C-terminal GPA/Q-rich domain. There is little known about the function of this myosin class. Two of the earliest members identified in this class are green alga Acetabularia cliftonii, Aclmyo1 and Aclmyo2. They are striking with their short tail of Aclmyo1 of 18 residues and the maximum of 7 IQ motifs in Aclmyo2. It is thought that these myosins are involved in organelle transport and tip growth. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276842 [Multi-domain]  Cd Length: 664  Bit Score: 357.58  E-value: 1.15e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  161 TLLENLRNRF-KHEKIYTYVGSILIAINPFKFLPiYNP-----KYVKMYDNHQLgklEPHIYAVADVAYHAM-LQRKKNQ 233
Cdd:cd14875      2 TLLHCIKERFeKLHQQYSLMGEMVLSVNPFRLMP-FNSeeerkKYLALPDPRLL---PPHIWQVAHKAFNAIfVQGLGNQ 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  234 CIVISGESGSGKTQSTNFLIHHLTALS--------QKGFASGVEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQ 305
Cdd:cd14875     78 SVVISGESGSGKTENAKMLIAYLGQLSymhssntsQRSIADKIDENLKWSNPVMESFGNARTVRNDNSSRFGKYIKLYFD 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  306 ET-GTVLGAYVEKYLLEKSRLVYQEHNERNYHVFYYLLAGASEEERLAF-HLKQPEEYHFLNQ-DCFT---VEGEDLR-- 377
Cdd:cd14875    158 PTsGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKCLNGgNTFVrrgVDGKTLDda 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  378 HDFERLQLAMEMVGFLPKTRRQIFSLLSAILHLGNISYKKKtyRDDSIDICNPEVLPIVSELLEVKEEMLFEA-LVTRKT 456
Cdd:cd14875    238 HEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESD--QNDKAQIADETPFLTACRLLQLDPAKLRECfLVKSKT 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  457 VTVgekLILPYKlAEAVTVRNSMAKSLYSALFDWIVFRINHALLNSKDLeqdTKTLSIGVLDIFGFEDYENNSFEQFCIN 536
Cdd:cd14875    316 SLV---TILANK-TEAEGFRNAFCKAIYVGLFDRLVEFVNASITPQGDC---SGCKYIGLLDIFGFENFTRNSFEQLCIN 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  537 FANERLQHYFNQHIFKLEQEEYRTEGISWHNIDYIDNTCCINLISKKPTGLLHLLDEESNFPQATNQTLLDKFKHQ-HEE 615
Cdd:cd14875    389 YANESLQNHYNKYTFINDEEECRREGIQIPKIEFPDNSECVNMFDQKRTGIFSMLDEECNFKGGTTERFTTNLWDQwANK 468
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  616 NSYIEFPAVMEP-AFIIKHYAGKVKYGVKDFREKNTDHMRPDIVALLRSSRNAFVSGMTGIDPVAVFR-WAVLRAFFRAV 693
Cdd:cd14875    469 SPYFVLPKSTIPnQFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTEKGLARRkQTVAIRFQRQL 548

                   ....*
gi 1907198218  694 VAFRE 698
Cdd:cd14875    549 TDLRT 553
MYSc_Myh19 cd15896
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ...
161-986 1.24e-104

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: 352.06  E-value: 1.24e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  161 TLLENLRNRFKHEKIYTYVGSILIAINPFKFLPIYNPKYVKMYDNHQLGKLEPHIYAVADVAYHAMLQRKKNQCIVISGE 240
Cdd:cd15896      2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  241 SGSGKTQST----NFLIH----HLTALSQKGFASG---VEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQETGT 309
Cdd:cd15896     82 SGAGKTENTkkviQYLAHvassHKTKKDQNSLALShgeLEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  310 VLGAYVEKYLLEKSRLVYQEHNERNYHVFYYLLAGASEEERLAFHLKQPEEYHFLNQDCFTVEGEDLRHDFERLQLAMEM 389
Cdd:cd15896    162 IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQDKDLFTETMEAFRI 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  390 VGFLPKTRRQIFSLLSAILHLGNISYKKKTYRDDSiDICNPEVLPIVSELLEVKEEMLFEALVTRKtVTVGEKLILPYKL 469
Cdd:cd15896    242 MGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQA-SMPDNTAAQKVCHLMGMNVTDFTRAILSPR-IKVGRDYVQKAQT 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  470 AE-AVTVRNSMAKSLYSALFDWIVFRINHALlnskDLEQDTKTLSIGVLDIFGFEDYENNSFEQFCINFANERLQHYFNQ 548
Cdd:cd15896    320 QEqAEFAVEALAKATYERMFRWLVMRINKAL----DKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  549 HIFKLEQEEYRTEGISWHNIDY-IDNTCCINLISK--KPTGLLHLLDEESNFPQATNQTLLDKFKHQHEENSYIEFPAVM 625
Cdd:cd15896    396 TMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIEKpaSPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKKL 475
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  626 --EPAFIIKHYAGKVKYGVKDFREKNTDHMRPDIVALLRSSRNAFVSGMtgidpvavfrWavlraffravvafreagkrh 703
Cdd:cd15896    476 kdEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSEL----------W-------------------- 525
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  704 iqrksghddttpcailKSMDSFsflqhpvhqrsleilqrckeekysitrknprTPLSDLQGMNTLneknqHDTFDiawnv 783
Cdd:cd15896    526 ----------------KDVDRI-------------------------------VGLDKVSGMSEM-----PGAFK----- 548
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  784 rtgirqsrlpasntslldkdgifahsasskllerahgilTRNKNFRskpvlpkhllevnslkhltrltlqdritksllhl 863
Cdd:cd15896    549 ---------------------------------------TRKGMFR---------------------------------- 555
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  864 hkkkkppSISAQFQASLSKLMETLGQAEPYFVKCIRSNAEKLPLRFSDALVLRQLRYTGMLETVRIRQSGYSSKYSFQDF 943
Cdd:cd15896    556 -------TVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEF 628
                          810       820       830       840
                   ....*....|....*....|....*....|....*....|....*..
gi 1907198218  944 VSHFHVLLPQHI----IPSKFNIQDFFRKININSDNYQVGKTMVFLK 986
Cdd:cd15896    629 RQRYEILTPNAIpkgfMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
MYSc_Myo19 cd14880
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ...
161-677 2.62e-104

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: 350.69  E-value: 2.62e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  161 TLLENLRNRFKHEKIYTYVGSILIAINPFKFLP-IYNPKYVKMYDNH-QLGKLEPHIYAVADVAYHAM--LQRKKNQCIV 236
Cdd:cd14880      2 TVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAApQPQKLKPHIFTVGEQTYRNVksLIEPVNQSIV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  237 ISGESGSGKTQSTNFLIH-------HLTALSQKGFASGVEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQETGT 309
Cdd:cd14880     82 VSGESGAGKTWTSRCLMKfyavvaaSPTSWESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQQ 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  310 VLGAYVEKYLLEKSRLVYQEHNERNYHVFYYLLAGASEEERLAFHLKQPEEYHFLNQDCFTVEgEDlrhDFERLQLAMEM 389
Cdd:cd14880    162 MTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPNPERNLE-ED---CFEVTREAMLH 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  390 VGFLPKTRRQIFSLLSAILHLGNISYKkktyrdDSIDICNP--------EVLPIVSELLEVKEEMLFEALVTRkTVTVGE 461
Cdd:cd14880    238 LGIDTPTQNNIFKVLAGLLHLGNIQFA------DSEDEAQPcqpmddtkESVRTSALLLKLPEDHLLETLQIR-TIRAGK 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  462 KLIL---PYKLAEAVTVRNSMAKSLYSALFDWIVFRINHALLnskdLEQDTKTLSIGVLDIFGFEDYENNSFEQFCINFA 538
Cdd:cd14880    311 QQQVfkkPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSIC----ADTDSWTTFIGLLDVYGFESFPENSLEQLCINYA 386
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  539 NERLQHYFNQHIFKLEQEEYRTEGISWHNIDYIDNTCCINLISKKPTGLLHLLDEESNFPQATN----QTLLDKFKHQHE 614
Cdd:cd14880    387 NEKLQQHFVAHYLRAQQEEYAVEGLEWSFINYQDNQTCLDLIEGSPISICSLINEECRLNRPSSaaqlQTRIESALAGNP 466
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907198218  615 ENSYIEFPAvmEPAFIIKHYAGKVKYGVKDFREKNTDHMRPDIVALLRSSRNAFVSGMTGIDP 677
Cdd:cd14880    467 CLGHNKLSR--EPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANP 527
MYSc_Myh14_mammals cd14930
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ...
161-986 5.91e-103

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: 347.08  E-value: 5.91e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  161 TLLENLRNRFKHEKIYTYVGSILIAINPFKFLPIYNPKYVKMYDNHQLGKLEPHIYAVADVAYHAMLQRKKNQCIVISGE 240
Cdd:cd14930      2 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  241 SGSGKTQSTNFLIHHLTALS-------QKGFASGVEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQETGTVLGA 313
Cdd:cd14930     82 SGAGKTENTKKVIQYLAHVAsspkgrkEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVGA 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  314 YVEKYLLEKSRLVYQEHNERNYHVFYYLLAGASEEERLAFHLKQPEEYHFLNQDCFTVEGEDlRHDFERLQLAMEMVGFL 393
Cdd:cd14930    162 NIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE-RELFQETLESLRVLGFS 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  394 PKTRRQIFSLLSAILHLGNISYKKKTYRDDSIDICNPEVLPIVsELLEVKEEMLFEALVTRKtVTVGEKLILPYKLAE-A 472
Cdd:cd14930    241 HEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLC-RLLGLGVTDFSRALLTPR-IKVGRDYVQKAQTKEqA 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  473 VTVRNSMAKSLYSALFDWIVFRINHALlnskDLEQDTKTLSIGVLDIFGFEDYENNSFEQFCINFANERLQHYFNQHIFK 552
Cdd:cd14930    319 DFALEALAKATYERLFRWLVLRLNRAL----DRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFV 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  553 LEQEEYRTEGISWHNIDY-IDNTCCINLISK--KPTGLLHLLDEESNFPQATNQTLLDKFKHQHEENSYIEFPAVM--EP 627
Cdd:cd14930    395 LEQEEYQREGIPWTFLDFgLDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLrdQA 474
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  628 AFIIKHYAGKVKYGVKDFREKNTDHMRPDIVALLRSSRNAFVSGMtgidpvavfrwavlraffravvafreagkrhiqrk 707
Cdd:cd14930    475 DFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEI----------------------------------- 519
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  708 sghddttpcailksmdsfsflqhpvhqrsleilqrckeekysitrknprtplsdlqgmntlneknqhdtfdiaWNvrtgi 787
Cdd:cd14930    520 -------------------------------------------------------------------------WK----- 521
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  788 rqsrlpasntsllDKDGIFAHSASSKLLERAHGILTRNKNFRskpvlpkhllevnslkhltrltlqdritksllhlhkkk 867
Cdd:cd14930    522 -------------DVEGIVGLEQVSSLGDGPPGGRPRRGMFR-------------------------------------- 550
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  868 kppSISAQFQASLSKLMETLGQAEPYFVKCIRSNAEKLPLRFSDALVLRQLRYTGMLETVRIRQSGYSSKYSFQDFVSHF 947
Cdd:cd14930    551 ---TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRY 627
                          810       820       830       840
                   ....*....|....*....|....*....|....*....|...
gi 1907198218  948 HVLLPQHI----IPSKFNIQDFFRKININSDNYQVGKTMVFLK 986
Cdd:cd14930    628 EILTPNAIpkgfMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
MYSc_Myh2_mammals cd14912
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ...
162-986 7.70e-103

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: 346.72  E-value: 7.70e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  162 LLENLRNRFKHEKIYTYVGSILIAINPFKFLPIYNPKYVKMYDNHQLGKLEPHIYAVADVAYHAMLQRKKNQCIVISGES 241
Cdd:cd14912      3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  242 GSGKTQSTNFLIHHLTALSQKG------FASG-----VEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQETGTV 310
Cdd:cd14912     83 GAGKTVNTKRVIQYFATIAVTGekkkeeITSGkmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  311 LGAYVEKYLLEKSRLVYQEHNERNYHVFYYLLAGASEEE-RLAFHLKQPEEYHFLNQDCFTVEGEDLRHDFERLQLAMEM 389
Cdd:cd14912    163 ASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELiEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAIDI 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  390 VGFLPKTRRQIFSLLSAILHLGNISYKKKTyRDDSIDICNPEVLPIVSELLEVKEEMLFEALVTRKtVTVGEKLILPYKL 469
Cdd:cd14912    243 LGFTNEEKVSIYKLTGAVMHYGNLKFKQKQ-REEQAEPDGTEVADKAAYLQSLNSADLLKALCYPR-VKVGNEYVTKGQT 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  470 AEAVT-VRNSMAKSLYSALFDWIVFRINHALlnskDLEQDTKTLsIGVLDIFGFEDYENNSFEQFCINFANERLQHYFNQ 548
Cdd:cd14912    321 VEQVTnAVGALAKAVYEKMFLWMVARINQQL----DTKQPRQYF-IGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNH 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  549 HIFKLEQEEYRTEGISWHNIDY-IDNTCCINLIsKKPTGLLHLLDEESNFPQATNQTLLDKFKHQH-EENSYIEFPAVM- 625
Cdd:cd14912    396 HMFVLEQEEYKKEGIEWTFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYEQHlGKSANFQKPKVVk 474
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  626 ---EPAFIIKHYAGKVKYGVKDFREKNTDHMRPDIVALLRSSrnafvsgmtgidpvavfrwavlraffravvafreagkr 702
Cdd:cd14912    475 gkaEAHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKS-------------------------------------- 516
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  703 hiqrksghddttpcailksmdsfsflqhpvhqrsleilqrckeekysitrknprtplsdlqGMNTLNEknqhdtfdiawn 782
Cdd:cd14912    517 -------------------------------------------------------------AMKTLAY------------ 523
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  783 vrtgirqsRLPASNTSLLDKDGIFAHSASSKllerahgiltRNKNFRskpvlpkhllevnslkhltrltlqdritksllh 862
Cdd:cd14912    524 --------LFSGAQTAEGASAGGGAKKGGKK----------KGSSFQ--------------------------------- 552
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  863 lhkkkkppSISAQFQASLSKLMETLGQAEPYFVKCIRSNAEKLPLRFSDALVLRQLRYTGMLETVRIRQSGYSSKYSFQD 942
Cdd:cd14912    553 --------TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYAD 624
                          810       820       830       840
                   ....*....|....*....|....*....|....*....|....*....
gi 1907198218  943 FVSHFHVL----LPQ-HIIPSKFNIQDFFRKININSDNYQVGKTMVFLK 986
Cdd:cd14912    625 FKQRYKVLnasaIPEgQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
MYSc_Myh8 cd14918
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ...
162-986 1.35e-102

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: 345.95  E-value: 1.35e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  162 LLENLRNRFKHEKIYTYVGSILIAINPFKFLPIYNPKYVKMYDNHQLGKLEPHIYAVADVAYHAMLQRKKNQCIVISGES 241
Cdd:cd14918      3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  242 GSGKTQSTNFLIHHLTALSQKG---------FASGVEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQETGTVLG 312
Cdd:cd14918     83 GAGKTVNTKRVIQYFATIAVTGekkkeesgkMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  313 AYVEKYLLEKSRLVYQEHNERNYHVFYYLLAGASEEE-RLAFHLKQPEEYHFLNQDCFTVEGEDLRHDFERLQLAMEMVG 391
Cdd:cd14918    163 ADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLiEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDILG 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  392 FLPKTRRQIFSLLSAILHLGNISYKKKTyRDDSIDICNPEVLPIVSELLEVKEEMLFEALVTRKtVTVGEKLILPYKLAE 471
Cdd:cd14918    243 FTPEEKVSIYKLTGAVMHYGNMKFKQKQ-REEQAEPDGTEVADKAAYLQSLNSADLLKALCYPR-VKVGNEYVTKGQTVQ 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  472 AV-TVRNSMAKSLYSALFDWIVFRINHALlnskDLEQDTKTLsIGVLDIFGFEDYENNSFEQFCINFANERLQHYFNQHI 550
Cdd:cd14918    321 QVyNAVGALAKAVYEKMFLWMVTRINQQL----DTKQPRQYF-IGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHM 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  551 FKLEQEEYRTEGISWHNIDY-IDNTCCINLIsKKPTGLLHLLDEESNFPQATNQTLLDKFKHQH-EENSYIEFPAVM--- 625
Cdd:cd14918    396 FVLEQEEYKKEGIEWTFIDFgMDLAACIELI-EKPLGIFSILEEECMFPKATDTSFKNKLYDQHlGKSANFQKPKVVkgk 474
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  626 -EPAFIIKHYAGKVKYGVKDFREKNTDHMRPDIVALLRSSrnafvsgmtgidpvavfrwavlraffravvafreagkrhi 704
Cdd:cd14918    475 aEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKS---------------------------------------- 514
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  705 qrksghddttpcailksmdsfsflqhpvhqrsleilqrckeekysitrknprtplsdlqGMNTLNEknqhdtfdiawnvr 784
Cdd:cd14918    515 -----------------------------------------------------------AMKTLAS-------------- 521
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  785 tgirqsrlpasntslldkdgIFAHSASSKLLERA-HGILTRNKNFRskpvlpkhllevnslkhltrltlqdritksllhl 863
Cdd:cd14918    522 --------------------LFSTYASAEADSGAkKGAKKKGSSFQ---------------------------------- 547
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  864 hkkkkppSISAQFQASLSKLMETLGQAEPYFVKCIRSNAEKLPLRFSDALVLRQLRYTGMLETVRIRQSGYSSKYSFQDF 943
Cdd:cd14918    548 -------TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDF 620
                          810       820       830       840
                   ....*....|....*....|....*....|....*....|....*...
gi 1907198218  944 VSHFHVL----LPQ-HIIPSKFNIQDFFRKININSDNYQVGKTMVFLK 986
Cdd:cd14918    621 KQRYKVLnasaIPEgQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
MYSc_Myh1_mammals cd14910
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ...
162-986 1.48e-102

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: 345.95  E-value: 1.48e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  162 LLENLRNRFKHEKIYTYVGSILIAINPFKFLPIYNPKYVKMYDNHQLGKLEPHIYAVADVAYHAMLQRKKNQCIVISGES 241
Cdd:cd14910      3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  242 GSGKTQSTNFLIHHLTALSQKG------FASG-----VEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQETGTV 310
Cdd:cd14910     83 GAGKTVNTKRVIQYFATIAVTGekkkeeATSGkmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  311 LGAYVEKYLLEKSRLVYQEHNERNYHVFYYLLAGASEEE-RLAFHLKQPEEYHFLNQDCFTVEGEDLRHDFERLQLAMEM 389
Cdd:cd14910    163 ASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLiEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIEI 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  390 VGFLPKTRRQIFSLLSAILHLGNISYKKKTyRDDSIDICNPEVLPIVSELLEVKEEMLFEALVTRKtVTVGEKLILPYKL 469
Cdd:cd14910    243 LGFTSDERVSIYKLTGAVMHYGNMKFKQKQ-REEQAEPDGTEVADKAAYLQNLNSADLLKALCYPR-VKVGNEYVTKGQT 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  470 AEAV-TVRNSMAKSLYSALFDWIVFRINHALlnskDLEQDTKTLsIGVLDIFGFEDYENNSFEQFCINFANERLQHYFNQ 548
Cdd:cd14910    321 VQQVyNAVGALAKAVYDKMFLWMVTRINQQL----DTKQPRQYF-IGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNH 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  549 HIFKLEQEEYRTEGISWHNIDY-IDNTCCINLIsKKPTGLLHLLDEESNFPQATNQTLLDKFKHQH---EENSYIEFPA- 623
Cdd:cd14910    396 HMFVLEQEEYKKEGIEWEFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYEQHlgkSNNFQKPKPAk 474
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  624 -VMEPAFIIKHYAGKVKYGVKDFREKNTDHMRPDIVALLRSSRNAFVSGMtgidpvavfrwavlraFFRAVVAFREAGKr 702
Cdd:cd14910    475 gKVEAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALL----------------FSGAAAAEAEEGG- 537
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  703 hiQRKSGHddttpcailKSMDSFSflqhpvhqrsleilqrckeekysitrknprtplsdlqgmntlneknqhdtfdiawn 782
Cdd:cd14910    538 --GKKGGK---------KKGSSFQ-------------------------------------------------------- 550
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  783 vrtgirqsrlpasntslldkdgifahsasskllerahgiltrnknfrskpvlpkhllevnslkhltrltlqdritksllh 862
Cdd:cd14910        --------------------------------------------------------------------------------
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  863 lhkkkkppSISAQFQASLSKLMETLGQAEPYFVKCIRSNAEKLPLRFSDALVLRQLRYTGMLETVRIRQSGYSSKYSFQD 942
Cdd:cd14910    551 --------TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYAD 622
                          810       820       830       840
                   ....*....|....*....|....*....|....*....|....*....
gi 1907198218  943 FVSHFHVL----LPQ-HIIPSKFNIQDFFRKININSDNYQVGKTMVFLK 986
Cdd:cd14910    623 FKQRYKVLnasaIPEgQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
MYSc_Myh4 cd14915
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ...
162-986 1.77e-101

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: 342.86  E-value: 1.77e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  162 LLENLRNRFKHEKIYTYVGSILIAINPFKFLPIYNPKYVKMYDNHQLGKLEPHIYAVADVAYHAMLQRKKNQCIVISGES 241
Cdd:cd14915      3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  242 GSGKTQSTNFLIHHLTALSQKG-----------FASGVEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQETGTV 310
Cdd:cd14915     83 GAGKTVNTKRVIQYFATIAVTGekkkeeaasgkMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  311 LGAYVEKYLLEKSRLVYQEHNERNYHVFYYLLAGASEEE-RLAFHLKQPEEYHFLNQDCFTVEGEDLRHDFERLQLAMEM 389
Cdd:cd14915    163 ASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELiEMLLITTNPYDFAFVSQGEITVPSIDDQEELMATDSAVDI 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  390 VGFLPKTRRQIFSLLSAILHLGNISYKKKTyRDDSIDICNPEVLPIVSELLEVKEEMLFEALVTRKtVTVGEKLILPYKL 469
Cdd:cd14915    243 LGFSADEKVAIYKLTGAVMHYGNMKFKQKQ-REEQAEPDGTEVADKAAYLTSLNSADLLKALCYPR-VKVGNEYVTKGQT 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  470 AEAV-TVRNSMAKSLYSALFDWIVFRINHALlnskDLEQDTKTLsIGVLDIFGFEDYENNSFEQFCINFANERLQHYFNQ 548
Cdd:cd14915    321 VQQVyNSVGALAKAIYEKMFLWMVTRINQQL----DTKQPRQYF-IGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNH 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  549 HIFKLEQEEYRTEGISWHNIDY-IDNTCCINLIsKKPTGLLHLLDEESNFPQATNQTLLDKFKHQH---EENSYIEFPA- 623
Cdd:cd14915    396 HMFVLEQEEYKKEGIEWEFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYEQHlgkSNNFQKPKPAk 474
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  624 -VMEPAFIIKHYAGKVKYGVKDFREKNTDHMRPDIVALLRSsrnafvSGMTgidpvavfrwavlraffraVVAFREAGKR 702
Cdd:cd14915    475 gKAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQK------SGMK-------------------TLAFLFSGGQ 529
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  703 HIQRKSGHDdttpcailksmdsfsflqhpvhqrsleilqrckeekysitRKNPRTPLSDLQgmntlneknqhdtfdiawn 782
Cdd:cd14915    530 TAEAEGGGG----------------------------------------KKGGKKKGSSFQ------------------- 550
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  783 vrtgirqsrlpasntslldkdgifahsasskllerahgiltrnknfrskpvlpkhllevnslkhltrltlqdritksllh 862
Cdd:cd14915        --------------------------------------------------------------------------------
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  863 lhkkkkppSISAQFQASLSKLMETLGQAEPYFVKCIRSNAEKLPLRFSDALVLRQLRYTGMLETVRIRQSGYSSKYSFQD 942
Cdd:cd14915    551 --------TVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYAD 622
                          810       820       830       840
                   ....*....|....*....|....*....|....*....|....*....
gi 1907198218  943 FVSHFHVL----LPQ-HIIPSKFNIQDFFRKININSDNYQVGKTMVFLK 986
Cdd:cd14915    623 FKQRYKVLnasaIPEgQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
MYSc_Myh7 cd14917
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ...
162-986 2.37e-101

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: 342.47  E-value: 2.37e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  162 LLENLRNRFKHEKIYTYVGSILIAINPFKFLPIYNPKYVKMYDNHQLGKLEPHIYAVADVAYHAMLQRKKNQCIVISGES 241
Cdd:cd14917      3 VLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGES 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  242 GSGKTQSTNFLIHHLTAL------SQKGFASG---VEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQETGTVLG 312
Cdd:cd14917     83 GAGKTVNTKRVIQYFAVIaaigdrSKKDQTPGkgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLAS 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  313 AYVEKYLLEKSRLVYQEHNERNYHVFYYLLAGASEE-ERLAFHLKQPEEYHFLNQDCFTVEGEDLRHDFERLQLAMEMVG 391
Cdd:cd14917    163 ADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPElLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDVLG 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  392 FLPKTRRQIFSLLSAILHLGNISYKKKTyRDDSIDICNPEVLPIVSELLEVKEEMLFEALVTRKTVTVGEKLILPYKLAE 471
Cdd:cd14917    243 FTSEEKNSMYKLTGAIMHFGNMKFKQKQ-REEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQ 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  472 AVTVRNSMAKSLYSALFDWIVFRINhALLNSKDLEQdtktLSIGVLDIFGFEDYENNSFEQFCINFANERLQHYFNQHIF 551
Cdd:cd14917    322 VIYATGALAKAVYEKMFNWMVTRIN-ATLETKQPRQ----YFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMF 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  552 KLEQEEYRTEGISWHNIDY-IDNTCCINLIsKKPTGLLHLLDEESNFPQATNQTLLDKFKHQH-EENSYIEFPAVM---- 625
Cdd:cd14917    397 VLEQEEYKKEGIEWTFIDFgMDLQACIDLI-EKPMGIMSILEEECMFPKATDMTFKAKLFDNHlGKSNNFQKPRNIkgkp 475
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  626 EPAFIIKHYAGKVKYGVKDFREKNTDHMRPDIVALLRSSrnafvsgmtgidpvavfrwavlraffravvafreagkrhiq 705
Cdd:cd14917    476 EAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKS----------------------------------------- 514
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  706 rksghddttpcailksmdsfsflqhpvhqrSLEILQRckeekysitrknprtplsdlqgmntlneknqhdtfdiawnvrt 785
Cdd:cd14917    515 ------------------------------SLKLLSN------------------------------------------- 521
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  786 girqsrlpasntslldkdgIFAHSASSKL-LERAHGILTRNKNFRskpvlpkhllevnslkhltrltlqdritksllhlh 864
Cdd:cd14917    522 -------------------LFANYAGADApIEKGKGKAKKGSSFQ----------------------------------- 547
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  865 kkkkppSISAQFQASLSKLMETLGQAEPYFVKCIRSNAEKLPLRFSDALVLRQLRYTGMLETVRIRQSGYSSKYSFQDFV 944
Cdd:cd14917    548 ------TVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFR 621
                          810       820       830       840
                   ....*....|....*....|....*....|....*....|....*..
gi 1907198218  945 SHFHVLLPQHI-----IPSKFNIQDFFRKININSDNYQVGKTMVFLK 986
Cdd:cd14917    622 QRYRILNPAAIpegqfIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
MYSc_Myh13 cd14923
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ...
162-986 7.38e-100

class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 13 (also called MyHC-eo) in mammals, chicken, and green anole. Myh13 is a myosin whose expression is restricted primarily to the extrinsic eye muscles which are specialized for function in eye movement. Class II myosins, also called conventional myosins, are the myosin type responsible for producing muscle contraction in muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276887 [Multi-domain]  Cd Length: 671  Bit Score: 338.20  E-value: 7.38e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  162 LLENLRNRFKHEKIYTYVGSILIAINPFKFLPIYNPKYVKMYDNHQLGKLEPHIYAVADVAYHAMLQRKKNQCIVISGES 241
Cdd:cd14923      3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGES 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  242 GSGKTQSTNFLIHHLTALSQKG----------FASGVEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQETGTVL 311
Cdd:cd14923     83 GAGKTVNTKRVIQYFATIAVTGdkkkeqqpgkMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  312 GAYVEKYLLEKSRLVYQEHNERNYHVFYYLLAGASEEE-RLAFHLKQPEEYHFLNQDCFTVEGEDLRHDFERLQLAMEMV 390
Cdd:cd14923    163 SADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELiDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNAIDIL 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  391 GFLPKTRRQIFSLLSAILHLGNISYKKKTyRDDSIDICNPEVLPIVSELLEVKEEMLFEALVTRKtVTVGEKLILPYKLA 470
Cdd:cd14923    243 GFSSEEKVGIYKLTGAVMHYGNMKFKQKQ-REEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPR-VKVGNEYVTKGQNV 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  471 EAVTVR-NSMAKSLYSALFDWIVFRINHALlnskDLEQDTKTLsIGVLDIFGFEDYENNSFEQFCINFANERLQHYFNQH 549
Cdd:cd14923    321 QQVTNSvGALAKAVYEKMFLWMVTRINQQL----DTKQPRQYF-IGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHH 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  550 IFKLEQEEYRTEGISWHNIDY-IDNTCCINLIsKKPTGLLHLLDEESNFPQATNQTLLDKFKHQH--EENSYIEFPAV-- 624
Cdd:cd14923    396 MFVLEQEEYKKEGIEWEFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYDQHlgKSNNFQKPKPAkg 474
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  625 -MEPAFIIKHYAGKVKYGVKDFREKNTDHMRPDIVALLRSSRNAFVSgmtgidpvavfrwavlraFFRAVVAFREAGKRH 703
Cdd:cd14923    475 kAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLS------------------FLFSNYAGAEAGDSG 536
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  704 IQRKSGHddttpcailKSMDSFSflqhpvhqrsleilqrckeekysitrknprtplsdlqgmntlneknqhdtfdiawnv 783
Cdd:cd14923    537 GSKKGGK---------KKGSSFQ--------------------------------------------------------- 550
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  784 rtgirqsrlpasntslldkdgifahsasskllerahgiltrnknfrskpvlpkhllevnslkhltrltlqdritksllhl 863
Cdd:cd14923        --------------------------------------------------------------------------------
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  864 hkkkkppSISAQFQASLSKLMETLGQAEPYFVKCIRSNAEKLPLRFSDALVLRQLRYTGMLETVRIRQSGYSSKYSFQDF 943
Cdd:cd14923    551 -------TVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADF 623
                          810       820       830       840
                   ....*....|....*....|....*....|....*....|....*...
gi 1907198218  944 VSHFHVL----LPQ-HIIPSKFNIQDFFRKININSDNYQVGKTMVFLK 986
Cdd:cd14923    624 KQRYRILnasaIPEgQFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
MYSc_Myh6 cd14916
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ...
162-664 2.50e-97

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: 330.48  E-value: 2.50e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  162 LLENLRNRFKHEKIYTYVGSILIAINPFKFLPIYNPKYVKMYDNHQLGKLEPHIYAVADVAYHAMLQRKKNQCIVISGES 241
Cdd:cd14916      3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGES 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  242 GSGKTQSTNFLIHHLTALSQKGF----------ASGVEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQETGTVL 311
Cdd:cd14916     83 GAGKTVNTKRVIQYFASIAAIGDrskkenpnanKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  312 GAYVEKYLLEKSRLVYQEHNERNYHVFYYLLAGASEE-ERLAFHLKQPEEYHFLNQDCFTVEGEDLRHDFERLQLAMEMV 390
Cdd:cd14916    163 SADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPElLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSAFDVL 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  391 GFLPKTRRQIFSLLSAILHLGNISYKKKTyRDDSIDICNPEVLPIVSELLEVKEEMLFEALVTRKtVTVGEKLILPYKLA 470
Cdd:cd14916    243 GFTAEEKAGVYKLTGAIMHYGNMKFKQKQ-REEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPR-VKVGNEYVTKGQSV 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  471 EAVTVR-NSMAKSLYSALFDWIVFRINHALLNSKdleqdTKTLSIGVLDIFGFEDYENNSFEQFCINFANERLQHYFNQH 549
Cdd:cd14916    321 QQVYYSiGALAKSVYEKMFNWMVTRINATLETKQ-----PRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHH 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  550 IFKLEQEEYRTEGISWHNIDY-IDNTCCINLIsKKPTGLLHLLDEESNFPQATNQTLLDKFKHQH--EENSYIE---FPA 623
Cdd:cd14916    396 MFVLEQEEYKKEGIEWEFIDFgMDLQACIDLI-EKPMGIMSILEEECMFPKASDMTFKAKLYDNHlgKSNNFQKprnVKG 474
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 1907198218  624 VMEPAFIIKHYAGKVKYGVKDFREKNTDHMRPDIVALLRSS 664
Cdd:cd14916    475 KQEAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKS 515
MYSc_Myo25 cd14886
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ...
166-669 3.78e-96

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: 326.46  E-value: 3.78e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  166 LRNRFKHEKIYTYVGSILIAINPFKFLP-IYNPKYVKMYD--NHQLG---KLEPHIYAVADVAYHAMLQRKKNQCIVISG 239
Cdd:cd14886      7 LRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRqaDTSRGfpsDLPPHSYAVAQSALNGLISDGISQSCIVSG 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  240 ESGSGKTQSTNFLIHHLtALSQKGFASGVEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQETGTVLGAYVEKYL 319
Cdd:cd14886     87 ESGAGKTETAKQLMNFF-AYGHSTSSTDVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGLKGGKITSYM 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  320 LEKSRLVYQEHNERNYHVFYYLLAGASEEERLAFHLKQPEEYHFLNQ-DCFTVEGEDLRHDFERLQLAMEMVgFLPKTRR 398
Cdd:cd14886    166 LELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNAsKCYDAPGIDDQKEFAPVRSQLEKL-FSKNEID 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  399 QIFSLLSAILHLGNISYKKKTYR--DDSIDICNPEVLPIVSELLEVKEEMLFEALVTRKTVTVGEKLILPYKLAEAVTVR 476
Cdd:cd14886    245 SFYKCISGILLAGNIEFSEEGDMgvINAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNETIISPVTQAQAEVNI 324
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  477 NSMAKSLYSALFDWIVFRINHALlnskDLEQDTKTLsIGVLDIFGFEDYENNSFEQFCINFANERLQHYFNQHIFKLEQE 556
Cdd:cd14886    325 RAVAKDLYGALFELCVDTLNEII----QFDADARPW-IGILDIYGFEFFERNTYEQLLINYANERLQQYFINQVFKSEIQ 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  557 EYRTEGISWHNIDYIDNTCCINLISKKPTGLLHLLDEESNFPQATNQTLLDKFKHQHEENSYIefPAVMEP-AFIIKHYA 635
Cdd:cd14886    400 EYEIEGIDHSMITFTDNSNVLAVFDKPNLSIFSFLEEQCLIQTGSSEKFTSSCKSKIKNNSFI--PGKGSQcNFTIVHTA 477
                          490       500       510
                   ....*....|....*....|....*....|....
gi 1907198218  636 GKVKYGVKDFREKNTDHMRPDIVALLRSSRNAFV 669
Cdd:cd14886    478 ATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIV 511
MYSc_Myo16 cd14878
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ...
161-672 2.38e-95

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: 324.46  E-value: 2.38e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  161 TLLENLRNRFKHEKIYTYVGSILIAINPFKFLPIYNPKYVKMYDNHQlGK----LEPHIYAVADVAYHAMLQRKKNQCIV 236
Cdd:cd14878      2 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLSSS-GQlcssLPPHLFSCAERAFHQLFQERRPQCFI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  237 ISGESGSGKTQSTNFLIHHLTAL---SQKGFASGVEQIILgagpVLEAFGNAKTAHNNNSSRFGKFIQVNY-QETGTVLG 312
Cdd:cd14878     81 LSGERGSGKTEASKQIMKHLTCRassSRTTFDSRFKHVNC----ILEAFGHAKTTLNDLSSCFIKYFELQFcERKKHLTG 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  313 AYVEKYLLEKSRLVYQEHNERNYHVFYYLLAGASEEERLAFHLKQPEEYHFLNQ----DCFTVEGEDLRHDFERLQLAME 388
Cdd:cd14878    157 ARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQtmreDVSTAERSLNREKLAVLKQALN 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  389 MVGFLPKTRRQIFSLLSAILHLGNISYKKKTyRDDSIDICNPEVLPIVSELLEVKEEMLFEALVTRKTVTVGEKLILPYK 468
Cdd:cd14878    237 VVGFSSLEVENLFVILSAILHLGDIRFTALT-EADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIRRHT 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  469 LAEAVTVRNSMAKSLYSALFDWIVFRINHALLNSKDLEQDtKTLSIGVLDIFGFEDYENNSFEQFCINFANERLQHYFNQ 548
Cdd:cd14878    316 IQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLQSQDEQKSM-QTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINE 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  549 HIFKLEQEEYRTEGISWHNIDYIDN-TCCINLISKKPTGLLHLLDEESNFPQATNQTLLDKFKHQHE-ENSYIEFPAVME 626
Cdd:cd14878    395 VLFLQEQTECVQEGVTMETAYSPGNqTGVLDFFFQKPSGFLSLLDEESQMIWSVEPNLPKKLQSLLEsSNTNAVYSPMKD 474
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907198218  627 -----------PAFIIKHYAGKVKYGVKDFREKNTDHMRPDIVALLRSSRNAFVSGM 672
Cdd:cd14878    475 gngnvalkdqgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHL 531
MYSc_Myo38 cd14899
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ...
161-672 9.65e-92

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: 315.88  E-value: 9.65e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  161 TLLENLRNRFKHEKIYTYVGSILIAINPFKFLP-IYNPKYVKMY---DNHQLGK-------LEPHIYAVADVAYHAMLQR 229
Cdd:cd14899      2 SILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydHNSQFGDrvtstdpREPHLFAVARAAYIDIVQN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  230 KKNQCIVISGESGSGKTQSTNFLIHHLTALSQKGFA----------------SGVEQIILGAGPVLEAFGNAKTAHNNNS 293
Cdd:cd14899     82 GRSQSILISGESGAGKTEATKIIMTYFAVHCGTGNNnltnsesisppaspsrTTIEEQVLQSNPILEAFGNARTVRNDNS 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  294 SRFGKFIQVNYQETGTVL-GAYVEKYLLEKSRLVYQEHNERNYHVFYYLLAG----ASEEERLAFHLKQ-PEEYHFLNQD 367
Cdd:cd14899    162 SRFGKFIELRFRDERRRLaGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncVSKEQKQVLALSGgPQSFRLLNQS 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  368 CFTVEGEDLRH--DFERLQLAMEMVGFLPKTRRQIFSLLSAILHLGNISYKKKTY-RDDSIDICNPEVL----------P 434
Cdd:cd14899    242 LCSKRRDGVKDgvQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQIPHkGDDTVFADEARVMssttgafdhfT 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  435 IVSELLEVKEEMLFEALVTRKTVTVGEKLILPYKLAEAVTVRNSMAKSLYSALFDWIVFRINHAL----------LNSKD 504
Cdd:cd14899    322 KAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLqrqasapwgaDESDV 401
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  505 LEQDTKTLSIGVLDIFGFEDYENNSFEQFCINFANERLQHYFNQHIFKLEQEEYRTEGISWHNIDYIDNTCCINLISKKP 584
Cdd:cd14899    402 DDEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNNRACLELFEHRP 481
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  585 TGLLHLLDEESNFPQATNQTLLDKFKHQHEENS----YIEFPAVMEPA-FIIKHYAGKVKYGVKDFREKNTDHMRPDIVA 659
Cdd:cd14899    482 IGIFSLTDQECVFPQGTDRALVAKYYLEFEKKNshphFRSAPLIQRTTqFVVAHYAGCVTYTIDGFLAKNKDSFCESAAQ 561
                          570
                   ....*....|...
gi 1907198218  660 LLRSSRNAFVSGM 672
Cdd:cd14899    562 LLAGSSNPLIQAL 574
MYSc_Myo37 cd14898
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ...
161-651 5.35e-89

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: 303.36  E-value: 5.35e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  161 TLLENLRNRFKHEKIYTYVGSILIAINPFKFLPIYNPKYVKMYDNhqlGKLEPHIYAVADVAYHAMLQRKkNQCIVISGE 240
Cdd:cd14898      2 ATLEILEKRYASGKIYTKSGLVFLALNPYETIYGAGAMKAYLKNY---SHVEPHVYDVAEASVQDLLVHG-NQTIVISGE 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  241 SGSGKTQSTNFLIHHLtaLSQKGFASGVEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQetGTVLGAYVEKYLL 320
Cdd:cd14898     78 SGSGKTENAKLVIKYL--VERTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITGAKFETYLL 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  321 EKSRLVYQEHNERNYHVFYYLLAgaSEEERL-------AFHLKQPEEYHFLNQDCFTVEGedlrhdferlqlAMEMVGFl 393
Cdd:cd14898    154 EKSRVTHHEKGERNFHIFYQFCA--SKRLNIkndfidtSSTAGNKESIVQLSEKYKMTCS------------AMKSLGI- 218
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  394 pKTRRQIFSLLSAILHLGNISYKKktyrDDSIDICNPEVLPIVSELLEVKEEMLFEALVTRKTVTVGEKLILPYKLAEAV 473
Cdd:cd14898    219 -ANFKSIEDCLLGILYLGSIQFVN----DGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQAR 293
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  474 TVRNSMAKSLYSALFDWIVFRINHALLNSKdleqdtkTLSIGVLDIFGFEDYENNSFEQFCINFANERLQHYFNQHIFKL 553
Cdd:cd14898    294 TIRNSMARLLYSNVFNYITASINNCLEGSG-------ERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRA 366
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  554 EQEEYRTEGISWHNIDYIDNTCCINLIsKKPTGLLHLLDEESNFPQATNQTLLDKFKHQHEENSYIEFpavmEPAFIIKH 633
Cdd:cd14898    367 KQGMYKEEGIEWPDVEFFDNNQCIRDF-EKPCGLMDLISEESFNAWGNVKNLLVKIKKYLNGFINTKA----RDKIKVSH 441
                          490
                   ....*....|....*...
gi 1907198218  634 YAGKVKYGVKDFREKNTD 651
Cdd:cd14898    442 YAGDVEYDLRDFLDKNRE 459
RhoGAP_myosin_IXB cd04407
RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
2115-2300 1.15e-88

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: 286.89  E-value: 1.15e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2115 FGVELSRLTSEDRAVPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDAESVNLDDYNIHVIASVFKQWLRD 2194
Cdd:cd04407      1 FGVRVGSLTSNKTSVPIVLEKLLEHVEMHGLYTEGIYRKSGSANRMKELHQLLQADPENVKLENYPIHAITGLLKQWLRE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2195 LPNPLMTFELYEEFLRAMGLQERKETIRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEDTNRMSANALAIVFAPCILRC 2274
Cdd:cd04407     81 LPEPLMTFAQYNDFLRAVELPEKQEQLQAIYRVLEQLPTANHNTLERLIFHLVKVALEEDVNRMSPNALAIVFAPCLLRC 160
                          170       180
                   ....*....|....*....|....*.
gi 1907198218 2275 PDTTDPLQSVQDISKTTTCVELIVVE 2300
Cdd:cd04407    161 PDSSDPLTSMKDVAKTTTCVEMLIKE 186
MYSc_Myo24A cd14937
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ...
162-672 8.68e-86

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: 295.77  E-value: 8.68e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  162 LLENLRNRFKHEKIYTYVGSILIAINPFKFLPIYnpkyVKMYDNHQLGKLEPHIYAVADVAYHAMLQRKKNQCIVISGES 241
Cdd:cd14937      3 VLNMLALRYKKNYIYTIAEPMLISINPYQVIDVD----INEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGES 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  242 GSGKTQSTNFLI-HHLTALSQKgfaSGVEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQETGTVLGAYVEKYLL 320
Cdd:cd14937     79 GSGKTEASKLVIkYYLSGVKED---NEISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSIEIFLL 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  321 EKSRLVYQEHNERNYHVFYYLLAGASEEERLAFHLKQPEEYHFLNQDCFTVEGEDLRHDFERLQLAMEMVGfLPKTRRQI 400
Cdd:cd14937    156 ENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKNVVIPEIDDAKDFGNLMISFDKMN-MHDMKDDL 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  401 FSLLSAILHLGNISY----KKKTYRDDSIDICNPEVLPIVSELLEVKEEMLFEALVTRKTVTVGEKLILPYKLAEAVTVR 476
Cdd:cd14937    235 FLTLSGLLLLGNVEYqeieKGGKTNCSELDKNNLELVNEISNLLGINYENLKDCLVFTEKTIANQKIEIPLSVEESVSIC 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  477 NSMAKSLYSALFDWIVFRINHALLNSKDLEQdtktlSIGVLDIFGFEDYENNSFEQFCINFANERLQHYFNQHIFKLEQE 556
Cdd:cd14937    315 KSISKDLYNKIFSYITKRINNFLNNNKELNN-----YIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYEKETE 389
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  557 EYRTEGISWHNIDYIDNTCCINLISKKpTGLLHLLDEESNFPQATNQTLL----DKF-KHQHeensYIEFPAVMEPAFII 631
Cdd:cd14937    390 LYKAEDILIESVKYTTNESIIDLLRGK-TSIISILEDSCLGPVKNDESIVsvytNKFsKHEK----YASTKKDINKNFVI 464
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 1907198218  632 KHYAGKVKYGVKDFREKNTDHMRPDIVALLRSSRNAFVSGM 672
Cdd:cd14937    465 KHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSL 505
MYSc_Myo26 cd14887
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ...
162-986 2.73e-85

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: 296.95  E-value: 2.73e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  162 LLENLRNRF--------KHEKIYTYVGSILIAINPFKFLPIYNPKYVKMYDNHQLGKLEPHIYAVADVAYHAMLQRKKNQ 233
Cdd:cd14887      3 LLENLYQRYnkayinkeNRNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRRSQ 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  234 CIVISGESGSGKTQSTNFLIHHLTALS--QKGFAS-GVEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQETGTV 310
Cdd:cd14887     83 SILISGESGAGKTETSKHVLTYLAAVSdrRHGADSqGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGRGKL 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  311 LGAYVEKYLLEKSRLVYQEHNERNYHVFYYLL--AGASEEERLAFHLKQPEEYhflnqdcftvegedlrhDFERLQLAME 388
Cdd:cd14887    163 TRASVATYLLANERVVRIPSDEFSFHIFYALCnaAVAAATQKSSAGEGDPEST-----------------DLRRITAAMK 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  389 MVGFLPKTRRQIFSLLSAILHLGNISY-------KKKTYRDDSIDICNPEVLPIVSELLEVK------------------ 443
Cdd:cd14887    226 TVGIGGGEQADIFKLLAAILHLGNVEFttdqepeTSKKRKLTSVSVGCEETAADRSHSSEVKclssglkvteasrkhlkt 305
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  444 -------------EEMLFEALVTRKtVTVGEKLilpYKLAEAVTVRNSMAKSLYSALFDWIVFRINHALLNS-------- 502
Cdd:cd14887    306 varllglppgvegEEMLRLALVSRS-VRETRSF---FDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRSakpsesds 381
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  503 -KDLEQDTKTLSIGVLDIFGFEDYEN---NSFEQFCINFANERLQHYFNQHIFKLEQEEYRTEGISWHNIDYIDNTccin 578
Cdd:cd14887    382 dEDTPSTTGTQTIGILDLFGFEDLRNhskNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDCSAFPF---- 457
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  579 liskkptgllhlldeesNFPQATNQTlldkfkhqHEENSYIEFpaVMEPAFiikhyagkvkygvKDFREKNTDHMRPDIV 658
Cdd:cd14887    458 -----------------SFPLASTLT--------SSPSSTSPF--SPTPSF-------------RSSSAFATSPSLPSSL 497
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  659 ALLRSSRNAFVSgmtgidpvavfrwavlraffravvafreagkrhiqRKSGHDdttpcailksmdsfsflqhpvhqrsle 738
Cdd:cd14887    498 SSLSSSLSSSPP-----------------------------------VWEGRD--------------------------- 515
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  739 ilqrCKEEKYSITRKNprtplsdlqgmntlneknqhdtfdiawnvRTGIRQSRLPASNTSLLDKDGIFAHSASSKLLErA 818
Cdd:cd14887    516 ----NSDLFYEKLNKN-----------------------------IINSAKYKNITPALSRENLEFTVSHFACDVTYD-A 561
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  819 HGILTRNKNFRSKPvLPKHLLEVNSlkhLTRLTLQDRitKSLLHLHKKKKpPSISAQFQASLSKLMETLGQAEPYFVKCI 898
Cdd:cd14887    562 RDFCRANREATSDE-LERLFLACST---YTRLVGSKK--NSGVRAISSRR-STLSAQFASQLQQVLKALQETSCHFIRCV 634
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  899 RSNAEKLPLRFSDALVLRQLRYTGMLETVRIRQSGYSSKYSFQDFVSHFHVLLPQHI---IPSKFNIQDFFRKININSDN 975
Cdd:cd14887    635 KPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYETKLPMALreaLTPKMFCKIVLMFLEINSNS 714
                          890
                   ....*....|.
gi 1907198218  976 YQVGKTMVFLK 986
Cdd:cd14887    715 YTFGKTKIFFR 725
MYSc_Myo44 cd14905
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ...
161-675 4.26e-82

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: 286.22  E-value: 4.26e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  161 TLLENLRNRFKHEKIYTYVGSILIAINPFKFLP-IYNPKYVKMYDnhQLGKLEPHIYAVADVAYHAMLQRKKNQCIVISG 239
Cdd:cd14905      2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNYN--QRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  240 ESGSGKTQSTNFLIHHL--TALSQKGFasgVEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQETGTVLGAYVEK 317
Cdd:cd14905     80 ESGSGKSENTKIIIQYLltTDLSRSKY---LRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKLYS 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  318 YLLEKSRLVYQEHNERNYHVFYYLLAGASEEERLAFHLKQPEEYHFLNQ-DCFTVEGEDLRHDFERLQLAMEMVGFLPKT 396
Cdd:cd14905    157 YFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQgGSISVESIDDNRVFDRLKMSFVFFDFPSEK 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  397 RRQIFSLLSAILHLGNISYKKKTYRDdsidicnpevlpivsellEVKEEMLFEAL---VTRKTVTVGEKLILPYKLA--E 471
Cdd:cd14905    237 IDLIFKTLSFIIILGNVTFFQKNGKT------------------EVKDRTLIESLshnITFDSTKLENILISDRSMPvnE 298
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  472 AVTVRNSMAKSLYSALFDWIVfrinhALLNSKdLEQDTKTLSIGVLDIFGFEDYENNSFEQFCINFANERLQHYFNQHIF 551
Cdd:cd14905    299 AVENRDSLARSLYSALFHWII-----DFLNSK-LKPTQYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVL 372
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  552 KLEQEEYRTEGISWHN-IDYIDNTCCINLISKkptgLLHLLDEESNFPQATNQTLLDKFKHQHEENSYIefpAVMEPAFI 630
Cdd:cd14905    373 KQEQREYQTERIPWMTpISFKDNEESVEMMEK----IINLLDQESKNINSSDQIFLEKLQNFLSRHHLF---GKKPNKFG 445
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*
gi 1907198218  631 IKHYAGKVKYGVKDFREKNTDHMRPDIVALLRSSRNAFVSGMTGI 675
Cdd:cd14905    446 IEHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYLFSRDGV 490
MYSc_Myo12 cd14874
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ...
162-666 7.03e-80

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


Pssm-ID: 276841 [Multi-domain]  Cd Length: 628  Bit Score: 278.29  E-value: 7.03e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  162 LLENLRNRFKHEKIYTYVGSILIAINPFKFLPIYNPKYVKMYdnhqlgklepHIYAVADVAYHAMLQRKKN-QCIVISGE 240
Cdd:cd14874      3 IAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFGGE 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  241 SGSGKTQSTNFLIHHLTALSQKGFASGVEQIIlgaGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQETgtVLGAYVEKYL- 319
Cdd:cd14874     73 SGSGKSYNAFQVFKYLTSQPKSKVTTKHSSAI---ESVFKSFGCAKTLKNDEATRFGCSIDLLYKRN--VLTGLNLKYTv 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  320 -LEKSRLVYQEHNERNYHVFYYLLAGASEEERLAFHLKQPEEYHFLNQ-DCFTVEGEDLRHdFERLQLAMEMVGFLPKTR 397
Cdd:cd14874    148 pLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQgNSTENIQSDVNH-FKHLEDALHVLGFSDDHC 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  398 RQIFSLLSAILHLGNISYKKKTYRD---DSIDICNPEVLPIVSELLEVKEEMLFEALVTRKTVTVgeklilPYKLAEAVT 474
Cdd:cd14874    227 ISIYKIISTILHIGNIYFRTKRNPNveqDVVEIGNMSEVKWVAFLLEVDFDQLVNFLLPKSEDGT------TIDLNAALD 300
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  475 VRNSMAKSLYSALFDWIVFRINHALlnskdlEQDTKTLSIGVLDIFGFEDYENNSFEQFCINFANERLQHYFNQHIFKLE 554
Cdd:cd14874    301 NRDSFAMLIYEELFKWVLNRIGLHL------KCPLHTGVISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHSFHDQ 374
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  555 QEEYRTEGISwhnIDY-----IDNTCCINLISKKPTGLLHLLDEESNFPQATNQTLLDKFKHQH-EENSYIEFPAVMEPA 628
Cdd:cd14874    375 LVDYAKDGIS---VDYkvpnsIENGKTVELLFKKPYGLLPLLTDECKFPKGSHESYLEHCNLNHtDRSSYGKARNKERLE 451
                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 1907198218  629 FIIKHYAGKVKYGVKDFREKNTDHMRPDIVALLRSSRN 666
Cdd:cd14874    452 FGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKN 489
MYSc_Myo20 cd14881
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ...
161-663 1.50e-79

class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such members as Drosophila, Daphnia, and mosquitoes. These myosins contain a single IQ motif in the neck region. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276847 [Multi-domain]  Cd Length: 633  Bit Score: 277.38  E-value: 1.50e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  161 TLLENLRNRFKHEKIYTYVGSILIAINPFKFLPiyNPKYVKMYDNHQLGklePHIYAVADVAYHAMLQRKKNQCIVISGE 240
Cdd:cd14881      2 AVMKCLQARFYAKEFFTNVGPILLSVNPYRDVG--NPLTLTSTRSSPLA---PQLLKVVQEAVRQQSETGYPQAIILSGT 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  241 SGSGKTQSTNFLIHHLTALSQKGFASGVEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQEtGTVLGAYVEKYLL 320
Cdd:cd14881     77 SGSGKTYASMLLLRQLFDVAGGGPETDAFKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQVTD-GALYRTKIHCYFL 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  321 EKSRLVYQEHNERNYHVFYYLLAGASEEERLAFHLK--QPEEYHFLNQ-DCFTVEGEDLRHdFERLQLAMEMVG--FLPK 395
Cdd:cd14881    156 DQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDgySPANLRYLSHgDTRQNEAEDAAR-FQAWKACLGILGipFLDV 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  396 TRrqifsLLSAILHLGNISYKKKTYRDdsIDICNPEVLPIVSELLEVKEEMLFEALVTRKTVTVGEKLILPYKLAEAVTV 475
Cdd:cd14881    235 VR-----VLAAVLLLGNVQFIDGGGLE--VDVKGETELKSVAALLGVSGAALFRGLTTRTHNARGQLVKSVCDANMSNMT 307
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  476 RNSMAKSLYSALFDWIVFRINHALLNSKDLEQDTKTLSIGVLDIFGFEDYENNSFEQFCINFANERLQHYFNQHIFKLEQ 555
Cdd:cd14881    308 RDALAKALYCRTVATIVRRANSLKRLGSTLGTHATDGFIGILDMFGFEDPKPSQLEHLCINLCAETMQHFYNTHIFKSSI 387
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  556 EEYRTEGISWH-NIDYIDNTCCINLISKKPTGLLHLLDEESNfPQATNQTLLDKFKHQHEENSYIEFPAVMEP-AFIIKH 633
Cdd:cd14881    388 ESCRDEGIQCEvEVDYVDNVPCIDLISSLRTGLLSMLDVECS-PRGTAESYVAKIKVQHRQNPRLFEAKPQDDrMFGIRH 466
                          490       500       510
                   ....*....|....*....|....*....|
gi 1907198218  634 YAGKVKYGVKDFREKNTDHMRPDIVALLRS 663
Cdd:cd14881    467 FAGRVVYDASDFLDTNRDVVPDDLVAVFYK 496
MYSc_Myo21 cd14882
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ...
161-672 3.76e-77

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: 270.84  E-value: 3.76e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  161 TLLENLRNRFKHEKIYTYVGSILIAINPFKFLPIYNPKYVKMYDNHQLGKLEPHIYAVADVAYHAMLQRKKNQCIVISGE 240
Cdd:cd14882      2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  241 SGSGKTQSTNFLIHHLTALSqKGfASGVEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQETGTVLGAYVEKYLL 320
Cdd:cd14882     82 SYSGKTTNARLLIKHLCYLG-DG-NRGATGRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFWMYQL 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  321 EKSRLVYQEHNERNYHVFYYLLAGASEEERL-AFHLKQPEEYHFLNQDCfTVEGEDLR-------------HDFERLQLA 386
Cdd:cd14882    160 EKLRVSTTDGNQSNFHIFYYFYDFIEAQNRLkEYNLKAGRNYRYLRIPP-EVPPSKLKyrrddpegnveryKEFEEILKD 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  387 MEMVgflPKTRRQIFSLLSAILHLGNISYKKKtyrDDSIDICNPEVLPIVSELLEVKEEMLFEALVTRKTVTVGEKLILP 466
Cdd:cd14882    239 LDFN---EEQLETVRKVLAAILNLGEIRFRQN---GGYAELENTEIASRVAELLRLDEKKFMWALTNYCLIKGGSAERRK 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  467 YKLAEAVTVRNSMAKSLYSALFDWIVFRINHALLNSKDLEQDTKtlSIGVLDIFGFEDYENNSFEQFCINFANERLQHYF 546
Cdd:cd14882    313 HTTEEARDARDVLASTLYSRLVDWIINRINMKMSFPRAVFGDKY--SISIHDMFGFECFHRNRLEQLMVNTLNEQMQYHY 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  547 NQHIFKLEQEEYRTEGISWHNIDYIDNTCCINLISKKPTGLLHLLDEESNFPQATNqTLLDKFKHQHeeNSYIEFPAVME 626
Cdd:cd14882    391 NQRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPDGLFYIIDDASRSCQDQN-YIMDRIKEKH--SQFVKKHSAHE 467
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*.
gi 1907198218  627 paFIIKHYAGKVKYGVKDFREKNTDHMRPDIVALLRSSRNAFVSGM 672
Cdd:cd14882    468 --FSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLM 511
MYSc_Myo18 cd01386
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ...
163-642 3.03e-76

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: 269.56  E-value: 3.03e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  163 LENLRNRFKHEKIYTYVGSILIAINPFKFLPIYNPKYVKMYDNHQLGKLEPHIYAVADVAYHAMLQRKKNQCIVISGESG 242
Cdd:cd01386      4 LHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLGRSG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  243 SGKTQSTNFLIHHLT--ALSQKGFASgVEQiILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQETGTVLGAYVEKYLL 320
Cdd:cd01386     84 SGKTTNCRHILEYLVtaAGSVGGVLS-VEK-LNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASIQTLLL 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  321 EKSRLVYQEHNERNYHVFYYLLAGASEEERLAFHLKQPEEyhflNQDCFTV---EGEDLRH---DFERLQLAMEMVGFLP 394
Cdd:cd01386    162 ERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAE----SNSFGIVplqKPEDKQKaaaAFSKLQAAMKTLGISE 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  395 KTRRQIFSLLSAILHLGNI------SYKKKTYRDdsidicnPEVLPIVSELLEVKEEMLFEAL--------VTRKTVTVG 460
Cdd:cd01386    238 EEQRAIWSILAAIYHLGAAgatkaaSAGRKQFAR-------PEWAQRAAYLLGCTLEELSSAIfkhhlsggPQQSTTSSG 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  461 EKLILPYKLAE----AVTVRNSMAKSLYSALFDWIVFRINHALlnskdLEQDTKTLSIGVLDIFGFEDYE------NNSF 530
Cdd:cd01386    311 QESPARSSSGGpkltGVEALEGFAAGLYSELFAAVVSLINRSL-----SSSHHSTSSITIVDTPGFQNPAhsgsqrGATF 385
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  531 EQFCINFANERLQHYFNQHIFKLEQEEYRTEGIswhNIDYIDNTCC----INLISKKPT--------------GLLHLLD 592
Cdd:cd01386    386 EDLCHNYAQERLQLLFHERTFVAPLERYKQENV---EVDFDLPELSpgalVALIDQAPQqalvrsdlrdedrrGLLWLLD 462
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907198218  593 EESNFPQATNQTLLDKFKHQHEENSYIEFPAVMEPA-----FIIKHYAGK--VKYGV 642
Cdd:cd01386    463 EEALYPGSSDDTFLERLFSHYGDKEGGKGHSLLRRSegplqFVLGHLLGTnpVEYDV 519
MYSc_Myo23 cd14884
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ...
161-670 5.52e-69

class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 IQ motifs and a single MyTH4 domain in its C-terminal tail. The lack of a FERM domain here is odd since MyTH4 domains are usually found alongside FERM domains where they bind to microtubules. At any rate these Class XXIII myosins are still proposed to function in the apicomplexan microtubule cytoskeleton. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276850 [Multi-domain]  Cd Length: 685  Bit Score: 247.90  E-value: 5.52e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  161 TLLENLRNRFKHEKIYTYVGSILIAINPFKFLP-IYNPKYVKMY-----DNHQLGK--LEPHIYAVADVAYHAMLQRKKN 232
Cdd:cd14884      2 NVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYlhkksNSAASAApfPKAHIYDIANMAYKNMRGKLKR 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  233 QCIVISGESGSGKTQSTNFLIHHLTALSQKGFASGVEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYQETGTVL- 311
Cdd:cd14884     82 QTIVVSGHSGSGKTENCKFLFKYFHYIQTDSQMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFEEVENTQk 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  312 --------GAYVEKYLLEKSRLVYQEHNERNYHVFYYLLAGASEEE----RLA-----FHLKQPEEYHF---------LN 365
Cdd:cd14884    162 nmfngcfrNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDlarrNLVrncgvYGLLNPDESHQkrsvkgtlrLG 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  366 QDCFTVEGEDLRHD---FERLQLAMEMVGFLPKTRRQIFSLLSAILHLGNISYKkktyrddsidicnpevlpIVSELLEV 442
Cdd:cd14884    242 SDSLDPSEEEKAKDeknFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRAYK------------------AAAECLQI 303
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  443 KEEMLFEALVTRKTVTVGEKLILPYKLAEAVTVRNSMAKSLYSALFDWIVFRINHALLNSKD----LEQDTKTLS---IG 515
Cdd:cd14884    304 EEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEkdesDNEDIYSINeaiIS 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  516 VLDIFGFEDYENNSFEQFCINFANERLQHYFNQHIFKLEQEEYRTEGISWHNIDYIDNTCCINLISKkptgLLHLLDEES 595
Cdd:cd14884    384 ILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAPSYSDTLIFIAK----IFRRLDDIT 459
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  596 NFPQATNQTLLDKF---------KHQHEENSYIEF------------PAVMEPAFIIKHYAGKVKYGVKDFREKNTDHMR 654
Cdd:cd14884    460 KLKNQGQKKTDDHFfryllnnerQQQLEGKVSYGFvlnhdadgtakkQNIKKNIFFIRHYAGLVTYRINNWIDKNSDKIE 539
                          570
                   ....*....|....*.
gi 1907198218  655 PDIVALLRSSRNAFVS 670
Cdd:cd14884    540 TSIETLISCSSNRFLR 555
RA_Myosin-IXa cd17216
Ras-associating (RA) domain found in Myosin-IXa; Myosin-IXa, also termed myosin-9a (Myo9a), is ...
15-110 2.90e-68

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


Pssm-ID: 340736  Cd Length: 96  Bit Score: 224.81  E-value: 2.90e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218   15 EHTLRIYPGTISEGTIYCPIPARKNSTAAEVIDSLINRLHLDKTKCYVLAEVKEFGGEEWILNPTDCPVQRMMLWPRMAL 94
Cdd:cd17216      1 EFTLRIYPGNIAEGTIYCPVPARKNTTAAEVIESLINKLQLDKTKCYVLAEVKEFGGEEWILNPTDCPVQRMMLWPRMAL 80
                           90
                   ....*....|....*.
gi 1907198218   95 ENRLSGEDYRFLLREK 110
Cdd:cd17216     81 ENRFSGEDYRFLLREK 96
MYSc_Myo32 cd14893
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ...
162-667 2.18e-62

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: 229.47  E-value: 2.18e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  162 LLENLRNRFKHEKIYTYVGSILIAINPFKFLPIYNPKYVKMYDNHQ----------LGKLEPHIYAVADVAYHAMLQRKK 231
Cdd:cd14893      3 ALYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSReqtplyekdtVNDAPPHVFALAQNALRCMQDAGE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  232 NQCIVISGESGSGKTQSTNFLIHHLT-----------ALSQKGFASGVEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFI 300
Cdd:cd14893     83 DQAVILLGGMGAGKSEAAKLIVQYLCeigdeteprpdSEGASGVLHPIGQQILHAFTILEAFGNAATRQNRNSSRFAKMI 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  301 QVNYQETGTVLGAYVEKYLLEKSRLVYQEHNERNYHVFYYLLAGASEEERLAFHL---KQPEEYHFLNQ--DCFTVEGED 375
Cdd:cd14893    163 SVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHDPTLRDSLemnKCVNEFVMLKQadPLATNFALD 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  376 LRhDFERLQLAMEMVGFLPKTRRQIFSLLSAILHLGNISYKKKTYRDDSIDICN--------------PEVLPIVSELLE 441
Cdd:cd14893    243 AR-DYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFVPDPEGGKSVGGANsttvsdaqscalkdPAQILLAAKLLE 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  442 VKEEMLFEALVTRKTVTV-GEKLILPYK---LAEAVTVRNSMAKSLYSALFDWIVFRINHALLNSKDLEQDT----KTLS 513
Cdd:cd14893    322 VEPVVLDNYFRTRQFFSKdGNKTVSSLKvvtVHQARKARDTFVRSLYESLFNFLVETLNGILGGIFDRYEKSniviNSQG 401
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  514 IGVLDIFGFEDYEN--NSFEQFCINFANERLQHYFNQHIFK-----LEQEEYRTEG-ISWH-NIDYI-DNTCCINLISKK 583
Cdd:cd14893    402 VHVLDMVGFENLTPsqNSFDQLCFNYWSEKVHHFYVQNTLAinfsfLEDESQQVENrLTVNsNVDITsEQEKCLQLFEDK 481
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  584 PTGLLHLLDEESNFPQATNQTLLDKFKHQHEE--------------NSYIEFPAVMEPAFIIKHYAGKVKYGVKDFREKN 649
Cdd:cd14893    482 PFGIFDLLTENCKVRLPNDEDFVNKLFSGNEAvgglsrpnmgadttNEYLAPSKDWRLLFIVQHHCGKVTYNGKGLSSKN 561
                          570
                   ....*....|....*...
gi 1907198218  650 TDHMRPDIVALLRSSRNA 667
Cdd:cd14893    562 MLSISSTCAAIMQSSKNA 579
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
2129-2301 4.97e-62

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: 210.20  E-value: 4.97e-62
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  2129 VPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDAE-SVNLDDYNIHVIASVFKQWLRDLPNPLMTFELYEE 2207
Cdd:smart00324    3 IPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDpDLDLSEYDVHDVAGLLKLFLRELPEPLITYELYEE 82
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  2208 FLRAMGLQERKETIRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEDTNRMSANALAIVFAPCILRCPDTTDPlqSVQDI 2287
Cdd:smart00324   83 FIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGEVA--SLKDI 160
                           170
                    ....*....|....
gi 1907198218  2288 SKTTTCVELIVVEQ 2301
Cdd:smart00324  161 RHQNTVIEFLIENA 174
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
2130-2276 5.24e-59

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


Pssm-ID: 459875  Cd Length: 148  Bit Score: 200.46  E-value: 5.24e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2130 PLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDAESV-NLDDYNIHVIASVFKQWLRDLPNPLMTFELYEEF 2208
Cdd:pfam00620    1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGPDVDlDLEEEDVHVVASLLKLFLRELPEPLLTFELYEEF 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907198218 2209 LRAMGLQERKETIRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEDTNRMSANALAIVFAPCILRCPD 2276
Cdd:pfam00620   81 IEAAKLPDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLLRPPD 148
RhoGAP cd00159
RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like ...
2130-2297 2.70e-57

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: 196.37  E-value: 2.70e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2130 PLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDAESVNLDDYNIHVIASVFKQWLRDLPNPLMTFELYEEFL 2209
Cdd:cd00159      1 PLIIEKCIEYLEKNGLNTEGIFRVSGSASKIEELKKKFDRGEDIDDLEDYDVHDVASLLKLYLRELPEPLIPFELYDEFI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2210 RAMGLQERKETIRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEDTNRMSANALAIVFAPCILRCPDTTDplQSVQDISK 2289
Cdd:cd00159     81 ELAKIEDEEERIEALKELLKSLPPENRDLLKYLLKLLHKISQNSEVNKMTASNLAIVFAPTLLRPPDSDD--ELLEDIKK 158

                   ....*...
gi 1907198218 2290 TTTCVELI 2297
Cdd:cd00159    159 LNEIVEFL 166
MYSc_Myo24B cd14938
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ...
161-669 6.82e-52

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


Pssm-ID: 276898 [Multi-domain]  Cd Length: 713  Bit Score: 197.37  E-value: 6.82e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  161 TLLENLRNRFKHEKIYTYVGSILIAINPFKFLPIYNPKYVKMYD-NHQLGKLEPHIYAVADVAYHAMLQRKKNQCIVISG 239
Cdd:cd14938      2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  240 ESGSGKTQSTNFLIHHLtALSQKGFASGVEQ-----------------------IILGAGPVLEAFGNAKTAHNNNSSRF 296
Cdd:cd14938     82 ESGSGKSEIAKNIINFI-AYQVKGSRRLPTNlndqeednihneentdyqfnmseMLKHVNVVMEAFGNAKTVKNNNSSRF 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  297 GKFIQVnYQETGTVLGAYVEKYLLEKSRLVYQEHNERNYHVFYYLLAGASEEERLAFHLKQPEEYHFLNQDCFTVEGEDL 376
Cdd:cd14938    161 SKFCTI-HIENEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSDY 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  377 RHDFERLQLAMEMVGFLPKTRRQIFSLLSAILHLGNISYKKKTYRDDSIDICNPEVLPIVSELLE--------------V 442
Cdd:cd14938    240 SGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTEIVKAFRKKSLLMGKNQCGQNINYETILselensedigldenV 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  443 KEEMLFEALVTRKTVTVGEKLILPYKLAEAVTVR-----------NSMAKSLYSALFDWIVFRINHALLNSKDLEQDTKt 511
Cdd:cd14938    320 KNLLLACKLLSFDIETFVKYFTTNYIFNDSILIKvhnetkiqkklENFIKTCYEELFNWIIYKINEKCTQLQNININTN- 398
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  512 lSIGVLDIFGFEDYENNSFEQFCINFANERLQHYFNQHIFKLEQEEYRTEGISW-HNIDYIDNTCCINLISKKPTGLLHL 590
Cdd:cd14938    399 -YINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCeYNSENIDNEPLYNLLVGPTEGSLFS 477
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  591 LDEESNFPQATNQ-----TLLDKFKHqheENSYIEFPAVME--PAFIIKHYAGKVKYGVKDFREKNTDHMRPDIVALLRS 663
Cdd:cd14938    478 LLENVSTKTIFDKsnlhsSIIRKFSR---NSKYIKKDDITGnkKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQ 554

                   ....*.
gi 1907198218  664 SRNAFV 669
Cdd:cd14938    555 SENEYM 560
RhoGAP_ARAP cd04385
RhoGAP_ARAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
2121-2298 2.50e-44

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: 159.78  E-value: 2.50e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2121 RLTSEDraVPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDAESVNLD--DYNIHVIASVFKQWLRDLPNP 2198
Cdd:cd04385      9 QLTDND--IPVIVDKCIDFITQHGLMSEGIYRKNGKNSSVKKLLEAFRKDARSVQLRegEYTVHDVADVLKRFLRDLPDP 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2199 LMTFELYEEFLRAMGLQERKETIRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEDTNRMSANALAIVFAPCILRcpdtT 2278
Cdd:cd04385     87 LLTSELHAEWIEAAELENKDERIARYKELIRRLPPINRATLKVLIGHLYRVQKHSDENQMSVHNLALVFGPTLFQ----T 162
                          170       180
                   ....*....|....*....|
gi 1907198218 2279 DPLQSVQDISKTTTCVELIV 2298
Cdd:cd04385    163 DEHSVGQTSHEVKVIEDLID 182
RA_Myosin-IX cd01779
Ras-associating (RA) domain found in Myosin-IX; Myosins IX (Myo9) is a class of unique motor ...
17-110 2.28e-42

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


Pssm-ID: 340477  Cd Length: 97  Bit Score: 150.55  E-value: 2.28e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218   17 TLRIYPGTISEGTIYCPIPARKNSTAAEVIDSLINRLHLDKTKCYVLAEVKE---FGGEEWILNPTDCPVQRMMLWPRMA 93
Cdd:cd01779      1 MVRVYPGALSPETEFLSVEATKQTTASEVIECLVAKLRLDKAECYELAEVCGsggQGCKERRLGPSENPVQVQLLWPKMA 80
                           90
                   ....*....|....*..
gi 1907198218   94 LENRLSGEDYRFLLREK 110
Cdd:cd01779     81 GDSDNQVTSYRFFLREK 97
C1_Myosin-IXa cd20883
protein kinase C conserved region 1 (C1 domain) found in unconventional myosin-IXa and similar ...
2049-2106 4.64e-40

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: 142.80  E-value: 4.64e-40
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907198218 2049 EEHNGHIFKATQYSIPTYCEYCSSLIWIMDRASVCKLCKYACHKKCCLKTTAKCSKKY 2106
Cdd:cd20883      1 EEHNGHIFKSTQYSIPTYCEYCSSLIWMMDRAYVCKLCRYACHKKCCLKTTTKCSKKY 58
RhoGAP_fRGD1 cd04398
RhoGAP_fRGD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
2115-2299 7.55e-38

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: 141.39  E-value: 7.55e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2115 FGVELSRLTSEDRA-VPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDAESVNLD-----DYNIHVIASVF 2188
Cdd:cd04398      1 FGVPLEDLILREGDnVPNIVYQCIQAIENFGLNLEGIYRLSGNVSRVNKLKELFDKDPLNVLLIspedyESDIHSVASLL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2189 KQWLRDLPNPLMTFELYEEFLRAmgLQERKETIR--GVYSVIDQLSRTHLNTLERLIFHLVRIALQEDTNRMSANALAIV 2266
Cdd:cd04398     81 KLFFRELPEPLLTKALSREFIEA--AKIEDESRRrdALHGLINDLPDANYATLRALMFHLARIKEHESVNRMSVNNLAII 158
                          170       180       190
                   ....*....|....*....|....*....|...
gi 1907198218 2267 FAPCILRcpdttDPLQSVQDISKTTTCVELIVV 2299
Cdd:cd04398    159 WGPTLMN-----AAPDNAADMSFQSRVIETLLD 186
RhoGAP-p50rhoGAP cd04404
RhoGAP-p50rhoGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
2110-2305 7.89e-35

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: 132.85  E-value: 7.89e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2110 LSSRQFGVELSRLTS---EDRAVPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTdAESVNLDDY-NIHVIA 2185
Cdd:cd04404      1 LPTQQFGVSLQFLKEknpEQEPIPPVVRETVEYLQAHALTTEGIFRRSANTQVVKEVQQKYNM-GEPVDFDQYeDVHLPA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2186 SVFKQWLRDLPNPLMTFELYEEFLRAMGLQErKETIRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEDTNRMSANALAI 2265
Cdd:cd04404     80 VILKTFLRELPEPLLTFDLYDDIVGFLNVDK-EERVERVKQLLQTLPEENYQVLKYLIKFLVQVSAHSDQNKMTNSNLAV 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1907198218 2266 VFAPCILRCPDTTDPLQSVQDISkttTCVELIVVEQMNKY 2305
Cdd:cd04404    159 VFGPNLLWAKDASMSLSAINPIN---TFTKFLLDHQDEIF 195
RhoGAP_ARHGAP20 cd04402
RhoGAP_ARHGAP20: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
2115-2298 2.39e-34

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: 131.65  E-value: 2.39e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2115 FGVELSRLTSEDrAVPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDAEsVNLDDYNIHVIASVFKQWLRD 2194
Cdd:cd04402      2 FGQPLSNICEDD-NLPKPILDMLSLLYQKGPSTEGIFRRSANAKACKELKEKLNSGVE-VDLKAEPVLLLASVLKDFLRN 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2195 LPNPLMTFELYEEFLRAMGLQERKETIRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEDTNRMSANALAIVFAPCILrC 2274
Cdd:cd04402     80 IPGSLLSSDLYEEWMSALDQENEEEKIAELQRLLDKLPRPNVLLLKHLICVLHNISQNSETNKMDAFNLAVCIAPSLL-W 158
                          170       180
                   ....*....|....*....|....
gi 1907198218 2275 PDTTDPLQsVQDISKTTTCVELIV 2298
Cdd:cd04402    159 PPASSELQ-NEDLKKVTSLVQFLI 181
RhoGAP_nadrin cd04386
RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
2113-2298 1.74e-33

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: 129.50  E-value: 1.74e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2113 RQFGVEL-SRLTSEDRAVPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDAESVNLDDYN--IHVIASVFK 2189
Cdd:cd04386      3 PVFGTPLeEHLKRTGREIALPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKAALDAGTFSLPLDEFYsdPHAVASALK 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2190 QWLRDLPNPLMTFELYEEFLRAMGLQERKETIRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEDTNRMSANALAIVFAP 2269
Cdd:cd04386     83 SYLRELPDPLLTYNLYEDWVQAANKPDEDERLQAIWRILNKLPRENRDNLRYLIKFLSKLAQKSDENKMSPSNIAIVLAP 162
                          170       180       190
                   ....*....|....*....|....*....|
gi 1907198218 2270 CILRCP-DTTDPLQSVQDISKTTTCVELIV 2298
Cdd:cd04386    163 NLLWAKnEGSLAEMAAGTSVHVVAIVELII 192
RhoGAP_chimaerin cd04372
RhoGAP_chimaerin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
2115-2298 9.56e-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: 126.86  E-value: 9.56e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2115 FGVELSRL-TSEDRAVPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDAESVNLDDY---NIHVIASVFKQ 2190
Cdd:cd04372      1 YGCDLTTLvKAHNTQRPMVVDMCIREIEARGLQSEGLYRVSGFAEEIEDVKMAFDRDGEKADISATvypDINVITGALKL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2191 WLRDLPNPLMTFELYEEFLRAMGLQERKETIRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEDTNRMSANALAIVFAPC 2270
Cdd:cd04372     81 YFRDLPIPVITYDTYPKFIDAAKISNPDERLEAVHEALMLLPPAHYETLRYLMEHLKRVTLHEKDNKMNAENLGIVFGPT 160
                          170       180
                   ....*....|....*....|....*...
gi 1907198218 2271 ILRCPDtTDPLQSVQDISKTTTCVELIV 2298
Cdd:cd04372    161 LMRPPE-DSALTTLNDMRYQILIVQLLI 187
RhoGAP_ARHGAP21 cd04395
RhoGAP_ARHGAP21: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
2115-2298 1.44e-31

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: 123.66  E-value: 1.44e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2115 FGVELSR--LTSEDRAVPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDAESVNLDD---YNIHVIASVFK 2189
Cdd:cd04395      2 FGVPLDDcpPSSENPYVPLIVEVCCNIVEARGLETVGIYRVPGNNAAISALQEELNRGGFDIDLQDprwRDVNVVSSLLK 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2190 QWLRDLPNPLMTFELYEEFLRAMGLQERKETIRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEDTNRMSANALAIVFAP 2269
Cdd:cd04395     82 SFFRKLPEPLFTNELYPDFIEANRIEDPVERLKELRRLIHSLPDHHYETLKHLIRHLKTVADNSEVNKMEPRNLAIVFGP 161
                          170       180       190
                   ....*....|....*....|....*....|
gi 1907198218 2270 CILRCPDttDPLQS-VQDISKTTTCVELIV 2298
Cdd:cd04395    162 TLVRTSD--DNMETmVTHMPDQCKIVETLI 189
RhoGAP_CdGAP cd04384
RhoGAP_CdGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
2113-2277 1.57e-31

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: 123.38  E-value: 1.57e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2113 RQFGVELSR-LTSEDRAVPLVVEKLINYIEMHGLYTeGIYRKSGSTNKIKELRQGLDTDAE-SVNLDDY--NIHVIASVF 2188
Cdd:cd04384      1 RVFGCDLTEhLLNSGQDVPQVLKSCTEFIEKHGIVD-GIYRLSGIASNIQRLRHEFDSEQIpDLTKDVYiqDIHSVSSLC 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2189 KQWLRDLPNPLMTFELYEEFLRAMGLQERKETIRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEDTNRMSANALAIVFA 2268
Cdd:cd04384     80 KLYFRELPNPLLTYQLYEKFSEAVSAASDEERLEKIHDVIQQLPPPHYRTLEFLMRHLSRLAKYCSITNMHAKNLAIVWA 159

                   ....*....
gi 1907198218 2269 PCILRCPDT 2277
Cdd:cd04384    160 PNLLRSKQI 168
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
182-302 3.13e-31

Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.


Pssm-ID: 276814 [Multi-domain]  Cd Length: 170  Bit Score: 121.68  E-value: 3.13e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  182 ILIAINPFKFLPIYNP-KYVKMYDNHQLGKLEPHIYAVADVAYHAMLQRKKNQCIVISGESGSGKTQSTNFLIHHLTALS 260
Cdd:cd01363      1 VLVRVNPFKELPIYRDsKIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907198218  261 QKGFASG--------------VEQIILGAGPVLEAFGNAKTAHNNNSSRFGKFIQV 302
Cdd:cd01363     81 FNGINKGetegwvylteitvtLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEI 136
RA_Myosin-IXb cd17217
Ras-associating (RA) domain found in Myosin-IXb; Myosin-IXb, also termed myosin-9b (Myo9b), is ...
18-110 8.69e-31

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


Pssm-ID: 340737  Cd Length: 96  Bit Score: 117.59  E-value: 8.69e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218   18 LRIYPGTISEGTIYCPIPARKNSTAAEVIDSLINRLHLDKTKCYVLAEVKEFGGEEWILNPTDCPVQRMMLWPRMALENR 97
Cdd:cd17217      4 LQIYPQLSAESSTCCIVLATKEATASDVIKDAVATLGLDSSKPYVLAEVKESGGEEWVLDANDSPVQRVLLWPRKAQDDH 83
                           90
                   ....*....|...
gi 1907198218   98 LSGEDYRFLLREK 110
Cdd:cd17217     84 PQSDGYYFLLQER 96
RhoGAP_ARHGAP27_15_12_9 cd04403
RhoGAP_ARHGAP27_15_12_9: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
2115-2273 1.86e-30

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: 120.19  E-value: 1.86e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2115 FGVELSRLTS-EDRAVPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDaESVNLDD---YNIHVIASVFKQ 2190
Cdd:cd04403      1 FGCHLEALCQrENSTVPKFVRLCIEAVEKRGLDVDGIYRVSGNLAVIQKLRFAVDHD-EKLDLDDskwEDIHVITGALKL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2191 WLRDLPNPLMTFELYEEFLRAMGLQERKETIRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEDTNRMSANALAIVFAPC 2270
Cdd:cd04403     80 FFRELPEPLFPYSLFNDFVAAIKLSDYEQRVSAVKDLIKSLPKPNHDTLKMLFRHLCRVIEHGEKNRMTTQNLAIVFGPT 159

                   ...
gi 1907198218 2271 ILR 2273
Cdd:cd04403    160 LLR 162
RhoGAP_GMIP_PARG1 cd04378
RhoGAP_GMIP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
2115-2288 2.13e-30

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: 120.61  E-value: 2.13e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2115 FGVELSRLT-SEDRAVPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDAESVNLDDYNIHVIASVFKQWLR 2193
Cdd:cd04378      1 FGVDFSQVPrDFPDEVPFIIKKCTSEIENRALGVQGIYRVSGSKARVEKLCQAFENGKDLVELSELSPHDISSVLKLFLR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2194 DLPNPLMTFELYEEF-------LRAMGLQERKET-------IRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEDTNRMS 2259
Cdd:cd04378     81 QLPEPLILFRLYNDFialakeiQRDTEEDKAPNTpievnriIRKLKDLLRQLPASNYNTLQHLIAHLYRVAEQFEENKMS 160
                          170       180
                   ....*....|....*....|....*....
gi 1907198218 2260 ANALAIVFAPCILRcpdttdPLQSVQDIS 2288
Cdd:cd04378    161 PNNLGIVFGPTLIR------PRPGDADVS 183
C1_Myosin-IX cd20818
protein kinase C conserved region 1 (C1 domain) found in the unconventional myosin-IX family; ...
2051-2106 1.12e-29

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: 113.16  E-value: 1.12e-29
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907198218 2051 HNGHIFKATQYSIPTYCEYCSSLIWIMDRASVCKLCKYACHKKCCLKTTAKCSKKY 2106
Cdd:cd20818      1 HNGHKFATVQFNIPTYCEVCNSFIWLMEKGLVCQVCKFTCHKKCYSKITAPCKGNS 56
RhoGAP_SYD1 cd04379
RhoGAP_SYD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
2115-2280 2.59e-29

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: 117.57  E-value: 2.59e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2115 FGVELSRLT---SEDRAVPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDAESVNL--DDY-NIHVIASVF 2188
Cdd:cd04379      1 FGVPLSRLVereGESRDVPIVLQKCVQEIERRGLDVIGLYRLCGSAAKKKELRDAFERNSAAVELseELYpDINVITGVL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2189 KQWLRDLPNPLMTFELYEEFLRAMG--LQERKETIR-GVYSVIDQLSRTHLNTLERLIFHLVRIALQEDTNRMSANALAI 2265
Cdd:cd04379     81 KDYLRELPEPLITPQLYEMVLEALAvaLPNDVQTNThLTLSIIDCLPLSAKATLLLLLDHLSLVLSNSERNKMTPQNLAV 160
                          170
                   ....*....|....*
gi 1907198218 2266 VFAPCILRCPDTTDP 2280
Cdd:cd04379    161 CFGPVLMFCSQEFSR 175
RhoGAP_GMIP cd04408
RhoGAP_GMIP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP ...
2115-2299 1.37e-28

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: 115.30  E-value: 1.37e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2115 FGVELSRLTSE-DRAVPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDAESVNLDDYNIHVIASVFKQWLR 2193
Cdd:cd04408      1 FGVDFSQLPRDfPEEVPFVVVRCTAEIENRALGVQGIYRISGSKARVEKLCQAFENGRDLVDLSGHSPHDITSVLKHFLK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2194 DLPNPLMTFELYEEF------LRAMGLQERKET------IRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEDTNRMSAN 2261
Cdd:cd04408     81 ELPEPVLPFQLYDDFialakeLQRDSEKAAESPsiveniIRSLKELLGRLPVSNYNTLRHLMAHLYRVAERFEDNKMSPN 160
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1907198218 2262 ALAIVFAPCILRCPDTTD-PLQSVQDISKTTTCVELIVV 2299
Cdd:cd04408    161 NLGIVFGPTLLRPLVGGDvSMICLLDTGYQAQLVEFLIS 199
MYSc_Myo33 cd14894
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ...
271-672 4.12e-28

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: 124.08  E-value: 4.12e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  271 IILGAGPVLEAFGNAKTAHNNNSSRFGKF--IQVNY---QETGTVLGAYVEKYLLEKSRLVYQ------EHNERNYHVFY 339
Cdd:cd14894    248 IVLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFglhPWEFQICGCHISPFLLEKSRVTSErgresgDQNELNFHILY 327
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  340 YLLAGASEeerLAFHLKQPEEYHFLNQDC---------------FTVEGEDLRHDFERLQLAMEMVGFL---PKTRRQIF 401
Cdd:cd14894    328 AMVAGVNA---FPFMRLLAKELHLDGIDCsaltylgrsdhklagFVSKEDTWKKDVERWQQVIDGLDELnvsPDEQKTIF 404
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  402 SLLSAILHLGNISYKkktYRDDSIDICNPEVLPI-----VSELLEVKEEMLFEALVTRKTVTV---GEKLILPYKLAEAV 473
Cdd:cd14894    405 KVLSAVLWLGNIELD---YREVSGKLVMSSTGALnapqkVVELLELGSVEKLERMLMTKSVSLqstSETFEVTLEKGQVN 481
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  474 TVRNSMAKSLYSALFDWIVFRINHALL--------NSKDLEQDTKTLS----IGVLDIFGFEDYENNSFEQFCINFANER 541
Cdd:cd14894    482 HVRDTLARLLYQLAFNYVVFVMNEATKmsalstdgNKHQMDSNASAPEavslLKIVDVFGFEDLTHNSLDQLCINYLSEK 561
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218  542 LqhyfnqhiFKLEQEEYRTEGISWHNIDYIDNTCCINLISKKPTGLLHLLDEESNFPQATNQTLLDKFKHQ-------HE 614
Cdd:cd14894    562 L--------YAREEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASLEELTILHQSENMNAQQEEKRNklfvrniYD 633
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907198218  615 ENS--YIEFPAVMEPA------------FIIKHYAGKVKYGVKDFREKNTDHMRPDIVALLRSSRNAFVSGM 672
Cdd:cd14894    634 RNSsrLPEPPRVLSNAkrhtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRM 705
RhoGAP_p190 cd04373
RhoGAP_p190: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
2115-2279 6.06e-27

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: 109.85  E-value: 6.06e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2115 FGVELSRLTSEDRAVPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDAE-SVNLDDYNIHVIASVFKQWLR 2193
Cdd:cd04373      1 FGVPLANVVTSEKPIPIFLEKCVEFIEATGLETEGIYRVSGNKTHLDSLQKQFDQDHNlDLVSKDFTVNAVAGALKSFFS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2194 DLPNPLMTFELYEEFLRAMGLQERKETIRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEDTNRMSANALAIVFAPCILR 2273
Cdd:cd04373     81 ELPDPLIPYSMHLELVEAAKINDREQRLHALKELLKKFPPENFDVFKYVITHLNKVSQNSKVNLMTSENLSICFWPTLMR 160

                   ....*.
gi 1907198218 2274 cPDTTD 2279
Cdd:cd04373    161 -PDFTS 165
RhoGAP_ARHGAP6 cd04376
RhoGAP_ARHGAP6: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
2127-2274 1.62e-26

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: 109.45  E-value: 1.62e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2127 RAVPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDAESVNLDDYNIHVIASVFKQWLRDLPNPLMTFELYE 2206
Cdd:cd04376      7 RQVPRLVESCCQHLEKHGLQTVGIFRVGSSKKRVRQLREEFDRGIDVVLDENHSVHDVAALLKEFFRDMPDPLLPRELYT 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2207 EFLRAMGL--QERKETIRgvySVIDQLSRTHLNTLERLIFHLVRIALQ-EDT----------NRMSANALAIVFAPCILR 2273
Cdd:cd04376     87 AFIGTALLepDEQLEALQ---LLIYLLPPCNCDTLHRLLKFLHTVAEHaADSidedgqevsgNKMTSLNLATIFGPNLLH 163

                   .
gi 1907198218 2274 C 2274
Cdd:cd04376    164 K 164
RhoGAP_MgcRacGAP cd04382
RhoGAP_MgcRacGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
2129-2287 1.76e-26

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: 108.92  E-value: 1.76e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2129 VPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDAESVNLDDYNIHVIASVFKQWLRDLPNPLMTFELYEEF 2208
Cdd:cd04382     17 IPALIVHCVNEIEARGLTEEGLYRVSGSEREVKALKEKFLRGKTVPNLSKVDIHVICGCLKDFLRSLKEPLITFALWKEF 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2209 LRAMGLQERKETIRGVYSVIDQLSRTHLNTLERLIFHLVRIAlQEDTNRMSANALAIVFAPCILRCPD-TTDPLQSVQDI 2287
Cdd:cd04382     97 MEAAEILDEDNSRAALYQAISELPQPNRDTLAFLILHLQRVA-QSPECKMDINNLARVFGPTIVGYSVpNPDPMTILQDT 175
RhoGAP_Graf cd04374
RhoGAP_Graf: GTPase-activator protein (GAP) domain for Rho-like GTPases found in GRAF (GTPase ...
2133-2273 3.10e-25

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: 105.55  E-value: 3.10e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2133 VEKLINYIEMHGLYTEGIYRKSGSTNKI-KELRQGLD---TDAESVNL--DDYNIHVIASVFKQWLRDLPNPLMTFELYE 2206
Cdd:cd04374     32 VRKCIEAVETRGINEQGLYRVVGVNSKVqKLLSLGLDpktSTPGDVDLdnSEWEIKTITSALKTYLRNLPEPLMTYELHN 111
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907198218 2207 EFLRAMGLQERKETIRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEDTNRMSANALAIVFAPCILR 2273
Cdd:cd04374    112 DFINAAKSENLESRVNAIHSLVHKLPEKNREMLELLIKHLTNVSDHSKKNLMTVSNLGVVFGPTLLR 178
RhoGAP_fBEM3 cd04400
RhoGAP_fBEM3: RhoGAP (GTPase-activator [GAP] protein for Rho-like small GTPases) domain of ...
2115-2269 7.53e-25

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: 103.98  E-value: 7.53e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2115 FGVELS---RLTSE---DRAVPLVVEKLINYIEMHG-LYTEGIYRKSGSTNKIKELRQGLDTDAEsVNLDDYN----IHV 2183
Cdd:cd04400      2 FGSPLEeavELSSHkynGRDLPSVVYRCIEYLDKNRaIYEEGIFRLSGSASVIKQLKERFNTEYD-VDLFSSSlypdVHT 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2184 IASVFKQWLRDLPNPLMTFELYEEFLRAMGLQ-ERKETIRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEDTNRMSANA 2262
Cdd:cd04400     81 VAGLLKLYLRELPTLILGGELHNDFKRLVEENhDRSQRALELKDLVSQLPQANYDLLYVLFSFLRKIIEHSDVNKMNLRN 160

                   ....*..
gi 1907198218 2263 LAIVFAP 2269
Cdd:cd04400    161 VCIVFSP 167
RhoGAP_FAM13A1a cd04393
RhoGAP_FAM13A1a: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
2115-2297 8.77e-25

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: 104.08  E-value: 8.77e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2115 FGVELSRLTSE---DRAVPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTdAESVNL-DDYNIHVIASVFKQ 2190
Cdd:cd04393      3 FGVPLQELQQAgqpENGVPAVVRHIVEYLEQHGLEQEGLFRVNGNAETVEWLRQRLDS-GEEVDLsKEADVCSAASLLRL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2191 WLRDLPNPLMTFELYEEFLRAMGLQERK-ETIRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEDTNRMSANALAIVFAP 2269
Cdd:cd04393     82 FLQELPEGLIPASLQIRLMQLYQDYNGEdEFGRKLRDLLQQLPPVNYSLLKFLCHFLSNVASQHHENRMTAENLAAVFGP 161
                          170       180
                   ....*....|....*....|....*...
gi 1907198218 2270 CILRCPDTTDPLQSVQDISKTTtcVELI 2297
Cdd:cd04393    162 DVFHVYTDVEDMKEQEICSRIM--AKLL 187
RhoGAP_Bcr cd04387
RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr ...
2115-2299 9.86e-25

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: 103.85  E-value: 9.86e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2115 FGVELSRLTSEDRA-VPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDAE--SVNLDDYNIHVIASVFKQW 2191
Cdd:cd04387      1 FGVKISTVTKRERSkVPYIVRQCVEEVERRGMEEVGIYRISGVATDIQALKAAFDTNNKdvSVMLSEMDVNAIAGTLKLY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2192 LRDLPNPLMTFELYEEFLRAMGLQERKETIRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEDTNRMSANALAIVFAPCI 2271
Cdd:cd04387     81 FRELPEPLFTDELYPNFAEGIALSDPVAKESCMLNLLLSLPDPNLVTFLFLLHHLKRVAEREEVNKMSLHNLATVFGPTL 160
                          170       180       190
                   ....*....|....*....|....*....|
gi 1907198218 2272 LRCP--DTTDPLQSVQDISKTTTCVELIVV 2299
Cdd:cd04387    161 LRPSekESKIPTNTMTDSWSLEVMSQVQVL 190
RhoGAP-ARHGAP11A cd04394
RhoGAP-ARHGAP11A: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
2115-2276 1.39e-24

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: 103.71  E-value: 1.39e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2115 FGVELSRLT----SEDRAVPLVVEKLINYIEMHgLYTEGIYRKSGSTNKIKELRQGLDTDAESvnLDDYNIHVIASVFKQ 2190
Cdd:cd04394      2 FGVPLHSLPhstvPEYGNVPKFLVDACTFLLDH-LSTEGLFRKSGSVVRQKELKAKLEGGEAC--LSSALPCDVAGLLKQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2191 WLRDLPNPLMTFELYEEFLRAMGLQERKETIRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEDTNRMSANALAIVFAPC 2270
Cdd:cd04394     79 FFRELPEPLLPYDLHEALLKAQELPTDEERKSATLLLTCLLPDEHVNTLRYFFSFLYDVAQRCSENKMDSSNLAVIFAPN 158

                   ....*.
gi 1907198218 2271 ILRCPD 2276
Cdd:cd04394    159 LFQSEE 164
RhoGap_RalBP1 cd04381
RhoGap_RalBP1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
2115-2271 2.03e-24

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: 102.51  E-value: 2.03e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2115 FGVELSRLTSEDRA-----VPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDaESVNLDDYNIHVIASVFK 2189
Cdd:cd04381      1 FGASLSLAVERSRChdgidLPLVFRECIDYVEKHGMKCEGIYKVSGIKSKVDELKAAYNRR-ESPNLEEYEPPTVASLLK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2190 QWLRDLPNPLMTFELYEEFLRAMGLQERKETIRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEDTNRMSANALAIVFAP 2269
Cdd:cd04381     80 QYLRELPEPLLTKELMPRFEEACGRPTEAEREQELQRLLKELPECNRLLLAWLIVHMDHVIAQELETKMNIQNISIVLSP 159

                   ..
gi 1907198218 2270 CI 2271
Cdd:cd04381    160 TV 161
RhoGAP_ARHGAP18 cd04391
RhoGAP_ARHGAP18: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
2115-2269 2.80e-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: 103.19  E-value: 2.80e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2115 FGVELSRLTSEDRA------VPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTD--AESVNLDDYNIHVIAS 2186
Cdd:cd04391      2 FGVPLSTLLERDQKkvpgskVPLIFQKLINKLEERGLETEGILRIPGSAQRVKFLCQELEAKfyEGTFLWDQVKQHDAAS 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2187 VFKQWLRDLPNPLMTFELYEEFLRAMGLQERKETIRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEDTNRMSANALAIV 2266
Cdd:cd04391     82 LLKLFIRELPQPLLTVEYLPAFYSVQGLPSKKDQLQALNLLVLLLPEANRDTLKALLEFLQKVVDHEEKNKMNLWNVAMI 161

                   ...
gi 1907198218 2267 FAP 2269
Cdd:cd04391    162 MAP 164
RhoGAP_ARHGAP22_24_25 cd04390
RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
2127-2281 3.78e-23

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


Pssm-ID: 239855 [Multi-domain]  Cd Length: 199  Bit Score: 99.44  E-value: 3.78e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2127 RAVPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDAESVNLDDYNIHVIASVFKQWLRDLPNPLMTFELYE 2206
Cdd:cd04390     20 RLVPILVEQCVDFIREHGLKEEGLFRLPGQANLVKQLQDAFDAGERPSFDSDTDVHTVASLLKLYLRELPEPVIPWAQYE 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2207 EFL---------RAMGLQERKETIRgvysvidQLSRTHLNTLERLIFHLVRIALQEDTNRMSANALAIVFAPCILRcPDT 2277
Cdd:cd04390    100 DFLscaqllskdEEKGLGELMKQVS-------ILPKVNYNLLSYICRFLDEVQSNSSVNKMSVQNLATVFGPNILR-PKV 171

                   ....
gi 1907198218 2278 TDPL 2281
Cdd:cd04390    172 EDPA 175
RhoGAP_PARG1 cd04409
RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
2115-2299 5.72e-23

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: 99.50  E-value: 5.72e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2115 FGVELSRLT-SEDRAVPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDAESVNLDDYNIHVIASVFKQWLR 2193
Cdd:cd04409      1 FGADFAQVAkKSPDGIPFIIKKCTSEIESRALCLKGIYRVNGAKSRVEKLCQAFENGKDLVELSELSPHDISNVLKLYLR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2194 DLPNPLMTFELYEEFlraMGLQerKETIRG---------------------------VYSVIDQLSRTHLNTLERLIFHL 2246
Cdd:cd04409     81 QLPEPLILFRLYNEF---IGLA--KESQHVnetqeakknsdkkwpnmctelnrillkSKDLLRQLPAPNYNTLQFLIVHL 155
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907198218 2247 VRIALQEDTNRMSANALAIVFAPCILRCPDTTDP--LQSVQDISKTTTCVELIVV 2299
Cdd:cd04409    156 HRVSEQAEENKMSASNLGIIFGPTLIRPRPTDATvsLSSLVDYPHQARLVELLIT 210
RhoGAP_KIAA1688 cd04389
RhoGAP_KIAA1688: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
2115-2299 1.12e-21

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: 94.77  E-value: 1.12e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2115 FGVELSRLTS------EDRAVPLVVEKLINYI-EMHGLYTEGIYRKSGSTNKIKELRQGLDT-DAESVNLDDynIHVIAS 2186
Cdd:cd04389      1 FGSSLEEIMDrqkekyPELKLPWILTFLSEKVlALGGFQTEGIFRVPGDIDEVNELKLRVDQwDYPLSGLED--PHVPAS 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2187 VFKQWLRDLPNPLMTFELYEEFLramglqERKETIRGVYSVIDQLSRTHLNTLERLIfHLVRIALQEDT---NRMSANAL 2263
Cdd:cd04389     79 LLKLWLRELEEPLIPDALYQQCI------SASEDPDKAVEIVQKLPIINRLVLCYLI-NFLQVFAQPENvahTKMDVSNL 151
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1907198218 2264 AIVFAPCILRCpDTTDPLQSVQDISKTTTCVELIVV 2299
Cdd:cd04389    152 AMVFAPNILRC-TSDDPRVIFENTRKEMSFLRTLIE 186
RhoGAP_DLC1 cd04375
RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
2115-2271 2.29e-21

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: 95.18  E-value: 2.29e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2115 FGVELS-RLTSEDRAVPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDAESVNLDDYNIHVIASVFKQWLR 2193
Cdd:cd04375      5 FGVPLLvNLQRTGQPLPRSIQQAMRWLRNNALDQVGLFRKSGVKSRIQKLRSMIESSTDNVNYDGQQAYDVADMLKQYFR 84
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907198218 2194 DLPNPLMTFELYEEFLRAMGLQERKETIRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEDTNRMSANALAIVFAPCI 2271
Cdd:cd04375     85 DLPEPLLTNKLSETFIAIFQYVPKEQRLEAVQCAILLLPDENREVLQTLLYFLSDVAANSQENQMTATNLAVCLAPSL 162
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
16-111 3.39e-21

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


Pssm-ID: 425871  Cd Length: 93  Bit Score: 90.08  E-value: 3.39e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218   16 HTLRIYPGTISEGTIYCPIPARKNSTAAEVIDSLINRLHL-DKTKCYVLAEVKEFGGEEWILNPTDCPVQRMMLWPRmal 94
Cdd:pfam00788    3 GVLKVYTEDGKPGTTYKTILVSSSTTAEEVIEALLEKFGLeDDPRDYVLVEVLERGGGERRLPDDECPLQIQLQWPR--- 79
                           90
                   ....*....|....*..
gi 1907198218   95 enrlSGEDYRFLLREKN 111
Cdd:pfam00788   80 ----DASDSRFLLRKRD 92
RhoGAP_fLRG1 cd04397
RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
2115-2273 1.80e-20

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: 92.04  E-value: 1.80e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2115 FGVELSRLTSEDRA------------VPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDA-ESVNLDDYNI 2181
Cdd:cd04397      1 FGVPLEILVEKFGAdstlgvgpgklrIPALIDDIISAMRQMDMSVEGVFRKNGNIRRLKELTEEIDKNPtEVPDLSKENP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2182 HVIASVFKQWLRDLPNPLMTFELYEEFLRAMGLQERKETIRGVYSVIDQLSRTHLNTLERLIFHLVRIA----LQEDT-N 2256
Cdd:cd04397     81 VQLAALLKKFLRELPDPLLTFKLYRLWISSQKIEDEEERKRVLHLVYCLLPKYHRDTMEVLFSFLKWVSsfshIDEETgS 160
                          170
                   ....*....|....*..
gi 1907198218 2257 RMSANALAIVFAPCILR 2273
Cdd:cd04397    161 KMDIHNLATVITPNILY 177
RhoGAP_fSAC7_BAG7 cd04396
RhoGAP_fSAC7_BAG7: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
2129-2276 1.77e-19

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: 89.78  E-value: 1.77e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2129 VPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTD---AESVNLDDYNIHVIASVFKQWLRDLPNPLMTFELY 2205
Cdd:cd04396     32 IPVVVAKCGVYLKENATEVEGIFRVAGSSKRIRELQLIFSTPpdyGKSFDWDGYTVHDAASVLRRYLNNLPEPLVPLDLY 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2206 EEFLRAM------------GLQERKETI--------RGVYSVIDQLSRTHLNTLERLifhLVRIALQEDTNRMSANALAI 2265
Cdd:cd04396    112 EEFRNPLrkrprilqymkgRINEPLNTDidqaikeyRDLITRLPNLNRQLLLYLLDL---LAVFARNSDKNLMTASNLAA 188
                          170
                   ....*....|.
gi 1907198218 2266 VFAPCILRCPD 2276
Cdd:cd04396    189 IFQPGILSHPD 199
RhoGAP_p85 cd04388
RhoGAP_p85: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
2126-2280 1.06e-18

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


Pssm-ID: 239853  Cd Length: 200  Bit Score: 86.85  E-value: 1.06e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2126 DRAVPLVVeKLINYIEMHGLYTEGIYRKSGSTNKIkELRQGLDTDAESVNLDDYNIHVIASVFKQWLRDLPNPLMTFELY 2205
Cdd:cd04388     13 DVAPPLLI-KLVEAIEKKGLESSTLYRTQSSSSLT-ELRQILDCDAASVDLEQFDVAALADALKRYLLDLPNPVIPAPVY 90
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907198218 2206 EEFLR-AMGLQERKETIRGVYSVIDQLSRTHLN--TLERLIFHLVRIALQEDTNRMSANALAIVFAPCILRCPDTTDP 2280
Cdd:cd04388     91 SEMISrAQEVQSSDEYAQLLRKLIRSPNLPHQYwlTLQYLLKHFFRLCQSSSKNLLSARALAEIFSPLLFRFQPASSD 168
RhoGAP_srGAP cd04383
RhoGAP_srGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
2119-2290 1.18e-18

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: 86.32  E-value: 1.18e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2119 LSRLTSEDRAVPLVVEKLINYIEMHGLYTEGIYRKSGS---TNKIKE-LRQGLDTDAEsvNLDDYNIHVIASVFKQWLRD 2194
Cdd:cd04383      8 EEYIQDSGQAIPLVVESCIRFINLYGLQHQGIFRVSGSqveVNDIKNaFERGEDPLAD--DQNDHDINSVAGVLKLYFRG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2195 LPNPLMTFELYEEFLRAMGLQERKETIRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEDTNRMSANALAIVFAPCILRC 2274
Cdd:cd04383     86 LENPLFPKERFEDLMSCVKLENPTERVHQIREILSTLPRSVIIVMRYLFAFLNHLSQFSDENMMDPYNLAICFGPTLMPV 165
                          170
                   ....*....|....*....
gi 1907198218 2275 PDTTDP---LQSVQDISKT 2290
Cdd:cd04383    166 PEGQDQvscQAHVNELIKT 184
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
15-111 2.91e-18

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


Pssm-ID: 214612  Cd Length: 90  Bit Score: 81.58  E-value: 2.91e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218    15 EHTLRIYPGTISEGTiYCPIPARKNSTAAEVIDSLINRLHLDKT-KCYVLAEVKEfGGEEWILNPTDCPVQRMMLWPRma 93
Cdd:smart00314    2 TFVLRVYVDDLPGGT-YKTLRVSSRTTARDVIQQLLEKFHLTDDpEEYVLVEVLP-DGKERVLPDDENPLQLQKLWPR-- 77
                            90
                    ....*....|....*...
gi 1907198218    94 lenrlSGEDYRFLLREKN 111
Cdd:smart00314   78 -----RGPNLRFVLRKRD 90
RA cd17043
Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA ...
17-109 1.11e-17

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


Pssm-ID: 340563  Cd Length: 87  Bit Score: 80.05  E-value: 1.11e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218   17 TLRIYPGTISEGTIYCPIPARKNSTAAEVIDSLINRLHL-DKTKCYVLAEVKEFGGEEWILNPTDCPVQRMMLWPRmale 95
Cdd:cd17043      1 VLKVYDDDLAPGSAYKSILVSSTTTAREVVQLLLEKYGLeEDPEDYSLYEVSEKQETERVLHDDECPLLIQLEWGP---- 76
                           90
                   ....*....|....
gi 1907198218   96 nrlSGEDYRFLLRE 109
Cdd:cd17043     77 ---QGTEFRFVLKR 87
C1_Myosin-IXb cd20884
protein kinase C conserved region 1 (C1 domain) found in unconventional myosin-IXb and similar ...
2049-2103 2.11e-17

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: 77.98  E-value: 2.11e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907198218 2049 EEHNGHIFKATQYSIPTYCEYCSSLIWIMDRASVCKLCKYACHKKCCLKTTAKCS 2103
Cdd:cd20884      1 EEYNGHVFTSYQVNIMQSCEQCSSYIWAMEKALLCSVCKMTCHKKCLSKIQSHCS 55
RhoGAP_fRGD2 cd04399
RhoGAP_fRGD2: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
2115-2274 4.37e-15

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: 76.60  E-value: 4.37e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2115 FGVELSRLTSEDR-AVPLVVEKLINYIEMHGLYTEG------IYRKSGSTNKIKELRQGLDT----DAESVNLDDYNIHV 2183
Cdd:cd04399      1 FGVDLETRCRLDKkVVPLIVSAILSYLDQLYPDLINdevrrnVWTDPVSLKETHQLRNLLNKpkkpDKEVIILKKFEPST 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2184 IASVFKQWLRDLPNPLMTFELYeEFLRAM-----GLQERKET--IRGVYSVIDQLSRTHLNTLERLIFHLVRIAlqeDTN 2256
Cdd:cd04399     81 VASVLKLYLLELPDSLIPHDIY-DLIRSLysaypPSQEDSDTarIQGLQSTLSQLPKSHIATLDAIITHFYRLI---EIT 156
                          170       180
                   ....*....|....*....|....
gi 1907198218 2257 RMSANA------LAIVFAPCILRC 2274
Cdd:cd04399    157 KMGESEeeyadkLATSLSREILRP 180
C1_SpBZZ1-like cd20824
protein kinase C conserved region 1 (C1 domain) found in Schizosaccharomyces pombe protein ...
2054-2104 1.32e-14

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: 70.04  E-value: 1.32e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907198218 2054 HIFKATQYSIPTYCEYCSSLIW-IMDRASVCKLCKYACHKKCCLKTTAKCSK 2104
Cdd:cd20824      2 HNFKPHSFSIPTKCDYCGEKIWgLSKKGLSCKDCGFNCHIKCELKVPPECPG 53
RhoGAP_ARHGAP19 cd04392
RhoGAP_ARHGAP19: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
2133-2307 4.19e-14

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: 73.65  E-value: 4.19e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2133 VEKLINYIEMHgLYTEGIYRKSGSTNKIKELRQGLDTDAEsVNLD--DYNIHVIASVFKQWLRDLPNPLMTFELYEEFLR 2210
Cdd:cd04392     13 IYQLIEYLEKN-LRVEGLFRKPGNSARQQELRDLLNSGTD-LDLEsgGFHAHDCATVLKGFLGELPEPLLTHAHYPAHLQ 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2211 AMGLQERKET------------IRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEDTNRMSANALAIVFAPCILrCPDTT 2278
Cdd:cd04392     91 IADLCQFDEKgnktsapdkerlLEALQLLLLLLPEENRNLLKLILDLLYQTAKHEDKNKMSADNLALLFTPHLI-CPRNL 169
                          170       180
                   ....*....|....*....|....*....
gi 1907198218 2279 DPLQSVQDISKTTTCVELIVVEQMNKYKA 2307
Cdd:cd04392    170 TPEDLHENAQKLNSIVTFMIKHSQKLFKA 198
C1 cd00029
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ...
2054-2102 1.16e-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: 64.46  E-value: 1.16e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2054 HIFKATQYSIPTYCEYCSSLIWIMDRASV-CKLCKYACHKKCCLKTTAKC 2102
Cdd:cd00029      1 HRFVPTTFSSPTFCDVCGKLIWGLFKQGLkCSDCGLVCHKKCLDKAPSPC 50
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
2054-2102 2.22e-12

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


Pssm-ID: 197519  Cd Length: 50  Bit Score: 63.64  E-value: 2.22e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 1907198218  2054 HIFKATQYSIPTYCEYCSSLIWIMDRASV-CKLCKYACHKKCCLKTTAKC 2102
Cdd:smart00109    1 HKHVFRTFTKPTFCCVCRKSIWGSFKQGLrCSECKVKCHKKCADKVPKAC 50
C1_PDZD8 cd20825
protein kinase C conserved region 1 (C1 domain) found in PDZ domain-containing protein 8 ...
2051-2104 8.10e-12

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: 62.30  E-value: 8.10e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907198218 2051 HNGHIFKATQYSIPTYCEYCSSLIWiMDRASVCKLCKYACHKKCCLKTTAK--CSK 2104
Cdd:cd20825      1 EGKHDFVLTQFQNATYCDFCKKKIW-LKEAFQCRLCGMICHKKCLDKCQAEtlCTR 55
RhoGAP_OCRL1 cd04380
RhoGAP_OCRL1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
2124-2297 2.56e-11

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: 65.83  E-value: 2.56e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2124 SEDRAVPLVVEK----LINYIEMHGLYTEGIYRKSGSTNKIK----ELRQGLDTDaeSVNLDDYNIHVIASVFKQWLRDL 2195
Cdd:cd04380     41 PDYSEVPLSIPKeiwrLVDYLYTRGLAQEGLFEEPGLPSEPGellaEIRDALDTG--SPFNSPGSAESVAEALLLFLESL 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2196 PNPLMTFELYEEFLRAMGLQERKEtirgvYSVID-QLSRTHLNTLERLIFHLVRIALQEDTNRMSANALAIVFAPCILRC 2274
Cdd:cd04380    119 PDPIIPYSLYERLLEAVANNEEDK-----RQVIRiSLPPVHRNVFVYLCSFLRELLSESADRGLDENTLATIFGRVLLRD 193
                          170       180
                   ....*....|....*....|...
gi 1907198218 2275 PdttDPLQSVQDISKTTTCVELI 2297
Cdd:cd04380    194 P---PRAGGKERRAERDRKRAFI 213
C1_nPKC_theta-like_rpt1 cd20834
first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
2048-2104 3.62e-11

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: 60.41  E-value: 3.62e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907198218 2048 VEEHNGHIFKATQYSIPTYCEYCSSLIW-IMDRASVCKLCKYACHKKCCLKTTAKCSK 2104
Cdd:cd20834      2 VHEVKGHEFIAKFFRQPTFCSVCKEFLWgFNKQGYQCRQCNAAVHKKCHDKILGKCPG 59
C1_TNS2-like cd20826
protein kinase C conserved region 1 (C1 domain) found in tensin-2 like (TNS2-like) proteins; ...
2053-2103 9.44e-11

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: 58.94  E-value: 9.44e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907198218 2053 GHIFKATQYSIPTYCEYCSSLIWimDRASVCKLCKYACHKKCCLKTTAKCS 2103
Cdd:cd20826      2 SHSFKEKSFRKPRTCDVCKQIIW--NEGSSCRVCKYACHRKCEPKVTAACS 50
C1_cPKC_nPKC_rpt1 cd20792
first protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) ...
2053-2104 1.20e-10

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: 58.80  E-value: 1.20e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907198218 2053 GHIFKATQYSIPTYCEYCSSLIW-IMDRASVCKLCKYACHKKCCLKTTAKCSK 2104
Cdd:cd20792      1 GHKFVATFFKQPTFCSHCKDFIWgLGKQGYQCQVCRFVVHKRCHEYVVFKCPG 53
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
2054-2102 8.93e-10

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: 56.30  E-value: 8.93e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2054 HIFKATQYSIPTYCEYCSSLIWIMDRASV-CKLCKYACHKKCCLKTTAKC 2102
Cdd:pfam00130    1 HHFVHRNFKQPTFCDHCGEFLWGLGKQGLkCSWCKLNVHKRCHEKVPPEC 50
C1_ARHGEF-like cd20832
protein kinase C conserved region 1 (C1 domain) found in uncharacterized Rho guanine ...
2053-2103 9.54e-09

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: 53.53  E-value: 9.54e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907198218 2053 GHIFKATQYSIPTYCEYCSSLIW-IMDRASVCKLCKYACHKKCCLKTTAKCS 2103
Cdd:cd20832      1 GHQFVLQHYYQVTFCNHCSGLLWgIGYQGYQCSDCEFNIHKQCIEVIEESCP 52
C1_RASSF1 cd20885
protein kinase C conserved region 1 (C1 domain) found in Ras association domain-containing ...
2051-2094 1.06e-08

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: 53.43  E-value: 1.06e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1907198218 2051 HNGHIFKATQYSIPTYCEYCSSLIW-IMDRASVCKLCKYACHKKC 2094
Cdd:cd20885      1 GEGHDFQPCSLTNPTWCDLCGDFIWgLYKQCLRCTHCKYTCHLRC 45
C1_DGKtheta_typeV_rpt1 cd20803
first protein kinase C conserved region 1 (C1 domain) found in type V diacylglycerol kinase, ...
2053-2103 1.68e-08

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: 52.69  E-value: 1.68e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907198218 2053 GHIFKATQYSIPTYCEYCSSLIW-IMDRASVCKLCKYACHKKCCLKTTAKCS 2103
Cdd:cd20803      1 GHSFRKKTFHKPTYCHHCTDLLWgLLNQGYQCEVCNFVSHERCLKTVVTPCS 52
C1_Sbf-like cd20827
protein kinase C conserved region 1 (C1 domain) found in the myotubularin-related protein Sbf ...
2054-2104 2.39e-08

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: 52.42  E-value: 2.39e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907198218 2054 HIFKATQYSIPTYCEYCSSLIW-IMDRASVCKLCKYACHKKCCLKTTAKCSK 2104
Cdd:cd20827      2 HRFEKHNFTTPTYCDYCSSLLWgLVKTGMRCADCGYSCHEKCLEHVPKNCTK 53
C1_ScPKC1-like_rpt1 cd20822
first protein kinase C conserved region 1 (C1 domain) found in Saccharomyces cerevisiae ...
2052-2105 4.86e-08

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: 51.52  E-value: 4.86e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907198218 2052 NGHIFKATQYSIPTYCEYCSSLIwiMDRASVCKLCKYACHKKCCLKTTAKCSKK 2105
Cdd:cd20822      1 RGHKFVQKQFYQIMRCAVCGEFL--VNAGYQCEDCKYTCHKKCYEKVVTKCISK 52
C1_nPKC_epsilon-like_rpt1 cd20835
first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
2048-2102 5.90e-08

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: 51.70  E-value: 5.90e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907198218 2048 VEEHNGHIFKATQYSIPTYCEYCSSLIW--IMDRASVCKLCKYACHKKCCLKTTAKC 2102
Cdd:cd20835      4 VHQVNGHKFMATYLRQPTYCSHCKDFIWgvIGKQGYQCQVCTCVVHKRCHQLVVTKC 60
C1_dGM13116p-like cd20831
protein kinase C conserved region 1 (C1 domain) found in Drosophila melanogaster GM13116p and ...
2051-2104 6.29e-08

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: 51.19  E-value: 6.29e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907198218 2051 HNGHIFKATQYSIPTYCEYCSSLI--WIMDRASVCKLCKYACHKKCCLKTTAKCSK 2104
Cdd:cd20831      3 YNDHTFVATHFKGGPSCAVCNKLIpgRFGKQGYQCRDCGLICHKRCHVKVETHCPS 58
C1_DEF8 cd20819
protein kinase C conserved region 1 (C1 domain) found in differentially expressed in FDCP 8 ...
2052-2094 7.37e-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: 51.13  E-value: 7.37e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1907198218 2052 NGHIFKATQYSIPT--YCEYCSSLIW-IMDRASVCKLCKYACHKKC 2094
Cdd:cd20819      4 LGHHFVLQKSKSSSkqYCDKCCGIIWgLLQTWYRCTDCGYRCHSKC 49
C1_cPKC_nPKC_rpt2 cd20793
second protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) ...
2054-2102 1.75e-07

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: 49.58  E-value: 1.75e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2054 HIFKATQYSIPTYCEYCSSLIW-IMDRASVCKLCKYACHKKCCLKTTAKC 2102
Cdd:cd20793      1 HKFKVHTYYSPTFCDHCGSLLYgLVRQGLKCKDCGMNVHHRCKENVPHLC 50
C1_PKD2_rpt2 cd20843
second protein kinase C conserved region 1 (C1 domain) found in protein kinase D2 (PKD2) and ...
2054-2102 4.39e-07

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: 49.59  E-value: 4.39e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2054 HIFKATQYSIPTYCEYCSSLIWIMDRASV-CKLCKYACHKKCCLKTTAKC 2102
Cdd:cd20843     12 HTFVIHSYTRPTVCQFCKKLLKGLFRQGLqCKDCKFNCHKRCATRVPNDC 61
C1_aPKC cd20794
protein kinase C conserved region 1 (C1 domain) found in the atypical protein kinase C (aPKC) ...
2052-2104 4.98e-07

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: 48.42  E-value: 4.98e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907198218 2052 NGHIFKATQYSIPTYCEYCSSLIWIMDRASV-CKLCKYACHKKCCLKTTAKCSK 2104
Cdd:cd20794      1 NGHLFQAKRFNRRAVCAYCSDRIWGLGRQGYkCINCKLLVHKKCHKLVKVACGQ 54
C1_nPKC_theta-like_rpt2 cd20837
second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
2054-2102 5.76e-07

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: 48.20  E-value: 5.76e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2054 HIFKATQYSIPTYCEYCSSLIWIMDRASV-CKLCKYACHKKCCLKTTAKC 2102
Cdd:cd20837      1 HRFKVYNYMSPTFCDHCGSLLWGLFRQGLkCEECGMNVHHKCQKKVANLC 50
C1_MTMR-like cd20828
protein kinase C conserved region 1 (C1 domain) found in uncharacterized proteins similar to ...
2054-2104 6.29e-07

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: 48.59  E-value: 6.29e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907198218 2054 HIFKATQYSIPTYCEYCSSLIW-IMDRASVCKLCKYACHKKCCLKTTAKCSK 2104
Cdd:cd20828      6 HNFEPHSFVTPTNCDYCLQILWgIVKKGMKCSECGYNCHEKCQPQVPKQCSK 57
C1_nPKC_epsilon-like_rpt2 cd20838
second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
2054-2094 8.26e-07

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: 48.04  E-value: 8.26e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1907198218 2054 HIFKATQYSIPTYCEYCSSLIW-IMDRASVCKLCKYACHKKC 2094
Cdd:cd20838      3 HRFSVHNYKRPTFCDHCGSLLYgLYKQGLQCKVCKMNVHKRC 44
C1_KSR cd20812
protein kinase C conserved region 1 (C1 domain) found in the kinase suppressor of Ras (KSR) ...
2054-2103 9.67e-07

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: 47.70  E-value: 9.67e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2054 HIFKaTQYSIPTYCEYCSSLIWimdRASVCKLCKYACHKKCCLKTTAKCS 2103
Cdd:cd20812      3 HRFS-KKLFMRQTCDYCHKQMF---FGLKCKDCKYKCHKKCAKKAPPSCG 48
C1_PKD_rpt2 cd20796
second protein kinase C conserved region 1 (C1 domain) found in the family of protein kinase D ...
2054-2094 1.38e-06

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: 47.28  E-value: 1.38e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1907198218 2054 HIFKATQYSIPTYCEYCSSLIWIMDRASV-CKLCKYACHKKC 2094
Cdd:cd20796      2 HTFVVHTYTKPTVCQHCKKLLKGLFRQGLqCKDCKFNCHKKC 43
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
1097-1118 2.28e-06

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


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 45.78  E-value: 2.28e-06
                            10        20
                    ....*....|....*....|..
gi 1907198218  1097 RHKAATCIQSRWRGYRQRKKYK 1118
Cdd:smart00015    2 LTRAAIIIQAAWRGYLARKRYK 23
C1_PKD3_rpt2 cd20844
second protein kinase C conserved region 1 (C1 domain) found in protein kinase D3 (PKD3) and ...
2054-2102 4.26e-06

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


Pssm-ID: 410394  Cd Length: 69  Bit Score: 46.54  E-value: 4.26e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2054 HIFKATQYSIPTYCEYCSSLIWIMDRASV-CKLCKYACHKKCCLKTTAKC 2102
Cdd:cd20844      6 HTFAVHSYTRPTICQYCKRLLKGLFRQGMqCKDCRFNCHKRCASKVPRDC 55
C1_MRCK cd20809
protein kinase C conserved region 1 (C1 domain) found in the Myotonic dystrophy kinase-related ...
2054-2102 5.31e-06

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: 45.73  E-value: 5.31e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2054 HIFKATQYSIPTYCEYCSSLIWIMDR-ASVCKLCKYACHKKCCLKTTAKC 2102
Cdd:cd20809      1 HKFIVRTFSTPTKCNHCTSLMVGLVRqGLVCEVCGYACHVSCADKAPQVC 50
C1_PKD1_rpt2 cd20842
second protein kinase C conserved region 1 (C1 domain) found in protein kinase D (PKD) and ...
2054-2102 5.48e-06

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: 46.93  E-value: 5.48e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2054 HIFKATQYSIPTYCEYCSSLIWIMDRASV-CKLCKYACHKKCCLKTTAKC 2102
Cdd:cd20842     35 HTFVIHSYTRPTVCQYCKKLLKGLFRQGLqCKDCKFNCHKRCAPKVPNNC 84
C1_RASGRP cd20808
protein kinase C conserved region 1 (C1 domain) found in the RAS guanyl-releasing protein ...
2054-2094 6.98e-06

protein kinase C conserved region 1 (C1 domain) found in the RAS guanyl-releasing protein (RASGRP) family; The RASGRP family includes RASGRP1-4. They function as cation-, usually calcium-, and diacylglycerol (DAG)-regulated nucleotide exchange factor activating Ras through the exchange of bound GDP for GTP. RASGRP1, also called calcium and DAG-regulated guanine nucleotide exchange factor II (CalDAG-GEFII) or Ras guanyl-releasing protein, activates the Erk/MAP kinase cascade and regulates T-cell/B-cell development, homeostasis and differentiation by coupling T-lymphocyte/B-lymphocyte antigen receptors to Ras. RASGRP1 also regulates NK cell cytotoxicity and ITAM-dependent cytokine production by activation of Ras-mediated ERK and JNK pathways. RASGRP2, also called calcium and DAG-regulated guanine nucleotide exchange factor I (CalDAG-GEFI), Cdc25-like protein (CDC25L), or F25B3.3 kinase-like protein, specifically activates Rap and may also activate other GTPases such as RRAS, RRAS2, NRAS, KRAS but not HRAS. RASGRP2 is involved in aggregation of platelets and adhesion of T-lymphocytes and neutrophils probably through inside-out integrin activation, as well as in the muscarinic acetylcholine receptor M1/CHRM1 signaling pathway. RASGRP3, also called calcium and DAG-regulated guanine nucleotide exchange factor III (CalDAG-GEFIII), or guanine nucleotide exchange factor for Rap1, is a guanine nucleotide-exchange factor activating H-Ras, R-Ras and Ras-associated protein-1/2. It functions as an important mediator of signaling downstream from receptor coupled phosphoinositide turnover in B and T cells. RASGRP4 may function in mast cell differentiation. 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: 410358  Cd Length: 52  Bit Score: 45.41  E-value: 6.98e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1907198218 2054 HIFKATQYSIPTYCEYCSSLIW-IMDRASVCKLCKYACHKKC 2094
Cdd:cd20808      2 HNFQETTYFKPTFCDHCTGLLWgLIKQGYKCKDCGINCHKHC 43
C1_RASGRP1 cd20860
protein kinase C conserved region 1 (C1 domain) found in RAS guanyl-releasing protein 1 ...
2054-2105 7.51e-06

protein kinase C conserved region 1 (C1 domain) found in RAS guanyl-releasing protein 1 (RASGRP1) and similar proteins; RASGRP1, also called calcium and DAG-regulated guanine nucleotide exchange factor II (CalDAG-GEFII) or Ras guanyl-releasing protein, functions as a calcium- and diacylglycerol (DAG)-regulated nucleotide exchange factor specifically activating Ras through the exchange of bound GDP for GTP. It activates the Erk/MAP kinase cascade and regulates T-cell/B-cell development, homeostasis and differentiation by coupling T-lymphocyte/B-lymphocyte antigen receptors to Ras. RASGRP1 also regulates NK cell cytotoxicity and ITAM-dependent cytokine production by activation of Ras-mediated ERK and JNK pathways. 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: 410410  Cd Length: 55  Bit Score: 45.31  E-value: 7.51e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907198218 2054 HIFKATQYSIPTYCEYCSSLIW-IMDRASVCKLCKYACHKKCCLKTTAKCSKK 2105
Cdd:cd20860      3 HNFQETTYLKPTFCDNCAGFLWgVIKQGYRCKDCGMNCHKQCKDLVVFECKKR 55
C1_DGKgamma_rpt1 cd20846
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase gamma ...
2048-2106 8.18e-06

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: 45.69  E-value: 8.18e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2048 VEEHNGHIFKATQYSIPTYCEYCSS-LIWIMDRASVCKLCKYACHKKCCLKTTAKCSKKY 2106
Cdd:cd20846     11 VKDDGQHAWRLKHFKKPAYCNFCHTmLLGVRKQGLCCSFCKYTVHERCVSKDIASCISTY 70
C1_DGK_typeII_rpt1 cd20800
first protein kinase C conserved region 1 (C1 domain) found in type II diacylglycerol kinases; ...
2051-2102 8.19e-06

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: 45.39  E-value: 8.19e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907198218 2051 HNGHIFKATQYSIPTYCEYC-SSLIWIMDRASVCKLCKYACHKKCCLKTTAKC 2102
Cdd:cd20800      2 SGSHNWYACSHARPTYCNVCrEALSGVTSHGLSCEVCKFKAHKRCAVKAPNNC 54
C1_RASGRP4 cd20863
protein kinase C conserved region 1 (C1 domain) found in RAS guanyl-releasing protein 4 ...
2051-2105 1.29e-05

protein kinase C conserved region 1 (C1 domain) found in RAS guanyl-releasing protein 4 (RASGRP4) and similar proteins; RASGRP4 functions as a cation- and diacylglycerol (DAG)-regulated nucleotide exchange factor activating Ras through the exchange of bound GDP for GTP. It may function in mast cell differentiation. 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: 410413  Cd Length: 57  Bit Score: 44.77  E-value: 1.29e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907198218 2051 HNGHIFKATQYSIPTYCEYCSSLIW-IMDRASVCKLCKYACHKKCCLKTTAKCSKK 2105
Cdd:cd20863      1 GFLHNFHETTFKKPTFCDSCSGFLWgVTKQGYRCQDCGINCHKHCKDQVDVECKKR 56
C1_CeDKF1-like_rpt1 cd20797
first protein kinase C conserved region 1 (C1 domain) found in Caenorhabditis elegans serine ...
2054-2103 1.64e-05

first protein kinase C conserved region 1 (C1 domain) found in Caenorhabditis elegans serine/threonine-protein kinase DKF-1 and similar proteins; DKF-1 converts transient diacylglycerol (DAG) signals into prolonged physiological effects, independently of PKC. It plays a role in the regulation of growth and neuromuscular control of movement. It is involved in immune response to Staphylococcus aureus bacterium by activating transcription factor hlh-30 downstream of phospholipase plc-1. Members of this group 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: 410347  Cd Length: 56  Bit Score: 44.39  E-value: 1.64e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907198218 2054 HIFKATQYSIPTYCEYCSSLIWIMDRASV-CKLCKYACHKKCCLKTTAKCS 2103
Cdd:cd20797      4 HVVEVEQYMTPTFCDYCGEMLTGLMKQGVkCKNCRCNFHKRCANAPRNNCA 54
C1_RASSF1-like cd20820
protein kinase C conserved region 1 (C1 domain) found in the Ras association domain-containing ...
2053-2094 1.87e-05

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: 43.97  E-value: 1.87e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1907198218 2053 GHIFKATQYSIPTYCEYCSSLIWIMDRASV-CKLCKYACHKKC 2094
Cdd:cd20820      1 GHRFVPLELEQPTWCDLCGSVILGLFRKCLrCANCKMTCHPRC 43
C1_TNS1_v cd20888
protein kinase C conserved region 1 (C1 domain) found in tensin-1 (TNS1) variant and similar ...
2049-2103 2.04e-05

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: 44.09  E-value: 2.04e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907198218 2049 EEHNGHIFKATQYSIPTYCEYCSSLIwiMDRASVCKLCKYACHKKCCLKTTAKCS 2103
Cdd:cd20888      1 EAPHTHTFKVKTFKKVKSCGICKQAI--TREGSTCRVCKLSCHKKCEAKVATPCV 53
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
1098-1118 3.41e-05

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 459869  Cd Length: 21  Bit Score: 42.69  E-value: 3.41e-05
                           10        20
                   ....*....|....*....|.
gi 1907198218 1098 HKAATCIQSRWRGYRQRKKYK 1118
Cdd:pfam00612    1 RKAAIKIQAAWRGYLARKRYK 21
C1_PKD_rpt1 cd20795
first protein kinase C conserved region 1 (C1 domain) found in the protein kinase D (PKD) ...
2054-2104 3.46e-05

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: 43.44  E-value: 3.46e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907198218 2054 HIFKATQYSIPTYCEYCSSLIWIMDRASV-CKLCKYACHKKCCLKTTAKCSK 2104
Cdd:cd20795      4 HSLFVHSYKSPTFCDFCGEMLFGLVRQGLkCEGCGLNFHKRCAYKIPNNCTG 55
C1_RASGRP3 cd20862
protein kinase C conserved region 1 (C1 domain) found in RAS guanyl-releasing protein 3 ...
2054-2094 3.74e-05

protein kinase C conserved region 1 (C1 domain) found in RAS guanyl-releasing protein 3 (RASGRP3) and similar proteins; RASGRP3, also called calcium and DAG-regulated guanine nucleotide exchange factor III (CalDAG-GEFIII), or guanine nucleotide exchange factor for Rap1, is a guanine nucleotide-exchange factor activating H-Ras, R-Ras and Ras-associated protein-1/2. It functions as an important mediator of signaling downstream from receptor coupled phosphoinositide turnover in B and T cells. 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: 410412  Cd Length: 59  Bit Score: 43.48  E-value: 3.74e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1907198218 2054 HIFKATQYSIPTYCEYCSSLIW-IMDRASVCKLCKYACHKKC 2094
Cdd:cd20862      8 HNFQEMTYLKPTFCEHCAGFLWgIIKQGYKCKDCGVNCHKQC 49
C1_ROCK2 cd20875
protein kinase C conserved region 1 (C1 domain) found in Rho-associated coiled-coil containing ...
2051-2107 4.02e-05

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


Pssm-ID: 410425  Cd Length: 71  Bit Score: 43.87  E-value: 4.02e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907198218 2051 HNGHIFKATQYSIPTYCEYCSSLIWIMDR---ASVCKLCKYACHKKCCLK---TTAKCSKKYD 2107
Cdd:cd20875      9 HKGHEFIPTLYHFPTNCEACMKPLWHMFKpppALECRRCHIKCHKDHMDKkeeIIAPCKVNYD 71
C1_DGK_typeI_rpt1 cd20799
first protein kinase C conserved region 1 (C1 domain) found in type I diacylglycerol kinases; ...
2054-2106 4.52e-05

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: 43.13  E-value: 4.52e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907198218 2054 HIFKATQYSIPTYCEYC-SSLIWIMDRASVCKLCKYACHKKCCLKTTAKCSKKY 2106
Cdd:cd20799      6 HVWRLKHFNKPAYCNVCeNMLVGLRKQGLCCTFCKYTVHERCVSRAPASCIRTY 59
C1_MgcRacGAP cd20821
protein kinase C conserved region 1 (C1 domain) found in male germ cell RacGap (MgcRacGAP) and ...
2054-2094 4.74e-05

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: 43.16  E-value: 4.74e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1907198218 2054 HIFKATQYSIPTYCEYCSSLIWIMDRASVCKLCKYACHKKC 2094
Cdd:cd20821      3 HRFVSKTVIKPETCVVCGKRIKFGKKALKCKDCRVVCHPDC 43
C1_ROCK cd20813
protein kinase C conserved region 1 (C1 domain) found in the Rho-associated coiled-coil ...
2048-2092 6.51e-05

protein kinase C conserved region 1 (C1 domain) found in the Rho-associated coiled-coil containing protein kinase (ROCK) family; ROCK is a serine/threonine protein kinase, catalyzing the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. It is also referred to as Rho-associated kinase or simply as Rho kinase. It contains 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. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain. It is activated via interaction with Rho GTPases and is involved in many cellular functions including contraction, adhesion, migration, motility, proliferation, and apoptosis. The ROCK subfamily consists of two isoforms, ROCK1 and ROCK2, which may be functionally redundant in some systems, but exhibit different tissue distributions. Both isoforms are ubiquitously expressed in most tissues, but ROCK2 is more prominent in brain and skeletal muscle while ROCK1 is more pronounced in the liver, testes, and kidney. Studies in knockout mice result in different phenotypes, suggesting that the two isoforms do not compensate for each other during embryonic development. 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: 410363  Cd Length: 65  Bit Score: 43.03  E-value: 6.51e-05
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gi 1907198218 2048 VEEHNGHIFKATQYSIPTYCEYCSSLIWIMDRASV---CKLCKYACHK 2092
Cdd:cd20813      2 TISHKGHEFVEITFHMPTTCDVCHKPLWHLFKPPPaleCKRCRMKIHK 49
C1_aPKC_iota cd21094
protein kinase C conserved region 1 (C1 domain) found in the atypical protein kinase C (aPKC) ...
2052-2104 7.56e-05

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: 42.68  E-value: 7.56e-05
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gi 1907198218 2052 NGHIFKATQYSIPTYCEYCSSLIWIMDRASV-CKLCKYACHKKCCLKTTAKCSK 2104
Cdd:cd21094      1 NGHTFQAKRFNRRAHCAICTDRIWGLGRQGYkCINCKLLVHKKCHKLVTIECGR 54
C1_aPKC_zeta cd21095
protein kinase C conserved region 1 (C1 domain) found in the atypical protein kinase C (aPKC) ...
2052-2104 7.81e-05

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: 42.28  E-value: 7.81e-05
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gi 1907198218 2052 NGHIFKATQYSIPTYCEYCSSLIWIMDRASV-CKLCKYACHKKCCLKTTAKCSK 2104
Cdd:cd21095      1 NGHLFQAKRFNRRAYCGQCSERIWGLGRQGYkCINCKLLVHKRCHKLVPLTCKR 54
C1_TNS3_v cd20889
protein kinase C conserved region 1 (C1 domain) found in tensin-3 (TNS3) variant and similar ...
2054-2102 8.24e-05

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: 42.57  E-value: 8.24e-05
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gi 1907198218 2054 HIFKATQYSIPTYCEYCSSLIwiMDRASVCKLCKYACHKKCCLKTTAKC 2102
Cdd:cd20889      3 HTFKNKTFKKPKVCSICKQVI--DSQGISCRVCKYACHKKCEAKVVTPC 49
C1_CHN cd20806
protein kinase C conserved region 1 (C1 domain) found in the chimaerin family; Chimaerins are ...
2054-2104 8.59e-05

protein kinase C conserved region 1 (C1 domain) found in the chimaerin family; Chimaerins are a family of phorbolester- and diacylglycerol-responsive GTPase activating proteins (GAPs) specific for the Rho-like GTPase Rac. Alpha1-chimerin (formerly known as N-chimerin) and alpha2-chimerin are alternatively spliced products of a single gene, as are beta1- and beta2-chimerin. Alpha1- and beta1-chimerin have a relatively short N-terminal region that does not encode any recognizable domains, whereas alpha2- and beta2-chimerin both include a functional SH2 domain that can bind to phosphotyrosine motifs within receptors. All the isoforms contain 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: 410356  Cd Length: 53  Bit Score: 42.30  E-value: 8.59e-05
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gi 1907198218 2054 HIFKATQYSIPTYCEYCSSLIW-IMDRASVCKLCKYACHKKCCLKTTAKCSK 2104
Cdd:cd20806      2 HNFKVHTFKGPHWCDYCGNFMWgLIAQGVKCEDCGFNAHKQCSKLVPHDCQP 53
C1_PKD3_rpt1 cd20841
first protein kinase C conserved region 1 (C1 domain) found in protein kinase D3 (PKD3) and ...
2054-2103 8.82e-05

first protein kinase C conserved region 1 (C1 domain) found in protein kinase D3 (PKD3) and similar proteins; PKD3 is also called PRKD3, PRKCN, serine/threonine-protein kinase D3 (nPKC-D3), protein kinase C nu type (nPKC-nu), or protein kinase EPK2. It converts transient diacylglycerol (DAG) signals into prolonged physiological effects, downstream of PKC. It is involved in the regulation of the cell cycle by modulating microtubule nucleation and dynamics. PKD3 acts as a key mediator in several cancer development signaling pathways. PKD3 contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the 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: 410391  Cd Length: 75  Bit Score: 43.11  E-value: 8.82e-05
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gi 1907198218 2054 HIFKATQYSIPTYCEYCSSLIWIMDRASV-CKLCKYACHKKCCLKTTAKCS 2103
Cdd:cd20841     11 HTLYVHSYKAPTFCDYCGEMLWGLVRQGLkCEGCGLNYHKRCAFKIPNNCS 61
C1_MRCKalpha cd20864
protein kinase C conserved region 1 (C1 domain) found in myotonic dystrophy kinase-related ...
2054-2102 9.03e-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: 42.31  E-value: 9.03e-05
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gi 1907198218 2054 HIFKATQYSIPTYCEYCSSL-IWIMDRASVCKLCKYACHKKCCLKTTAKC 2102
Cdd:cd20864      3 HQFVVKSFTTPTKCNQCTSLmVGLIRQGCTCEVCGFSCHVTCADKAPSVC 52
C1_cPKC_rpt2 cd20836
second protein kinase C conserved region 1 (C1 domain) found in the classical (or conventional) ...
2054-2094 1.38e-04

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: 41.55  E-value: 1.38e-04
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gi 1907198218 2054 HIFKATQYSIPTYCEYCSSLIW-IMDRASVCKLCKYACHKKC 2094
Cdd:cd20836      1 HKFKVHTYSSPTFCDHCGSLLYgLIHQGMKCDTCDMNVHKRC 42
C1_Munc13 cd20807
protein kinase C conserved region 1 (C1 domain) found in the Munc13 family; The Munc13 gene ...
2054-2094 1.40e-04

protein kinase C conserved region 1 (C1 domain) found in the Munc13 family; The Munc13 gene family encodes a family of neuron-specific, synaptic molecules that bind to syntaxin, an essential mediator of neurotransmitter release. Munc13-1 is a component of presynaptic active zones in which it acts as an essential synaptic vesicle priming protein. Munc13-2 is essential for normal release probability at hippocampal mossy fiber synapses. Munc13-3 is almost exclusively expressed in the cerebellum. It acts as a tumor suppressor and plays a critical role in the formation of release sites with calcium channel nanodomains. 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: 410357  Cd Length: 53  Bit Score: 41.70  E-value: 1.40e-04
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gi 1907198218 2054 HIFKATQYSIPTYCEYCSSLIWIMDRASV-CKLCKYACHKKC 2094
Cdd:cd20807      1 HNFEVWTATTPTYCYECEGLLWGIARQGVrCTECGVKCHEKC 42
C1_Munc13-1 cd20858
protein kinase C conserved region 1 (C1 domain) found in Munc13-1 and similar proteins; ...
2050-2102 1.51e-04

protein kinase C conserved region 1 (C1 domain) found in Munc13-1 and similar proteins; Munc13-1, also called protein unc-13 homolog A (Unc13A), is a diacylglycerol (DAG) receptor that plays a role in vesicle maturation during exocytosis as a target of the diacylglycerol second messenger pathway. It is involved in neurotransmitter release by acting in synaptic vesicle priming prior to vesicle fusion and participates in the activity-dependent refilling of readily releasable vesicle pool (RRP). Loss of MUNC13-1 function causes microcephaly, cortical hyperexcitability, and fatal myasthenia. 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: 410408  Cd Length: 60  Bit Score: 42.00  E-value: 1.51e-04
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gi 1907198218 2050 EHNGHIFKATQysiPTYCEYCSSLIWIMDRASV-CKLCKYACHKKCCLKTTAKC 2102
Cdd:cd20858      7 PHNFEVWTATT---PTYCYECEGLLWGIARQGMrCTECGVKCHEKCQDLLNADC 57
C1_DGKbeta_rpt1 cd20845
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase beta (DAG ...
2048-2106 1.90e-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: 41.76  E-value: 1.90e-04
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gi 1907198218 2048 VEEHNGHIFKATQYSIPTYCEYC-SSLIWIMDRASVCKLCKYACHKKCCLKTTAKCSKKY 2106
Cdd:cd20845      2 VKDDGQHVWRLKHFNKPAYCNLClNMLVGLGKQGLCCSFCKYTVHERCVQRAPASCIKTY 61
C1_ROCK1 cd20874
protein kinase C conserved region 1 (C1 domain) found in Rho-associated coiled-coil containing ...
2051-2107 3.87e-04

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: 40.77  E-value: 3.87e-04
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gi 1907198218 2051 HNGHIFKATQYSIPTYCEYCSSLIWIMDR---ASVCKLCKYACHKKCCLKT---TAKCSKKYD 2107
Cdd:cd20874      5 HKGHEFIPTLYHFPANCEACAKPLWHVFKpppALECRRCHVKCHKDHLDKKedmITPCKVNYD 67
C1_Raf cd20811
protein kinase C conserved region 1 (C1 domain) found in the Raf (Rapidly Accelerated ...
2054-2103 5.07e-04

protein kinase C conserved region 1 (C1 domain) found in the Raf (Rapidly Accelerated Fibrosarcoma) kinase family; Raf kinases are serine/threonine kinases (STKs) that catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. They act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. Aberrant expression or activation of components in this pathway are associated with tumor initiation, progression, and metastasis. Raf proteins contain a Ras binding domain, a zinc finger cysteine-rich domain (C1), and a catalytic kinase domain. Vertebrates have three Raf isoforms (A-, B-, and C-Raf) with different expression profiles, modes of regulation, and abilities to function in the ERK cascade, depending on cellular context and stimuli. They have essential and non-overlapping roles during embryo- and organogenesis. Knockout of each isoform results in a lethal phenotype or abnormality in most mouse strains. 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: 410361  Cd Length: 49  Bit Score: 39.97  E-value: 5.07e-04
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gi 1907198218 2054 HIFKATQYSIPTYCEYCSSLIWIMDRasvCKLCKYACHKKCCLKTTAKCS 2103
Cdd:cd20811      3 HNFVRKTFFTLAFCDVCRKLLFQGFR---CQTCGFKFHQRCSDQVPALCE 49
C1_Stac cd20817
protein kinase C conserved region 1 (C1 domain) found in the SH3 and cysteine-rich ...
2054-2094 6.61e-04

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: 39.62  E-value: 6.61e-04
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gi 1907198218 2054 HIFKATQYSIPTYCEYCSSLIWIMDRASV-CKLCKYACHKKC 2094
Cdd:cd20817      1 HSFQEHTFKKPTFCDVCKELLVGLSKQGLrCKNCKMNVHHKC 42
C1_DGKeta_rpt1 cd20848
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase eta (DAG ...
2048-2102 8.31e-04

first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase eta (DAG kinase eta) and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase eta, also called diglyceride kinase eta (DGK-eta), plays a key role in promoting cell growth. It is classified as a type II DAG kinase (DGK), containing 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. The diacylglycerol kinase eta gene, DGKH, is a replicated risk gene of bipolar disorder (BPD). DAG kinase eta contains 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: 410398  Cd Length: 86  Bit Score: 40.53  E-value: 8.31e-04
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gi 1907198218 2048 VEEHNG-HIFKATQYSIPTYCEYC-SSLIWIMDRASVCKLCKYACHKKCCLKTTAKC 2102
Cdd:cd20848     23 VEHFSGmHNWYACSHARPTFCNVCrESLSGVTSHGLSCEVCKFKAHKRCAVRATNNC 79
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
1097-1123 9.13e-04

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


Pssm-ID: 467745 [Multi-domain]  Cd Length: 37  Bit Score: 38.68  E-value: 9.13e-04
                           10        20
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gi 1907198218 1097 RHKAATCIQSRWRGYRQRKKYKEQRNK 1123
Cdd:cd23767      8 MNRAATLIQALWRGYKVRKELKKKKKK 34
C1_MRCKgamma cd20866
protein kinase C conserved region 1 (C1 domain) found in myotonic dystrophy kinase-related ...
2054-2099 1.03e-03

protein kinase C conserved region 1 (C1 domain) found in myotonic dystrophy kinase-related Cdc42-binding kinase gamma (MRCK gamma) and similar proteins; MRCK gamma (MRCKG), also called Cdc42-binding protein kinase gamma, DMPK-like gamma, myotonic dystrophy protein kinase-like gamma, or myotonic dystrophy protein kinase-like alpha, is a serine/threonine-protein kinase expressed in heart and skeletal muscles. It may act as a downstream effector of Cdc42 in cytoskeletal reorganization and contributes to the actomyosin contractility required for cell invasion, through the regulation of MYPT1 and thus MLC2 phosphorylation. 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: 410416  Cd Length: 52  Bit Score: 39.35  E-value: 1.03e-03
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gi 1907198218 2054 HIFKATQYSIPTYCEYCSSLIWIMDRASV-CKLCKYACHKKCCLKTT 2099
Cdd:cd20866      1 HTFKPKTFTSPTKCLRCTSLMVGLVRQGLaCEACNYVCHVSCAEGAP 47
C1_cPKC_rpt1 cd20833
first protein kinase C conserved region 1 (C1 domain) found in the classical (or conventional) ...
2052-2094 1.47e-03

first 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 domains. 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 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: 410383  Cd Length: 58  Bit Score: 38.93  E-value: 1.47e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1907198218 2052 NGHIFKATQYSIPTYCEYCSSLIW-IMDRASVCKLCKYACHKKC 2094
Cdd:cd20833      1 KDHKFIARFFKQPTFCSHCTDFIWgFGKQGFQCQVCSFVVHKRC 44
C1_Munc13-2-like cd20859
protein kinase C conserved region 1 (C1 domain) found in Munc13-2, Munc13-3 and similar ...
2051-2106 1.68e-03

protein kinase C conserved region 1 (C1 domain) found in Munc13-2, Munc13-3 and similar proteins; Munc13-2, also called protein unc-13 homolog B (Unc13B), plays a role in vesicle maturation during exocytosis as a target of the diacylglycerol second messenger pathway. It is involved in neurotransmitter release by acting in synaptic vesicle priming prior to vesicle fusion and participates in the activity-dependent refilling of readily releasable vesicle pool (RRP). Munc13-2 is essential for normal release probability at hippocampal mossy fiber synapses. Munc13-3 is almost exclusively expressed in the cerebellum. It acts as a tumor suppressor and plays a critical role in the formation of release sites with calcium channel nanodomains. 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: 410409  Cd Length: 82  Bit Score: 39.66  E-value: 1.68e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907198218 2051 HNGHIFKATQysiPTYCEYCSSLIWIMDRASV-CKLCKYACHKKC-------CLKTTAKCSKKY 2106
Cdd:cd20859     20 HNFEVWTATT---PTYCYECEGLLWGIARQGMrCSECGVKCHEKCqdllnadCLQRAAEKSSKH 80
C1_TNS2 cd20887
protein kinase C conserved region 1 (C1 domain) found in tensin-2 and similar proteins; ...
2054-2103 2.26e-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: 2.26e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907198218 2054 HIFKATQYSIPTYCEYCSSLIwiMDRASVCKLCKYACHKKCCLKTTAKCS 2103
Cdd:cd20887      3 HSFKEKTFKKKRACAVCREPV--GGQGLVCRVCKVASHKKCEAKVTSACQ 50
C1_MRCKbeta cd20865
protein kinase C conserved region 1 (C1 domain) found in myotonic dystrophy kinase-related ...
2054-2094 2.39e-03

protein kinase C conserved region 1 (C1 domain) found in myotonic dystrophy kinase-related Cdc42-binding kinase beta (MRCK beta) and similar proteins; MRCK beta, also called Cdc42-binding protein kinase beta (Cdc42BP-beta), DMPK-like beta, or myotonic dystrophy protein kinase-like beta, is a serine/threonine-protein kinase expressed ubiquitously in many tissues. MRCK beta 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: 410415  Cd Length: 53  Bit Score: 38.04  E-value: 2.39e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1907198218 2054 HIFKATQYSIPTYCEYCSSL-IWIMDRASVCKLCKYACHKKC 2094
Cdd:cd20865      1 HQLSIKSFSSPTQCSHCTSLmVGLVRQGYACEVCSFACHVSC 42
C1_DGKdelta_rpt1 cd20847
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase delta ...
2051-2102 2.44e-03

first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase delta (DAG kinase delta) and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase delta, also called 130 kDa diacylglycerol 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. It is classified as a type II DAG kinase (DGK), containing 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. DAG kinase delta contains 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: 410397  Cd Length: 85  Bit Score: 39.31  E-value: 2.44e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907198218 2051 HNGHIFKATQYSI----------------PTYCEYC-SSLIWIMDRASVCKLCKYACHKKCCLKTTAKC 2102
Cdd:cd20847      6 QNREHFESTQYSMdhfsgmhnwyacsharPTYCNVCrEALSGVTSHGLSCEVCKFKAHKRCAVRATNNC 74
RA2_DAGK-theta cd01783
Ras-associating (RA) domain 2 found in diacylgylcerol kinase theta (DAGK-theta) and similar ...
18-110 2.68e-03

Ras-associating (RA) domain 2 found in diacylgylcerol kinase theta (DAGK-theta) and similar proteins; DAGK phosphorylates the second messenger diacylglycerol to phosphatidic acid as part of a protein kinase C pathway. DAGK-theta is characterized as a type V DAGK that has three cysteine-rich domains (all other isoforms have two), a proline/glycine-rich domain at its N-terminal, and a proposed Ras-associating (RA) domain. RA domain-containing proteins function by interacting with Ras proteins directly or indirectly and are involved in several different functions ranging from tumor suppression to being oncoproteins. Ras proteins are small GTPases that are involved in cellular signal transduction. The RA domain has a beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub). Ub is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair in eukaryotes. There are ten mammalian isoforms of DAGK have been identified to date, these are organized into five categories based on the domain architecture. DAGK-theta also contains a pleckstrin homology (PH) domain. The subcellular localization and the activity of DAGK-theta are regulated in a complex (stimulation- and cell type-dependent) manner. This family corresponds to the second RA domain of DAGK-theta.


Pssm-ID: 340481  Cd Length: 95  Bit Score: 39.13  E-value: 2.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218   18 LRIYPGTISEGTIYCPIPARKNSTAAEVIDSLINRLHLDKTKC--YVLAEVK-EFGGEEWILNPTDCPVQRMMLWPRMAL 94
Cdd:cd01783      3 IRVYPGWLKVGVAYKSIPVTKETTVEEVIKEALPKFGLQDEDPedFRLVEVLmDKGVVERVMLRDECPWLILLDIRKESL 82
                           90
                   ....*....|....*..
gi 1907198218   95 -ENRLSgedyRFLLREK 110
Cdd:cd01783     83 rQMRQT----RFYLQQK 95
C1_VAV cd20810
protein kinase C conserved region 1 (C1 domain) found in VAV proteins; VAV proteins function ...
2052-2103 2.71e-03

protein kinase C conserved region 1 (C1 domain) found in VAV proteins; VAV proteins function both as cytoplasmic guanine nucleotide exchange factors (GEFs) for Rho GTPases and as scaffold proteins, and they play important roles in cell signaling by coupling cell surface receptors to various effector functions. They play key roles in processes that require cytoskeletal reorganization including immune synapse formation, phagocytosis, cell spreading, and platelet aggregation, among others. Vertebrates have three VAV proteins (VAV1, VAV2, and VAV3). VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 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: 410360  Cd Length: 52  Bit Score: 38.01  E-value: 2.71e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907198218 2052 NGHIFKATQYSIPTYCEYCSSLIW-IMDRASVCKLCKYACHKKcCLKTTAKCS 2103
Cdd:cd20810      1 TGHSFELTTFKEPTTCSVCKKLLKgLFFQGYKCSVCGAAVHKE-CIAKVKRCG 52
C1_PKD1_rpt1 cd20839
first protein kinase C conserved region 1 (C1 domain) found in protein kinase D (PKD) and ...
2054-2103 4.04e-03

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: 38.08  E-value: 4.04e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907198218 2054 HIFKATQYSIPTYCEYCSSLIWIMDRASV-CKLCKYACHKKCCLKTTAKCS 2103
Cdd:cd20839      8 HALFVHSYRAPAFCDHCGEMLWGLVRQGLkCEGCGLNYHKRCAFKIPNNCS 58
RA2_Afadin cd01781
Ras-associating (RA) domain 2 found in Afadin; Afadin, also termed ALL1-fused gene from ...
17-91 5.40e-03

Ras-associating (RA) domain 2 found in Afadin; Afadin, also termed ALL1-fused gene from chromosome 6 protein (AF-6), or canoe, is involved in many fundamental signaling cascades in cells. In addition, it is involved in oncogenesis and metastasis. Afadin has multiple domains: from the N-terminus to the C-terminus it has two Ras-associated (RA) domains, a forkhead-associated domain, a dilute domain, a PDZ domain, three proline-rich domains, and an F-actin binding domain. RA domain-containing proteins function by interacting with Ras proteins directly or indirectly and are involved in several different functions ranging from tumor suppression to being oncoproteins. Ras proteins are small GTPases that are involved in cellular signal transduction. The RA domain has a beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub). Ub is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair in eukaryotes. Afadin is abundant at cadherin-based adherens junctions in epithelial cells, endothelial cells, and fibroblasts. This family corresponds to the second RA domain of afadin.


Pssm-ID: 340479  Cd Length: 102  Bit Score: 38.80  E-value: 5.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907198218   17 TLRIYPGTISEGTIYCPIPARKNSTAAEVIDSLINRLHLDKT--KCYVLAEV----------KEFGGEEWILNPTDCPVQ 84
Cdd:cd01781      3 TLKIYGDSLKPEVPYKTLLLSTNDTADFVVREALEKYGLEKEnpKDYCLVQVvlppggsprlDGGGGKERILDDDECPLA 82

                   ....*..
gi 1907198218   85 RMMLWPR 91
Cdd:cd01781     83 ILMRWPP 89
 
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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