|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
116-784 |
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: 1329.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 116 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRDNQSILITG 195
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 196 ESGAGKTVNTKRVIQYFAVIAAIGDRKKDSGpTGKGTLEDQIIQANPALEAFGNAKTLRNDNSSRFGKFIRIHFGATGKL 275
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKESG-KKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 276 ASADIETYLLEKSRVIFQLKSERDYHIFYQILSNKKPELLDMLLVTNNPYDYAYISQGETTVASIDDAEELLATDSAFDV 355
Cdd:cd01377 160 AGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAFDI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 356 LGFTQDEKNSIYKLTGAVMHFGNMKFKQKQREEQAEPDGTEEADKVAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQ 435
Cdd:cd01377 240 LGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 436 QVYYSTGALGKSVYEKMFLWMVVRINTTLETKQPRQYFIGVLDIAGFEIFDFNSFEQMCINFTNEKLQQFFNHHMFVLEQ 515
Cdd:cd01377 320 QVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 516 EEYKKEGIEWEFIDFGMDLQACIDLIEKP-MGIMSILEEECMFPKATDVTFKAKLYDNHLGKSNNFQKPRnlKGRPEAHF 594
Cdd:cd01377 400 EEYKKEGIEWTFIDFGLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKPK--PKKSEAHF 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 595 ALVHYAGTVDYNINGWLVKNKDPLNETVVGLYQKSALKLLAHLFANYASAESDQAtkgkGSKKKGSSFQTVSALHRENLN 674
Cdd:cd01377 478 ILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEESGGGGG----KKKKKGGSFRTVSQLHKEQLN 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 675 KLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRKGYPNRILYGDFRQRYRILNPAAIPEGQFi 754
Cdd:cd01377 554 KLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIPKGFD- 632
|
650 660 670
....*....|....*....|....*....|
gi 1072253241 755 DSRKGAEKLLASLEMDHTQYKFGHTKVFFK 784
Cdd:cd01377 633 DGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
116-784 |
0e+00 |
|
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: 1275.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 116 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRDNQSILITG 195
Cdd:cd14913 1 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 196 ESGAGKTVNTKRVIQYFAVIAAIGDRKKDSGPTGKGTLEDQIIQANPALEAFGNAKTLRNDNSSRFGKFIRIHFGATGKL 275
Cdd:cd14913 81 ESGAGKTVNTKRVIQYFATIAATGDLAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 276 ASADIETYLLEKSRVIFQLKSERDYHIFYQILSNKKPELLDMLLVTNNPYDYAYISQGETTVASIDDAEELLATDSAFDV 355
Cdd:cd14913 161 ASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSAIDI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 356 LGFTQDEKNSIYKLTGAVMHFGNMKFKQKQREEQAEPDGTEEADKVAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQ 435
Cdd:cd14913 241 LGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 436 QVYYSTGALGKSVYEKMFLWMVVRINTTLETKQPRQYFIGVLDIAGFEIFDFNSFEQMCINFTNEKLQQFFNHHMFVLEQ 515
Cdd:cd14913 321 QVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 516 EEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDVTFKAKLYDNHLGKSNNFQKPRNLKGRPEAHFA 595
Cdd:cd14913 401 EEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGRAEAHFS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 596 LVHYAGTVDYNINGWLVKNKDPLNETVVGLYQKSALKLLAHLFANYASAESDqATKGKGSKKKGSSFQTVSALHRENLNK 675
Cdd:cd14913 481 LIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATADAD-SGKKKVAKKKGSSFQTVSALFRENLNK 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 676 LMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRKGYPNRILYGDFRQRYRILNPAAIPEGQFID 755
Cdd:cd14913 560 LMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQFID 639
|
650 660
....*....|....*....|....*....
gi 1072253241 756 SRKGAEKLLASLEMDHTQYKFGHTKVFFK 784
Cdd:cd14913 640 SKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
116-784 |
0e+00 |
|
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: 1247.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 116 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRDNQSILITG 195
Cdd:cd14917 1 PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 196 ESGAGKTVNTKRVIQYFAVIAAIGDRKKDSGPTGKGTLEDQIIQANPALEAFGNAKTLRNDNSSRFGKFIRIHFGATGKL 275
Cdd:cd14917 81 ESGAGKTVNTKRVIQYFAVIAAIGDRSKKDQTPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 276 ASADIETYLLEKSRVIFQLKSERDYHIFYQILSNKKPELLDMLLVTNNPYDYAYISQGETTVASIDDAEELLATDSAFDV 355
Cdd:cd14917 161 ASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 356 LGFTQDEKNSIYKLTGAVMHFGNMKFKQKQREEQAEPDGTEEADKVAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQ 435
Cdd:cd14917 241 LGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 436 QVYYSTGALGKSVYEKMFLWMVVRINTTLETKQPRQYFIGVLDIAGFEIFDFNSFEQMCINFTNEKLQQFFNHHMFVLEQ 515
Cdd:cd14917 321 QVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 516 EEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDVTFKAKLYDNHLGKSNNFQKPRNLKGRPEAHFA 595
Cdd:cd14917 401 EEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPRNIKGKPEAHFS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 596 LVHYAGTVDYNINGWLVKNKDPLNETVVGLYQKSALKLLAHLFANYASAESdQATKGKGSKKKGSSFQTVSALHRENLNK 675
Cdd:cd14917 481 LIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANYAGADA-PIEKGKGKAKKGSSFQTVSALHRENLNK 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 676 LMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRKGYPNRILYGDFRQRYRILNPAAIPEGQFID 755
Cdd:cd14917 560 LMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFID 639
|
650 660
....*....|....*....|....*....
gi 1072253241 756 SRKGAEKLLASLEMDHTQYKFGHTKVFFK 784
Cdd:cd14917 640 SRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
116-784 |
0e+00 |
|
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: 1218.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 116 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRDNQSILITG 195
Cdd:cd14916 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 196 ESGAGKTVNTKRVIQYFAVIAAIGDR-KKDSGPTGKGTLEDQIIQANPALEAFGNAKTLRNDNSSRFGKFIRIHFGATGK 274
Cdd:cd14916 81 ESGAGKTVNTKRVIQYFASIAAIGDRsKKENPNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 275 LASADIETYLLEKSRVIFQLKSERDYHIFYQILSNKKPELLDMLLVTNNPYDYAYISQGETTVASIDDAEELLATDSAFD 354
Cdd:cd14916 161 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSAFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 355 VLGFTQDEKNSIYKLTGAVMHFGNMKFKQKQREEQAEPDGTEEADKVAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNV 434
Cdd:cd14916 241 VLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 435 QQVYYSTGALGKSVYEKMFLWMVVRINTTLETKQPRQYFIGVLDIAGFEIFDFNSFEQMCINFTNEKLQQFFNHHMFVLE 514
Cdd:cd14916 321 QQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 515 QEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDVTFKAKLYDNHLGKSNNFQKPRNLKGRPEAHF 594
Cdd:cd14916 401 QEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRNVKGKQEAHF 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 595 ALVHYAGTVDYNINGWLVKNKDPLNETVVGLYQKSALKLLAHLFANYASAESDQATKGKGSKKKGSSFQTVSALHRENLN 674
Cdd:cd14916 481 SLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTGDSGKGKGGKKKGSSFQTVSALHRENLN 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 675 KLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRKGYPNRILYGDFRQRYRILNPAAIPEGQFI 754
Cdd:cd14916 561 KLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFI 640
|
650 660 670
....*....|....*....|....*....|
gi 1072253241 755 DSRKGAEKLLASLEMDHTQYKFGHTKVFFK 784
Cdd:cd14916 641 DSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
117-784 |
0e+00 |
|
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: 1196.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 117 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRDNQSILITGE 196
Cdd:cd14927 2 SVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 197 SGAGKTVNTKRVIQYFAVIAAIGD--RKKDSGPTGK--GTLEDQIIQANPALEAFGNAKTLRNDNSSRFGKFIRIHFGAT 272
Cdd:cd14927 82 SGAGKTVNTKRVIQYFAIVAALGDgpGKKAQFLATKtgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 273 GKLASADIETYLLEKSRVIFQLKSERDYHIFYQILSNKKPELLDMLLVTNNPYDYAYISQGETTVASIDDAEELLATDSA 352
Cdd:cd14927 162 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSMNPYDYHFCSQGVTTVDNMDDGEELMATDHA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 353 FDVLGFTQDEKNSIYKLTGAVMHFGNMKFKQKQREEQAEPDGTEEADKVAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 432
Cdd:cd14927 242 MDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTKGQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 433 NVQQVYYSTGALGKSVYEKMFLWMVVRINTTLETKQPRQYFIGVLDIAGFEIFDFNSFEQMCINFTNEKLQQFFNHHMFV 512
Cdd:cd14927 322 SVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFI 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 513 LEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDVTFKAKLYDNHLGKSNNFQKPRNLKGRP-E 591
Cdd:cd14927 402 LEQEEYKREGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPDKKRKyE 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 592 AHFALVHYAGTVDYNINGWLVKNKDPLNETVVGLYQKSALKLLAHLFANYASAES--DQATKGKGSKKKGSSFQTVSALH 669
Cdd:cd14927 482 AHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENYVGSDSteDPKSGVKEKRKKAASFQTVSQLH 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 670 RENLNKLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRKGYPNRILYGDFRQRYRILNPAAIP 749
Cdd:cd14927 562 KENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPSAIP 641
|
650 660 670
....*....|....*....|....*....|....*
gi 1072253241 750 EGQFIDSRKGAEKLLASLEMDHTQYKFGHTKVFFK 784
Cdd:cd14927 642 DDKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
116-784 |
0e+00 |
|
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: 1148.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 116 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRDNQSILITG 195
Cdd:cd14923 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 196 ESGAGKTVNTKRVIQYFAVIAAIGDRKKDSGPTG-KGTLEDQIIQANPALEAFGNAKTLRNDNSSRFGKFIRIHFGATGK 274
Cdd:cd14923 81 ESGAGKTVNTKRVIQYFATIAVTGDKKKEQQPGKmQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 275 LASADIETYLLEKSRVIFQLKSERDYHIFYQILSNKKPELLDMLLVTNNPYDYAYISQGETTVASIDDAEELLATDSAFD 354
Cdd:cd14923 161 LASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNAID 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 355 VLGFTQDEKNSIYKLTGAVMHFGNMKFKQKQREEQAEPDGTEEADKVAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNV 434
Cdd:cd14923 241 ILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQNV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 435 QQVYYSTGALGKSVYEKMFLWMVVRINTTLETKQPRQYFIGVLDIAGFEIFDFNSFEQMCINFTNEKLQQFFNHHMFVLE 514
Cdd:cd14923 321 QQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 515 QEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDVTFKAKLYDNHLGKSNNFQKPRNLKGRPEAHF 594
Cdd:cd14923 401 QEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPAKGKAEAHF 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 595 ALVHYAGTVDYNINGWLVKNKDPLNETVVGLYQKSALKLLAHLFANYASAES-DQATKGKGSKKKGSSFQTVSALHRENL 673
Cdd:cd14923 481 SLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAgDSGGSKKGGKKKGSSFQTVSAVFRENL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 674 NKLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRKGYPNRILYGDFRQRYRILNPAAIPEGQF 753
Cdd:cd14923 561 NKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPEGQF 640
|
650 660 670
....*....|....*....|....*....|.
gi 1072253241 754 IDSRKGAEKLLASLEMDHTQYKFGHTKVFFK 784
Cdd:cd14923 641 IDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
116-784 |
0e+00 |
|
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: 1141.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 116 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRDNQSILITG 195
Cdd:cd14910 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 196 ESGAGKTVNTKRVIQYFAVIAAIGDRKKDSGPTGK--GTLEDQIIQANPALEAFGNAKTLRNDNSSRFGKFIRIHFGATG 273
Cdd:cd14910 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEATSGKmqGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 274 KLASADIETYLLEKSRVIFQLKSERDYHIFYQILSNKKPELLDMLLVTNNPYDYAYISQGETTVASIDDAEELLATDSAF 353
Cdd:cd14910 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 354 DVLGFTQDEKNSIYKLTGAVMHFGNMKFKQKQREEQAEPDGTEEADKVAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQN 433
Cdd:cd14910 241 EILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 434 VQQVYYSTGALGKSVYEKMFLWMVVRINTTLETKQPRQYFIGVLDIAGFEIFDFNSFEQMCINFTNEKLQQFFNHHMFVL 513
Cdd:cd14910 321 VQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 514 EQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDVTFKAKLYDNHLGKSNNFQKPRNLKGRPEAH 593
Cdd:cd14910 401 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKVEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 594 FALVHYAGTVDYNINGWLVKNKDPLNETVVGLYQKSALKLLAHLFANYASAESDQATKGKGSKKKGSSFQTVSALHRENL 673
Cdd:cd14910 481 FSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAAAEAEEGGGKKGGKKKGSSFQTVSALFRENL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 674 NKLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRKGYPNRILYGDFRQRYRILNPAAIPEGQF 753
Cdd:cd14910 561 NKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQF 640
|
650 660 670
....*....|....*....|....*....|.
gi 1072253241 754 IDSRKGAEKLLASLEMDHTQYKFGHTKVFFK 784
Cdd:cd14910 641 IDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
116-784 |
0e+00 |
|
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: 1140.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 116 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRDNQSILITG 195
Cdd:cd14918 1 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 196 ESGAGKTVNTKRVIQYFAVIAAIGDRKKDSGPTGKGTLEDQIIQANPALEAFGNAKTLRNDNSSRFGKFIRIHFGATGKL 275
Cdd:cd14918 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 276 ASADIETYLLEKSRVIFQLKSERDYHIFYQILSNKKPELLDMLLVTNNPYDYAYISQGETTVASIDDAEELLATDSAFDV 355
Cdd:cd14918 161 ASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 356 LGFTQDEKNSIYKLTGAVMHFGNMKFKQKQREEQAEPDGTEEADKVAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQ 435
Cdd:cd14918 241 LGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 436 QVYYSTGALGKSVYEKMFLWMVVRINTTLETKQPRQYFIGVLDIAGFEIFDFNSFEQMCINFTNEKLQQFFNHHMFVLEQ 515
Cdd:cd14918 321 QVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 516 EEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDVTFKAKLYDNHLGKSNNFQKPRNLKGRPEAHFA 595
Cdd:cd14918 401 EEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAHFS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 596 LVHYAGTVDYNINGWLVKNKDPLNETVVGLYQKSALKLLAHLFANYASAESDqATKGKGSKKKGSSFQTVSALHRENLNK 675
Cdd:cd14918 481 LIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEAD-SGAKKGAKKKGSSFQTVSALFRENLNK 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 676 LMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRKGYPNRILYGDFRQRYRILNPAAIPEGQFID 755
Cdd:cd14918 560 LMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQFID 639
|
650 660
....*....|....*....|....*....
gi 1072253241 756 SRKGAEKLLASLEMDHTQYKFGHTKVFFK 784
Cdd:cd14918 640 SKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
116-784 |
0e+00 |
|
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: 1138.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 116 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRDNQSILITG 195
Cdd:cd14915 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 196 ESGAGKTVNTKRVIQYFAVIAAIGDRKKDSGPTGK--GTLEDQIIQANPALEAFGNAKTLRNDNSSRFGKFIRIHFGATG 273
Cdd:cd14915 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEAASGKmqGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 274 KLASADIETYLLEKSRVIFQLKSERDYHIFYQILSNKKPELLDMLLVTNNPYDYAYISQGETTVASIDDAEELLATDSAF 353
Cdd:cd14915 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDFAFVSQGEITVPSIDDQEELMATDSAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 354 DVLGFTQDEKNSIYKLTGAVMHFGNMKFKQKQREEQAEPDGTEEADKVAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQN 433
Cdd:cd14915 241 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 434 VQQVYYSTGALGKSVYEKMFLWMVVRINTTLETKQPRQYFIGVLDIAGFEIFDFNSFEQMCINFTNEKLQQFFNHHMFVL 513
Cdd:cd14915 321 VQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 514 EQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDVTFKAKLYDNHLGKSNNFQKPRNLKGRPEAH 593
Cdd:cd14915 401 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKAEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 594 FALVHYAGTVDYNINGWLVKNKDPLNETVVGLYQKSALKLLAHLFANYASAESDQATKGKGSKKKGSSFQTVSALHRENL 673
Cdd:cd14915 481 FSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQTAEAEGGGGKKGGKKKGSSFQTVSALFRENL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 674 NKLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRKGYPNRILYGDFRQRYRILNPAAIPEGQF 753
Cdd:cd14915 561 NKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQF 640
|
650 660 670
....*....|....*....|....*....|.
gi 1072253241 754 IDSRKGAEKLLASLEMDHTQYKFGHTKVFFK 784
Cdd:cd14915 641 IDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
116-784 |
0e+00 |
|
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: 1118.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 116 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRDNQSILITG 195
Cdd:cd14912 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 196 ESGAGKTVNTKRVIQYFAVIAAIGDRKKDSGPTGK--GTLEDQIIQANPALEAFGNAKTLRNDNSSRFGKFIRIHFGATG 273
Cdd:cd14912 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEITSGKmqGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 274 KLASADIETYLLEKSRVIFQLKSERDYHIFYQILSNKKPELLDMLLVTNNPYDYAYISQGETTVASIDDAEELLATDSAF 353
Cdd:cd14912 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 354 DVLGFTQDEKNSIYKLTGAVMHFGNMKFKQKQREEQAEPDGTEEADKVAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQN 433
Cdd:cd14912 241 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 434 VQQVYYSTGALGKSVYEKMFLWMVVRINTTLETKQPRQYFIGVLDIAGFEIFDFNSFEQMCINFTNEKLQQFFNHHMFVL 513
Cdd:cd14912 321 VEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 514 EQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDVTFKAKLYDNHLGKSNNFQKPRNLKGRPEAH 593
Cdd:cd14912 401 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVVKGKAEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 594 FALVHYAGTVDYNINGWLVKNKDPLNETVVGLYQKSALKLLAHLFANYASAESDQA--TKGKGSKKKGSSFQTVSALHRE 671
Cdd:cd14912 481 FSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEGASAggGAKKGGKKKGSSFQTVSALFRE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 672 NLNKLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRKGYPNRILYGDFRQRYRILNPAAIPEG 751
Cdd:cd14912 561 NLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEG 640
|
650 660 670
....*....|....*....|....*....|...
gi 1072253241 752 QFIDSRKGAEKLLASLEMDHTQYKFGHTKVFFK 784
Cdd:cd14912 641 QFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
104-784 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1064.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 104 IEDMAMLTFLNEPAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYML 183
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 184 TDRDNQSILITGESGAGKTVNTKRVIQYFAVIAAIGDRKKdsgptgKGTLEDQIIQANPALEAFGNAKTLRNDNSSRFGK 263
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGN------VGRLEEQILQSNPILEAFGNAKTVRNNNSSRFGK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 264 FIRIHFGATGKLASADIETYLLEKSRVIFQLKSERDYHIFYQILSNKKPELLDMLLVTnNPYDYAYISQ-GETTVASIDD 342
Cdd:pfam00063 155 YIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLT-NPKDYHYLSQsGCYTIDGIDD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 343 AEELLATDSAFDVLGFTQDEKNSIYKLTGAVMHFGNMKFKQKQREEQAEPDGTEEADKVAYLMGLNSADLLKGLCHPRVK 422
Cdd:pfam00063 234 SEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 423 VGNEYVTKGQNVQQVYYSTGALGKSVYEKMFLWMVVRINTTLETKQ-PRQYFIGVLDIAGFEIFDFNSFEQMCINFTNEK 501
Cdd:pfam00063 314 TGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTiEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 502 LQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLQACIDLIE-KPMGIMSILEEECMFPKATDVTFKAKLYDNHlGKSNNF 580
Cdd:pfam00063 394 LQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEkKPLGILSLLDEECLFPKATDQTFLDKLYSTF-SKHPHF 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 581 QKPRNLKgrpEAHFALVHYAGTVDYNINGWLVKNKDPLNETVVGLYQKSALKLLAHLFANYASAESDQATKGKGSK---K 657
Cdd:pfam00063 472 QKPRLQG---ETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGKSTpkrT 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 658 KGSSFQTVSALHRENLNKLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRKGYPNRILYGDFR 737
Cdd:pfam00063 549 KKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFV 628
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1072253241 738 QRYRILNPAAIPEGqFIDSRKGAEKLLASLEMDHTQYKFGHTKVFFK 784
Cdd:pfam00063 629 QRYRILAPKTWPKW-KGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
116-784 |
0e+00 |
|
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: 1056.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 116 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRDNQSILITG 195
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 196 ESGAGKTVNTKRVIQYFAVIAAIGDRKKDsgptgKGTLEDQIIQANPALEAFGNAKTLRNDNSSRFGKFIRIHFGATGKL 275
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKK-----LGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGML 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 276 ASADIETYLLEKSRVIFQLKSERDYHIFYQILSNKKpELLDMLLVTNNPYDYAYISQGETTVASIDDAEELLATDSAFDV 355
Cdd:cd14929 156 SSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKK-ELRDLLLVSANPSDFHFCSCGAVAVESLDDAEELLATEQAMDI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 356 LGFTQDEKNSIYKLTGAVMHFGNMKFKQKQREEQAEPDGTEEADKVAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQ 435
Cdd:cd14929 235 LGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 436 QVYYSTGALGKSVYEKMFLWMVVRINTTLETKQPRQYFIGVLDIAGFEIFDFNSFEQMCINFTNEKLQQFFNHHMFVLEQ 515
Cdd:cd14929 315 QVTYAVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLEQ 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 516 EEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDVTFKAKLYDNHLGKSNNFQKPRNLKGRPEAHFA 595
Cdd:cd14929 395 EEYRKEGIDWVSIDFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKPDKKKFEAHFE 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 596 LVHYAGTVDYNINGWLVKNKDPLNETVVGLYQKSALKLLAHLFANYASAESdQATKGKGSKKKGSSFQTVSALHRENLNK 675
Cdd:cd14929 475 LVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYISTDS-AIQFGEKKRKKGASFQTVASLHKENLNK 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 676 LMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRKGYPNRILYGDFRQRYRILNPAAIPEGQFID 755
Cdd:cd14929 554 LMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTFPKSKFVS 633
|
650 660
....*....|....*....|....*....
gi 1072253241 756 SRKGAEKLLASLEMDHTQYKFGHTKVFFK 784
Cdd:cd14929 634 SRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
117-784 |
0e+00 |
|
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: 1014.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 117 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRDNQSILITGE 196
Cdd:cd14934 2 SVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 197 SGAGKTVNTKRVIQYFAVIAAIGDRKKDsgptGKGTLEDQIIQANPALEAFGNAKTLRNDNSSRFGKFIRIHFGATGKLA 276
Cdd:cd14934 82 SGAGKTENTKKVIQYFANIGGTGKQSSD----GKGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 277 SADIETYLLEKSRVIFQLKSERDYHIFYQILSNKKPELLDMLLVTNNPYDYAYISQGETTVASIDDAEELLATDSAFDVL 356
Cdd:cd14934 158 GADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQITDVAFDVL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 357 GFTQDEKNSIYKLTGAVMHFGNMKFKQKQREEQAEPDGTEEADKVAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQ 436
Cdd:cd14934 238 GFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNMEQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 437 VYYSTGALGKSVYEKMFLWMVVRINTTLETKQPRQYFIGVLDIAGFEIFDFNSFEQMCINFTNEKLQQFFNHHMFVLEQE 516
Cdd:cd14934 318 CNNSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 517 EYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDVTFKAKLYDNHLGKSNNFQKPRNLKGR-PEAHFA 595
Cdd:cd14934 398 EYKREGIEWVFIDFGLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKPKGGKGKgPEAHFE 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 596 LVHYAGTVDYNINGWLVKNKDPLNETVVGLYQKSALKLLAHLFanyasaESDQATKGKGSKKKGSSFQTVSALHRENLNK 675
Cdd:cd14934 478 LVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLF------KEEEAPAGSKKQKRGSSFMTVSNFYREQLNK 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 676 LMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRKGYPNRILYGDFRQRYRILNPAAIPEGqFID 755
Cdd:cd14934 552 LMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVIPQG-FVD 630
|
650 660
....*....|....*....|....*....
gi 1072253241 756 SRKGAEKLLASLEMDHTQYKFGHTKVFFK 784
Cdd:cd14934 631 NKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
116-784 |
0e+00 |
|
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: 1010.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 116 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRDNQSILITG 195
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 196 ESGAGKTVNTKRVIQYFAVIAAigDRKKDSGPTGKGTLEDQIIQANPALEAFGNAKTLRNDNSSRFGKFIRIHFGATGKL 275
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGA--SKKTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 276 ASADIETYLLEKSRVIFQLKSERDYHIFYQILSNKKPELLDMLLVTNNPYDYAYISQGETTVASIDDAEELLATDSAFDV 355
Cdd:cd14909 159 AGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLSDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQAFDI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 356 LGFTQDEKNSIYKLTGAVMHFGNMKFKQKQREEQAEPDGTEEADKVAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQ 435
Cdd:cd14909 239 LGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 436 QVYYSTGALGKSVYEKMFLWMVVRINTTLETKQPRQYFIGVLDIAGFEIFDFNSFEQMCINFTNEKLQQFFNHHMFVLEQ 515
Cdd:cd14909 319 QVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 516 EEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDVTFKAKLYDNHLGKSNNFQKPRNLK-GRPEAHF 594
Cdd:cd14909 399 EEYKREGIDWAFIDFGMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKpGQQAAHF 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 595 ALVHYAGTVDYNINGWLVKNKDPLNETVVGLYQKSALKLLAHLFANYASAESDQATKGKGSKKKGSSFQTVSALHRENLN 674
Cdd:cd14909 479 AIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGEQAKGGRGKKGGGFATVSSAYKEQLN 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 675 KLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRKGYPNRILYGDFRQRYRILNPAAIPEGQfi 754
Cdd:cd14909 559 SLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGIQGEE-- 636
|
650 660 670
....*....|....*....|....*....|
gi 1072253241 755 DSRKGAEKLLASLEMDHTQYKFGHTKVFFK 784
Cdd:cd14909 637 DPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
97-796 |
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: 1008.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 97 NPPKFDKIEDMAMLTFLNEPAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISD 176
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 177 NAYQYMLTDRDNQSILITGESGAGKTVNTKRVIQYFAVIAaigdrkkdSGPTGKGTLEDQIIQANPALEAFGNAKTLRND 256
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVS--------GSNTEVGSVEDQILESNPILEAFGNAKTLRNN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 257 NSSRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKSERDYHIFYQILSNKKPELLDMLLVTNnPYDYAYISQGET- 335
Cdd:smart00242 153 NSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKS-PEDYRYLNQGGCl 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 336 TVASIDDAEELLATDSAFDVLGFTQDEKNSIYKLTGAVMHFGNMKFKQKQREEQA-EPDGTEEADKVAYLMGLNSADLLK 414
Cdd:smart00242 232 TVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAAsTVKDKEELSNAAELLGVDPEELEK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 415 GLCHPRVKVGNEYVTKGQNVQQVYYSTGALGKSVYEKMFLWMVVRINTTLETKQPRQYFIGVLDIAGFEIFDFNSFEQMC 494
Cdd:smart00242 312 ALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSFEQLC 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 495 INFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLQACIDLIE-KPMGIMSILEEECMFPKATDVTFKAKLYdNH 573
Cdd:smart00242 392 INYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEkKPPGILSLLDEECRFPKGTDQTFLEKLN-QH 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 574 LGKSNNFQKPRNlkgRPEAHFALVHYAGTVDYNINGWLVKNKDPLNETVVGLYQKSALKLLAHLFANYASAESDQATkgk 653
Cdd:smart00242 470 HKKHPHFSKPKK---KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVSNAGSKKR--- 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 654 gskkkgssFQTVSALHRENLNKLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRKGYPNRILY 733
Cdd:smart00242 544 --------FQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPF 615
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1072253241 734 GDFRQRYRILNPAAIPEGQFiDSRKGAEKLLASLEMDHTQYKFGHTKVFFKAGLLGQLEEMRD 796
Cdd:smart00242 616 DEFLQRYRVLLPDTWPPWGG-DAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
116-784 |
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: 835.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 116 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKR-SEAPPHIFSISDNAYQYMLTDRDNQSILIT 194
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRsADLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 195 GESGAGKTVNTKRVIQYFAVIAAIGDRKKDSGptgKGTLEDQIIQANPALEAFGNAKTLRNDNSSRFGKFIRIHFGATGK 274
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSKSSSS---ASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 275 LASADIETYLLEKSRVIFQLKSERDYHIFYQILSNKKPELLDML----LVTNNPYDYAYISQGETTVASIDDAEELLATD 350
Cdd:cd00124 158 LVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELklelLLSYYYLNDYLNSSGCDRIDGVDDAEEFQELL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 351 SAFDVLGFTQDEKNSIYKLTGAVMHFGNMKFKQKQREE--QAEPDGTEEADKVAYLMGLNSADLLKGLCHPRVKVGNEYV 428
Cdd:cd00124 238 DALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEdsSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 429 TKGQNVQQVYYSTGALGKSVYEKMFLWMVVRINTTL--ETKQPRQYFIGVLDIAGFEIFDFNSFEQMCINFTNEKLQQFF 506
Cdd:cd00124 318 TKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALspTDAAESTSFIGILDIFGFENFEVNSFEQLCINYANEKLQQFF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 507 NHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKATDVTFKAKLYDNHLGKSNNFQKPRn 585
Cdd:cd00124 398 NQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEgKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKR- 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 586 lkgRPEAHFALVHYAGTVDYNINGWLVKNKDPLNETVVGLYQKsalkllahlfanyasaesdqatkgkgskkkgssfqtv 665
Cdd:cd00124 476 ---KAKLEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRS------------------------------------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 666 SALHRENLNKLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRKGYPNRILYGDFRQRYRILNP 745
Cdd:cd00124 516 GSQFRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAP 595
|
650 660 670
....*....|....*....|....*....|....*....
gi 1072253241 746 AAiPEGQFIDSRKGAEKLLASLEMDHTQYKFGHTKVFFK 784
Cdd:cd00124 596 GA-TEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
46-1539 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 833.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 46 RPFDMKKDIFVPDDTEEYVKAKVTSregdnvTAETEHGKKVNVKDSLLMQ--QNPPKFDKIEDMAMLTFLNEPAVLYNLK 123
Cdd:COG5022 14 IPDEEKGWIWAEIIKEAFNKGKVTE------EGKKEDGESVSVKKKVLGNdrIKLPKFDGVDDLTELSYLNEPAVLHNLE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 124 ERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRDNQSILITGESGAGKTV 203
Cdd:COG5022 88 KRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 204 NTKRVIQYFAVIAAigdrkkdSGPTGKGTLEDQIIQANPALEAFGNAKTLRNDNSSRFGKFIRIHFGATGKLASADIETY 283
Cdd:COG5022 168 NAKRIMQYLASVTS-------SSTVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 284 LLEKSRVIFQLKSERDYHIFYQILSNKKPELLDMLLVTNnPYDYAYISQGE-TTVASIDDAEELLATDSAFDVLGFTQDE 362
Cdd:COG5022 241 LLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQN-PKDYIYLSQGGcDKIDGIDDAKEFKITLDALKTIGIDEEE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 363 KNSIYKLTGAVMHFGNMKFKqKQREEQAEPDGTEEADKVAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQVYYSTG 442
Cdd:COG5022 320 QDQIFKILAAILHIGNIEFK-EDRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 443 ALGKSVYEKMFLWMVVRINTTLETKQPRQYFIGVLDIAGFEIFDFNSFEQMCINFTNEKLQQFFNHHMFVLEQEEYKKEG 522
Cdd:COG5022 399 SLAKALYSNLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 523 IEWEFIDFgMDLQACIDLIEK--PMGIMSILEEECMFPKATDVTFKAKLYDNHLGKSNNFQKPRNLKGRpeaHFALVHYA 600
Cdd:COG5022 479 IEWSFIDY-FDNQPCIDLIEKknPLGILSLLDEECVMPHATDESFTSKLAQRLNKNSNPKFKKSRFRDN---KFVVKHYA 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 601 GTVDYNINGWLVKNKDPLNETVVGLYQKSALKLLAHLFANYASAESDQatkgkgskkkgsSFQTVSALHRENLNKLMTNL 680
Cdd:COG5022 555 GDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENIESKG------------RFPTLGSRFKESLNSLMSTL 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 681 RATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRKGYPNRILYGDFRQRYRILNPAAIPEGQFI---DSR 757
Cdd:COG5022 623 NSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKSWTGEYTwkeDTK 702
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 758 KGAEKLLASLEMDHTQYKFGHTKVFFKAGLLGQLEEMRDERLSRIITRIQAQSRGALSRIEFKKIVERRDALLVIQWNIR 837
Cdd:COG5022 703 NAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFR 782
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 838 AFMGVKNWPWMKLYFKIKPLLKSAETEKEMQTMKEEFQKLKEALEKSEARRKDLEEKMvsLLQEKNDLQLQVQAEQD-NL 916
Cdd:COG5022 783 LRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIKREKKLRETEEVEF--SLKAEVLIQKFGRSLKAkKR 860
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 917 ADADERCEQLIKNKIQLEAKLKEQTERLEDEEEMNaELTAKKRKLEDECSELKKDID-----DLELTLAKVEKEKHATEN 991
Cdd:COG5022 861 FSLLKKETIYLQSAQRVELAERQLQELKIDVKSIS-SLKLVNLELESEIIELKKSLSsdlieNLEFKTELIARLKKLLNN 939
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 992 -KVKNLTEEMAGLDEIIVKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKIRMDLERVK 1070
Cdd:COG5022 940 iDLEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLK 1019
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1071 RKlegDVKLSQeslmdlendKQQLEEKLKKKDFEVSQLNtrieDEQNVCIQLQKKMKELQARIEELEEeleaertarAKV 1150
Cdd:COG5022 1020 EL---PVEVAE---------LQSASKIISSESTELSILK----PLQKLKGLLLLENNQLQARYKALKL---------RRE 1074
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1151 EKLRCDLSRELEEISERLEEAGGATSVQMelnKKREAEFLKlrrdlEESTLHSEATAASLRKKHADSVaeLSEQIDNLQR 1230
Cdd:COG5022 1075 NSLLDDKQLYQLESTENLLKTINVKDLEV---TNRNLVKPA-----NVLQFIVAQMIKLNLLQEISKF--LSQLVNTLEP 1144
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1231 VKQKLEkeksefKLELDDVTSNMEQMVKAKANLEKLCRSLED---QANEHRTKSEENQRTVNELSS-LRAKLQTENGELS 1306
Cdd:COG5022 1145 VFQKLS------VLQLELDGLFWEANLEALPSPPPFAALSEKrlyQSALYDEKSKLSSSEVNDLKNeLIALFSKIFSGWP 1218
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1307 RRLDEKESLVSQMTrGKQTYTQHLEDLKRQLEEETKAKNALAHALQSARHDSDLLREQFEEEQEAKAELQRILSKANSEV 1386
Cdd:COG5022 1219 RGDKLKKLISEGWV-PTEYSTSLKGFNNLNKKFDTPASMSNEKLLSLLNSIDNLLSSYKLEEEVLPATINSLLQYINVGL 1297
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1387 AQ--------WRTKYETDAIQRTEELEEAKKK-----LAQRLQEAEEAVEAVNAKCSSLEKTKHRLQ-------NEIEDL 1446
Cdd:COG5022 1298 FNalrtkassLRWKSATEVNYNSEELDDWCREfeisdVDEELEELIQAVKVLQLLKDDLNKLDELLDacyslnpAEIQNL 1377
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1447 MVDLERsnaaaaaLDKKQRNFDKILAEWKQKFEESQTELESSQK-EARSLSTELFKLKNAyEESLDHLETFKRENKNLQE 1525
Cdd:COG5022 1378 KSRYDP-------ADKENNLPKEILKKIEALLIKQELQLSLEGKdETEVHLSEIFSEEKS-LISLDRNSIYKEEVLSSLS 1449
|
1530
....*....|....
gi 1072253241 1526 EISDLTEQLGESGK 1539
Cdd:COG5022 1450 ALLTKEKIALLDRK 1463
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
117-784 |
0e+00 |
|
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: 797.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 117 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRDNQSILITGE 196
Cdd:cd14911 2 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 197 SGAGKTVNTKRVIQYFAVIAAIGDRKKDSGPTGK-------GTLEDQIIQANPALEAFGNAKTLRNDNSSRFGKFIRIHF 269
Cdd:cd14911 82 SGAGKTENTKKVIQFLAYVAASKPKGSGAVPHPAvnpavliGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 270 GATGKLASADIETYLLEKSRVIFQLKSERDYHIFYQILSNKKPELLDMLLVtNNPYDYAYISQGETTVASIDDAEELLAT 349
Cdd:cd14911 162 DASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFIL-DDVKSYAFLSNGSLPVPGVDDYAEFQAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 350 DSAFDVLGFTQDEKNSIYKLTGAVMHFGNMKFKQKQREEQAE-PDGTEeADKVAYLMGLNSADLLKGLCHPRVKVGNEYV 428
Cdd:cd14911 241 VKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATlPDNTV-AQKIAHLLGLSVTDMTRAFLTPRIKVGRDFV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 429 TKGQNVQQVYYSTGALGKSVYEKMFLWMVVRINTTLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQMCINFTNEKLQQFFN 507
Cdd:cd14911 320 TKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 508 HHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDVTFKAKLYDNHLgksnnfQKPRNLK 587
Cdd:cd14911 400 HTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAHS------MHPKFMK 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 588 G--RPEAHFALVHYAGTVDYNINGWLVKNKDPLNETVVGLYQKSALKLLAHLFANYASAESDQATKGKGS---KKKGSSF 662
Cdd:cd14911 474 TdfRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIVGMAQQALTDTQfgaRTRKGMF 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 663 QTVSALHRENLNKLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRKGYPNRILYGDFRQRYRI 742
Cdd:cd14911 554 RTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEL 633
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1072253241 743 LNPAAIPEGqFIDSRKGAEKLLASLEMDHTQYKFGHTKVFFK 784
Cdd:cd14911 634 LTPNVIPKG-FMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
117-784 |
0e+00 |
|
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: 756.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 117 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRDNQSILITGE 196
Cdd:cd14920 2 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 197 SGAGKTVNTKRVIQYFAVIAAIGDRKKDSgpTGKGTLEDQIIQANPALEAFGNAKTLRNDNSSRFGKFIRIHFGATGKLA 276
Cdd:cd14920 82 SGAGKTENTKKVIQYLAHVASSHKGRKDH--NIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 277 SADIETYLLEKSRVIFQLKSERDYHIFYQILSNKKPEL-LDMLLVTNNpyDYAYISQGETTVASIDDAEELLATDSAFDV 355
Cdd:cd14920 160 GANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLkSDLLLEGFN--NYRFLSNGYIPIPGQQDKDNFQETMEAMHI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 356 LGFTQDEKNSIYKLTGAVMHFGNMKFKQKQREEQAE-PDGTeEADKVAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNV 434
Cdd:cd14920 238 MGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASmPENT-VAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 435 QQVYYSTGALGKSVYEKMFLWMVVRINTTLETKQpRQ--YFIGVLDIAGFEIFDFNSFEQMCINFTNEKLQQFFNHHMFV 512
Cdd:cd14920 317 EQADFAVEALAKATYERLFRWLVHRINKALDRTK-RQgaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 513 LEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDVTFKAKLyDNHLGKSNNFQKPRNLKGr 589
Cdd:cd14920 396 LEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKL-VQEQGSHSKFQKPRQLKD- 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 590 pEAHFALVHYAGTVDYNINGWLVKNKDPLNETVVGLYQKSALKLLAHLFANY-ASAESDQATKGKGS------KKKGSSF 662
Cdd:cd14920 474 -KADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVdRIVGLDQVTGMTETafgsayKTKKGMF 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 663 QTVSALHRENLNKLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRKGYPNRILYGDFRQRYRI 742
Cdd:cd14920 553 RTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 632
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1072253241 743 LNPAAIPEGqFIDSRKGAEKLLASLEMDHTQYKFGHTKVFFK 784
Cdd:cd14920 633 LTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
117-784 |
0e+00 |
|
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: 714.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 117 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRDNQSILITGE 196
Cdd:cd14932 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 197 SGAGKTVNTKRVIQYFAVIAAIGDRKKDSGPT--GKGTLEDQIIQANPALEAFGNAKTLRNDNSSRFGKFIRIHFGATGK 274
Cdd:cd14932 82 SGAGKTENTKKVIQYLAYVASSFKTKKDQSSIalSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 275 LASADIETYLLEKSRVIFQLKSERDYHIFYQILSNKKPELLDMLLVTNNPyDYAYISQGETTVASIDDAEELLATDSAFD 354
Cdd:cd14932 162 IVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYS-KYRFLSNGNVTIPGQQDKELFAETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 355 VLGFTQDEKNSIYKLTGAVMHFGNMKFKQKQREEQAE-PDGTeEADKVAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQN 433
Cdd:cd14932 241 IMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASmPDDT-AAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 434 VQQVYYSTGALGKSVYEKMFLWMVVRINTTLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQMCINFTNEKLQQFFNHHMFV 512
Cdd:cd14932 320 QEQAEFAVEALAKASYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 513 LEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDVTFKAKLYdNHLGKSNNFQKPRNLKGr 589
Cdd:cd14932 400 LEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVV-QEQGNNPKFQKPKKLKD- 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 590 pEAHFALVHYAGTVDYNINGWLVKNKDPLNETVVGLYQKSALKLLAHLFANY----------ASAESDQATkgkgSKKKG 659
Cdd:cd14932 478 -DADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVdrivgldkvaGMGESLHGA----FKTRK 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 660 SSFQTVSALHRENLNKLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRKGYPNRILYGDFRQR 739
Cdd:cd14932 553 GMFRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQR 632
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1072253241 740 YRILNPAAIPEGqFIDSRKGAEKLLASLEMDHTQYKFGHTKVFFK 784
Cdd:cd14932 633 YEILTPNAIPKG-FMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
117-784 |
0e+00 |
|
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: 689.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 117 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRDNQSILITGE 196
Cdd:cd14921 2 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 197 SGAGKTVNTKRVIQYFAVIAAIGDRKKDSGPTGKgtLEDQIIQANPALEAFGNAKTLRNDNSSRFGKFIRIHFGATGKLA 276
Cdd:cd14921 82 SGAGKTENTKKVIQYLAVVASSHKGKKDTSITGE--LEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 277 SADIETYLLEKSRVIFQLKSERDYHIFYQILSNKKPELL-DMLLVTNNpyDYAYISQGETTVASIDDAEELLATDSAFDV 355
Cdd:cd14921 160 GANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRsDLLLEGFN--NYTFLSNGFVPIPAAQDDEMFQETLEAMSI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 356 LGFTQDEKNSIYKLTGAVMHFGNMKFKQKQREEQAE-PDGTeEADKVAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNV 434
Cdd:cd14921 238 MGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASmPDNT-AAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 435 QQVYYSTGALGKSVYEKMFLWMVVRINTTLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQMCINFTNEKLQQFFNHHMFVL 513
Cdd:cd14921 317 EQADFAIEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFIL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 514 EQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDVTFKAKLYDNHlGKSNNFQKPRNLKGRP 590
Cdd:cd14921 397 EQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GNHPKFQKPKQLKDKT 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 591 EahFALVHYAGTVDYNINGWLVKNKDPLNETVVGLYQKSALKLLAHLFANY-------ASAESDQATKGKGSKKKGSSFQ 663
Cdd:cd14921 476 E--FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVdrivgldQMAKMTESSLPSASKTKKGMFR 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 664 TVSALHRENLNKLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRKGYPNRILYGDFRQRYRIL 743
Cdd:cd14921 554 TVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 633
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1072253241 744 NPAAIPEGqFIDSRKGAEKLLASLEMDHTQYKFGHTKVFFK 784
Cdd:cd14921 634 AANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
116-784 |
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: 689.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 116 PAVLYNLKERYA-AWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRDNQSILIT 194
Cdd:cd01380 1 PAVLHNLKVRFCqRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 195 GESGAGKTVNTKRVIQYFAVIAAIGdrkkdsgpTGKGTLEDQIIQANPALEAFGNAKTLRNDNSSRFGKFIRIHFGATGK 274
Cdd:cd01380 81 GESGAGKTVSAKYAMRYFATVGGSS--------SGETQVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 275 LASADIETYLLEKSRVIFQLKSERDYHIFYQILSNK-KPELLDMLLVTNNpyDYAYISQGE-TTVASIDDAEELLATDSA 352
Cdd:cd01380 153 IIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAAsLPELKELHLGSAE--DFFYTNQGGsPVIDGVDDAAEFEETRKA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 353 FDVLGFTQDEKNSIYKLTGAVMHFGNMKFKQKQREEQAEPDGTEEADKVAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 432
Cdd:cd01380 231 LTLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 433 NVQQVYYSTGALGKSVYEKMFLWMVVRINTTLETKQP--RQYFIGVLDIAGFEIFDFNSFEQMCINFTNEKLQQFFNHHM 510
Cdd:cd01380 311 TLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKekQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 511 FVLEQEEYKKEGIEWEFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKATDVTFKAKLYDNHLGKSNN-FQKPRNLKGR 589
Cdd:cd01380 391 FKLEQEEYVKEEIEWSFIDF-YDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNKhFKKPRFSNTA 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 590 peahFALVHYAGTVDYNINGWLVKNKDPLNETVVGLYQKSALKLlahlfanyasaesdqatkgkgskkkgssfQTVSALH 669
Cdd:cd01380 470 ----FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKNRK-----------------------------KTVGSQF 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 670 RENLNKLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRKGYPNRILYGDFRQRYRILNPAAip 749
Cdd:cd01380 517 RDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSK-- 594
|
650 660 670
....*....|....*....|....*....|....*
gi 1072253241 750 EGQFIDSRKGAEKLLASLEMDHTQYKFGHTKVFFK 784
Cdd:cd01380 595 EWLRDDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
117-784 |
0e+00 |
|
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: 674.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 117 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRDNQSILITGE 196
Cdd:cd14919 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 197 SGAGKTVNTKRVIQYFAVIAAIGDRKKDsgptgKGTLEDQIIQANPALEAFGNAKTLRNDNSSRFGKFIRIHFGATGKLA 276
Cdd:cd14919 82 SGAGKTENTKKVIQYLAHVASSHKSKKD-----QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 277 SADIETYLLEKSRVIFQLKSERDYHIFYQILSNKKPELLDMLLVtnNPYD-YAYISQGETTVASIDDAEELLATDSAFDV 355
Cdd:cd14919 157 GANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAMRI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 356 LGFTQDEKNSIYKLTGAVMHFGNMKFKQKQREEQAEPDGTEEADKVAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQ 435
Cdd:cd14919 235 MGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 436 QVYYSTGALGKSVYEKMFLWMVVRINTTLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQMCINFTNEKLQQFFNHHMFVLE 514
Cdd:cd14919 315 QADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 515 QEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDVTFKAKLYDNHlGKSNNFQKPRNLKGRpe 591
Cdd:cd14919 395 QEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQEQ-GTHPKFQKPKQLKDK-- 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 592 AHFALVHYAGTVDYNINGWLVKNKDPLNETVVGLYQKSALKLLAHLFANY-------ASAESDQATKGKGSKKKGSSFQT 664
Cdd:cd14919 472 ADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVdriigldQVAGMSETALPGAFKTRKGMFRT 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 665 VSALHRENLNKLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRKGYPNRILYGDFRQRYRILN 744
Cdd:cd14919 552 VGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILT 631
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1072253241 745 PAAIPEGqFIDSRKGAEKLLASLEMDHTQYKFGHTKVFFK 784
Cdd:cd14919 632 PNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
117-784 |
0e+00 |
|
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: 671.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 117 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRDNQSILITGE 196
Cdd:cd15896 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 197 SGAGKTVNTKRVIQYFAVIAAIGDRKKDSGP--TGKGTLEDQIIQANPALEAFGNAKTLRNDNSSRFGKFIRIHFGATGK 274
Cdd:cd15896 82 SGAGKTENTKKVIQYLAHVASSHKTKKDQNSlaLSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 275 LASADIETYLLEKSRVIFQLKSERDYHIFYQILSNKKPELLDMLLVTNNPyDYAYISQGETTVASIDDAEELLATDSAFD 354
Cdd:cd15896 162 IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYN-NYRFLSNGNVTIPGQQDKDLFTETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 355 VLGFTQDEKNSIYKLTGAVMHFGNMKFKQKQREEQAEPDGTEEADKVAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNV 434
Cdd:cd15896 241 IMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 435 QQVYYSTGALGKSVYEKMFLWMVVRINTTLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQMCINFTNEKLQQFFNHHMFVL 513
Cdd:cd15896 321 EQAEFAVEALAKATYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 514 EQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDVTFKAKLYDNHlGKSNNFQKPRNLKGrp 590
Cdd:cd15896 401 EQEEYQREGIEWSFIDFGLDLQPCIDLIEKPAsppGILALLDEECWFPKATDKSFVEKVLQEQ-GTHPKFFKPKKLKD-- 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 591 EAHFALVHYAGTVDYNINGWLVKNKDPLNETVVGLYQKSALKLLAHLFANYASAES-DQATKGKGS----KKKGSSFQTV 665
Cdd:cd15896 478 EADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVGlDKVSGMSEMpgafKTRKGMFRTV 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 666 SALHRENLNKLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRKGYPNRILYGDFRQRYRILNP 745
Cdd:cd15896 558 GQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 637
|
650 660 670
....*....|....*....|....*....|....*....
gi 1072253241 746 AAIPEGqFIDSRKGAEKLLASLEMDHTQYKFGHTKVFFK 784
Cdd:cd15896 638 NAIPKG-FMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
117-784 |
0e+00 |
|
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: 660.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 117 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRDNQSILITGE 196
Cdd:cd14930 2 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 197 SGAGKTVNTKRVIQYFAVIAAIGDRKKDSGPTGKgtLEDQIIQANPALEAFGNAKTLRNDNSSRFGKFIRIHFGATGKLA 276
Cdd:cd14930 82 SGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGE--LERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 277 SADIETYLLEKSRVIFQLKSERDYHIFYQILSNKKPELLDMLLVTNNPYdYAYISQGETTVASiDDAEELLATDSAFDVL 356
Cdd:cd14930 160 GANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQETLESLRVL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 357 GFTQDEKNSIYKLTGAVMHFGNMKFKQKQREEQAE-PDGTeEADKVAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQ 435
Cdd:cd14930 238 GFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 436 QVYYSTGALGKSVYEKMFLWMVVRINTTLEtKQPRQ--YFIGVLDIAGFEIFDFNSFEQMCINFTNEKLQQFFNHHMFVL 513
Cdd:cd14930 317 QADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 514 EQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDVTFKAKLYDNHlGKSNNFQKPRNLkgRP 590
Cdd:cd14930 396 EQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRPRHL--RD 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 591 EAHFALVHYAGTVDYNINGWLVKNKDPLNETVVGLYQKSALKLLAHLFANYA-----SAESDQATKGKGSKKKGSSFQTV 665
Cdd:cd14930 473 QADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEgivglEQVSSLGDGPPGGRPRRGMFRTV 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 666 SALHRENLNKLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRKGYPNRILYGDFRQRYRILNP 745
Cdd:cd14930 553 GQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTP 632
|
650 660 670
....*....|....*....|....*....|....*....
gi 1072253241 746 AAIPEGqFIDSRKGAEKLLASLEMDHTQYKFGHTKVFFK 784
Cdd:cd14930 633 NAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
117-784 |
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: 652.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 117 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRDNQSILITGE 196
Cdd:cd01381 2 GILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 197 SGAGKTVNTKRVIQYFAVIaaigdrkkdSGPtgKGTLEDQIIQANPALEAFGNAKTLRNDNSSRFGKFIRIHFGATGKLA 276
Cdd:cd01381 82 SGAGKTESTKLILQYLAAI---------SGQ--HSWIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 277 SADIETYLLEKSRVIFQLKSERDYHIFYQILSNKKPELLDMLLVTnNPYDYAYISQGETTVAS-IDDAEELLATDSAFDV 355
Cdd:cd01381 151 GAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELG-DASDYYYLTQGNCLTCEgRDDAAEFADIRSAMKV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 356 LGFTQDEKNSIYKLTGAVMHFGNMKFKQKQRE--EQAEPDGTEEADKVAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQN 433
Cdd:cd01381 230 LMFTDEEIWDIFKLLAAILHLGNIKFEATVVDnlDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 434 VQQVYYSTGALGKSVYEKMFLWMVVRINTTLETKQPRQYF---IGVLDIAGFEIFDFNSFEQMCINFTNEKLQQFFNHHM 510
Cdd:cd01381 310 AEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtsIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 511 FVLEQEEYKKEGIEWEFIDFgMDLQACIDLI-EKPMGIMSILEEECMFPKATDVTFKAKLYDNHlGKSNNFQKPRNlkgR 589
Cdd:cd01381 390 FKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMNIMSLIDEESKFPKGTDQTMLEKLHSTH-GNNKNYLKPKS---D 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 590 PEAHFALVHYAGTVDYNINGWLVKNKDPLNETVVGLYQKSALKLLAHLFANYASAESDQATKGkgskkkgssfQTVSALH 669
Cdd:cd01381 465 LNTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDISMGSETRKKS----------PTLSSQF 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 670 RENLNKLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRKGYPNRILYGDFRQRYRILNPaAIP 749
Cdd:cd01381 535 RKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVP-GIP 613
|
650 660 670
....*....|....*....|....*....|....*
gi 1072253241 750 EGQFIDSRKGAEKLLASLEMDHTQYKFGHTKVFFK 784
Cdd:cd01381 614 PAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
117-784 |
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: 647.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 117 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRDNQSILITGE 196
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 197 SGAGKTVNTKRVIQYFAVIaaigdrkkdSGPTGK--GTLEDQIIQANPALEAFGNAKTLRNDNSSRFGKFIRIHFGATGK 274
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAV---------SGGSESevERVKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 275 LASADIETYLLEKSRVIFQLKSERDYHIFYQILSNKKPELLDMLLVTNNPYDYAYISQGETTVASIDDAEELLATDSAFD 354
Cdd:cd01378 153 PVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 355 VLGFTQDEKNSIYKLTGAVMHFGNMKFKQKQREEQAEPDgTEEADKVAYLMGLNSADLLKGLCHPRVKVGNEY---VTKG 431
Cdd:cd01378 233 VIGFTEEEQDSIFRILAAILHLGNIQFAEDEEGNAAISD-TSVLDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvYEVP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 432 QNVQQVYYSTGALGKSVYEKMFLWMVVRINTTLETKQPRQ-YFIGVLDIAGFEIFDFNSFEQMCINFTNEKLQQFFNHhm 510
Cdd:cd01378 312 LNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKkKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIE-- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 511 FVL--EQEEYKKEGIEWEFIDFgMDLQACIDLIE-KPMGIMSILEEECMFP-KATDVTFKAKLyDNHLGKSNNFQKPRNL 586
Cdd:cd01378 390 LTLkaEQEEYVREGIEWTPIKY-FNNKIICDLIEeKPPGIFAILDDACLTAgDATDQTFLQKL-NQLFSNHPHFECPSGH 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 587 KGRPEAHFALVHYAGTVDYNINGWLVKNKDPLNETVVGLYQKSALKLLAHLFANYASAESDQATKgkgskkkgssfqTVS 666
Cdd:cd01378 468 FELRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVDLDSKKRPP------------TAG 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 667 ALHRENLNKLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRKGYPNRILYGDFRQRYRILNPA 746
Cdd:cd01378 536 TKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPK 615
|
650 660 670
....*....|....*....|....*....|....*...
gi 1072253241 747 AIPEGQFIDsRKGAEKLLASLEMDHTQYKFGHTKVFFK 784
Cdd:cd01378 616 TWPAWDGTW-QGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
116-784 |
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: 631.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 116 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRgkKRSEAPPHIFSISDNAYQYMLTDRDNQSILITG 195
Cdd:cd01383 1 PSVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 196 ESGAGKTVNTKRVIQYfavIAAIGdrkkdsgpTGKGTLEDQIIQANPALEAFGNAKTLRNDNSSRFGKFIRIHFGATGKL 275
Cdd:cd01383 79 ESGAGKTETAKIAMQY---LAALG--------GGSSGIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 276 ASADIETYLLEKSRVIFQLKSERDYHIFYQILSNKKPELLDMLLVTnNPYDYAYISQGET-TVASIDDAEELLATDSAFD 354
Cdd:cd01383 148 CGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLK-SASEYKYLNQSNClTIDGVDDAKKFHELKEALD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 355 VLGFTQDEKNSIYKLTGAVMHFGNMKFKQKQREEQAEPDGTEEADKVAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNV 434
Cdd:cd01383 227 TVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 435 QQVYYSTGALGKSVYEKMFLWMVVRINTTLET-KQPRQYFIGVLDIAGFEIFDFNSFEQMCINFTNEKLQQFFNHHMFVL 513
Cdd:cd01383 307 QQAIDARDALAKAIYASLFDWLVEQINKSLEVgKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 514 EQEEYKKEGIEWEFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKATDVTFKAKLyDNHLgKSNnfqkpRNLKGRPEA 592
Cdd:cd01383 387 EQEEYELDGIDWTKVDF-EDNQECLDLIEkKPLGLISLLDEESNFPKATDLTFANKL-KQHL-KSN-----SCFKGERGG 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 593 HFALVHYAGTVDYNINGWLVKNKDPLNETVVGLYQKSALKLLaHLFANYASAESDQATKGKGSKKKGSSFQTVSALHREN 672
Cdd:cd01383 459 AFTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQLP-QLFASKMLDASRKALPLTKASGSDSQKQSVATKFKGQ 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 673 LNKLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRKGYPNRILYGDFRQRYRILNPAAIPEGQ 752
Cdd:cd01383 538 LFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDVSASQ 617
|
650 660 670
....*....|....*....|....*....|..
gi 1072253241 753 FIDSRKGAekLLASLEMDHTQYKFGHTKVFFK 784
Cdd:cd01383 618 DPLSTSVA--ILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
117-784 |
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: 603.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 117 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRDNQSILITGE 196
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 197 SGAGKTVNTKRVIQYFAVIaaigdrkkdsgpTGKGT-LEDQIIQANPALEAFGNAKTLRNDNSSRFGKFIRIHFGATGKL 275
Cdd:cd14883 82 SGAGKTETTKLILQYLCAV------------TNNHSwVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 276 ASADIETYLLEKSRVIFQLKSERDYHIFYQILSNKK--PELLDMLLVtNNPYDYAYISQ-GETTVASIDDAEELLATDSA 352
Cdd:cd14883 150 KGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKhsKELKEKLKL-GEPEDYHYLNQsGCIRIDNINDKKDFDHLRLA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 353 FDVLGFTQDEKNSIYKLTGAVMHFGNMKFKQKQREEQAE-PDGTEEADKVAYLMGLNSADLLKGLCHPRVKVGNEYVTKG 431
Cdd:cd14883 229 MNVLGIPEEMQEGIFSVLSAILHLGNLTFEDIDGETGALtVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 432 QNVQQVYYSTGALGKSVYEKMFLWMVVRINTTLETKQPRQYFIGVLDIAGFEIFDFNSFEQMCINFTNEKLQQFFNHHMF 511
Cdd:cd14883 309 LKVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 512 VLEQEEYKKEGIEWEFIDFgMDLQACIDLIEK-PMGIMSILEEECMFPKATDVTFKAKLYDNHlGKSNNFQKPRnlKGRP 590
Cdd:cd14883 389 KLEQEEYEKEGINWSHIVF-TDNQECLDLIEKpPLGILKLLDEECRFPKGTDLTYLEKLHAAH-EKHPYYEKPD--RRRW 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 591 EAHFALVHYAGTVDYNINGWLVKNKDPLNETVVGLYQKSALKLLAHLFANYASAESDQATKGKGSKKKGSSFQ----TVS 666
Cdd:cd14883 465 KTEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTYPDLLALTGLSISLGGDTTSRGTSkgkpTVG 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 667 ALHRENLNKLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRKGYPNRILYGDFRQRYRILNPA 746
Cdd:cd14883 545 DTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPR 624
|
650 660 670
....*....|....*....|....*....|....*....
gi 1072253241 747 AIPEGQfiDSRKGAEK-LLASLEMDHTQYKFGHTKVFFK 784
Cdd:cd14883 625 ARSADH--KETCGAVRaLMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
116-784 |
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: 583.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 116 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRDNQSILIT 194
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 195 GESGAGKTVNTKRVIQYfavIAAIGDRKKDSGptgkGTLEDQIIQANPALEAFGNAKTLRNDNSSRFGKFIRIHFGATGK 274
Cdd:cd01384 81 GESGAGKTETTKMLMQY---LAYMGGRAVTEG----RSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 275 LASADIETYLLEKSRVIFQLKSERDYHIFYQILSNKKPELLDMLLVtNNPYDYAYISQGET-TVASIDDAEELLATDSAF 353
Cdd:cd01384 154 ISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKL-KDPKQFHYLNQSKCfELDGVDDAEEYRATRRAM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 354 DVLGFTQDEKNSIYKLTGAVMHFGNMKFKQKQREEQAEP--DGTEEADK-VAYLMGLNSADLLKGLCHPRVKVGNEYVTK 430
Cdd:cd01384 233 DVVGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPkdEKSEFHLKaAAELLMCDEKALEDALCKRVIVTPDGIITK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 431 GQNVQQVYYSTGALGKSVYEKMFLWMVVRINTTLETKQPRQYFIGVLDIAGFEIFDFNSFEQMCINFTNEKLQQFFNHHM 510
Cdd:cd01384 313 PLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQHV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 511 FVLEQEEYKKEGIEWEFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKATDVTFKAKLYDNhLGKSNNFQKPRnlkgR 589
Cdd:cd01384 393 FKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPRSTHETFAQKLYQT-LKDHKRFSKPK----L 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 590 PEAHFALVHYAGTVDYNINGWLVKNKDPLNETVVGLYQKSALKLLAHLFANYASAESDQATkgkgskkkgsSFQTVSALH 669
Cdd:cd01384 467 SRTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPREGTSSSS----------KFSSIGSRF 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 670 RENLNKLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRKGYPNRILYGDFRQRYRILNPAAIp 749
Cdd:cd01384 537 KQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPEVL- 615
|
650 660 670
....*....|....*....|....*....|....*
gi 1072253241 750 eGQFIDSRKGAEKLLASLEMDhtQYKFGHTKVFFK 784
Cdd:cd01384 616 -KGSDDEKAACKKILEKAGLK--GYQIGKTKVFLR 647
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
116-784 |
3.79e-173 |
|
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: 541.67 E-value: 3.79e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 116 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRDNQSILITG 195
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 196 ESGAGKTVNTKRVIQYFAVIAaigdrkkdsGPTGkgTLEDQIIQANPALEAFGNAKTLRNDNSSRFGKFIRIHFGATGKL 275
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVA---------GSTN--GVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 276 ASADIETYLLEKSRVIFQLKSERDYHIFYQILSNKKPElldMLLVTNNPYDYAYISQGET-TVASIDDAEELLATDSAFD 354
Cdd:cd14872 150 CGASTENYLLEKSRVVYQIKGERNFHIFYQLLASPDPA---SRGGWGSSAAYGYLSLSGCiEVEGVDDVADFEEVVLAME 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 355 VLGFTQDEKNSIYKLTGAVMHFGNMKFKQKQREEQAEPDGT---EEADKVAYLMGLNSADLLKGLCHPRVKVgneyvtKG 431
Cdd:cd14872 227 QLGFDDADINNVMSLIAAILKLGNIEFASGGGKSLVSGSTVanrDVLKEVATLLGVDAATLEEALTSRLMEI------KG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 432 QNV-------QQVYYSTGALGKSVYEKMFLWMVVRINTTLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQMCINFTNEKLQ 503
Cdd:cd14872 301 CDPtripltpAQATDACDALAKAAYSRLFDWLVKKINESMRpQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQ 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 504 QFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLIEK-PMGIMSILEEECMFPKATDVTFKAKLYDNHLGKSnnFQK 582
Cdd:cd14872 381 QHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEKkQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKS--TFV 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 583 PRNLKGRPEaHFALVHYAGTVDYNINGWLVKNKDPLNETVVGLYQKSALKLLAHLFanyASAESDQATKGKgskkkgssf 662
Cdd:cd14872 458 YAEVRTSRT-EFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLF---PPSEGDQKTSKV--------- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 663 qTVSALHRENLNKLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRKGYPNRILYGDFRQRYRI 742
Cdd:cd14872 525 -TLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRF 603
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1072253241 743 LnPAAIPEGQFIDSRKGAEKLLASLEMDHTQYKFGHTKVFFK 784
Cdd:cd14872 604 L-VKTIAKRVGPDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
116-784 |
4.62e-169 |
|
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: 531.27 E-value: 4.62e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 116 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRDNQSILIT 194
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 195 GESGAGKTVNTKRVIQYFAVIAaigdrkkdsgptgkGTLED----QIIQANPALEAFGNAKTLRNDNSSRFGKFIRIHFG 270
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIA--------------GGLNDstikKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 271 ATGKLASADIETYLLEKSRVIFQLKSERDYHIFYQILSNKKPELLDMLlvtNNPYDYAYIsqGETTVASID---DAEELL 347
Cdd:cd14903 147 KNGTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEERLFL---DSANECAYT--GANKTIKIEgmsDRKHFA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 348 ATDSAFDVLGFTQDEKNSIYKLTGAVMHFGNMKFKQKQREEQAE--PDGTEEADKVAYLMGLNSADLLKGLCHPRVKVGN 425
Cdd:cd14903 222 RTKEALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSaiAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 426 EYVTKGQNVQQVYYSTGALGKSVYEKMFLWMVVRINTTLETKQPRQYFIGVLDIAGFEIFDFNSFEQMCINFTNEKLQQF 505
Cdd:cd14903 302 DVYTVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQK 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 506 FNHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKATDVTFKAKLYDNHLGKSNNFQKPRN 585
Cdd:cd14903 382 FTQDVFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFPRT 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 586 LKgrpeAHFALVHYAGTVDYNINGWLVKNKDPLNETVVGLYQKSALKLLAHLFANYASAESDQATKGKGSKKKGS----S 661
Cdd:cd14903 461 SR----TQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAASTSLARGARRRRggalT 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 662 FQTVSALHRENLNKLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRKGYPNRILYGDFRQRYR 741
Cdd:cd14903 537 TTTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFW 616
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1072253241 742 ILNPAAipEGQFIDSRKGAEKLLASLEMDH-TQYKFGHTKVFFK 784
Cdd:cd14903 617 LFLPEG--RNTDVPVAERCEALMKKLKLESpEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
117-784 |
2.64e-168 |
|
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: 529.35 E-value: 2.64e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 117 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYML----TDRDNQSI 191
Cdd:cd14890 2 SLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIqsgvLDPSNQSI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 192 LITGESGAGKTVNTKRVIQYFAVIAA--------IGDRKKDSGPTGKGTLEDQIIQANPALEAFGNAKTLRNDNSSRFGK 263
Cdd:cd14890 82 IISGESGAGKTEATKIIMQYLARITSgfaqgasgEGEAASEAIEQTLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 264 FIRIHFGATGKLASADIETYLLEKSRVIFQLKSERDYHIFYQILSNKKPELLDMLLVTNnPYDYAYISQGETTVASIDDA 343
Cdd:cd14890 162 FIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQT-PVEYFYLRGECSSIPSCDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 344 EELLATDSAFDVLGFTQDEKNSIYKLTGAVMHFGNMKFKQKQREEQAEPDGTEEA-DKVAYLMGLNSADLLKGLCHPRVK 422
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLEDATTLQSlKLAAELLGVNEDALEKALLTRQLF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 423 VGNEYVTKGQNVQQVYYSTGALGKSVYEKMFLWMVVRINTTLETKQPRQYFIGVLDIAGFEIFDFNSFEQMCINFTNEKL 502
Cdd:cd14890 321 VGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYANEKL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 503 QQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLIE-KPMGIMSILE--EEC--MFPKATDVTFKAKLYDNHLGKS 577
Cdd:cd14890 401 QRHFNQHMFEVEQVEYSNEGIDWQYITF-NDNQACLELIEgKVNGKPGIFItlDDCwrFKGEEANKKFVSQLHASFGRKS 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 578 NNFQKPRNLKGRP---------EAHFALVHYAGTVDYNINGWLVKNKDPLNETvvglyqksaLKLLAhlfanyasAESDQ 648
Cdd:cd14890 480 GSGGTRRGSSQHPhfvhpkfdaDKQFGIKHYAGDVIYDASGFNEKNNETLNAE---------MKELI--------KQSRR 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 649 ATKGKgskkkgssfqTVSALHRENLNKLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRKGYP 728
Cdd:cd14890 543 SIREV----------SVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQIRQQGFA 612
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 1072253241 729 NRILYGDFRQRYRILNPAAipegqfiDSRKGAEKLLAS-LEMDHTQYKFGHTKVFFK 784
Cdd:cd14890 613 LREEHDSFFYDFQVLLPTA-------ENIEQLVAVLSKmLGLGKADWQIGSSKIFLK 662
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
864-1941 |
6.18e-167 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 540.15 E-value: 6.18e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 864 EKEMQTMKEEFQKLKEALEKSEARRKDLEEKMVSLLQEKNDLQLQVQAEQDNLADADERCEQLIKNKIQLEAKLKEQTER 943
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 944 LEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIVKLTKEKKALQEAHQQ 1023
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1024 ALDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKIRMDLERVKRKLEGDVKLSQESLMDLENDKQQLEEKLKKKDF 1103
Cdd:pfam01576 164 FTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1104 EVSQLNTRIEDEQNVCIQLQKKMKELQARIEELEEELEAERTARAKVEKLRCDLSRELEEISERLEEAGGATSVQMELNK 1183
Cdd:pfam01576 244 ELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1184 KREAEFLKLRRDLEESTLHSEATAASLRKKHADSVAELSEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQMVKAKANL 1263
Cdd:pfam01576 324 KREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1264 EKLCRSLEDQANEHRTKSEENQRTVNELSSLRAKLQTENGELSRRLDEKESLVSQMTRGKQTYTQHLEDLKRQLEEETKA 1343
Cdd:pfam01576 404 EHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1344 KNALAHALQSARHDSDLLREQFEEEQEAKAELQRILSKANSEVAQWRTKYETDAiQRTEELEEAKKKLAQRLQEAEEAVE 1423
Cdd:pfam01576 484 KLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDA-GTLEALEEGKKRLQRELEALTQQLE 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1424 AVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAALDKKQRNFDKILAEWKQKFEESQTELESSQKEARSLSTELFKLK 1503
Cdd:pfam01576 563 EKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLA 642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1504 NAYEESLDHLETFKRENKNLQEEISDLTEQLGESGKSIHELEKIRKQLDQEKMEIQSALEEAEATLEHEEGKILHAQLEL 1583
Cdd:pfam01576 643 RALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNM 722
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1584 HQIKADSERKLAEKDEEMEQAKRNYQRMVDTLQTSLEAETRSRNEALRIKKKMEGDLNEMEIQLSQANRQAAEAQKQVKI 1663
Cdd:pfam01576 723 QALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKK 802
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1664 LQSYLKDTQIQLDDALRASEDLKENIAIVERRNTLLQAELEELRSLVEQTERARKLSEQELIETSERVQLLHSQNTSLIN 1743
Cdd:pfam01576 803 LQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQD 882
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1744 QKKKMESDLSQLQTEMEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQQRLDEAEQIAL 1823
Cdd:pfam01576 883 EKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVK 962
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1824 KGGKKQLQKLEARVRELDNELEAEQKRNAESVKGMRKYERRIKELTYQTEEDRKNLARLQDLVDKLQLKVKTYKRQAEES 1903
Cdd:pfam01576 963 SKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEA 1042
|
1050 1060 1070
....*....|....*....|....*....|....*...
gi 1072253241 1904 EEQANTSLSKFRKVQHELDEAEERADIAESQVNKLRAK 1941
Cdd:pfam01576 1043 EEEASRANAARRKLQRELDDATESNESMNREVSTLKSK 1080
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
119-784 |
8.90e-167 |
|
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: 524.51 E-value: 8.90e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 119 LYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRDNQSILITGES 197
Cdd:cd01382 4 LNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVSGES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 198 GAGKTVNTKRVIQYFAviaaigdrkkDSGPTGKGTLEDQIIQANPALEAFGNAKTLRNDNSSRFGKFIRIHFGATGKLAS 277
Cdd:cd01382 84 GAGKTESTKYILRYLT----------ESWGSGAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 278 ADIETYLLEKSRVIFQLKSERDYHIFYQILSNKKPELLDMLLvtnnpydyayisqgetTVASIDDAEELLATDSAFDVLG 357
Cdd:cd01382 154 GFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLL----------------KDPLLDDVGDFIRMDKAMKKIG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 358 FTQDEKNSIYKLTGAVMHFGNMKFKQKQREE----QAEPDGTEEADKVAYLMGLNSADLLKGLCHpRVKVGNEYVTKGQ- 432
Cdd:cd01382 218 LSDEEKLDIFRVVAAVLHLGNIEFEENGSDSgggcNVKPKSEQSLEYAAELLGLDQDELRVSLTT-RVMQTTRGGAKGTv 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 433 -----NVQQVYYSTGALGKSVYEKMFLWMVVRINTTLETKQpRQYFIGVLDIAGFEIFDFNSFEQMCINFTNEKLQQFFN 507
Cdd:cd01382 297 ikvplKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFET-SSYFIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQFFN 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 508 HHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKATDVTFKAKLYDNHLgksNNF--QKPR 584
Cdd:cd01382 376 ERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEaKLVGILDLLDEESKLPKPSDQHFTSAVHQKHK---NHFrlSIPR 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 585 nlKGRPEAH--------FALVHYAGTVDYNINGWLVKNKDPLNETVVGLYQKSALKLLAHLFANYASAESDQATkgkgsK 656
Cdd:cd01382 452 --KSKLKIHrnlrddegFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNNNKDSKQ-----K 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 657 KKGSSFQTVSALHRENLNKLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRKGYPNRILYGDF 736
Cdd:cd01382 525 AGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSFHDL 604
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1072253241 737 RQRYRILNPAAIPEgqfIDSRKGAEKLLASLEMDHTQYKFGHTKVFFK 784
Cdd:cd01382 605 YNMYKKYLPPKLAR---LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
116-784 |
9.22e-164 |
|
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: 517.32 E-value: 9.22e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 116 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRgKKRSEAPPHIFSISDNAYQYMLTDRDNQSILIT 194
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 195 GESGAGKTVNTKRVIQYFAViAAIGDRKKDSgptgkgTLEDQIIQANPALEAFGNAKTLRNDNSSRFGKFIRIHF----- 269
Cdd:cd14888 80 GESGAGKTESTKYVMKFLAC-AGSEDIKKRS------LVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFsklks 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 270 ----GATGKLASADIETYLLEKSRVIFQLKSERDYHIFYQILS-----------------------NKKPELLDMLL-VT 321
Cdd:cd14888 153 krmsGDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAaareakntglsyeendeklakgaDAKPISIDMSSfEP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 322 NNPYDYAYISqGETTVASIDDAEELLATDSAFDVLGFTQDEKNSIYKLTGAVMHFGNMKFKQKQREEQA---EPDGTEEA 398
Cdd:cd14888 233 HLKFRYLTKS-SCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGavvSASCTDDL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 399 DKVAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQVYYSTGALGKSVYEKMFLWMVVRINTTLE-TKQPRQYFIGVL 477
Cdd:cd14888 312 EKVASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGySKDNSLLFCGVL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 478 DIAGFEIFDFNSFEQMCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLQACIDLI-EKPMGIMSILEEECM 556
Cdd:cd14888 392 DIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLqEKPLGIFCMLDEECF 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 557 FPKATDVTFKAKLYDNHLGkSNNFQKprnLKGRPEAhFALVHYAGTVDYNINGWLVKNKDPLNETVVGLYQKSALKLLAH 636
Cdd:cd14888 471 VPGGKDQGLCNKLCQKHKG-HKRFDV---VKTDPNS-FVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISN 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 637 LFANYASAESDQATkgkgskkKGSSFQTVSALHRENLNKLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGV 716
Cdd:cd14888 546 LFSAYLRRGTDGNT-------KKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGV 618
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1072253241 717 LEGIRICRKGYPNRILYGDFRQRYRILNPaaipegqfidsrkGAEKLLaslemdHTQYKFGHTKVFFK 784
Cdd:cd14888 619 LQAVQVSRAGYPVRLSHAEFYNDYRILLN-------------GEGKKQ------LSIWAVGKTLCFFK 667
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
117-784 |
3.14e-163 |
|
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: 515.46 E-value: 3.14e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 117 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRDNQSILITGE 196
Cdd:cd01387 2 TVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 197 SGAGKTVNTKRVIQYFAVIAaigdrkkdsgPTGKGTLEDQIIQANPALEAFGNAKTLRNDNSSRFGKFIRIHFgATGKLA 276
Cdd:cd01387 82 SGSGKTEATKLIMQYLAAVN----------QRRNNLVTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-EGGVIV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 277 SADIETYLLEKSRVIFQLKSERDYHIFYQILSNKkPELLDMLLVTNNPYDYAYISQGETT-VASIDDAEELLATDSAFDV 355
Cdd:cd01387 151 GAITSQYLLEKSRIVTQAKNERNYHVFYELLAGL-PAQLRQKYGLQEAEKYFYLNQGGNCeIAGKSDADDFRRLLAAMQV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 356 LGFTQDEKNSIYKLTGAVMHFGNMKFKQKQRE---EQAEPDGTEEADKVAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 432
Cdd:cd01387 230 LGFSSEEQDSIFRILASVLHLGNVYFHKRQLRhgqEGVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRERIFTPL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 433 NVQQVYYSTGALGKSVYEKMFLWMVVRINTTLETKQPRQYFIGVLDIAGFEIFDFNSFEQMCINFTNEKLQQFFNHHMFV 512
Cdd:cd01387 310 TIDQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVFK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 513 LEQEEYKKEGIEWEFIDFgMDLQACIDLI-EKPMGIMSILEEECMFPKATDVTFKAKLYDNHlGKSNNFQKPRnlKGRPE 591
Cdd:cd01387 390 LEQEEYIREQIDWTEIAF-ADNQPVINLIsKKPVGILHILDDECNFPQATDHSFLEKCHYHH-ALNELYSKPR--MPLPE 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 592 ahFALVHYAGTVDYNINGWLVKNKDPLNETVVGLYQKSALKLLAHLFANYAsAESDQATKGKGSKK---KGSSFQTVSAL 668
Cdd:cd01387 466 --FTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHR-AQTDKAPPRLGKGRfvtMKPRTPTVAAR 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 669 HRENLNKLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRKGYPNRILYGDFRQRYRILNPAAI 748
Cdd:cd01387 543 FQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVALKL 622
|
650 660 670
....*....|....*....|....*....|....*.
gi 1072253241 749 PEGQFIDSRKGAEKLLASLeMDHTQYKFGHTKVFFK 784
Cdd:cd01387 623 PRPAPGDMCVSLLSRLCTV-TPKDMYRLGATKVFLR 657
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
116-784 |
1.09e-162 |
|
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: 512.98 E-value: 1.09e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 116 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRDNQSILITG 195
Cdd:cd01379 1 DTIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 196 ESGAGKTVNTKRVIQYFAVIaaigdrkkdsGPTGKGTLEDQIIQANPALEAFGNAKTLRNDNSSRFGKFIRIHFGATGKL 275
Cdd:cd01379 81 ESGAGKTESANLLVQQLTVL----------GKANNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 276 ASADIETYLLEKSRVIFQLKSERDYHIFYQIL----SNKKpeLLDMLLVTNNPYDY-AYISQGETTVASID-DAEELLAT 349
Cdd:cd01379 151 TGARISEYLLEKSRVVHQAIGERNFHIFYYIYaglaEDKK--LAKYKLPENKPPRYlQNDGLTVQDIVNNSgNREKFEEI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 350 DSAFDVLGFTQDEKNSIYKLTGAVMHFGNMKFKQKQREEQ----AEPDGTEEADKVAYLMGLNSADLLKGLCHPRVKVGN 425
Cdd:cd01379 229 EQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTEVESNHQtdksSRISNPEALNNVAKLLGIEADELQEALTSHSVVTRG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 426 EYVTKGQNVQQVYYSTGALGKSVYEKMFLWMVVRINTTL---ETKQPRQYFIGVLDIAGFEIFDFNSFEQMCINFTNEKL 502
Cdd:cd01379 309 ETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpdRSASDEPLSIGILDIFGFENFQKNSFEQLCINIANEQI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 503 QQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLQACID-LIEKPMGIMSILEEECMFPKATDVTFKAKLYDNHlgKSNNFQ 581
Cdd:cd01379 389 QYYFNQHIFAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFLQKPMGLLALLDEESRFPKATDQTLVEKFHNNI--KSKYYW 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 582 KPRnlkgRPEAHFALVHYAGTVDYNINGWLVKNKDPLNETVVGLYQKSALKLLAhlfanyasaesdqatkgkgskkkgss 661
Cdd:cd01379 466 RPK----SNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVR-------------------------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 662 fQTVSALHRENLNKLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRKGYPNRILYGDFRQRYR 741
Cdd:cd01379 516 -QTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYY 594
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1072253241 742 IL--NPAAIPEGqfidSRKGAEKLLASLEMDHtqYKFGHTKVFFK 784
Cdd:cd01379 595 FLafKWNEEVVA----NRENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
116-782 |
1.82e-158 |
|
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: 502.40 E-value: 1.82e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 116 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAY------RGKKRSEAPPHIFSISDNAYQYMLTDRD-- 187
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 188 --NQSILITGESGAGKTVNTKRVIQYFAVIAAIgdRKKDSGPTGKGTLEDQIIQANPALEAFGNAKTLRNDNSSRFGKFI 265
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSSA--TTHGQNATERENVRDRVLESNPILEAFGNARTNRNNNSSRFGKFI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 266 RIHFGATGKLASADIETYLLEKSRVIFQLKSERDYHIFYQILSNKKPELLDMLLVTNNPyDYAYISQGETTVA--SIDDA 343
Cdd:cd14901 159 RLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVE-EYKYLNSSQCYDRrdGVDDS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 344 EELLATDSAFDVLGFTQDEKNSIYKLTGAVMHFGNMKFKQKQREEQAEPDGTE-EADKVAYLMGLNSADLLKGLCHPRVK 422
Cdd:cd14901 238 VQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGGTFSMSSLaNVRAACDLLGLDMDVLEKTLCTREIR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 423 VGNEYVTKGQNVQQVYYSTGALGKSVYEKMFLWMVVRINTTLETKQP--RQYFIGVLDIAGFEIFDFNSFEQMCINFTNE 500
Cdd:cd14901 318 AGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSEStgASRFIGIVDIFGFEIFATNSLEQLCINFANE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 501 KLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDlQACIDLIE-KPMGIMSILEEECMFPKATDVTFKAKLYDNhLGKSNN 579
Cdd:cd14901 398 KLQQLFGKFVFEMEQDEYVAEAIPWTFVEYPNN-DACVAMFEaRPTGLFSLLDEQCLLPRGNDEKLANKYYDL-LAKHAS 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 580 FQKPRNLKGRpeAHFALVHYAGTVDYNINGWLVKNKDPLNETVVGLYQKSALKLLAhlfanyasaesdqatkgkgskkkg 659
Cdd:cd14901 476 FSVSKLQQGK--RQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLS------------------------ 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 660 ssfQTVSALHRENLNKLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRKGYPNRILYGDFRQR 739
Cdd:cd14901 530 ---STVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHT 606
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1072253241 740 YRILNPAAIPEGQFIDSRKGAEKLLASLEM----DHTQYKFGHTKVF 782
Cdd:cd14901 607 YSCLAPDGASDTWKVNELAERLMSQLQHSElnieHLPPFQVGKTKVF 653
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
119-784 |
3.07e-156 |
|
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: 497.67 E-value: 3.07e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 119 LYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRDNQSILITGESG 198
Cdd:cd01385 4 LENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISGESG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 199 AGKTVNTKRVIQYFAVIAAIGdrkkdsgpTGKGTlEDQIIQANPALEAFGNAKTLRNDNSSRFGKFIRIHFGATGKLASA 278
Cdd:cd01385 84 SGKTESTNFLLHHLTALSQKG--------YGSGV-EQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 279 DIETYLLEKSRVIFQLKSERDYHIFYQILSNKKPELLDMLLVTnNPYDYAYISQGET-TVASIDDAEELLATDSAFDVLG 357
Cdd:cd01385 155 VVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLK-QPEDYHYLNQSDCyTLEGEDEKYEFERLKQAMEMVG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 358 FTQDEKNSIYKLTGAVMHFGNMKFKQK--QREEQAEPDGTEEADKVAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQ 435
Cdd:cd01385 234 FLPETQRQIFSVLSAVLHLGNIEYKKKayHRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLILPYKLP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 436 QVYYSTGALGKSVYEKMFLWMVVRINTTLETKQ----PRQYFIGVLDIAGFEIFDFNSFEQMCINFTNEKLQQFFNHHMF 511
Cdd:cd01385 314 EAIATRDAMAKCLYSALFDWIVLRINHALLNKKdleeAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 512 VLEQEEYKKEGIEWEFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKATDVTFKAKlYDNHLGKSNNFQKPRnlkgRP 590
Cdd:cd01385 394 KLEQEEYKKEGISWHNIEY-TDNTGCLQLISkKPTGLLCLLDEESNFPGATNQTLLAK-FKQQHKDNKYYEKPQ----VM 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 591 EAHFALVHYAGTVDYNINGWLVKNKDPLNETVVGLYQKSAL-----------------KLLAHLF-ANYASAES------ 646
Cdd:cd01385 468 EPAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSafvreligidpvavfrwAVLRAFFrAMAAFREAgrrraq 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 647 ----------DQATKGKGSKKKGSSFQTVSALHRENLNKLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGV 716
Cdd:cd01385 548 rtaghsltlhDRTTKSLLHLHKKKKPPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTGM 627
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1072253241 717 LEGIRICRKGYPNRILYGDFRQRYRILnpaaIPEGQfIDSRKGAEKLLASLEMDHTQYKFGHTKVFFK 784
Cdd:cd01385 628 LETVRIRRSGYSVRYTFQEFITQFQVL----LPKGL-ISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
122-784 |
3.92e-150 |
|
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: 479.64 E-value: 3.92e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 122 LKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRG--KKRSEAPPHIFSISDNAYQYMLTDR----DNQSILIT 194
Cdd:cd14892 7 LRRRYERDAIYTFTADILISINPYKSIPlLYDVPGFDSQRKeeATASSPPPHVFSIAERAYRAMKGVGkgqgTPQSIVVS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 195 GESGAGKTVNTKRVIQYFAVIAAIG-DRKKDSGPTGKGT-LEDQIIQANPALEAFGNAKTLRNDNSSRFGKFIRIHFGAT 272
Cdd:cd14892 87 GESGAGKTEASKYIMKYLATASKLAkGASTSKGAANAHEsIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQIHYNSD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 273 GKLASADIETYLLEKSRVIFQLKSERDYHIFYQILSNKKpELLDMLLVTNNPYDYAYISQGE-TTVASIDDAEELLATDS 351
Cdd:cd14892 167 GRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLD-ANENAALELTPAESFLFLNQGNcVEVDGVDDATEFKQLRD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 352 AFDVLGFTQDEKNSIYKLTGAVMHFGNMKFKQ--KQREEQAEPDGTEEADKVAYLMGLNSADLLKGLC-----HPRVKVG 424
Cdd:cd14892 246 AMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEEnaDDEDVFAQSADGVNVAKAAGLLGVDAAELMFKLVtqttsTARGSVL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 425 NEYVTKGQNVQqvyySTGALGKSVYEKMFLWMVVRIN----------TTLETKQPRQYFIGVLDIAGFEIFDFNSFEQMC 494
Cdd:cd14892 326 EIKLTAREAKN----ALDALCKYLYGELFDWLISRINachkqqtsgvTGGAASPTFSPFIGILDIFGFEIMPTNSFEQLC 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 495 INFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLIEK-PMGIMSILEEECMFP-KATDVTFKAKLYDN 572
Cdd:cd14892 402 INFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEF-QDNQDCLDLIQKkPLGLLPLLEEQMLLKrKTTDKQLLTIYHQT 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 573 HLGKSNNFQKPRNlkgrPEAHFALVHYAGTVDYNINGWLVKNKDPLNETVVGLYQKSalkllahlfanyasaesdqatkg 652
Cdd:cd14892 481 HLDKHPHYAKPRF----ECDEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSS----------------------- 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 653 kgskkkgSSFqtvsalhRENLNKLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRKGYPNRIL 732
Cdd:cd14892 534 -------SKF-------RTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREGFPIRRQ 599
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1072253241 733 YGDFRQRYRIL-----NPAAIPEGQ--FIDSRKGAEKLLASLEMDHTQykFGHTKVFFK 784
Cdd:cd14892 600 FEEFYEKFWPLarnkaGVAASPDACdaTTARKKCEEIVARALERENFQ--LGRTKVFLR 656
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
117-784 |
2.10e-149 |
|
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: 477.36 E-value: 2.10e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 117 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRDNQSILITG 195
Cdd:cd14873 2 SIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 196 ESGAGKTVNTKRVIQYFAVIAaigDRKKDSGPTGKGT-LEDQIIQANPALEAFGNAKTLRNDNSSRFGKFIRIHFGATGK 274
Cdd:cd14873 82 ESGAGKTESTKLILKFLSVIS---QQSLELSLKEKTScVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 275 LASADIETYLLEKSRVIFQLKSERDYHIFYQILSNKKPELLDMLLVTnNPYDYAYISQ-GETTVASIDDAEELLATDSAF 353
Cdd:cd14873 159 IQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLS-TPENYHYLNQsGCVEDKTISDQESFREVITAM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 354 DVLGFTQDEKNSIYKLTGAVMHFGNMKFKQKQREEQAEPDGTEEAdkvAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQN 433
Cdd:cd14873 238 EVMQFSKEEVREVSRLLAGILHLGNIEFITAGGAQVSFKTALGRS---AELLGLDPTQLTDALTQRSMFLRGEEILTPLN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 434 VQQVYYSTGALGKSVYEKMFLWMVVRINTTLETKQPRQyFIGVLDIAGFEIFDFNSFEQMCINFTNEKLQQFFNHHMFVL 513
Cdd:cd14873 315 VQQAVDSRDSLAMALYARCFEWVIKKINSRIKGKEDFK-SIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 514 EQEEYKKEGIEWEFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKATDVTFKAKLYDNHlgkSNN--FQKPRnlkgRPE 591
Cdd:cd14873 394 EQLEYSREGLVWEDIDW-IDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQH---ANNhfYVKPR----VAV 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 592 AHFALVHYAGTVDYNINGWLVKNKDPLNETVVGLYQKSALKLLAHLFANYASAESDQATKGKGSKKKgssfQTVSALHRE 671
Cdd:cd14873 466 NNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSRNNQDTLKCGSKHRR----PTVSSQFKD 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 672 NLNKLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRKGYPNRILYGDFRQRYRILNP-AAIPE 750
Cdd:cd14873 542 SLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRnLALPE 621
|
650 660 670
....*....|....*....|....*....|....
gi 1072253241 751 gqfiDSRKGAEKLLASLEMDHTQYKFGHTKVFFK 784
Cdd:cd14873 622 ----DVRGKCTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
118-784 |
4.72e-146 |
|
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: 467.25 E-value: 4.72e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 118 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKK-RSEAPPHIFSISDNAYQYMLTDRDNQSILITGE 196
Cdd:cd14897 3 IVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVSGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 197 SGAGKTVNTKRVIQYFAVIAaigdrkkdsgPTGKGTLEDQIIQANPALEAFGNAKTLRNDNSSRFGKFIRIHFGATGKLA 276
Cdd:cd14897 83 SGAGKTESTKYMIKHLMKLS----------PSDDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 277 SADIETYLLEKSRVIFQLKSERDYHIFYQILSNKKPELLDMLLVtNNPYDYAYISQGETTVASIDDAEELLATDSAFDVL 356
Cdd:cd14897 153 GAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFL-EDPDCHRILRDDNRNRPVFNDSEELEYYRQMFHDL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 357 -------GFTQDEKNSIYKLTGAVMHFGNMKFkqkqrEEQAEPDGTEEADK-----VAYLMGLNSADLLKGLCHPRVKVG 424
Cdd:cd14897 232 tnimkliGFSEEDISVIFTILAAILHLTNIVF-----IPDEDTDGVTVADEyplhaVAKLLGIDEVELTEALISNVNTIR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 425 NEYVTKGQNVQQVYYSTGALGKSVYEKMFLWMVVRINTTLETKQPRQYF-----IGVLDIAGFEIFDFNSFEQMCINFTN 499
Cdd:cd14897 307 GERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDFQIMtrgpsIGILDMSGFENFKINSFDQLCINLSN 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 500 EKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLI-EKPMGIMSILEEECMFPKATDVTFKAKLyDNHLGKSN 578
Cdd:cd14897 387 ERLQQYFNDYVFPRERSEYEIEGIEWRDIEY-HDNDDVLELFfKKPLGILPLLDEESTFPQSTDSSLVQKL-NKYCGESP 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 579 NFQKPrnLKGRPEahFALVHYAGTVDYNINGWLVKNKDPLNETVVGLYQKSALKLLAHLFANYasaesdqatkgkgskkk 658
Cdd:cd14897 465 RYVAS--PGNRVA--FGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFTSY----------------- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 659 gssfqtvsalHRENLNKLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRKGYPNRILYGDFRQ 738
Cdd:cd14897 524 ----------FKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVK 593
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1072253241 739 RYRILNP-----AAIPEGQFIDSRKGAekllaslemDHTQYKFGHTKVFFK 784
Cdd:cd14897 594 RYKEICDfsnkvRSDDLGKCQKILKTA---------GIKGYQFGKTKVFLK 635
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
116-784 |
1.37e-145 |
|
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: 466.73 E-value: 1.37e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 116 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRDNQSILIT 194
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 195 GESGAGKTVNTKRVIQYFAVIAaiGDRKKDSgptgkgtlEDQIIQANPALEAFGNAKTLRNDNSSRFGKFIRIHFGATGK 274
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVA--GGRKDKT--------IAKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 275 LASADIETYLLEKSRVIFQLKSERDYHIFYQILSN-KKPELLDMLLVTNNPYDYAYISQGETTVASIDDAEELLATDSAF 353
Cdd:cd14904 151 LIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGlSSEERKEFGLDPNCQYQYLGDSLAQMQIPGLDDAKLFASTQKSL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 354 DVLGFTQDEKNSIYKLTGAVMHFGNMKFkQKQREEQAEPDGTEEADKVAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQN 433
Cdd:cd14904 231 SLIGLDNDAQRTLFKILSGVLHLGEVMF-DKSDENGSRISNGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 434 VQQVYYSTGALGKSVYEKMFLWMVVRINTTLETKQPRQY-FIGVLDIAGFEIFDFNSFEQMCINFTNEKLQQFFNHHMFV 512
Cdd:cd14904 310 PVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKgQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 513 LEQEEYKKEGIEWEFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKATDVTFKAKLYDNH--LGKSNNFQKPRNLKgrp 590
Cdd:cd14904 390 TVEEEYIREGLQWDHIEY-QDNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHqtKKDNESIDFPKVKR--- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 591 eAHFALVHYAGTVDYNINGWLVKNKDPLNETVVGLYQKSALKLLAHLFanyASAESDQATKGKGSKKKGSSFQTVSALHR 670
Cdd:cd14904 466 -TQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELF---GSSEAPSETKEGKSGKGTKAPKSLGSQFK 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 671 ENLNKLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRKGYPNRILYGDFRQRYRILNPAAIPE 750
Cdd:cd14904 542 TSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFPPSMHS 621
|
650 660 670
....*....|....*....|....*....|....*
gi 1072253241 751 GqfiDSRKGAEKLLASL-EMDHTQYKFGHTKVFFK 784
Cdd:cd14904 622 K---DVRRTCSVFMTAIgRKSPLEYQIGKSLIYFK 653
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
118-749 |
4.21e-139 |
|
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: 447.83 E-value: 4.21e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 118 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAY-----------RGKKRSEAPPHIFSISDNAYQYM--- 182
Cdd:cd14900 3 ILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMmlg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 183 -LTDRDNQSILITGESGAGKTVNTKRVIQYFAVIAAIGDRKKDSGPTGKGTLEDQIIQANPALEAFGNAKTLRNDNSSRF 261
Cdd:cd14900 83 lNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAGDNNLAASVSMGKSTSGIAAKVLQTNILLESFGNARTLRNDNSSRF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 262 GKFIRIHFGATGKLASADIETYLLEKSRVIFQLKSERDYHIFYQILSNKKPELLdmllvtnnpydyayisqgettvaSID 341
Cdd:cd14900 163 GKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAAR-----------------------KRD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 342 DAEELLAtdsAFDVLGFTQDEKNSIYKLTGAVMHFGNMKFKQKQREEQAEPDGTEEA-------DKVAYLMGLNSADLLK 414
Cdd:cd14900 220 MYRRVMD---AMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSDLApssiwsrDAAATLLSVDATKLEK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 415 GLCHPRVKVGNEYVTKGQNVQQVYYSTGALGKSVYEKMFLWMVVRINTTL-----ETKQPRQYFIGVLDIAGFEIFDFNS 489
Cdd:cd14900 297 ALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmddsSKSHGGLHFIGILDIFGFEVFPKNS 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 490 FEQMCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLI-EKPMGIMSILEEECMFPKATDVTFKAK 568
Cdd:cd14900 377 FEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEF-CDNQDCVNLIsQRPTGILSLIDEECVMPKGSDTTLASK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 569 LYdNHLGKSNNFQKPRNLKGRpeAHFALVHYAGTVDYNINGWLVKNKDPLNETVVGLYQKSAlkllahlfanyasaesdq 648
Cdd:cd14900 456 LY-RACGSHPRFSASRIQRAR--GLFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDLFVYGL------------------ 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 649 atkgkgskkkgsSFqtvsalhRENLNKLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRKGYP 728
Cdd:cd14900 515 ------------QF-------KEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVARAGFP 575
|
650 660
....*....|....*....|.
gi 1072253241 729 NRILYGDFRQRYRILNPAAIP 749
Cdd:cd14900 576 IRLLHDEFVARYFSLARAKNR 596
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
116-784 |
9.26e-137 |
|
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: 441.79 E-value: 9.26e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 116 PAVLYNLKERYAA--WMIYTYSGLFCVTVNPYKWLPvyNAEVvAAYRGKKRSEAPPHIFSISDNAYQYMLTDRD---NQS 190
Cdd:cd14891 1 AGILHNLEERSKLdnQRPYTFMANVLIAVNPLRRLP--EPDK-SDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqNQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 191 ILITGESGAGKTVNTKRVIQYFAVIAAIGDRKK--------DSGPTGKGTLEDQIIQANPALEAFGNAKTLRNDNSSRFG 262
Cdd:cd14891 78 IVISGESGAGKTETSKIILRFLTTRAVGGKKASgqdieqssKKRKLSVTSLDERLMDTNPILESFGNAKTLRNHNSSRFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 263 KFIRIHFGATG-KLASADIETYLLEKSRVIFQLKSERDYHIFYQILSNKKPELLDMLLVTnNPYDYAYISQ-GETTVASI 340
Cdd:cd14891 158 KFMKLQFTKDKfKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLL-SPEDFIYLNQsGCVSDDNI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 341 DDAEELLATDSAFDVLGFTQDEKNSIYKLTGAVMHFGNMKFKQKQREE----QAEPDGTEEADKVAYLMGLNSADLLKGL 416
Cdd:cd14891 237 DDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSEgeaeIASESDKEALATAAELLGVDEEALEKVI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 417 CHPRVKVGNEYVTKGQNVQQVYYSTGALGKSVYEKMFLWMVVRINTTLETKQPRQYFIGVLDIAGFEIFD-FNSFEQMCI 495
Cdd:cd14891 317 TQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFEtKNDFEQLLI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 496 NFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLQACIDLI-EKPMGIMSILEEECMFPKATDVTFKAKLYDNHl 574
Cdd:cd14891 397 NYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIaSKPNGILPLLDNEARNPNPSDAKLNETLHKTH- 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 575 GKSNNF--QKPRNLKgrpeAHFALVHYAGTVDYNINGWLVKNKDPLNETvvglyqksalklLAHLFANyASAESDQatkg 652
Cdd:cd14891 475 KRHPCFprPHPKDMR----EMFIVKHYAGTVSYTIGSFIDKNNDIIPED------------FEDLLAS-SAKFSDQ---- 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 653 kgskkkgssfqtvsalhrenLNKLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRKGYPNRIL 732
Cdd:cd14891 534 --------------------MQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRVT 593
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 1072253241 733 YGDFRQRYRILNPAAI------PEGQFIdsrkgaEKLLASLEMDHTQYKFGHTKVFFK 784
Cdd:cd14891 594 YAELVDVYKPVLPPSVtrlfaeNDRTLT------QAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
118-784 |
2.32e-136 |
|
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: 441.27 E-value: 2.32e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 118 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYML----TDRDNQSILI 193
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 194 TGESGAGKTVNTKRVIQYFAVIAaigdrkkdsgpTGKGTLEDQIIQANPALEAFGNAKTLRNDNSSRFGKFIRIHFgATG 273
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELC-----------RGNSQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RNG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 274 KLASADIETYLLEKSRVIFQLKSERDYHIFYQI---LSNKKPELLDMLlvtnNPYDYAYISQG---ETTVASIDDAEELL 347
Cdd:cd14889 151 HVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMfagISAEDRENYGLL----DPGKYRYLNNGagcKREVQYWKKKYDEV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 348 AtdSAFDVLGFTQDEKNSIYKLTGAVMHFGNMKFKQKQREE-QAEPDGTEEADKVAYLMGLNSADLLKGLCHPRVKVGNE 426
Cdd:cd14889 227 C--NAMDMVGFTEQEEVDMFTILAGILSLGNITFEMDDDEAlKVENDSNGWLKAAAGQFGVSEEDLLKTLTCTVTFTRGE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 427 YVTKGQNVQQVYYSTGALGKSVYEKMFLWMVVRINTTLETKQPRQY---FIGVLDIAGFEIFDFNSFEQMCINFTNEKLQ 503
Cdd:cd14889 305 QIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSVelrEIGILDIFGFENFAVNRFEQACINLANEQLQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 504 QFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDL-IEKPMGIMSILEEECMFPKATDVTFKAKLyDNHLGKSNNFQK 582
Cdd:cd14889 385 YFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLfLNKPIGILSLLDEQSHFPQATDESFVDKL-NIHFKGNSYYGK 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 583 PRNlkgrPEAHFALVHYAGTVDYNINGWLVKNKDPLNETVVGLYQKSALKLLAHLFANYASAESDQATKGKGSKKKGSSF 662
Cdd:cd14889 463 SRS----KSPKFTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTATRSRTGTLMPRAKLPQAGSDNF 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 663 -----QTVSALHRENLNKLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRKGYPNRILYGDFR 737
Cdd:cd14889 539 nstrkQSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFA 618
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1072253241 738 QRYRIL-NPAAIPegqfiDSRKGAEKLLASLEMdhTQYKFGHTKVFFK 784
Cdd:cd14889 619 ERYKILlCEPALP-----GTKQSCLRILKATKL--VGWKCGKTRLFFK 659
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
118-784 |
2.84e-136 |
|
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: 441.39 E-value: 2.84e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 118 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGK--------KRSEAPPHIFSISDNAYQYMLTDRDN 188
Cdd:cd14907 3 LLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQiiqngeyfDIKKEPPHIYAIAALAFKQLFENNKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 189 QSILITGESGAGKTVNTKRVIQYFAVIAA-------IGDRKKDSGPTGKGT--LEDQIIQANPALEAFGNAKTLRNDNSS 259
Cdd:cd14907 83 QAIVISGESGAGKTENAKYAMKFLTQLSQqeqnseeVLTLTSSIRATSKSTksIEQKILSCNPILEAFGNAKTVRNDNSS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 260 RFGKFIRIHFG-ATGKLASADIETYLLEKSRVIFQLKSERDYHIFYQILSNKKPELLDMLLVTNNP--YDYAYISQGET- 335
Cdd:cd14907 163 RFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNQLsgDRYDYLKKSNCy 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 336 TVASIDDAEELLATDSAFDVLGFTQDEKNSIYKLTGAVMHFGNMKFKQKQ--REEQAEPDGTEEADKVAYLMGLNSADLL 413
Cdd:cd14907 243 EVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTldDNSPCCVKNKETLQIIAKLLGIDEEELK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 414 KGLCHPRVKVGNEYVTKGQNVQQVYYSTGALGKSVYEKMFLWMVVRINTTL--------ETKQPRQYFIGVLDIAGFEIF 485
Cdd:cd14907 323 EALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdqQLFQNKYLSIGLLDIFGFEVF 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 486 DFNSFEQMCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEF--IDFgMDLQACIDLIEK-PMGIMSILEEECMFPKATD 562
Cdd:cd14907 403 QNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSY-TDNQDVIDLLDKpPIGIFNLLDDSCKLATGTD 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 563 VTFKAKLYDNHlGKSNNFQKPRNLKgrpEAHFALVHYAGTVDYNINGWLVKNKDPLNETVVGLYQKSALKLLAHLFANYA 642
Cdd:cd14907 482 EKLLNKIKKQH-KNNSKLIFPNKIN---KDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFSGED 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 643 SAESDQATKGKGSKKKGssfQTVSALHRENLNKLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRI 722
Cdd:cd14907 558 GSQQQNQSKQKKSQKKD---KFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLESIRV 634
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1072253241 723 CRKGYPNRILYGDFRQRYRILNpaaipegqfidsrkgaekllaslemdhTQYKFGHTKVFFK 784
Cdd:cd14907 635 RKQGYPYRKSYEDFYKQYSLLK---------------------------KNVLFGKTKIFMK 669
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
116-745 |
3.58e-133 |
|
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: 433.18 E-value: 3.58e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 116 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYR--GKKRS---EAP----PHIFSISDNAYQYMLTD- 185
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSqgiESPqalgPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 186 RDNQSILITGESGAGKTVNTKRVIQYFAVIAAIGDR-KKDSGPTGKGTLEDQIIQANPALEAFGNAKTLRNDNSSRFGKF 264
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGaPNEGEELGKLSIMDRVLQSNPILEAFGNARTLRNDNSSRFGKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 265 IRIHFGATGKLASADIETYLLEKSRVIFQLKSERDYHIFYQIL------SNKKPELLDMLLVTNN-PYDYAYISQGET-T 336
Cdd:cd14908 161 IELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLrggdeeEHEKYEFHDGITGGLQlPNEFHYTGQGGApD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 337 VASIDDAEELLATDSAFDVLGFTQDEKNSIYKLTGAVMHFGNMKFKQKQREEQAEPDGTEEADKVAY---LMGLNSADLL 413
Cdd:cd14908 241 LREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEEGNEKCLARvakLLGVDVDKLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 414 KGLCHPRVKVGNEYVTKGQNVQQVYYSTGALGKSVYEKMFLWMVVRINTTL--ETKQPRQYFIGVLDIAGFEIFDFNSFE 491
Cdd:cd14908 321 RALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSInwENDKDIRSSVGVLDIFGFECFAHNSFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 492 QMCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLQACIDLIE-KPMGIMSILEEECMFP-KATDVTFKAKL 569
Cdd:cd14908 401 QLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQaKKKGILTMLDDECRLGiRGSDANYASRL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 570 YDNHLGKSNN-------FQKPRNLKGRpeAHFALVHYAGTVDYNI-NGWLVKNKDPLNETVVGLYqksalkllahlfany 641
Cdd:cd14908 480 YETYLPEKNQthsentrFEATSIQKTK--LIFAVRHFAGQVQYTVeTTFCEKNKDEIPLTADSLF--------------- 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 642 asAESDQatkgkgskkkgssfqtvsalHRENLNKLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIR 721
Cdd:cd14908 543 --ESGQQ--------------------FKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAVR 600
|
650 660
....*....|....*....|....
gi 1072253241 722 ICRKGYPNRILYGDFRQRYRILNP 745
Cdd:cd14908 601 VARSGYPVRLPHKDFFKRYRMLLP 624
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
116-745 |
4.37e-131 |
|
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: 428.54 E-value: 4.37e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 116 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYR--------GKKRSEAPPHIFSISDNAYQYML-TD 185
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLkPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 186 RDNQSILITGESGAGKTVNTKRVIQYFAVIAAIGDRKKDSGpTGKGTLEDQIIQANPALEAFGNAKTLRNDNSSRFGKFI 265
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGRDQSSTEQEG-SDAVEIGKRILQTNPILESFGNAQTIRNDNSSRFGKFI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 266 RIHFGATGKLASADIETYLLEKSRVIFQLKSERDYHIFYQILSNKKPELLDmLLVTNNPYDYAYISQGETTVA-----SI 340
Cdd:cd14902 160 KIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLD-LLGLQKGGKYELLNSYGPSFArkravAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 341 DDAEELLATDSAFDVLGFTQDEKNSIYKLTGAVMHFGNMKFKQKQREEQAEPDGTEEA---DKVAYLMGLNSADLLKGLC 417
Cdd:cd14902 239 KYAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAVTAASRfhlAKCAELMGVDVDKLETLLS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 418 HPRVKVGNEYVTKGQNVQQVYYSTGALGKSVYEKMFLWMVVRINTTL-------ETKQPRQYF--IGVLDIAGFEIFDFN 488
Cdd:cd14902 319 SREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEInyfdsavSISDEDEELatIGILDIFGFESLNRN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 489 SFEQMCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLqACIDLIE-KPMGIMSILEEECMFPKATDVTFKA 567
Cdd:cd14902 399 GFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYPSNA-ACLALFDdKSNGLFSLLDQECLMPKGSNQALST 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 568 KLYDNHLgksnnfqkprnlkgrPEAHFALVHYAGTVDYNINGWLVKNKDPLNETVVGLYQKSALKLLAHLFANyASAESD 647
Cdd:cd14902 478 KFYRYHG---------------GLGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGAD-ENRDSP 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 648 QATKGKGSKKKGSSFQT--VSALHRENLNKLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRK 725
Cdd:cd14902 542 GADNGAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRIARH 621
|
650 660
....*....|....*....|
gi 1072253241 726 GYPNRILYGDFRQRYRILNP 745
Cdd:cd14902 622 GYSVRLAHASFIELFSGFKC 641
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
94-837 |
1.04e-125 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 416.74 E-value: 1.04e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 94 MQQNPPKFDkieDMAMLTFLNEPAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYR-GKKRSEAPPHIF 172
Cdd:PTZ00014 91 SQIDPMTYG---DIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRdAKDSDKLPPHVF 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 173 SISDNAYQYMLTDRDNQSILITGESGAGKTVNTKRVIQYFAviaaigdrkkdSGPTGKGTLEDQ--IIQANPALEAFGNA 250
Cdd:PTZ00014 168 TTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFA-----------SSKSGNMDLKIQnaIMAANPVLEAFGNA 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 251 KTLRNDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKSERDYHIFYQILSNKKPELLDMLLVTNNPyDYAYI 330
Cdd:PTZ00014 237 KTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLE-EYKYI 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 331 SQGETTVASIDDAEELLATDSAFDVLGFTQDEKNSIYKLTGAVMHFGNMKFKQKQREEQAE-----PDGTEEADKVAYLM 405
Cdd:PTZ00014 316 NPKCLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEGGLTDaaaisDESLEVFNEACELL 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 406 GLNSADLLKGLCHPRVKVGNEYVTKGQNVQQVYYSTGALGKSVYEKMFLWMVVRINTTLETKQPRQYFIGVLDIAGFEIF 485
Cdd:PTZ00014 396 FLDYESLKKELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKVFIGMLDIFGFEVF 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 486 DFNSFEQMCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDVTF 565
Cdd:PTZ00014 476 KNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGKSVLSILEDQCLAPGGTDEKF 555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 566 KAKLYDNHlgKSNNFQKPRnlKGRPEAHFALVHYAGTVDYNINGWLVKNKDPLNETVVGLYQKSALKLLAHLFanyasaE 645
Cdd:PTZ00014 556 VSSCNTNL--KNNPKYKPA--KVDSNKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLF------E 625
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 646 SDQATKGKGSKKKGSSFQTVsalhrENLNKLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRK 725
Cdd:PTZ00014 626 GVEVEKGKLAKGQLIGSQFL-----NQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQL 700
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 726 GYPNRILYGDFRQRYRILNpAAIPEGQFIDSRKGAEKLLASLEMDHTQYKFGHTKVFFKAGLLGQLEEMRDERLSRIITR 805
Cdd:PTZ00014 701 GFSYRRTFAEFLSQFKYLD-LAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLKKDAAKELTQIQREKLAAWEPL 779
|
730 740 750
....*....|....*....|....*....|...
gi 1072253241 806 IQAQSrGALSRIEFKKIVERRDALLV-IQWNIR 837
Cdd:PTZ00014 780 VSVLE-ALILKIKKKRKVRKNIKSLVrIQAHLR 811
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
116-784 |
7.27e-123 |
|
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: 402.62 E-value: 7.27e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 116 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRDNQSILITG 195
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 196 ESGAGKTVNTKRVIQYfavIAAIGDRKKdsgptgkgtlEDQIIQAN---PALEAFGNAKTLRNDNSSRFGKFIRIHFgAT 272
Cdd:cd14896 81 HSGSGKTEAAKKIVQF---LSSLYQDQT----------EDRLRQPEdvlPILESFGHAKTILNANASRFGQVLRLHL-QH 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 273 GKLASADIETYLLEKSRVIFQLKSERDYHIFYQILSNKKPELLDMLLVtNNPYDYAYISQGET-TVASIDDAEELLATDS 351
Cdd:cd14896 147 GVIVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSL-QGPETYYYLNQGGAcRLQGKEDAQDFEGLLK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 352 AFDVLGFTQDEKNSIYKLTGAVMHFGNMKFKQKQRE--EQAEPDGTEEADKVAYLMGLnSADLLKGLCHPRVKVGN-EYV 428
Cdd:cd14896 226 ALQGLGLCAEELTAIWAVLAAILQLGNICFSSSEREsqEVAAVSSWAEIHTAARLLQV-PPERLEGAVTHRVTETPyGRV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 429 TKGQNVQQVYYSTGALGKSVYEKMFLWMVVRINTTLETKQPRQYF--IGVLDIAGFEIFDFNSFEQMCINFTNEKLQQFF 506
Cdd:cd14896 305 SRPLPVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESDatIGVVDAYGFEALRVNGLEQLCINLASERLQLFS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 507 NHHMFVLEQEEYKKEGIEWEFIDfGMDLQACIDLI-EKPMGIMSILEEECMFPKATDVTFKAKLYDNHlGKSNNFQKPRN 585
Cdd:cd14896 385 SQTLLAQEEEECQRELLPWVPIP-QPPRESCLDLLvDQPHSLLSILDDQTWLSQATDHTFLQKCHYHH-GDHPSYAKPQL 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 586 lkgrPEAHFALVHYAGTVDYNINGWLVKNKDPLNETVVGLYQKSALKLLAHLFanyASAEsDQATKGKGSKKKGSSFQtv 665
Cdd:cd14896 463 ----PLPVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLF---QEAE-PQYGLGQGKPTLASRFQ-- 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 666 salhrENLNKLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRKGYPNRILYGDFRQRYRILNP 745
Cdd:cd14896 533 -----QSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALGS 607
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1072253241 746 AAIPEgqfIDSRKGAEKLLASLEMDHTQ-YKFGHTKVFFK 784
Cdd:cd14896 608 ERQEA---LSDRERCGAILSQVLGAESPlYHLGATKVLLK 644
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
116-784 |
4.12e-122 |
|
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: 402.79 E-value: 4.12e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 116 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNaevVAAYRGK--KRSEAPPHIFSISDNAYQYMLT-------D 185
Cdd:cd14895 1 PAFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIPgLYD---LHKYREEmpGWTALPPHVFSIAEGAYRSLRRrlhepgaS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 186 RDNQSILITGESGAGKTVNTKRVIQYFAVIAAIGDRKKDSgPTGKGTLEDQIIQANPALEAFGNAKTLRNDNSSRFGKFI 265
Cdd:cd14895 78 KKNQTILVSGESGAGKTETTKFIMNYLAESSKHTTATSSS-KRRRAISGSELLSANPILESFGNARTLRNDNSSRFGKFV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 266 RIHFG-----ATGKLASADIETYLLEKSRVIFQLKSERDYHIFYQILSNKKPELLDML-LVTNNPYDYAYISQGETTVAS 339
Cdd:cd14895 157 RMFFEgheldTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELqLELLSAQEFQYISGGQCYQRN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 340 --IDDAEELLATDSAFDVLGFTQDEKNSIYKLTGAVMHFGNMKFKQKQREEQAEPDGT------------------EEAD 399
Cdd:cd14895 237 dgVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEGEEDNGAasapcrlasaspssltvqQHLD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 400 KVAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQVYYSTGALGKSVYEKMFLWMVVRINTTLETKQPRQY------- 472
Cdd:cd14895 317 IVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQFALNpnkaank 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 473 ----FIGVLDIAGFEIFDFNSFEQMCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLQACIDLIE-KPMGI 547
Cdd:cd14895 397 dttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYE-DNSVCLEMLEqRPSGI 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 548 MSILEEECMFPKATDVTFKAKLYdNHLGKSNNFQKPRnlKGRPEAHFALVHYAGTVDYNINGWLVKNKDPLNETVVGLYQ 627
Cdd:cd14895 476 FSLLDEECVVPKGSDAGFARKLY-QRLQEHSNFSASR--TDQADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAELFSVLG 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 628 KSALKLLAHLFANYASAESDQATKGKGSKKKGSSFQT---VSALHRENLNKLMTNLRATHPHFVRCIIPNETKSPGMMDN 704
Cdd:cd14895 553 KTSDAHLRELFEFFKASESAELSLGQPKLRRRSSVLSsvgIGSQFKQQLASLLDVVQQTQTHYIRCIKPNDESASDQFDM 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 705 RLVMHQLRCNGVLEGIRICRKGYPNRILYGDFRQRYRILNPAAIPegqfidSRKGAEKLLASLEMDHTQykFGHTKVFFK 784
Cdd:cd14895 633 AKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKNA------SDATASALIETLKVDHAE--LGKTRVFLR 704
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
116-784 |
1.09e-116 |
|
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: 385.50 E-value: 1.09e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 116 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRG-KKRSEAPPHIFSIS----DNAYQYmltdRDNQS 190
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDaPDLTKLPPHVFYTArralENLHGV----NKSQT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 191 ILITGESGAGKTVNTKRVIQYFAviaaigdrkkdSGPTGKGTLEDQ--IIQANPALEAFGNAKTLRNDNSSRFGKFIRIH 268
Cdd:cd14876 77 IIVSGESGAGKTEATKQIMRYFA-----------SAKSGNMDLRIQtaIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 269 FGATGKLASADIETYLLEKSRVIFQLKSERDYHIFYQILSNKKPELLD--MLLVTNnpyDYAYISQGETTVASIDDAEEL 346
Cdd:cd14876 146 VASEGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSkyHLLGLK---EYKFLNPKCLDVPGIDDVADF 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 347 LATDSAFDVLGFTQDEKNSIYKLTGAVMHFGNMKFKQKQREEQ-----AEPDGTEEADKVAYLMGLNSADLLKGLCHPRV 421
Cdd:cd14876 223 EEVLESLKSMGLTEEQIDTVFSIVSGVLLLGNVKITGKTEQGVddaaaISNESLEVFKEACSLLFLDPEALKRELTVKVT 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 422 KVGNEYVTKGQNVQQVYYSTGALGKSVYEKMFLWMVVRINTTLETKQPRQYFIGVLDIAGFEIFDFNSFEQMCINFTNEK 501
Cdd:cd14876 303 KAGGQEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLFINITNEM 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 502 LQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDVTFKAKLYDNHlgKSNNFQ 581
Cdd:cd14876 383 LQKNFIDIVFERESKLYKDEGIPTAELEYTSNAEVIDVLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSKL--KSNGKF 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 582 KPrnLKGRPEAHFALVHYAGTVDYNINGWLVKNKDPLNETVVGLYQKSALKLLAHLFANYASAESDQATKgkgskkkgss 661
Cdd:cd14876 461 KP--AKVDSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVVVEKGKIAKG---------- 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 662 fQTVSALHRENLNKLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRKGYPNRILYGDFRQRYR 741
Cdd:cd14876 529 -SLIGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFK 607
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1072253241 742 ILNPaAIPEGQFIDSRKGAEKLLASLEMDHTQYKFGHTKVFFK 784
Cdd:cd14876 608 FLDL-GIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVFLK 649
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
118-782 |
4.57e-109 |
|
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: 363.79 E-value: 4.57e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 118 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRSEA-PPHIFSISDNAYQYMLTDRD--NQSILI 193
Cdd:cd14880 3 VLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQPQKlKPHIFTVGEQTYRNVKSLIEpvNQSIVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 194 TGESGAGKTVNTKRVIQYFAVIAAigdrkKDSGPTGKGT---LEDQIIQANPALEAFGNAKTLRNDNSSRFGKFIRIHFG 270
Cdd:cd14880 83 SGESGAGKTWTSRCLMKFYAVVAA-----SPTSWESHKIaerIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 271 ATGKLASADIETYLLEKSRVIFQLKSERDYHIFYQILsnkKPELLDMLLVTNNP--YDYAYISQGETTVASiDDAEellA 348
Cdd:cd14880 158 RAQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQIC---KGASADERLQWHLPegAAFSWLPNPERNLEE-DCFE---V 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 349 TDSAFDVLGFTQDEKNSIYKLTGAVMHFGNMKFKQKQREEQAEP--DGTEEADKV-AYLMGLNSADLLKGLCHPRVKVGN 425
Cdd:cd14880 231 TREAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQpmDDTKESVRTsALLLKLPEDHLLETLQIRTIRAGK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 426 EYVTKGQNVQQVYYST--GALGKSVYEKMFLWMVVRINTTLETKQPR-QYFIGVLDIAGFEIFDFNSFEQMCINFTNEKL 502
Cdd:cd14880 311 QQQVFKKPCSRAECDTrrDCLAKLIYARLFDWLVSVINSSICADTDSwTTFIGLLDVYGFESFPENSLEQLCINYANEKL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 503 QQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKATDVTFKAKLYDNHLgkSNNFQ 581
Cdd:cd14880 391 QQHFVAHYLRAQQEEYAVEGLEWSFINY-QDNQTCLDLIEgSPISICSLINEECRLNRPSSAAQLQTRIESAL--AGNPC 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 582 KPRNlKGRPEAHFALVHYAGTVDYNINGWLVKNKDPLNETVVGLYQKSALKLLAHLFanyaSAESDQATKGKGSKKKGSS 661
Cdd:cd14880 468 LGHN-KLSREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLF----PANPEEKTQEEPSGQSRAP 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 662 FQTVSALHRENLNKLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRKGYPNRILYGDFRQRYR 741
Cdd:cd14880 543 VLTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYK 622
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1072253241 742 IL---NPAAIPEGQFIDSRKGAEKLLASlemdhtqykfGHTKVF 782
Cdd:cd14880 623 LLrrlRPHTSSGPHSPYPAKGLSEPVHC----------GRTKVF 656
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
117-741 |
5.01e-106 |
|
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: 357.10 E-value: 5.01e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 117 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYR-------GKKRSEA---PPHIFSISDNAYQYMLTD 185
Cdd:cd14899 2 SILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYAydhnsqfGDRVTSTdprEPHLFAVARAAYIDIVQN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 186 RDNQSILITGESGAGKTVNTKRVIQYFAVIAAIGDRKKDSGPTG-------KGTLEDQIIQANPALEAFGNAKTLRNDNS 258
Cdd:cd14899 82 GRSQSILISGESGAGKTEATKIIMTYFAVHCGTGNNNLTNSESIsppaspsRTTIEEQVLQSNPILEAFGNARTVRNDNS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 259 SRFGKFIRIHF-GATGKLASADIETYLLEKSRVIFQLKSERDYHIFYQILSNK----KPELLDMLLVTNNPYDYAYISQG 333
Cdd:cd14899 162 SRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSADnncvSKEQKQVLALSGGPQSFRLLNQS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 334 ETTVA--SIDDAEELLATDSAFDVLGFTQDEKNSIYKLTGAVMHFGNMKFKQ--KQREEQAEPDGTEEA----------D 399
Cdd:cd14899 242 LCSKRrdGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQipHKGDDTVFADEARVMssttgafdhfT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 400 KVAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQVYYSTGALGKSVYEKMFLWMVVRINTTLETKQPRQY------- 472
Cdd:cd14899 322 KAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQASAPWgadesdv 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 473 --------FIGVLDIAGFEIFDFNSFEQMCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDlQACIDLIE-K 543
Cdd:cd14899 402 ddeedatdFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNN-RACLELFEhR 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 544 PMGIMSILEEECMFPKATDVTFKAKLYDNHLGKSNNFQKPRNLKGRPEAHFALVHYAGTVDYNINGWLVKNKDPLNETVV 623
Cdd:cd14899 481 PIGIFSLTDQECVFPQGTDRALVAKYYLEFEKKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFCESAA 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 624 GLYQKSALKLLAHLFANYASAESDQATKGKGSKKKGSSFQ-------TVSALHRENLNKLMTNLRATHPHFVRCIIPNET 696
Cdd:cd14899 561 QLLAGSSNPLIQALAAGSNDEDANGDSELDGFGGRTRRRAksaiaavSVGTQFKIQLNELLSTVRATTPRYVRCIKPNDS 640
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1072253241 697 KSPGMMDNRLVMHQLRCNGVLEGIRICRKGYPNRILYGDFRQRYR 741
Cdd:cd14899 641 HVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRYR 685
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
118-744 |
9.97e-106 |
|
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: 356.21 E-value: 9.97e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 118 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKR-SEAPPHIFSISDNAYQYMLTDRDNQSILITG 195
Cdd:cd14906 3 ILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIIISG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 196 ESGAGKTVNTKRVIQYFAVIAAIGDRKKDSGPTGKGTLEDQIIQANPALEAFGNAKTLRNDNSSRFGKFIRIHFGAT-GK 274
Cdd:cd14906 83 ESGSGKTEASKTILQYLINTSSSNQQQNNNNNNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSdGK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 275 LASADIETYLLEKSRVIFQL-KSERDYHIFYQILSNKKPELLDMLLVTNNPYDYAYISQGETTVASI------------- 340
Cdd:cd14906 163 IDGASIETYLLEKSRISHRPdNINLSYHIFYYLVYGASKDERSKWGLNNDPSKYRYLDARDDVISSFksqssnknsnhnn 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 341 --DDAEELLATDSAFDVLGFTQDEKNSIYKLTGAVMHFGNMKFKQKQ---REEQAEPDGTEEADKVAYLMGLNSADLLKG 415
Cdd:cd14906 243 ktESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSdfsKYAYQKDKVTASLESVSKLLGYIESVFKQA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 416 LCHPRVKVGNE--YVTKGQNVQQVYYSTGALGKSVYEKMFLWMVVRINTT-LETKQPRQ----------YFIGVLDIAGF 482
Cdd:cd14906 323 LLNRNLKAGGRgsVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKfNQNTQSNDlaggsnkknnLFIGVLDIFGF 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 483 EIFDFNSFEQMCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKAT 561
Cdd:cd14906 403 ENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEkKSDGILSLLDDECIMPKGS 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 562 DVTFKAKlYDNHLGKSNNFQKPRNLKGRpeahFALVHYAGTVDYNINGWLVKNKDPLNETVVGLYQKSALKLLAHLFany 641
Cdd:cd14906 482 EQSLLEK-YNKQYHNTNQYYQRTLAKGT----LGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLF--- 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 642 asaeSDQATKGKGSKKKGSSFQTVSALHRENLNKLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIR 721
Cdd:cd14906 554 ----QQQITSTTNTTKKQTQSNTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLNTIK 629
|
650 660
....*....|....*....|...
gi 1072253241 722 ICRKGYPNRILYGDFRQRYRILN 744
Cdd:cd14906 630 VRKMGYSYRRDFNQFFSRYKCIV 652
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
118-784 |
4.60e-103 |
|
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: 346.41 E-value: 4.60e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 118 VLYNLKERYAAWMI-YTYSGLFCVTVNPYKWLPvYNAEVvaaYRGKKRSEA-----PPHIFSISDNAY-QYMLTDRDNQS 190
Cdd:cd14875 3 LLHCIKERFEKLHQqYSLMGEMVLSVNPFRLMP-FNSEE---ERKKYLALPdprllPPHIWQVAHKAFnAIFVQGLGNQS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 191 ILITGESGAGKTVNTKRVIQYFAVIAAIgdrkkDSGPTGKGTLEDQIIQ----ANPALEAFGNAKTLRNDNSSRFGKFIR 266
Cdd:cd14875 79 VVISGESGSGKTENAKMLIAYLGQLSYM-----HSSNTSQRSIADKIDEnlkwSNPVMESFGNARTVRNDNSSRFGKYIK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 267 IHF-GATGKLASADIETYLLEKSRVIFQLKSERDYHIFYQILSNKKPELLDMLLVTNNPYDYAYISQGETTV------AS 339
Cdd:cd14875 154 LYFdPTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELGGLKTAQDYKCLNGGNTFVrrgvdgKT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 340 IDDAEELLATDSAFDVLGFTQDEKNSIYKLTGAVMHFGNMKFKQKQREEQAEPDGTEEAdKVAYLMGLNSADLLKGLChp 419
Cdd:cd14875 234 LDDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQNDKAQIADETPFL-TACRLLQLDPAKLRECFL-- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 420 rVKVGNEYVTKGQNVQQVYYSTGALGKSVYEKMFLWMVVRINTTLetkQPRQ-----YFIGVLDIAGFEIFDFNSFEQMC 494
Cdd:cd14875 311 -VKSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASI---TPQGdcsgcKYIGLLDIFGFENFTRNSFEQLC 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 495 INFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLQACIDLIE-KPMGIMSILEEECMFPKATDVTFKAKLYDNH 573
Cdd:cd14875 387 INYANESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFDqKRTGIFSMLDEECNFKGGTTERFTTNLWDQW 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 574 LGKSNNFQKPrnlKGRPEAHFALVHYAGTVDYNINGWLVKNKDPLNETVVGLYQKSALKLLAHLFanyaSAESDQATKGk 653
Cdd:cd14875 466 ANKSPYFVLP---KSTIPNQFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLL----STEKGLARRK- 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 654 gskkkgssfQTVSALHRENLNKLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRKGYPNRILY 733
Cdd:cd14875 538 ---------QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPI 608
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1072253241 734 GDF-RQRYRILNPAAIPEGQFIDSRKGAEKLLAS----LEMDHTQYKFGHTKVFFK 784
Cdd:cd14875 609 EQFcRYFYLIMPRSTASLFKQEKYSEAAKDFLAYyqrlYGWAKPNYAVGKTKVFLR 664
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
122-784 |
9.05e-100 |
|
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: 336.47 E-value: 9.05e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 122 LKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRS-----EAPPHIFSISDNAYQYMLTDRDNQSILITG 195
Cdd:cd14886 7 LRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQSCIVSG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 196 ESGAGKTVNTKRVIQYFAVIAAIGDRKkdsgptgkgtLEDQIIQANPALEAFGNAKTLRNDNSSRFGKFIRIHFGATGKL 275
Cdd:cd14886 87 ESGAGKTETAKQLMNFFAYGHSTSSTD----------VQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 276 ASADIETYLLEKSRVIFQLKSERDYHIFYQILSNKKPELLDMLLVTNNPYdYAYISQGET-TVASIDDAEELLATDSAFD 354
Cdd:cd14886 157 KGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLES-YNFLNASKCyDAPGIDDQKEFAPVRSQLE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 355 VLgFTQDEKNSIYKLTGAVMHFGNMKFKQKQR---EEQAEPDGTEEADKVAYLMGLNSADLLKGLCHPRVKVGNEYVTKG 431
Cdd:cd14886 236 KL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgvINAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNETIISP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 432 QNVQQVYYSTGALGKSVYEKMFLWMVVRINTTLETKQPRQYFIGVLDIAGFEIFDFNSFEQMCINFTNEKLQQFFNHHMF 511
Cdd:cd14886 315 VTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFINQVF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 512 VLEQEEYKKEGIEWEFIDFgMDLQACIDLIEKP-MGIMSILEEECMFPKATDVTFKAKLyDNHLgKSNNFqkprnLKGRP 590
Cdd:cd14886 395 KSEIQEYEIEGIDHSMITF-TDNSNVLAVFDKPnLSIFSFLEEQCLIQTGSSEKFTSSC-KSKI-KNNSF-----IPGKG 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 591 EA-HFALVHYAGTVDYNINGWLVKNKDPLNETVVGLYQKSALKLLAHLFANYASAESDQATkgkgskkkgssfQTVSALH 669
Cdd:cd14886 467 SQcNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNEDGNMKG------------KFLGSTF 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 670 RENLNKLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRKGYPNRILYGDFRQRYRIL---NPA 746
Cdd:cd14886 535 QLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILishNSS 614
|
650 660 670
....*....|....*....|....*....|....*...
gi 1072253241 747 AIPEGQfiDSRKGAEKLLASLEMDHTQYKFGHTKVFFK 784
Cdd:cd14886 615 SQNAGE--DLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
118-784 |
6.51e-99 |
|
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: 335.43 E-value: 6.51e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 118 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRDNQSILITGES 197
Cdd:cd01386 3 VLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLGRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 198 GAGKTVNTKRVIQYFAVIAaigdrkkdsGPTGKGTLEDQIIQANPALEAFGNAKTLRNDNSSRFGKFIRIHFGATGKLAS 277
Cdd:cd01386 83 GSGKTTNCRHILEYLVTAA---------GSVGGVLSVEKLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLAS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 278 ADIETYLLEKSRVIFQLKSERDYHIFYQILSNKKPEL-----LDMLLVTNNPYDYAYISQGETTvasiDDAEELLATDSA 352
Cdd:cd01386 154 ASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALrtelhLNQLAESNSFGIVPLQKPEDKQ----KAAAAFSKLQAA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 353 FDVLGFTQDEKNSIYKLTGAVMHFGN---MKFKQKQREEQAEPdgtEEADKVAYLMGLNSADLLKGLCHPRVKVGNEYVT 429
Cdd:cd01386 230 MKTLGISEEEQRAIWSILAAIYHLGAagaTKAASAGRKQFARP---EWAQRAAYLLGCTLEELSSAIFKHHLSGGPQQST 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 430 KGQNVQQVYYSTG------------ALGKSVYEKMFLWMVVRINTTLETKQPRQYFIGVLDIAGFEIFDFN------SFE 491
Cdd:cd01386 307 TSSGQESPARSSSggpkltgvealeGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPAHSgsqrgaTFE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 492 QMCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEK---------------PMGIMSILEEECM 556
Cdd:cd01386 387 DLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQapqqalvrsdlrdedRRGLLWLLDEEAL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 557 FPKATDVTFKAKLYdNHLGKSNNFQKPRNLKgRPEA--HFALVHYAGT--VDYNINGWLVKNK-DPLNETVVGLYQKSAL 631
Cdd:cd01386 467 YPGSSDDTFLERLF-SHYGDKEGGKGHSLLR-RSEGplQFVLGHLLGTnpVEYDVSGWLKAAKeNPSAQNATQLLQESQK 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 632 KLLAH----LFANyasaesdqatkgkgskkkgSSFQtvsalhrenLNKLMTNLRATHPHFVRCIIPN------------E 695
Cdd:cd01386 545 ETAAVkrksPCLQ-------------------IKFQ---------VDALIDTLRRTGLHFVHCLLPQhnagkderstssP 596
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 696 TKSPGMMDNRLVMHQLRCNGVLEGIRICRKGYPNRILYGDFRQRYRILNPA----AIPEGQFIDSRKGAEKLLASLEMDH 771
Cdd:cd01386 597 AAGDELLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPltkkLGLNSEVADERKAVEELLEELDLEK 676
|
730
....*....|...
gi 1072253241 772 TQYKFGHTKVFFK 784
Cdd:cd01386 677 SSYRIGLSQVFFR 689
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
117-784 |
3.51e-93 |
|
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: 317.53 E-value: 3.51e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 117 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYR---GKKRSEAPPHIFSISDNAYQYMLTDRDNQSILI 193
Cdd:cd14878 2 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 194 TGESGAGKTVNTKRVIQYFAViaaigdRKKDSGPTgkgtLEDQIIQANPALEAFGNAKTLRNDNSSRFGKFIRIHFGATG 273
Cdd:cd14878 82 SGERGSGKTEASKQIMKHLTC------RASSSRTT----FDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFCERK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 274 K-LASADIETYLLEKSRVIFQLKSERDYHIFYQILSNKKPELLDMLLVtNNPYDYAYISQGE----TTVASIDDAEELLA 348
Cdd:cd14878 152 KhLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHL-NNLCAHRYLNQTMredvSTAERSLNREKLAV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 349 TDSAFDVLGFTQDEKNSIYKLTGAVMHFGNMKFKQKQREEQAEPDGTEEADKVAYLMGLNSADLLKGLCHPRVKVGNEYV 428
Cdd:cd14878 231 LKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 429 TKGQNVQQVYYSTGALGKSVYEKMFLWMVVRINTTL----ETKQPRQYFIGVLDIAGFEIFDFNSFEQMCINFTNEKLQQ 504
Cdd:cd14878 311 IRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqdEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHH 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 505 FFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLI-EKPMGIMSILEEECMFPKATDVTFKAKLyDNHLGKSNN---F 580
Cdd:cd14878 391 YINEVLFLQEQTECVQEGVTMETAYSPGNQTGVLDFFfQKPSGFLSLLDEESQMIWSVEPNLPKKL-QSLLESSNTnavY 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 581 QKPRNLKGRPE-----AHFALVHYAGTVDYNINGWLVKNKDPLNETVVGLYQKSALKLLAHLFanyasaesdqatkgkgs 655
Cdd:cd14878 470 SPMKDGNGNVAlkdqgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLF----------------- 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 656 kkkGSSFQTVSALHRENLNKLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRKGYPNRILYGD 735
Cdd:cd14878 533 ---QSKLVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSD 609
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1072253241 736 FRQRYRILNPAAIPEGQfidSRKGAEKLLASLEMDHTQ-YKFGHTKVFFK 784
Cdd:cd14878 610 FLSRYKPLADTLLGEKK---KQSAEERCRLVLQQCKLQgWQMGVRKVFLK 656
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
117-759 |
7.89e-93 |
|
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: 314.14 E-value: 7.89e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 117 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKwlPVYNAEVVAAYRgKKRSEAPPHIFSISDNAYQYMLTdRDNQSILITGE 196
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYE--TIYGAGAMKAYL-KNYSHVEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 197 SGAGKTVNTKRVIQYFAviaaigdrkkdSGPTGKGTLEDQIIQANPALEAFGNAKTLRNDNSSRFGKFIRIHFgaTGKLA 276
Cdd:cd14898 78 SGSGKTENAKLVIKYLV-----------ERTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKF--DGKIT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 277 SADIETYLLEKSRVIFQLKSERDYHIFYQILSNKKpelldmLLVTNNPYDYAYISQGETTVasIDDAEELLATDSAFDVL 356
Cdd:cd14898 145 GAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKR------LNIKNDFIDTSSTAGNKESI--VQLSEKYKMTCSAMKSL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 357 GFTQDEknSIYKLTGAVMHFGNMKFKQkqrEEQAEPDGTEEADKVAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQ 436
Cdd:cd14898 217 GIANFK--SIEDCLLGILYLGSIQFVN---DGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQ 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 437 VYYSTGALGKSVYEKMFLWMVVRINTTLETKQPRQyfIGVLDIAGFEIFDFNSFEQMCINFTNEKLQQFFNHHMFVLEQE 516
Cdd:cd14898 292 ARTIRNSMARLLYSNVFNYITASINNCLEGSGERS--ISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 517 EYKKEGIEWEFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKAT--DVTFKAKLYDNHLGKSNNFQKprnlkgrpeahF 594
Cdd:cd14898 370 MYKEEGIEWPDVEF-FDNNQCIRDFEKPCGLMDLISEESFNAWGNvkNLLVKIKKYLNGFINTKARDK-----------I 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 595 ALVHYAGTVDYNINGWLVKNKdplnetvvglyQKSALKLLAHLFANYASAESDqatkgkgskkkgssfqtVSALHRENLN 674
Cdd:cd14898 438 KVSHYAGDVEYDLRDFLDKNR-----------EKGQLLIFKNLLINDEGSKED-----------------LVKYFKDSMN 489
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 675 KLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRKGYPNRILYGDFRQRYRILNPAAIpegQFI 754
Cdd:cd14898 490 KLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGITLF---EVV 566
|
....*
gi 1072253241 755 DSRKG 759
Cdd:cd14898 567 DYRKG 571
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
118-784 |
7.01e-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: 7.01e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 118 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEvvaaYRGKKRSEAPPHIFSISDNAYQYMLTDRDNQSILITGES 197
Cdd:cd14937 3 VLNMLALRYKKNYIYTIAEPMLISINPYQVIDVDINE----YKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 198 GAGKTVNTKRVIQYFAviaaigdrkkdSGPTGKGTLEDQIIQANPALEAFGNAKTLRNDNSSRFGKFIRIHFGATGKLAS 277
Cdd:cd14937 79 GSGKTEASKLVIKYYL-----------SGVKEDNEISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 278 ADIETYLLEKSRVIFQLKSERDYHIFYQILSNKKPELLDMLLVTNNPyDYAYISQGETTVASIDDAEELLATDSAFDVLG 357
Cdd:cd14937 148 SSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSEN-EYKYIVNKNVVIPEIDDAKDFGNLMISFDKMN 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 358 FTqDEKNSIYKLTGAVMHFGNMKFKQ-----KQREEQAEPDGTEEADKVAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 432
Cdd:cd14937 227 MH-DMKDDLFLTLSGLLLLGNVEYQEiekggKTNCSELDKNNLELVNEISNLLGINYENLKDCLVFTEKTIANQKIEIPL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 433 NVQQVYYSTGALGKSVYEKMFLWMVVRINTTLETKQPRQYFIGVLDIAGFEIFDFNSFEQMCINFTNEKLQQFFNHHMFV 512
Cdd:cd14937 306 SVEESVSICKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 513 LEQEEYKKEGIEWEFIDFGMDlQACIDLIEKPMGIMSILEEECMFPKATDVTFkAKLYDNHLGKSNNFQkprNLKGRPEA 592
Cdd:cd14937 386 KETELYKAEDILIESVKYTTN-ESIIDLLRGKTSIISILEDSCLGPVKNDESI-VSVYTNKFSKHEKYA---STKKDINK 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 593 HFALVHYAGTVDYNINGWLVKNKDPLNETVVGLYQKSALKLLAHLFANYASAESdqatkgkgskkkGSSFQTVSALHREN 672
Cdd:cd14937 461 NFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVSES------------LGRKNLITFKYLKN 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 673 LNKLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRIcRKGYPNRILYGDFRQRYRILNPAAIPEGQ 752
Cdd:cd14937 529 LNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEYLDYSTSKDSS 607
|
650 660 670
....*....|....*....|....*....|..
gi 1072253241 753 FIDSRKGAEKLLASLEMDhtQYKFGHTKVFFK 784
Cdd:cd14937 608 LTDKEKVSMILQNTVDPD--LYKVGKTMVFLK 637
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
116-784 |
3.46e-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: 296.17 E-value: 3.46e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 116 PAVLYNLKERYAA--------WMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRD 187
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 188 NQSILITGESGAGKTVNTKRVIQYfavIAAIGDRKKDSGPTGkgtLEDQIIQANPALEAFGNAKTLRNDNSSRFGKFIRI 267
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTY---LAAVSDRRHGADSQG---LEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 268 HFGATGKLASADIETYLLEKSRVIFQLKSERDYHIFYQILSNKK-PELLDMLLVTNNPYDYayisqgettvasiddaeEL 346
Cdd:cd14887 155 HFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVaAATQKSSAGEGDPEST-----------------DL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 347 LATDSAFDVLGFTQDEKNSIYKLTGAVMHFGNMKFKQKQREEQAEPD-------GTEEADK----VAYLMGLNS------ 409
Cdd:cd14887 218 RRITAAMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRkltsvsvGCEETAAdrshSSEVKCLSSglkvte 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 410 ------ADLLKGLCHPRVKVGNEYV------------TKGQNVQQVYYSTGALGKSVYEKMFLWMVVRINTTLETKQPRQ 471
Cdd:cd14887 298 asrkhlKTVARLLGLPPGVEGEEMLrlalvsrsvretRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKPS 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 472 Y--------------FIGVLDIAGFEIF---DFNSFEQMCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFI--DFGM 532
Cdd:cd14887 378 EsdsdedtpsttgtqTIGILDLFGFEDLrnhSKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDcsAFPF 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 533 DLQACIDLIEKP------------------------MGIMSILEEE-CMFP-----KATDVTFKAKLYDNHLGKSNNFQK 582
Cdd:cd14887 458 SFPLASTLTSSPsstspfsptpsfrsssafatspslPSSLSSLSSSlSSSPpvwegRDNSDLFYEKLNKNIINSAKYKNI 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 583 PRNLKgRPEAHFALVHYAGTVDYNINGWLVKNKDPLNETVVGLYqksalkllahLFANYASAE--SDQATKGKGSKKKGs 660
Cdd:cd14887 538 TPALS-RENLEFTVSHFACDVTYDARDFCRANREATSDELERLF----------LACSTYTRLvgSKKNSGVRAISSRR- 605
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 661 sfQTVSALHRENLNKLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRKGYPNRILYGDFRQRY 740
Cdd:cd14887 606 --STLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRY 683
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 1072253241 741 RILNPAAIPEgqFIDSRKGAEKLLASLEMDHTQYKFGHTKVFFK 784
Cdd:cd14887 684 ETKLPMALRE--ALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
113-783 |
1.68e-82 |
|
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: 285.98 E-value: 1.68e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 113 LNEPAVLYNLKERYAAWMIYTY---SGLfcVTVNPYKWLPVYNAEVVAAYR-------GKKRSEAPPHIFSISDNAYQYM 182
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 183 LTDRDNQSILITGESGAGKTVNTKRVIQyfaviaAIGDRkkdSGPTGKGT-LEDQIIQANPALEAFGNAKTLRNDNSSRF 261
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLR------QLLRL---SSHSKKGTkLSSQISAAEFVLDSFGNAKTLTNPNASRF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 262 GKFIRIHFGATGKLASADIETYLLEKSRVIfQLKS-ERDYHIFYQILSNKKPELLDmLLVTNNPYDYAYI--SQGETTVA 338
Cdd:cd14879 150 GRYTELQFNERGRLIGAKVLDYRLERSRVA-SVPTgERNFHVFYYLLAGASPEERQ-HLGLDDPSDYALLasYGCHPLPL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 339 S--IDDAE--ELLATdsAFDVLGFTQDEKNSIYKLTGAVMHFGNMKFKQkqreeqaEPDGTEEA---------DKVAYLM 405
Cdd:cd14879 228 GpgSDDAEgfQELKT--ALKTLGFKRKHVAQICQLLAAILHLGNLEFTY-------DHEGGEESavvkntdvlDIVAAFL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 406 GLNSADLLKGLCHPRVKVGNEYVTKGQNVQQVYYSTGALGKSVYEKMFLWMVVRINTTL-ETKQPRQYFIGVLDIAGFEI 484
Cdd:cd14879 299 GVSPEDLETSLTYKTKLVRKELCTVFLDPEGAAAQRDELARTLYSLLFAWVVETINQKLcAPEDDFATFISLLDFPGFQN 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 485 FD---FNSFEQMCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLI-EKPMGIMSILEEEC-MFPK 559
Cdd:cd14879 379 RSstgGNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLrGKPGGLLGILDDQTrRMPK 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 560 ATDVTFKAKLyDNHLGKSNNFQKPRNLKGRPEAH-FALVHYAGTVDYNINGWLVKNKDPLNETVVglyqksalkllaHLF 638
Cdd:cd14879 458 KTDEQMLEAL-RKRFGNHSSFIAVGNFATRSGSAsFTVNHYAGEVTYSVEGFLERNGDVLSPDFV------------NLL 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 639 ANyasaesdqatkgkgskkkgssfqtvSALHRENLNKLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLE 718
Cdd:cd14879 525 RG-------------------------ATQLNAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPE 579
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1072253241 719 GIRICRKGYPNRILYGDFRQRYrilnpaaIPEGQFIDSRKGAEKLLASLEMDHTQYKFGHTKVFF 783
Cdd:cd14879 580 LAARLRVEYVVSLEHAEFCERY-------KSTLRGSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
117-752 |
3.65e-73 |
|
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: 258.26 E-value: 3.65e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 117 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYrgkkrseappHIFSISDNAYQYMLTDRDN-QSILITG 195
Cdd:cd14874 2 GIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFGG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 196 ESGAGKTVNTKRVIQYFAviaaigdrkkdSGPTGK-GTLEDQIIQAnpALEAFGNAKTLRNDNSSRFGKFIRIHFGATGK 274
Cdd:cd14874 72 ESGSGKSYNAFQVFKYLT-----------SQPKSKvTTKHSSAIES--VFKSFGCAKTLKNDEATRFGCSIDLLYKRNVL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 275 LASADIETYLLEKSRVIFQLKSERDYHIFYQILSNKKPELLDMLLVTNNpYDYAYISQGETTVASIDDAEELLATDSAFD 354
Cdd:cd14874 139 TGLNLKYTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGL-QKFFYINQGNSTENIQSDVNHFKHLEDALH 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 355 VLGFTQDEKNSIYKLTGAVMHFGNMKFKQKQ----REEQAEPDGTEEADKVAYLMGLNSADLLKGLChPRVKVGNEYvtk 430
Cdd:cd14874 218 VLGFSDDHCISIYKIISTILHIGNIYFRTKRnpnvEQDVVEIGNMSEVKWVAFLLEVDFDQLVNFLL-PKSEDGTTI--- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 431 gqNVQQVYYSTGALGKSVYEKMFLWMVVRINttLETKQPRQY-FIGVLDIAGFEIFDFNSFEQMCINFTNEKLQQFFNHH 509
Cdd:cd14874 294 --DLNAALDNRDSFAMLIYEELFKWVLNRIG--LHLKCPLHTgVISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKH 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 510 MFVLEQEEYKKEGIEwefIDFGMdlQACID-------LIEKPMGIMSILEEECMFPKATDVTFKAKLYDNHLGKSNnFQK 582
Cdd:cd14874 370 SFHDQLVDYAKDGIS---VDYKV--PNSIEngktvelLFKKPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSS-YGK 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 583 PRNlKGRPEahFALVHYAGTVDYNINGWLVKNKDPLNETVVGLYQKSALKLLAHLFANYASAESDQATkgkgskkkgssf 662
Cdd:cd14874 444 ARN-KERLE--FGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESYSSNTSDMIV------------ 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 663 qTVSALHRENLNKLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRKGYPNRILYGDFRQRYRI 742
Cdd:cd14874 509 -SQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRC 587
|
650
....*....|
gi 1072253241 743 LNPAAIPEGQ 752
Cdd:cd14874 588 LLPGDIAMCQ 597
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
117-783 |
3.74e-71 |
|
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: 252.34 E-value: 3.74e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 117 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPvyNAEVVAAYRGKKRSeapPHIFSISDNAYQYMLTDRDNQSILITGE 196
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPYRDVG--NPLTLTSTRSSPLA---PQLLKVVQEAVRQQSETGYPQAIILSGT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 197 SGAGKTVNTKRVI-QYFAViaaigdrkkdsgpTGKGTLED---QIIQANPALEAFGNAKTLRNDNSSRFGKFIRIHFgAT 272
Cdd:cd14881 77 SGSGKTYASMLLLrQLFDV-------------AGGGPETDafkHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQV-TD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 273 GKLASADIETYLLEKSRVIFQLKSERDYHIFYQILSNKKPELLDML-LVTNNPYDYAYISQGETTVASIDDAEELLATDS 351
Cdd:cd14881 143 GALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLhLDGYSPANLRYLSHGDTRQNEAEDAARFQAWKA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 352 AFDVLG--FTqdeknSIYKLTGAVMHFGNMKFKQKQrEEQAEPDGTEEADKVAYLMGLNSADLLKGL---CHprvkvgne 426
Cdd:cd14881 223 CLGILGipFL-----DVVRVLAAVLLLGNVQFIDGG-GLEVDVKGETELKSVAALLGVSGAALFRGLttrTH-------- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 427 yVTKGQNVQQV---YYSTG---ALGKSVYEKMFLWMVVRINT------TLETKQpRQYFIGVLDIAGFEIFDFNSFEQMC 494
Cdd:cd14881 289 -NARGQLVKSVcdaNMSNMtrdALAKALYCRTVATIVRRANSlkrlgsTLGTHA-TDGFIGILDMFGFEDPKPSQLEHLC 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 495 INFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEF-IDFgMDLQACIDLIEK-PMGIMSILEEECMfPKATDVTFKAKLYDN 572
Cdd:cd14881 367 INLCAETMQHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCIDLISSlRTGLLSMLDVECS-PRGTAESYVAKIKVQ 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 573 HlgKSNN-FQKPRNLKGRpeaHFALVHYAGTVDYNINGWLVKNKDPLNETVVGLYQKSALKLlahlfaNYASAESDqatk 651
Cdd:cd14881 445 H--RQNPrLFEAKPQDDR---MFGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQNCNF------GFATHTQD---- 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 652 gkgskkkgssFQTvsalhreNLNKLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRKGYPNRI 731
Cdd:cd14881 510 ----------FHT-------RLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRM 572
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1072253241 732 LYGDFRQRYRILNPAAiPEGQFIDSRKGAEKLLASLEMDH---------TQYKFGHTKVFF 783
Cdd:cd14881 573 RFKAFNARYRLLAPFR-LLRRVEEKALEDCALILQFLEAQppsklssvsTSWALGKRHIFL 632
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
116-732 |
1.42e-70 |
|
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: 252.13 E-value: 1.42e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 116 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRSEA-------PPHIFSISDNAYQYMLTDRD 187
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSAasaapfpKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 188 NQSILITGESGAGKTVNTKRVIQYFAVIaaigdrkkdSGPTGKGTLEDQIIQANPALEAFGNAKTLRNDNSSRFGKFIRI 267
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYI---------QTDSQMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINLL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 268 HF---------GATGKLASADIETYLLEKSRVIFQLKSERDYHIFYQILSNKKPELLDMLLVTNNPYDYAYISQGE---- 334
Cdd:cd14884 152 IFeeventqknMFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLARRNLVRNCGVYGLLNPDEshqk 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 335 --------TTVASIDDAEELLATDSA-FDVL-------GFTQDEKNSIYKLTGAVMHFGNMKFKQkqreeqaepdgteea 398
Cdd:cd14884 232 rsvkgtlrLGSDSLDPSEEEKAKDEKnFVALlhglhyiKYDERQINEFFDIIAGILHLGNRAYKA--------------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 399 dkVAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQVYYSTGALGKSVYEKMFLWMVVRINTT----------LETKQ 468
Cdd:cd14884 297 --AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNvlkckekdesDNEDI 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 469 PR--QYFIGVLDIAGFEIFDFNSFEQMCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEW--EFIDFGMDLQACIDLIEKP 544
Cdd:cd14884 375 YSinEAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICcsDVAPSYSDTLIFIAKIFRR 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 545 MGIMSILEEECMfpKATDVTFKAKLYDNH----------LGKSNNF-----QKPRNLKgrpEAHFALVHYAGTVDYNING 609
Cdd:cd14884 455 LDDITKLKNQGQ--KKTDDHFFRYLLNNErqqqlegkvsYGFVLNHdadgtAKKQNIK---KNIFFIRHYAGLVTYRINN 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 610 WLVKNKDPLNETVVGLYQKSALKLLAHLFANyasaesdqatkgkgskKKGSSFQTVSALHRENLNKLMTNLRATHPHFVR 689
Cdd:cd14884 530 WIDKNSDKIETSIETLISCSSNRFLREANNG----------------GNKGNFLSVSKKYIKELDNLFTQLQSTDMYYIR 593
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1072253241 690 CIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRKGYPNRIL 732
Cdd:cd14884 594 CFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIP 636
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
122-736 |
7.05e-65 |
|
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: 234.99 E-value: 7.05e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 122 LKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYrgKKRSEAPPHIFSISDNAYQYMLTDRDNQSILITGESGAG 200
Cdd:cd14905 7 IQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNY--NQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGGESGSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 201 KTVNTKRVIQYfaVIAAIGDRKKdsgptgkgTLEDQIIQANPALEAFGNAKTLRNDNSSRFGKFIRIHFGATGKLASADI 280
Cdd:cd14905 85 KSENTKIIIQY--LLTTDLSRSK--------YLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 281 ETYLLEKSRVIFQLKSERDYHIFYQILSNKKPElLDMLLVTNNPYDYAYISQGET-TVASIDDAEELLATDSAFDVLGFT 359
Cdd:cd14905 155 YSYFLDENRVTYQNKGERNFHIFYQFLKGITDE-EKAAYQLGDINSYHYLNQGGSiSVESIDDNRVFDRLKMSFVFFDFP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 360 QDEKNSIYKLTGAVMHFGNMKFKQKQREEQAEPDGTEEAdkVAYLMGLNSADLLKGLCHPRVKVGNEYVTkgqnvqqvyy 439
Cdd:cd14905 234 SEKIDLIFKTLSFIIILGNVTFFQKNGKTEVKDRTLIES--LSHNITFDSTKLENILISDRSMPVNEAVE---------- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 440 STGALGKSVYEKMFLWMVVRINTTLetkQPRQY--FIGVLDIAGFEIFDFNSFEQMCINFTNEKLQQFFNHHMFVLEQEE 517
Cdd:cd14905 302 NRDSLARSLYSALFHWIIDFLNSKL---KPTQYshTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQRE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 518 YKKEGIEWEFIDFGMDLQACIDLIEKpmgIMSILEEECMFPKATDVTFKAKLydnhlgksNNFQKPRNLKGRPEAHFALV 597
Cdd:cd14905 379 YQTERIPWMTPISFKDNEESVEMMEK---IINLLDQESKNINSSDQIFLEKL--------QNFLSRHHLFGKKPNKFGIE 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 598 HYAGTVDYNINGWLVKNKDPLNETVVGLYQKSALKllaHLFA-------NYASAESDQA-----TKGKGSKKKGSSFQTV 665
Cdd:cd14905 448 HYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITK---YLFSrdgvfniNATVAELNQMfdaknTAKKSPLSIVKVLLSC 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 666 SALHRENLNK-----------------------LMTNLRATHP---------HFVRCIIPNETKSPGMMDNRLVMHQLRC 713
Cdd:cd14905 525 GSNNPNNVNNpnnnsgggggggnsgggsgsggsTYTTYSSTNKainnsncdfHFIRCIKPNSKKTHLTFDVKSVNEQIKS 604
|
650 660
....*....|....*....|....*..
gi 1072253241 714 NGVLEGIRICRKGYP----NRILYGDF 736
Cdd:cd14905 605 LCLLETTRIQRFGYTihynNKIFFDRF 631
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
119-783 |
1.15e-61 |
|
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: 226.78 E-value: 1.15e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 119 LYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKR----------SEAPPHIFSISDNAYQYMLTDRDN 188
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 189 QSILITGESGAGKTVNTKRVIQYFAVIAAIGDRKKDS-GPTGKG-TLEDQIIQANPALEAFGNAKTLRNDNSSRFGKFIR 266
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPDSeGASGVLhPIGQQILHAFTILEAFGNAATRQNRNSSRFAKMIS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 267 IHFGATGKLASADIETYLLEKSRVIFQLKSERDYHIFYQILSNKK--PELLDMLLVTNNPYDYAYISQGETTVASID-DA 343
Cdd:cd14893 164 VEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQhdPTLRDSLEMNKCVNEFVMLKQADPLATNFAlDA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 344 EELLATDSAFDVLGFTQDEKNSIYKLTGAVMHFGNMKF----KQKQREEQAEPDGTEEADKVAY---LMGLNSADLLKgl 416
Cdd:cd14893 244 RDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpEGGKSVGGANSTTVSDAQSCALkdpAQILLAAKLLE-- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 417 CHPRV------------KVGNEYVT--KGQNVQQVYYSTGALGKSVYEKMFLWMVVRINTTLETKQPR---------QYF 473
Cdd:cd14893 322 VEPVVldnyfrtrqffsKDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILGGIFDRyeksnivinSQG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 474 IGVLDIAGFEIFD--FNSFEQMCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWE-------FIDFGMDLQACIDLIE-K 543
Cdd:cd14893 402 VHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYVQNTLAINFSFLEDESQQVEnrltvnsNVDITSEQEKCLQLFEdK 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 544 PMGIMSILEEECMFPKATDVTFKAKLYDNH-----LGKSNNFQKPRNLKGRPEAH----FALVHYAGTVDYNINGWLVKN 614
Cdd:cd14893 482 PFGIFDLLTENCKVRLPNDEDFVNKLFSGNeavggLSRPNMGADTTNEYLAPSKDwrllFIVQHHCGKVTYNGKGLSSKN 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 615 KDPLNETVVGLYQKSALKLL-----AHLFANYASAESDQATkgkGSKKKGSSFQTVSALHRENLN--------------K 675
Cdd:cd14893 562 MLSISSTCAAIMQSSKNAVLhavgaAQMAAASSEKAAKQTE---ERGSTSSKFRKSASSARESKNitdsaatdvynqadA 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 676 LMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRKGYPNRILYGDFRQRYRilnpaaipegQFID 755
Cdd:cd14893 639 LLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYK----------NVCG 708
|
730 740 750
....*....|....*....|....*....|..
gi 1072253241 756 SRKGAEKLLASLE----MDHTQYKFGHTKVFF 783
Cdd:cd14893 709 HRGTLESLLRSLSaigvLEEEKFVVGKTKVYL 740
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
118-784 |
4.50e-60 |
|
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: 219.61 E-value: 4.50e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 118 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRDNQSILITGES 197
Cdd:cd14882 3 ILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 198 GAGKTVNTKRVIQYFAVIAaigdrKKDSGPTGKgtledqIIQANPALEAFGNAKTLRNDNSSRFGKFIRIHFGATGKLAS 277
Cdd:cd14882 83 YSGKTTNARLLIKHLCYLG-----DGNRGATGR------VESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 278 ADIETYLLEKSRVIFQLKSERDYHIFYQILS--NKKPELLDMLLVTNNPYDYAYISQG-------------ETTVASIDD 342
Cdd:cd14882 152 AIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDfiEAQNRLKEYNLKAGRNYRYLRIPPEvppsklkyrrddpEGNVERYKE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 343 AEELLAtdsafdVLGFTQDEKNSIYKLTGAVMHFGNMKFKQKQREeqAEPDGTEEADKVAYLMGLNSADLLKGLCHPRVK 422
Cdd:cd14882 232 FEEILK------DLDFNEEQLETVRKVLAAILNLGEIRFRQNGGY--AELENTEIASRVAELLRLDEKKFMWALTNYCLI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 423 VGNEYVTKGQNVQQVYYSTGALGKSVYEKMFLWMVVRINTTLETkqPR-----QYFIGVLDIAGFEIFDFNSFEQMCINF 497
Cdd:cd14882 304 KGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSF--PRavfgdKYSISIHDMFGFECFHRNRLEQLMVNT 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 498 TNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDVTFkaklyDNHLGKS 577
Cdd:cd14882 382 LNEQMQYHYNQRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPDGLFYIIDDASRSCQDQNYIM-----DRIKEKH 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 578 NNFQKPRNlkgrpeAH-FALVHYAGTVDYNINGWLVKNKDPLNETVVGLYQKSALKLLAHLFANyasaesdqatkgkgsk 656
Cdd:cd14882 457 SQFVKKHS------AHeFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN---------------- 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 657 KKGSSFQTVSALHR----ENLNKLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICRKGYPNRIL 732
Cdd:cd14882 515 SQVRNMRTLAATFRatslELLKMLSIGANSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIP 594
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1072253241 733 YGDFRQRYRILnpaAIPEGQFID-SRKGAEKLLASLEMDhtQYKFGHTKVFFK 784
Cdd:cd14882 595 FQEFLRRYQFL---AFDFDETVEmTKDNCRLLLIRLKME--GWAIGKTKVFLK 642
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
138-267 |
2.24e-59 |
|
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: 201.80 E-value: 2.24e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 138 FCVTVNPYKWLPVYNAEVV-AAYRGKKRSEAPPHIFSISDNAYQYMLTDRDNQSILITGESGAGKTVNTKRVIQYFAVIA 216
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIiVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1072253241 217 AIGDRKKDSGPT-----GKGTLEDQIIQANPALEAFGNAKTLRNDNSSRFGKFIRI 267
Cdd:cd01363 81 FNGINKGETEGWvylteITVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEI 136
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
116-782 |
6.99e-44 |
|
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: 172.33 E-value: 6.99e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 116 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSE-APPHIFSISDNAYQYMLTDRDNQSILIT 194
Cdd:cd14938 1 PSVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKCIDCIEdLSLNEYHVVHNALKNLNELKRNQSIIIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 195 GESGAGKTVNTKRVIQYFAViAAIGDRKKDSGP--------------TGKGTLEDQIIQANPALEAFGNAKTLRNDNSSR 260
Cdd:cd14938 81 GESGSGKSEIAKNIINFIAY-QVKGSRRLPTNLndqeednihneentDYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 261 FGKFIRIHFgATGKLASADIETYLLEKSRVIFQLKSERDYHIFYQILSNKKPELLDMLLVTNNPYdYAYISQGETTVASI 340
Cdd:cd14938 160 FSKFCTIHI-ENEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIEN-YSMLNNEKGFEKFS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 341 DDAEELLATDSAFDVLGFTQDEKNSIYKLTGAVMHFGN-------------MKFKQKQRE----------EQAEPDGTEE 397
Cdd:cd14938 238 DYSGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNteivkafrkksllMGKNQCGQNinyetilselENSEDIGLDE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 398 ADKVAYL----MGLNSADLLKGLCHPRVkVGNEYVTKGQNVQQVYYSTGALGKSVYEKMFLWMVVRIN---TTLETKQPR 470
Cdd:cd14938 318 NVKNLLLacklLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINekcTQLQNININ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 471 QYFIGVLDIAGFEIFDFNSFEQMCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM--GIM 548
Cdd:cd14938 397 TNYINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTegSLF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 549 SILEEECMfPKATDVTFKAKLYDNHLGKSNNFQKPRNLKGRPEAhFALVHYAGTVDYNINGWLVKNKDPLNETVVGLYQK 628
Cdd:cd14938 477 SLLENVST-KTIFDKSNLHSSIIRKFSRNSKYIKKDDITGNKKT-FVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQ 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 629 SALKLLAHL--FANYASAE---------SDQATKGKGSKKKGSSFQTVSALHRENLNKLMTNLRATHPHFVRCIIPNETK 697
Cdd:cd14938 555 SENEYMRQFcmFYNYDNSGniveekrrySIQSALKLFKRRYDTKNQMAVSLLRNNLTELEKLQETTFCHFIVCMKPNESK 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 698 SP-GMMDNRLVMHQLRCNGVLEGIRICRKGYPNRILYGDFRQRYRILNPaaipegqfiDSRKGAEKLLASLEMDHTQYKF 776
Cdd:cd14938 635 RElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE---------DLKEKVEALIKSYQISNYEWMI 705
|
....*.
gi 1072253241 777 GHTKVF 782
Cdd:cd14938 706 GNNMIF 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1162-1943 |
6.93e-31 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 133.26 E-value: 6.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1162 EEISERLEEAGGATSVQMelnKKREAEfLKLRRdleestlhseaTAASLrKKHADSVAELSEQIDNLQRVKQK----LEK 1237
Cdd:TIGR02168 155 EERRAIFEEAAGISKYKE---RRKETE-RKLER-----------TRENL-DRLEDILNELERQLKSLERQAEKaeryKEL 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1238 EKSEFKLELDDVTSNMEQMVKAKANLEKLCRSLEDQANEHRTKSEENQRTVNELSSLRAKLQTENGELSRRLDEKESLVS 1317
Cdd:TIGR02168 219 KAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIS 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1318 QMTRGKQTYTQHLEDLKRQLEEETKAKNALAHALQSARHDSDLLREQFEEEQEAKAELQRILSKANSEVAQWRTKYETda 1397
Cdd:TIGR02168 299 RLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE-- 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1398 iqRTEELEEAKKKLAQRLQEAEEA---VEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAALDKKQRnfDKILAEW 1474
Cdd:TIGR02168 377 --LEEQLETLRSKVAQLELQIASLnneIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEEL--EEELEEL 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1475 KQKFEESQTELESSQKEARSLSTELFKLKN----------AYEESLDHLETFKRENKNL---QEEISDLTEQLGESGKSI 1541
Cdd:TIGR02168 453 QEELERLEEALEELREELEEAEQALDAAERelaqlqarldSLERLQENLEGFSEGVKALlknQSGLSGILGVLSELISVD 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1542 HELEK-----IRKQLDQEKME-IQSALEEAEATLEHEEGKIlhAQLELHQIKAdseRKLAEKDEEMEQAKRNYQRMVDTL 1615
Cdd:TIGR02168 533 EGYEAaieaaLGGRLQAVVVEnLNAAKKAIAFLKQNELGRV--TFLPLDSIKG---TEIQGNDREILKNIEGFLGVAKDL 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1616 QTSleaetrsrneALRIKKKMEGDLNEMEI--QLSQANRQAAEAQKQVKILQsylKDTQIQLDDALRASEDLKENIAIVE 1693
Cdd:TIGR02168 608 VKF----------DPKLRKALSYLLGGVLVvdDLDNALELAKKLRPGYRIVT---LDGDLVRPGGVITGGSAKTNSSILE 674
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1694 RRNtllqaELEELRSLVEQTERARKLSEQELIETSERVQLLHSQNTSLINQKKKMESDLSQLQTEMEEAVQECRNAEEKA 1773
Cdd:TIGR02168 675 RRR-----EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1774 KKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQQRLDEAeQIALKGGKKQLQKLEARVRELDNELEAEQKRNAE 1853
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL-KEELKALREALDELRAELTLLNEEAANLRERLES 828
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1854 SVKGMRKYERRIKELTYQTEEDRKNLARLQDLVDKLQLKVKTYKRQAEESEEQANTSLSKFRKVQHELDEAEERADIAES 1933
Cdd:TIGR02168 829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
810
....*....|
gi 1072253241 1934 QVNKLRAKSR 1943
Cdd:TIGR02168 909 KRSELRRELE 918
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
861-1690 |
5.21e-29 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 127.09 E-value: 5.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 861 AETEKEMQTMK------EEFQKLKEALEKSE-----ARRKDLEEKMVSLLQEKNDLQLQVQAEQDNLADADERCEQLIKN 929
Cdd:TIGR02168 196 NELERQLKSLErqaekaERYKELKAELRELElallvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 930 KIQLEAKLKEQTERLEdeeemnaELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIVK 1009
Cdd:TIGR02168 276 VSELEEEIEELQKELY-------ALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1010 LTKEKKALQEAHQQALDDLQAEEDKVNTLTKAkakLEQQVDDLEGSLEQEKKIRMDLERVKRKLEGdvklSQESLMDLEN 1089
Cdd:TIGR02168 349 LKEELESLEAELEELEAELEELESRLEELEEQ---LETLRSKVAQLELQIASLNNEIERLEARLER----LEDRRERLQQ 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1090 DKQQLEEKLKKKDFEVSQlnTRIEDEQNVCIQLQKKMKELQARIEELEEELEAERTARAKVEKLRCDLSRELEEISERLE 1169
Cdd:TIGR02168 422 EIEELLKKLEEAELKELQ--AELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQE 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1170 EAGGATS--VQMELNKKREAEFLKLRRDLEESTLHSEATAASLRKKHADSVAelseqIDNLQRVKQKLE--KEKSEFK-- 1243
Cdd:TIGR02168 500 NLEGFSEgvKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVV-----VENLNAAKKAIAflKQNELGRvt 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1244 -LELDDVTSNmeQMVKAKANLEKLCRSLEDQANEHRTKSEENQRTVNELSSLRA---KLQTENgELSRRLDEKESLVSQ- 1318
Cdd:TIGR02168 575 fLPLDSIKGT--EIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLvvdDLDNAL-ELAKKLRPGYRIVTLd 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1319 ---------MTRGK-------QTYTQHLEDLKRQLEEETKAKNALAHALQSARHDSDLLREQFEEEQEAKAELQRILSKA 1382
Cdd:TIGR02168 652 gdlvrpggvITGGSaktnssiLERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAL 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1383 NSEVAQWRtkyetdaiQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAALDK 1462
Cdd:TIGR02168 732 RKDLARLE--------AEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE 803
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1463 KQRNFDKILAEWKQKFEESQTELESSQKEARSLSTELFKLKNAYEESLDHLETFKRENKNLQEEISDLTEQLgesgksiH 1542
Cdd:TIGR02168 804 ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL-------E 876
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1543 ELEKIRKQLDQEKMEIQSALEEAEATLEHEEGKILhaqlelhqikaDSERKLAEKDEEMEQAKRNYQR---MVDTLQTSL 1619
Cdd:TIGR02168 877 ALLNERASLEEALALLRSELEELSEELRELESKRS-----------ELRRELEELREKLAQLELRLEGlevRIDNLQERL 945
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1620 -EAETRSRNEALRIKKKMEGDLNEMEIQLSQANRQ----------AAEAQKQVKILQSYLKDtqiQLDDALRASEDLKEN 1688
Cdd:TIGR02168 946 sEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKikelgpvnlaAIEEYEELKERYDFLTA---QKEDLTEAKETLEEA 1022
|
..
gi 1072253241 1689 IA 1690
Cdd:TIGR02168 1023 IE 1024
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
858-1625 |
2.74e-26 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 118.25 E-value: 2.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 858 LKSAETEKEMqtmKEEFQKLKEalEKSEARRKDLEEKMVSLLQEKNDLQLQVQAEQDNLADADERCEQLIKNKIQLEAKL 937
Cdd:TIGR02169 200 LERLRREREK---AERYQALLK--EKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 938 KEQTERLED--EEEMNA------ELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIVK 1009
Cdd:TIGR02169 275 EELNKKIKDlgEEEQLRvkekigELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDK 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1010 LTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKIRMDLERVKRKLEGDVKLSQESLMDLEN 1089
Cdd:TIGR02169 355 LTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEA 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1090 DKQQLEEKLKKKDFEVSQLNTRIEdeqnvciQLQKKMKELQARIEELeeeleaeRTARAKVEKLRCDLSRELEEISERL- 1168
Cdd:TIGR02169 435 KINELEEEKEDKALEIKKQEWKLE-------QLAADLSKYEQELYDL-------KEEYDRVEKELSKLQRELAEAEAQAr 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1169 ---EEAGGATSVQMELNKKREAEFLKLRRDLEESTLHSEA--TAASLRKKHA----DSVAElsEQIDNLQRVKQ------ 1233
Cdd:TIGR02169 501 aseERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAieVAAGNRLNNVvvedDAVAK--EAIELLKRRKAgratfl 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1234 KLEKEKSEFKL-----------------ELDD--------------VTSNME---------QMVKAKANLEKLCRSLEDQ 1273
Cdd:TIGR02169 579 PLNKMRDERRDlsilsedgvigfavdlvEFDPkyepafkyvfgdtlVVEDIEaarrlmgkyRMVTLEGELFEKSGAMTGG 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1274 ANEHRTKSEENQRTVNELSSLRAKLQTENGELSRRLDEKESLVSQMtrgkQTYTQHLEDLKRQLEEETKAKNALAHALQS 1353
Cdd:TIGR02169 659 SRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRL----DELSQELSDASRKIGEIEKEIEQLEQEEEK 734
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1354 ARHDSDLLREQFEEEQEAKAELQRILSKANSEVAQwrtkYETDAIQRTEELEEAKKKLAQrlqeaeEAVEAVNAKCSSLE 1433
Cdd:TIGR02169 735 LKERLEELEEDLSSLEQEIENVKSELKELEARIEE----LEEDLHKLEEALNDLEARLSH------SRIPEIQAELSKLE 804
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1434 KTKHRLQNEIEDLMVDLERSNAAAAALDKKQRNFDKILAEWKQKFEESQTELESSQKEARSLSTELFKLKNAYEESLDHL 1513
Cdd:TIGR02169 805 EEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL 884
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1514 ETFKRENKNLQEEISDLTEQLGESGKSIHELEKIRKQLDQEKMEIQSALEEAEATLEHEEgKILHAQLELHQIKADSERK 1593
Cdd:TIGR02169 885 GDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE-EIPEEELSLEDVQAELQRV 963
|
810 820 830 840
....*....|....*....|....*....|....*....|..
gi 1072253241 1594 LAE----------KDEEMEQAKRNYQRMVDTLQTsLEAETRS 1625
Cdd:TIGR02169 964 EEEiralepvnmlAIQEYEEVLKRLDELKEKRAK-LEEERKA 1004
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
928-1889 |
3.03e-26 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 118.24 E-value: 3.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 928 KNKIQLEAKLKEQTERLEDEEEMNAELTAKKRKLEDECS------ELKKDIDDLELTLAKVEKEKHatENKVKNLTEEMA 1001
Cdd:TIGR02168 172 ERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEkaerykELKAELRELELALLVLRLEEL--REELEELQEELK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1002 GLDEIIVKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKIRMDLERVKRKLEgdvklsq 1081
Cdd:TIGR02168 250 EAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELE------- 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1082 ESLMDLENDKQQLEEKLKKKDFEVSQLNTRIEDEQNVCIQLQKKMKELQARIEELEEELEAERTARAKVEKLRCDLSREL 1161
Cdd:TIGR02168 323 AQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1162 EEISERLEeaggatsvqmelnkkreaeflklrrdleestlhseataaslrkkhadsvaELSEQIDNLQRVKQKLEKEKSE 1241
Cdd:TIGR02168 403 ERLEARLE--------------------------------------------------RLEDRRERLQQEIEELLKKLEE 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1242 FKLElddvtsnmeqmvKAKANLEKLCRSLEDQANEHRTKSEENQRTVNELSSLRAKLQTENGELSRRLDEKESLVSQMtr 1321
Cdd:TIGR02168 433 AELK------------ELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQ-- 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1322 gkqtytQHLEDLKRQLEEETKAKNALAHALQSArhdSDLLReqFEEEQEAKAE------LQRILSKANSEVAQ-WRTKYE 1394
Cdd:TIGR02168 499 ------ENLEGFSEGVKALLKNQSGLSGILGVL---SELIS--VDEGYEAAIEaalggrLQAVVVENLNAAKKaIAFLKQ 567
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1395 TDAIQRT--EELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDL-----MVD-LERSNAAAAALDKKQRN 1466
Cdd:TIGR02168 568 NELGRVTflPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLlggvlVVDdLDNALELAKKLRPGYRI 647
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1467 F----DKILAEWKQKFEESQTElessqkearslstelfklknayeesldhLETFKRENknlqeEISDLTEQLGESGKSIH 1542
Cdd:TIGR02168 648 VtldgDLVRPGGVITGGSAKTN----------------------------SSILERRR-----EIEELEEKIEELEEKIA 694
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1543 ELEKIRKQLDQEKMEIQSALEEAEATLEHEEGKILHAQLELHQIKADSERkLAEKDEEMEQAKRNYQRMVDTLQTSLEAE 1622
Cdd:TIGR02168 695 ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ-LEERIAQLSKELTELEAEIEELEERLEEA 773
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1623 TRSRNEALRIKKKMEGDLNEMEIQLSQANRQAAEAQKQvkilqsyLKDTQIQLDDALRASEDLKENIAIVERRNTLLQAE 1702
Cdd:TIGR02168 774 EEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE-------LTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1703 LEELRSLVEQTERARKlSEQELIETservqlLHSQNTSLINQKKKMESDLSQLQTEMEEAVQECRNAEEKAKKAItdaam 1782
Cdd:TIGR02168 847 IEELSEDIESLAAEIE-ELEELIEE------LESELEALLNERASLEEALALLRSELEELSEELRELESKRSELR----- 914
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1783 maEELKKEQDTSAHLERMKKNMEQTIKDLQQRLDEAEQIAL-------KGGKKQLQKLEARVRELDNELEAEQKRNAESV 1855
Cdd:TIGR02168 915 --RELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLeeaealeNKIEDDEEEARRRLKRLENKIKELGPVNLAAI 992
|
970 980 990
....*....|....*....|....*....|....
gi 1072253241 1856 KGMRKYERRIKELTYQTEEDRKNLARLQDLVDKL 1889
Cdd:TIGR02168 993 EEYEELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
851-1470 |
2.48e-25 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 115.03 E-value: 2.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 851 YFKIKPLLKSAETE---KEMQTMKEEFQKLKEALEKSEARRKDLEEKMVSLLQEKNDLQLQVQAEQDNLADADERCEQLI 927
Cdd:COG1196 215 YRELKEELKELEAElllLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 928 KNKIQLEAKLKEQTERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEII 1007
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1008 VKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKIRMDLERVKRKLEGDVKLSQESLMDL 1087
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1088 ENDKQQLEEKLKKKDFEVSQLNTRIEDEQNVCIQLQKKMKELQARIEELEEELEAERTARAK---------VEKLRCDLS 1158
Cdd:COG1196 455 EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLaglrglagaVAVLIGVEA 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1159 RELEEISERLEEAGGATSVQMELNKKREAEFLKLRRDLEESTLHSEATAASLRKKHADSVAELSEQIDNLQRVKQKLEKE 1238
Cdd:COG1196 535 AYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADAR 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1239 KSEFKLELDDVTSNMEQMVKAKANLEKLCRSLEDQANEHRTKSEENQRTVNELSSLRAKLQTENGELSRRLDEKESLvsq 1318
Cdd:COG1196 615 YYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEE--- 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1319 mtrgkqtyTQHLEDLKRQLEEETKAKNALAHALQSARHDSDLLREQFEEEQEAKAELQRILSKANSEVAqwrtKYETDAI 1398
Cdd:COG1196 692 --------ELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEA----LEELPEP 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1399 QRTEELEEAKKKLAQRLQE-------AEEAVEAVNAKCSSLEKTKHRLQNEIEDLM-----VDLERSNAAAAALDKKQRN 1466
Cdd:COG1196 760 PDLEELERELERLEREIEAlgpvnllAIEEYEELEERYDFLSEQREDLEEARETLEeaieeIDRETRERFLETFDAVNEN 839
|
....
gi 1072253241 1467 FDKI 1470
Cdd:COG1196 840 FQEL 843
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1330-1941 |
1.17e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 112.72 E-value: 1.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1330 LEDLKRQ-----------LEEETKAKNALAHALQSARHDSDLLREQFEEEQEAKAELQRILSKANSEVaqwrtkyetdai 1398
Cdd:COG1196 202 LEPLERQaekaeryrelkEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAEL------------ 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1399 qrtEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAALDKKQRNFDKILAEWKQKF 1478
Cdd:COG1196 270 ---EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1479 EESQTELESSQKEARSLSTELFKLKNAYEESLDHLETFKRENKNLQEEISDLTEQLGESGKSIHELEKIRKQLDQEKMEI 1558
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1559 QSALEEAEATLEHEEGKILHAQLELHQIKADSERKLAEKDEEMEQAKRnyqrmvdtlqtsLEAETRSRNEALRIKKKMEG 1638
Cdd:COG1196 427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL------------LEAALAELLEELAEAAARLL 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1639 DLNEMEIQLSQANRQAAEAQkqvkilqsylkdtqiQLDDALRASEDLKENIAIVERRNTLLQAELEELR--SLVEQTERA 1716
Cdd:COG1196 495 LLLEAEADYEGFLEGVKAAL---------------LLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALqnIVVEDDEVA 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1717 RKLSEQELIETSERVQLLHSqntSLINQKKKMESDLSQLQTEMEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAH 1796
Cdd:COG1196 560 AAAIEYLKAAKAGRATFLPL---DKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAAL 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1797 LERMKKNMEQTIKDLQQRLDEAEQIALKGGKKQLQKLEARVRELDNELEAEQKRNAESVkgmRKYERRIKELTYQTEEDR 1876
Cdd:COG1196 637 RRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELEL---EEALLAEEEEERELAEAE 713
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1072253241 1877 KNLARLQDLVDKLQLKVKTYKRQAEESEEQANTSLSkfrKVQHELDEAEERADIAESQVNKLRAK 1941
Cdd:COG1196 714 EERLEEELEEEALEEQLEAEREELLEELLEEEELLE---EEALEELPEPPDLEELERELERLERE 775
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1234-1846 |
1.47e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 109.26 E-value: 1.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1234 KLEKEKSEFKLE--------LDDVTSNMEQMVKakanleklcrSLEDQAN---EHRTKSEE-----NQRTVNELSSLRAK 1297
Cdd:COG1196 171 KERKEEAERKLEateenlerLEDILGELERQLE----------PLERQAEkaeRYRELKEElkeleAELLLLKLRELEAE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1298 LQTENGELSRRLDEKESLVSQMTR---GKQTYTQHLEDLKRQLEEETKAKNALAHALQSARHDSDLLREQFEEEQEAKAE 1374
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAEleaELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1375 LQRilskansEVAQWRTKYETDAiQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSN 1454
Cdd:COG1196 321 LEE-------ELAELEEELEELE-EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1455 AAAAALDKKQRNFDKILaewkqkfEESQTELESSQKEARSLSTELFKLKNAYEESLDHLETFKRENKNLQEEISDLTEQL 1534
Cdd:COG1196 393 RAAAELAAQLEELEEAE-------EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1535 GESGKSIHELEKIRKQLDQEKMEIQS---ALEEAEATLEHEEGKILHAQLELHQIKADSERKLAEKDEEMEQAKRNYQRM 1611
Cdd:COG1196 466 AELLEEAALLEAALAELLEELAEAAArllLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALA 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1612 VDTLQTSLEAETRSRNEALRIKKKMEGDLNemEIQLSQANRQAAEAQKQVKILQSYLKDTQIQLDDALRASEDLKENIAI 1691
Cdd:COG1196 546 AALQNIVVEDDEVAAAAIEYLKAAKAGRAT--FLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLL 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1692 VERRNTLLQAELEELRSLVEQTERARKLSEQELIETSERVQLLHSQNTSLINQKKKMESDLSQLQTEMEEAVQECRNAEE 1771
Cdd:COG1196 624 GRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEE 703
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1072253241 1772 KAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQQRLDEAEQIALKGGKKQLQKLEARVRELDNELEA 1846
Cdd:COG1196 704 EEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1105-1927 |
3.65e-22 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 104.76 E-value: 3.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1105 VSQLNTRIEDEQNVCIQLQKKMKELQARIEELEEELEAERTARAKVEKLRcDLSRELEEIserleeaggatsvqmelnkk 1184
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQ-ALLKEKREY-------------------- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1185 REAEFLKLRRDLEESTLHSEATAASLRKKHADSVAELSEQIDNLQRVKQKLEkeksEFKLELDDVTSNMEQMVKAK-ANL 1263
Cdd:TIGR02169 224 EGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLE----ELNKKIKDLGEEEQLRVKEKiGEL 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1264 EKLCRSLEDQANEHRTKSEENQRTVNELSSLRAKLQTENGELSRRLDEKESLVSQMTRGKQTYTQHLEDLKRQLEEETKA 1343
Cdd:TIGR02169 300 EAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKE 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1344 KNALAHALQSARHDSDLLREQFEEEQEAKAELQRILSKANSEVAQWRTKYEtDAIQRTEELEEAKKKLAQRLQEAEEAVE 1423
Cdd:TIGR02169 380 FAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIA-GIEAKINELEEEKEDKALEIKKQEWKLE 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1424 AVNAKCSSLEKTKHRLQNEIEDLMVDLErsnaaaaaldKKQRNFDKILAEWKQKFEES------QTELESSQKEARSLST 1497
Cdd:TIGR02169 459 QLAADLSKYEQELYDLKEEYDRVEKELS----------KLQRELAEAEAQARASEERVrggravEEVLKASIQGVHGTVA 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1498 ELFKLKNAYEESLD-----HLETFKRENKNLQEEISDLTEQLGESGKSIHELEKIR-KQLDQEKMEIQSALEEAEATLEH 1571
Cdd:TIGR02169 529 QLGSVGERYATAIEvaagnRLNNVVVEDDAVAKEAIELLKRRKAGRATFLPLNKMRdERRDLSILSEDGVIGFAVDLVEF 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1572 EEgkilhaqlelhqiKADSERKLAEKD----EEMEQAKR---NYqRMVdtlqtSLEAE-----------TRSRNEALRIK 1633
Cdd:TIGR02169 609 DP-------------KYEPAFKYVFGDtlvvEDIEAARRlmgKY-RMV-----TLEGElfeksgamtggSRAPRGGILFS 669
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1634 KKMEGDLNEMEIQLSQANRQAAEAQKQVKILQSYLKDTQIQLDDALRASEDLKENIAIVERRNTLLQAELEELRSLVEQT 1713
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSL 749
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1714 ERARKLSEQELIETSERVQLLHSQNTSLINQKKKMESDLSqlQTEMEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDT 1793
Cdd:TIGR02169 750 EQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLS--HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLE 827
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1794 SAHLERMKKNMEQTIKDLQ-QRLDEAEQIALKGGKK-----QLQKLEARVRELDNELEAEQKRNAESVKGMRKYERRIKE 1867
Cdd:TIGR02169 828 KEYLEKEIQELQEQRIDLKeQIKSIEKEIENLNGKKeeleeELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE 907
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1868 LTYQTEEDRKNLARLQDLVDKLQLKVKTYKRQAEESEEQANTSLSkFRKVQHELDEAEER 1927
Cdd:TIGR02169 908 LEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELS-LEDVQAELQRVEEE 966
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1218-1952 |
6.94e-22 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 103.99 E-value: 6.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1218 VAELSEQIDNLQRVKQKLE--------KEKSEFKLELDDVTSNMEQMVKAKANLEKLCRSLED---QANEHRTKSEENQR 1286
Cdd:TIGR02169 193 IDEKRQQLERLRREREKAEryqallkeKREYEGYELLKEKEALERQKEAIERQLASLEEELEKlteEISELEKRLEEIEQ 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1287 TVNELSS-LRAKLQTENGELSRRLDEKESLVSQMTRGKQTYTQHLEDLKRQLEEetkaknalahaLQSARHDSDLLREQF 1365
Cdd:TIGR02169 273 LLEELNKkIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAK-----------LEAEIDKLLAEIEEL 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1366 EEEQEAKAELQRILSkanSEVAQWRTKYEtDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIED 1445
Cdd:TIGR02169 342 EREIEEERKRRDKLT---EEYAELKEELE-DLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQR 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1446 LMVDLERSNAAAAALDKKQRNFDKILAEWKQKFEESQTELESSQKEARSLSTELFKLKNAY----------EESLDHLET 1515
Cdd:TIGR02169 418 LSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYdrvekelsklQRELAEAEA 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1516 FKRENKNLQEEISDLTEQLGESGKSIHELekiRKQLDQEKMEIQSALEEA-----------------EATLEHEEGKILH 1578
Cdd:TIGR02169 498 QARASEERVRGGRAVEEVLKASIQGVHGT---VAQLGSVGERYATAIEVAagnrlnnvvveddavakEAIELLKRRKAGR 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1579 AQ-LELHQIKADSE--RKLAEKD-----------------------------EEMEQAKR---NYqRMVdtlqtSLEAE- 1622
Cdd:TIGR02169 575 ATfLPLNKMRDERRdlSILSEDGvigfavdlvefdpkyepafkyvfgdtlvvEDIEAARRlmgKY-RMV-----TLEGEl 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1623 ----------TRSRNEALRIKKKMEGDLNEMEIQLSQANRQAAEAQKQVKILQSYLKDTQIQLDDALRASEDLKENIAIV 1692
Cdd:TIGR02169 649 feksgamtggSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQL 728
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1693 ERRNTLLQAELEELRSLVEQTERARKLSEQELIETSERVQLLHSQNTSLINQKKKMESDLSQlqTEMEEAVQECRNAEEK 1772
Cdd:TIGR02169 729 EQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEE 806
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1773 AKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQQRLDEAEQialkggkkQLQKLEARVRELDNELEAEQKRNA 1852
Cdd:TIGR02169 807 VSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK--------EIENLNGKKEELEEELEELEAALR 878
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1853 ESVKGMRKYERRIKELTYQTEEDRKNLARLQDLVDKLQLKVKTYKRQAEESEEQantsLSKFRKVQHELDEAEERADIAE 1932
Cdd:TIGR02169 879 DLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE----LSEIEDPKGEDEEIPEEELSLE 954
|
810 820
....*....|....*....|
gi 1072253241 1933 SQVNKLRAKSRDVSTKKSLN 1952
Cdd:TIGR02169 955 DVQAELQRVEEEIRALEPVN 974
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
859-1551 |
1.02e-21 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 103.21 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 859 KSAETEKEMQTMKEEFQKLKEALEKSEARRKDLEEKMVSLLQEKNDLQLQVQAEQDNLADADERCEQLIKNKIQL----- 933
Cdd:TIGR02168 345 KLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLqqeie 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 934 -------EAKLKEQTERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKV---KNLTEEMAGL 1003
Cdd:TIGR02168 425 ellkkleEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLdslERLQENLEGF 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1004 DEIIVKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKAKLEQQ--VDDLE------GSLEQEKKIRMDL-------ER 1068
Cdd:TIGR02168 505 SEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAvvVENLNaakkaiAFLKQNELGRVTFlpldsikGT 584
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1069 VKRKLEGDVKLSQESLMDLENDKQQLEEKLKKKdfeVSQL--NTRIEDEQNVCIQLQKKMKElQARIEELEEELEAERTA 1146
Cdd:TIGR02168 585 EIQGNDREILKNIEGFLGVAKDLVKFDPKLRKA---LSYLlgGVLVVDDLDNALELAKKLRP-GYRIVTLDGDLVRPGGV 660
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1147 ----RAKVEKLRCDLSRELEEISERLEEAGG-ATSVQMELNKKR------EAEFLKLRRDLEESTLHSEATAASLrKKHA 1215
Cdd:TIGR02168 661 itggSAKTNSSILERRREIEELEEKIEELEEkIAELEKALAELRkeleelEEELEQLRKELEELSRQISALRKDL-ARLE 739
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1216 DSVAELSEQIDNLQRVKQKLEKEKSEfklELDDVTSNMEQMVKAKANLEKLCRSLEDQANEHRTKSEEnqrtvneLSSLR 1295
Cdd:TIGR02168 740 AEVEQLEERIAQLSKELTELEAEIEE---LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA-------LDELR 809
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1296 AKLQTENGELSRRLDEKESLVSQMTRGKQtytqHLEDLKRQLEEETKAKNALAHALQSARHDSDLLREQFEEEQEAKAEL 1375
Cdd:TIGR02168 810 AELTLLNEEAANLRERLESLERRIAATER----RLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASL 885
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1376 QRILSKANSEvaqwrtkyETDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKcssLEKTKHRLQNEIEDLMVDLERSna 1455
Cdd:TIGR02168 886 EEALALLRSE--------LEELSEELRELESKRSELRRELEELREKLAQLELR---LEGLEVRIDNLQERLSEEYSLT-- 952
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1456 aaaaldkkqrnfdkiLAEWKQKFEESQTELESSQKEARSLSTELFKLKNAYEESLDHLETFKRENKNLQEEISDLTEQLG 1535
Cdd:TIGR02168 953 ---------------LEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKE 1017
|
730
....*....|....*.
gi 1072253241 1536 ESGKSIHELEKIRKQL 1551
Cdd:TIGR02168 1018 TLEEAIEEIDREARER 1033
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1232-1929 |
1.20e-20 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 100.22 E-value: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1232 KQKLEKEKSEFKLELDDVTSNMEQMVKAKA--NLEKLCRSLEDQANEHRTKSEENQRT--VNELSSLRAKLQTENGELSR 1307
Cdd:PTZ00121 1097 FGKAEEAKKTETGKAEEARKAEEAKKKAEDarKAEEARKAEDARKAEEARKAEDAKRVeiARKAEDARKAEEARKAEDAK 1176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1308 RLDE--KESLVSQMTRGKQTYTQHLEDLKRQLEEETKAKNALAHALQSARHDSDLLREQFEEEQEAK-AELQRilskANS 1384
Cdd:PTZ00121 1177 KAEAarKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKkAEEER----NNE 1252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1385 EVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDlmvdlersNAAAAALDKKQ 1464
Cdd:PTZ00121 1253 EIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEE--------AKKADEAKKKA 1324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1465 RNFDKILAEWKQKFEESQTELESSQKEARSLSTELfklkNAYEESLDHLETFKRENKNLQEEISDLTEQLGESGKSIHEL 1544
Cdd:PTZ00121 1325 EEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEA----EAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKA 1400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1545 EKIRKQLDQEKMEIQSALEEAEATLEHEEGKilhaqlelhqiKADSERKLAEKDEEMEQAKRNYQRMVDTLQTSLEAETR 1624
Cdd:PTZ00121 1401 EEDKKKADELKKAAAAKKKADEAKKKAEEKK-----------KADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEA 1469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1625 SRNEALRIKKKMEGDLNEMEIQLSQANRQAAEAQKQV---KILQSYLKDTQIQLDDALRASEDLKeniaiveRRNTLLQA 1701
Cdd:PTZ00121 1470 KKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAeakKKADEAKKAEEAKKADEAKKAEEAK-------KADEAKKA 1542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1702 ELEELRSLVEQTERARKLSEQELIETSERVQllHSQNTSLINQKKKMESDLSQLQTEMEEAVQECRNAEEKAKKAiTDAA 1781
Cdd:PTZ00121 1543 EEKKKADELKKAEELKKAEEKKKAEEAKKAE--EDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA-EEAK 1619
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1782 MMAEELKKEQDTSAHLERMKKNMEQTIKDLQQRLDEAEQIALKggKKQLQKLEARVRELDNEL---EAEQKRNAESVKGM 1858
Cdd:PTZ00121 1620 IKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIK--AAEEAKKAEEDKKKAEEAkkaEEDEKKAAEALKKE 1697
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1072253241 1859 RKYERRIKELTYQTEEDRKNLARLQDLVDKLQLKVKTYKRQAEESE---EQANTSLSKFRKVQHELDEAEERAD 1929
Cdd:PTZ00121 1698 AEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKkkaEEAKKDEEEKKKIAHLKKEEEKKAE 1771
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1288-1949 |
2.41e-20 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 98.99 E-value: 2.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1288 VNELSSLRAKLQTENGELSRRLDEKESLVS----QMTRGKQTYTQHLEDLKRQLEEETKAKNALAHALQSARHDSDLLRE 1363
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDekrqQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1364 QFEEEQEAKAELQRILSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEI 1443
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1444 EDLMVDLERSNAAAAALDKKQRNFDKILAEWKQKFEESQTELESSQKEARSLST-------ELFKLKNAYEESLDHLETF 1516
Cdd:TIGR02169 325 AKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKefaetrdELKDYREKLEKLKREINEL 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1517 KRENKNLQEEISDLTEQLGESGKSIHELEKIRKQLDQEKMEIQSALEEAEATLEHEEGKILHAQLELHQIKADserkLAE 1596
Cdd:TIGR02169 405 KRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEE----YDR 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1597 KDEEMEQAKRNYQRMVDTLQTSLEAETRSRNEALRIKKKMEG------DLNEMEIQLSQANRQAAEAQKQVKILQS---- 1666
Cdd:TIGR02169 481 VEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGvhgtvaQLGSVGERYATAIEVAAGNRLNNVVVEDdava 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1667 -----YLKDTQI---------QLDDALRASEDLKENIAI------VER------------RNTLLQAELEELRSLVEQ-- 1712
Cdd:TIGR02169 561 keaieLLKRRKAgratflplnKMRDERRDLSILSEDGVIgfavdlVEFdpkyepafkyvfGDTLVVEDIEAARRLMGKyr 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1713 -------------------------TERARKLSEqELIETSERVQLLHSQNTSLINQKKKMESDLSQLQTEMEEAVQECR 1767
Cdd:TIGR02169 641 mvtlegelfeksgamtggsraprggILFSRSEPA-ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIG 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1768 NAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQQRLDEAEQiALKGGKKQLQKLEAR-----VRELDN 1842
Cdd:TIGR02169 720 EIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEE-DLHKLEEALNDLEARlshsrIPEIQA 798
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1843 ELEAEQKRNAESVKGMRKYERRIKELTYQTEEDRKNLARLQDLVDKLQLKVKTYKRQAEESEEQANTSLSKFRKVQHELD 1922
Cdd:TIGR02169 799 ELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALR 878
|
730 740
....*....|....*....|....*..
gi 1072253241 1923 EAEERADIAESQVNKLRAKSRDVSTKK 1949
Cdd:TIGR02169 879 DLESRLGDLKKERDELEAQLRELERKI 905
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1254-1949 |
4.20e-20 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 97.94 E-value: 4.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1254 EQMVKAKANLEKLCRSLEDQANEHRTKSEENqrtvnelSSLRAKLQTENgELsrrLDEKESLVSQMTRGKQTYTQHLEDL 1333
Cdd:pfam01576 12 EELQKVKERQQKAESELKELEKKHQQLCEEK-------NALQEQLQAET-EL---CAEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1334 KRQLEEETKAKNALAHALQSARHDSDLLREQFEEEQEAKAELQRILSKANSEVAQWRTKYETDAIQRTEeLEEAKKKLAQ 1413
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSK-LSKERKLLEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1414 RLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAALDKKQRNFDKILAEWKQKFEESQTELESSQKEAR 1493
Cdd:pfam01576 160 RISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1494 SLSTELFKLKNAYEESLDHLETFKRENKNLQEEISDLTEQLGESGKSIHELEKIRKQLDQEKMEIQSALEEAEATLEHEE 1573
Cdd:pfam01576 240 KKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1574 GKILHAQLELHQIKADSERKLAEKDEEMEQAKRNYQRMVDTLQTSLEAETRSRNEALRIKKKMEGDLNEMEIQLSQANRQ 1653
Cdd:pfam01576 320 ELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1654 AAEAQKQVKILQSYLKDTQIQLDDALRASEDLKEniaiverRNTLLQAELEELRSLVEQTE-RARKLS------EQELIE 1726
Cdd:pfam01576 400 KQDSEHKRKKLEGQLQELQARLSESERQRAELAE-------KLSKLQSELESVSSLLNEAEgKNIKLSkdvsslESQLQD 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1727 TSERVQLLHSQNTSLINQKKKMESDLSQLQTEMEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQ 1806
Cdd:pfam01576 473 TQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQR 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1807 TIKDLQQRLDEAEQIALKggkkqLQKLEARVRELDNELEAEQKRNAESVKGMRKYERRIKELTyqtEEDRKNLARLQDLV 1886
Cdd:pfam01576 553 ELEALTQQLEEKAAAYDK-----LEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQML---AEEKAISARYAEER 624
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1072253241 1887 DKLQlkvktykRQAEESEeqantslSKFRKVQHELDEAEERADIAESQVNKLRAKSRDVSTKK 1949
Cdd:pfam01576 625 DRAE-------AEAREKE-------TRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSK 673
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1092-1765 |
6.23e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 97.31 E-value: 6.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1092 QQLEEKLKKKDFEVSQLNTRiedeqnvciQLQKKMKELQARIEELEEELEAERTARAKVEKLRCDLSRELEEISERLEEA 1171
Cdd:COG1196 216 RELKEELKELEAELLLLKLR---------ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1172 GGatsvQMELNKKREAEFLKLRRDLEESTLHSEATAASLRKKHADSVAELSEQIDNLQRVKQKLEKEKSEFKLELDDVTS 1251
Cdd:COG1196 287 QA----EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1252 NMEQMVKAKANLEKLCRSLEDQANEHRTKSEENQRTVNELSSLRAKLQTENGELSRRLDEKESLVSQMTRGKQTytqhLE 1331
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE----EE 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1332 DLKRQLEEETKAKNALAHALQSARHDSDLLREQFEEEQEAKAELQRILSKANSEvaqwrtKYETDAIQRTEELEEAKKKL 1411
Cdd:COG1196 439 EEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR------LLLLLEAEADYEGFLEGVKA 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1412 AQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAAldkKQRNFDKILAEWKQKFEESQTELESSQKE 1491
Cdd:COG1196 513 ALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAA---AAIEYLKAAKAGRATFLPLDKIRARAALA 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1492 ARSLSTELFKLKNAYEESLDHLETFKRENKNLQEEISDLTEQLGESGKSIHELEkirkqldqekmeiqsaLEEAEATLEH 1571
Cdd:COG1196 590 AALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLA----------------GRLREVTLEG 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1572 EEGKILHAQLELHQIKADSERKLAEKDEEMEQAKRNYQRmvdtlqtsLEAETRSRNEALRIKKKMEGDLNEMEIQLSQAN 1651
Cdd:COG1196 654 EGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEE--------LELEEALLAEEEEERELAEAEEERLEEELEEEA 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1652 RQAAEAQKQVKILQSYLKDTQIQLDDALRASEDLkeniaiverrntllqAELEELRSLVEQTERARK-------LSEQEL 1724
Cdd:COG1196 726 LEEQLEAEREELLEELLEEEELLEEEALEELPEP---------------PDLEELERELERLEREIEalgpvnlLAIEEY 790
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1072253241 1725 IETSERVQLLHSQNTSLINQKKKMESDLSQLQTEMEEAVQE 1765
Cdd:COG1196 791 EELEERYDFLSEQREDLEEARETLEEAIEEIDRETRERFLE 831
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1101-1952 |
1.08e-19 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 97.13 E-value: 1.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1101 KDFEVSQLNTRIEDEQNVciQLQKKMKELQARIEELEEELEAERTARAKVEKLRCDLSRELEEISERLEEAGGATSVQME 1180
Cdd:PTZ00121 1077 KDFDFDAKEDNRADEATE--EAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRV 1154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1181 LNKKR--EAEFLKLRRDLEESTLHSEA-TAASLRKKHADSVAELSEQIDNLQRVKQKLEKEKSEfKLELDDVTSNMEQMV 1257
Cdd:PTZ00121 1155 EIARKaeDARKAEEARKAEDAKKAEAArKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEAR-KAEDAKKAEAVKKAE 1233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1258 KAKANLEKLCRSLEDQANEHRTKSEENQrtVNELSSLRAKLQTENGELSRRLDEKESLVSQMTRGKQTYTQHLEDLKRQL 1337
Cdd:PTZ00121 1234 EAKKDAEEAKKAEEERNNEEIRKFEEAR--MAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKA 1311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1338 EEETKAKNALAHAlQSARHDSDLLREQFEEEQEAKAELQRILSKANSEVAQWRTKYETDAIQRteelEEAKKKLAQRLQE 1417
Cdd:PTZ00121 1312 EEAKKADEAKKKA-EEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKK----EEAKKKADAAKKK 1386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1418 AEEAVEAVNAKCSSLEKTKhrlqneiedlmvdlERSNAAAAALDKKQRNFDKILAEWKQKFEESQTELESSQK--EARSL 1495
Cdd:PTZ00121 1387 AEEKKKADEAKKKAEEDKK--------------KADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKadEAKKK 1452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1496 STELFKLKNAYEesldhletfKRENKNLQEEISDLTEQLGESGKSIHELEKIRKQLDQEKmEIQSALEEAEATLEHEEGK 1575
Cdd:PTZ00121 1453 AEEAKKAEEAKK---------KAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAK-KAAEAKKKADEAKKAEEAK 1522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1576 ilhaqlelhqiKADSERKLAEKDEEMEQAKRNYQRMVDTLQTSLEAETRSRNEALRIKKKMEGDLNeMEIQLSQANRQAA 1655
Cdd:PTZ00121 1523 -----------KADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKN-MALRKAEEAKKAE 1590
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1656 EAQKQvKILQSYLKDTQIQLDDALRASEdlkeniaivERRNTLLQAELEELRSLVEQTerarKLSEQELIETSERVQLLH 1735
Cdd:PTZ00121 1591 EARIE-EVMKLYEEEKKMKAEEAKKAEE---------AKIKAEELKKAEEEKKKVEQL----KKKEAEEKKKAEELKKAE 1656
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1736 SQNTSLINQKKKMESdlsqlqtEMEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQQRL 1815
Cdd:PTZ00121 1657 EENKIKAAEEAKKAE-------EDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENK 1729
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1816 DEAEQIALKGGKKQLQKLEARVRELDNELEAEQKRNAESvkgMRKYERRIKELTYQTEEDRKNLARLQDlVDKLQLKVKT 1895
Cdd:PTZ00121 1730 IKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEK---KAEEIRKEKEAVIEEELDEEDEKRRME-VDKKIKDIFD 1805
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*..
gi 1072253241 1896 YKRQAEESEEQANTSLSKFRKVqhELDEAEERADIAESQVNKLRAKSRDVSTKKSLN 1952
Cdd:PTZ00121 1806 NFANIIEGGKEGNLVINDSKEM--EDSAIKEVADSKNMQLEEADAFEKHKFNKNNEN 1860
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
237-724 |
1.56e-19 |
|
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: 95.97 E-value: 1.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 237 IIQANPALEAFGNAKTLRNDNSSRFGKF--IRIHFGATG---KLASADIETYLLEKSRVIFQL------KSERDYHIFYQ 305
Cdd:cd14894 249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPwefQICGCHISPFLLEKSRVTSERgresgdQNELNFHILYA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 306 ILSNKKPELLDMLLVTNNPYD------YAYISQGETTVASIDDAEELLATD--------SAFDVLGFTQDEKNSIYKLTG 371
Cdd:cd14894 329 MVAGVNAFPFMRLLAKELHLDgidcsaLTYLGRSDHKLAGFVSKEDTWKKDverwqqviDGLDELNVSPDEQKTIFKVLS 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 372 AVMHFGNMKFKQKQREEQAEPDGT---EEADKVAYLMGLNSADLLKGLCHPR---VKVGNEYVTKGQNVQQVYYSTGALG 445
Cdd:cd14894 409 AVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGSVEKLERMLMTKsvsLQSTSETFEVTLEKGQVNHVRDTLA 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 446 KSVYEKMFLWMVVRIN-----TTLETKQPRQY------------FIGVLDIAGFEIFDFNSFEQMCINFTNEKLQQFFNH 508
Cdd:cd14894 489 RLLYQLAFNYVVFVMNeatkmSALSTDGNKHQmdsnasapeavsLLKIVDVFGFEDLTHNSLDQLCINYLSEKLYAREEQ 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 509 HMFVLEQEEYKKEGIEWEfidfgmdlQACIDLIEKPMGIMSILEEECMFPKATDVT----------FKAKLYDNHlgkSN 578
Cdd:cd14894 569 VIAVAYSSRPHLTARDSE--------KDVLFIYEHPLGVFASLEELTILHQSENMNaqqeekrnklFVRNIYDRN---SS 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 579 NFQKPRNLKGRPEAH---------FALVHYAGTVDYNINGWLVKNKDPL-NETVVGLYQKSALKLLAHLFANYASAESDQ 648
Cdd:cd14894 638 RLPEPPRVLSNAKRHtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVyANLLVGLKTSNSSHFCRMLNESSQLGWSPN 717
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1072253241 649 ATKGKGSKKKGSSFQTVSAL--HRENLNKLMTNLRATHPHFVRCIIPNETKSPGMMDNRLVMHQLRCNGVLEGIRICR 724
Cdd:cd14894 718 TNRSMLGSAESRLSGTKSFVgqFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQMEICR 795
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1019-1812 |
1.59e-18 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 92.87 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1019 EAHQQALDDLQAEEDKVNTL-TKAKAKLEQQVDDLEGSLEQekkirMDLERvkrklegdvklsqESLMDLENDKQQLEEK 1097
Cdd:pfam15921 81 EEYSHQVKDLQRRLNESNELhEKQKFYLRQSVIDLQTKLQE-----MQMER-------------DAMADIRRRESQSQED 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1098 LKKkdfevsqlntriedeqnvciQLQKKMKELQArieeleeeleaertARAKVEKLRCDLSRELEEISE-RLEEAGGATS 1176
Cdd:pfam15921 143 LRN--------------------QLQNTVHELEA--------------AKCLKEDMLEDSNTQIEQLRKmMLSHEGVLQE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1177 VQMELNKKREAEFLKLRRDLEESTLHSEATAASLRKKHADSVAELSEQIDNLQRVKQKLEKEKSE----FKLELDDVTSN 1252
Cdd:pfam15921 189 IRSILVDFEEASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSEsqnkIELLLQQHQDR 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1253 MEQMVKAKanlEKLCRSLEDQANEHRTKSEENQrtvNELSSLRAKLQTENGELSRRLDEKESLVSQMT----RGKQTYTQ 1328
Cdd:pfam15921 269 IEQLISEH---EVEITGLTEKASSARSQANSIQ---SQLEIIQEQARNQNSMYMRQLSDLESTVSQLRselrEAKRMYED 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1329 HLEDLKRQL----EEETKAKNALAHALQSARHDSDLLREQFEEEQEAKAEL-------QRILSK-ANSEVAQWRTKYETD 1396
Cdd:pfam15921 343 KIEELEKQLvlanSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELslekeqnKRLWDRdTGNSITIDHLRRELD 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1397 ----AIQRTEELEEAKKKLAQ--------RLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLM---VDLERSNAA----A 1457
Cdd:pfam15921 423 drnmEVQRLEALLKAMKSECQgqmerqmaAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTakkMTLESSERTvsdlT 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1458 AALDKKQRNFDKILAEWKQ-------KFEESQtELESSQKEARSLSTELFKLKNAYEESLDHLETfkrenknLQEEISDL 1530
Cdd:pfam15921 503 ASLQEKERAIEATNAEITKlrsrvdlKLQELQ-HLKNEGDHLRNVQTECEALKLQMAEKDKVIEI-------LRQQIENM 574
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1531 TEQLGESGKSIHELEKIRKQLDQEKMEIQSALEEAEATLEHEEGKILH-----AQLELHQIK---ADSERKLAEKDEEME 1602
Cdd:pfam15921 575 TQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRElearvSDLELEKVKlvnAGSERLRAVKDIKQE 654
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1603 QakrnyQRMVDTLQTSLEAETRSRNEALRIKKKMEGDLNEMEIQLSQANRQAAEAQKQVKILQSYLKDTQIQLDDALRAS 1682
Cdd:pfam15921 655 R-----DQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVA 729
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1683 EDLKENIaiverrnTLLQAELEELRSLVEQTERARKLSEQELIETSERVQLLHSQNTSLINQKKKMESDLSQLQTEMEEA 1762
Cdd:pfam15921 730 MGMQKQI-------TAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRL 802
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1763 VQECRNAEEKAKKAITDAAMMAEELKKEQDTSAhleRMKKNMEQTIKDLQ 1812
Cdd:pfam15921 803 KEKVANMEVALDKASLQFAECQDIIQRQEQESV---RLKLQHTLDVKELQ 849
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
853-1557 |
3.18e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 92.13 E-value: 3.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 853 KIKPLLKSAETEKEMQTMKEEFQKLKEALEKSEARRKDLEEKMVSllqekndlqLQVQAEQDNLADADERCEQLIKNKIQ 932
Cdd:PTZ00121 1201 KAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKA---------EEERNNEEIRKFEEARMAHFARRQAA 1271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 933 LEAKLKEQTERLEDEEEMNAELTAKKRKLEDECSELKKdiddleltlaKVEKEKHATENKVKnlTEEMAGLDEIIVKLTK 1012
Cdd:PTZ00121 1272 IKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKK----------KAEEAKKADEAKKK--AEEAKKKADAAKKKAE 1339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1013 EKKALQEA----HQQALDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKK---IRMDLERVKRKLEgDVKLSQESLM 1085
Cdd:PTZ00121 1340 EAKKAAEAakaeAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKadeAKKKAEEDKKKAD-ELKKAAAAKK 1418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1086 DLENDKQQLEEKLKKKDFEVSQLNTRIEDEQNVCIQLQKKMKELQARIEELEEELEAERTARAKveKLRCDLSRELEEIS 1165
Cdd:PTZ00121 1419 KADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEA--KKADEAKKKAEEAK 1496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1166 ERLEEAGGATSVQM---ELNKKREAEFLKLRRDLEESTLHSEATAASLRKKhADSVAElSEQIDNLQRVKQKLEKEKSE- 1241
Cdd:PTZ00121 1497 KKADEAKKAAEAKKkadEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKK-ADELKK-AEELKKAEEKKKAEEAKKAEe 1574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1242 ---------------FKLELDDVTSNMEQMVKAKANLEKLCRSLEDQANEHRtKSEENQRTVNELSSLRAKLQTENGELS 1306
Cdd:PTZ00121 1575 dknmalrkaeeakkaEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELK-KAEEEKKKVEQLKKKEAEEKKKAEELK 1653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1307 RRLDEKESLVSQMTRGKQTYTQHLEDLKRQLEEETKAKNALAHALQSARHDSDLlrEQFEEEQEAKAELQRILSKANSEV 1386
Cdd:PTZ00121 1654 KAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEEL--KKKEAEEKKKAEELKKAEEENKIK 1731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1387 AQWRTKYETDAIQRTEEL---EEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLE----RSNAAAAA 1459
Cdd:PTZ00121 1732 AEEAKKEAEEDKKKAEEAkkdEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKikdiFDNFANII 1811
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1460 LDKKQRNFdkILAEWKQKFEESQTEL----ESSQKEARSLSTELFKLKNAYEESLDHLETFKRENKNLQEEISDLTEQlg 1535
Cdd:PTZ00121 1812 EGGKEGNL--VINDSKEMEDSAIKEVadskNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEA-- 1887
|
730 740
....*....|....*....|..
gi 1072253241 1536 esgksiheleKIRKQLDQEKME 1557
Cdd:PTZ00121 1888 ----------DEIEKIDKDDIE 1899
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
858-1403 |
5.22e-18 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 90.89 E-value: 5.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 858 LKSAETEKEMQTMKEEFQKLKEALEKSEARRKDLEEKMVSL--LQEKNDLQLQVQAEQDNLADADERCEQLIKNKIQLEA 935
Cdd:PRK03918 245 KELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELkeLKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIN 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 936 KLKEQTERLEDEEEMNAELTAKKRKLEDECSELKKD-------------------------IDDLELTLAKVEKEKHATE 990
Cdd:PRK03918 325 GIEERIKELEEKEERLEELKKKLKELEKRLEELEERhelyeeakakkeelerlkkrltgltPEKLEKELEELEKAKEEIE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 991 NKVKNLTEEMAGLDEIIVKLTKEKKALQEAHQQ--ALDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKIRMDLER 1068
Cdd:PRK03918 405 EEISKITARIGELKKEIKELKKAIEELKKAKGKcpVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRE 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1069 VKRKLEGDVKLSqeSLMDLENDKQQLEEKLKKKDFE-VSQLNTRIEDEQNVCIQLQKKMKELQARIEELEEELEAERTAR 1147
Cdd:PRK03918 485 LEKVLKKESELI--KLKELAEQLKELEEKLKKYNLEeLEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELE 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1148 AKVEKLRcdlsRELEEISERLEEAGGATSVQMELNKKREAEFLKlrrdleestlhseataaslrkkhadSVAELSEQIDN 1227
Cdd:PRK03918 563 KKLDELE----EELAELLKELEELGFESVEELEERLKELEPFYN-------------------------EYLELKDAEKE 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1228 LQRVKQKLEKEKSEFKLELDDVTSNMEQMVKAKANLEKLCRSLEDQanEHRTKSEENQRTVNELSSLRAKLQtengELSR 1307
Cdd:PRK03918 614 LEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEE--EYEELREEYLELSRELAGLRAELE----ELEK 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1308 RLDEKESLvsqmtrgkqtytqhLEDLKRQLEEETKAKNALaHALQSARHDSDLLREQF-----EEEQEAKAELQRILSKA 1382
Cdd:PRK03918 688 RREEIKKT--------------LEKLKEELEEREKAKKEL-EKLEKALERVEELREKVkkykaLLKERALSKVGEIASEI 752
|
570 580
....*....|....*....|.
gi 1072253241 1383 NSEVAQwrTKYETDAIQRTEE 1403
Cdd:PRK03918 753 FEELTE--GKYSGVRVKAEEN 771
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
859-1744 |
9.74e-18 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 90.23 E-value: 9.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 859 KSAETEKEMQTMKEEFQKLKEALEKS----EARRKDLEEKMVSLLQEKNDLQLQVQAEQDNLADADERCEQLIKNKIQLE 934
Cdd:pfam01576 353 KHTQALEELTEQLEQAKRNKANLEKAkqalESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELA 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 935 AKLKEQTERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEiivkltkek 1014
Cdd:pfam01576 433 EKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQE--------- 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1015 kalqeahqqaldDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKIRMDLERVKRKLEgdvklsqeslMDLENDKQQL 1094
Cdd:pfam01576 504 ------------QLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQ----------RELEALTQQL 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1095 EEKLKKKDfevsqlntriedeqnvciQLQKKMKELQARIEELEEELEAERTARAKVEKLRCDLSRELEE---ISERLEEA 1171
Cdd:pfam01576 562 EEKAAAYD------------------KLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEekaISARYAEE 623
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1172 GGATSVQmelNKKREAEFLKLRRDLEEstlhseataaslrkkhadsvaelseqidnLQRVKQKLEKEKSEFKLELDDVTS 1251
Cdd:pfam01576 624 RDRAEAE---AREKETRALSLARALEE-----------------------------ALEAKEELERTNKQLRAEMEDLVS 671
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1252 NMEQMVKAKANLEKLCRSLEDQANEHRTKSEEnqrtvnelssLRAKLQTEngelsrrldekeslvsqmtrgkqtytqhlE 1331
Cdd:pfam01576 672 SKDDVGKNVHELERSKRALEQQVEEMKTQLEE----------LEDELQAT-----------------------------E 712
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1332 DLKRQLEEETKAknalahalqsarhdsdlLREQFEEEQEAKAEL----QRILSKansEVAQWRTKYETDAIQRTEELeEA 1407
Cdd:pfam01576 713 DAKLRLEVNMQA-----------------LKAQFERDLQARDEQgeekRRQLVK---QVRELEAELEDERKQRAQAV-AA 771
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1408 KKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAaaldkkqrnfDKILAEWKQkfeesqteles 1487
Cdd:pfam01576 772 KKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASR----------DEILAQSKE----------- 830
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1488 SQKEARSLSTELFKLKNAYEESLDHLETFKRENKNLQEEISDlteqlGESGKSIHELEKirKQLDQEKMEIQSALEEAEA 1567
Cdd:pfam01576 831 SEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIAS-----GASGKSALQDEK--RRLEARIAQLEEELEEEQS 903
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1568 TLEHEEGKILHAQLELHQIKAD--SERKLAEKDEEM-EQAKRNYQRMVDTLQtSLEAETRSRNEALriKKKMEGDLNEME 1644
Cdd:pfam01576 904 NTELLNDRLRKSTLQVEQLTTElaAERSTSQKSESArQQLERQNKELKAKLQ-EMEGTVKSKFKSS--IAALEAKIAQLE 980
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1645 IQLSQANRQAAEAQKQVKILQSYLKDTQIQLDDALRASEDLKENIAIVERRNTLLQAELEELRSLVEQTERARKLSEQEL 1724
Cdd:pfam01576 981 EQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQREL 1060
|
890 900
....*....|....*....|
gi 1072253241 1725 IETSERVQLLHSQNTSLINQ 1744
Cdd:pfam01576 1061 DDATESNESMNREVSTLKSK 1080
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
981-1879 |
1.03e-17 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 90.03 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 981 KVEKEKHATENKVKNLTEEMAGLDEIIvkltKEKKALQEAHQQALDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEK 1060
Cdd:pfam02463 143 KIEIIAMMKPERRLEIEEEAAGSRLKR----KKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEK 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1061 KIRMDLERVKRKLEGDVKLSQESLMDLENDKQQLEEKLKKKDFEVSQLNTRIEDEQNVCIQLQKKMKELQARIeelEEEL 1140
Cdd:pfam02463 219 LELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLL---AKEE 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1141 EAERTARAKVEKLRCDLSRELEEISERLEEAggatSVQMELNKKREAEFLKLRRDLEESTLHSEATAASLRKKHADSVAE 1220
Cdd:pfam02463 296 EELKSELLKLERRKVDDEEKLKESEKEKKKA----EKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQL 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1221 LSEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQMVKAKANLEKLCRSLEDQANEHRTKSEENQRTVNELSSLRAKLQT 1300
Cdd:pfam02463 372 EEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKE 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1301 ENGELSRRLDEKESLVSQMTRGKQTYTQHLEDLKRQLEEETKAKNALAHALQSARHDSDLLREQFEEEQEAKAELQRILS 1380
Cdd:pfam02463 452 ELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRL 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1381 KANSEVAqwrtkyETDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAAL 1460
Cdd:pfam02463 532 GDLGVAV------ENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNL 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1461 DKKQR-----NFDKILAEWKQKFEESQTELESSQKEARSLSTELF-----KLKNAYEESLDHLETFKRENKNLQEEISDL 1530
Cdd:pfam02463 606 AQLDKatleaDEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKgvsleEGLAEKSEVKASLSELTKELLEIQELQEKA 685
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1531 TEQLGESGKSIHELEKIRKQLDQEKMEIQSALEEaeatlehEEGKILHAQLELHQIKADSERKLAEKDEEMEQAKRNYQR 1610
Cdd:pfam02463 686 ESELAKEEILRRQLEIKKKEQREKEELKKLKLEA-------EELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLK 758
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1611 MVDTLQTSLEAETRSRNEALRIKKkmegDLNEMEIQLSQANRQAAEAQKQVKILQSYLKDTQIQLDDALRASEDLKENia 1690
Cdd:pfam02463 759 KEEKEEEKSELSLKEKELAEEREK----TEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKE-- 832
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1691 ivERRNTLLQAELEELRSLVEQTERARKLSEQELIETSERVQLLHSQNTSLINQKKKMESDLSQLQTEMEEAVQECRNAE 1770
Cdd:pfam02463 833 --EELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLN 910
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1771 EKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQQRLDEAEQIALKGGKKQLQKLEARVRELDNELEAEQKR 1850
Cdd:pfam02463 911 LLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERY 990
|
890 900
....*....|....*....|....*....
gi 1072253241 1851 NAESVKGMRKYERRIKELTYQTEEDRKNL 1879
Cdd:pfam02463 991 NKDELEKERLEEEKKKLIRAIIEETCQRL 1019
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1330-1858 |
2.41e-17 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 88.56 E-value: 2.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1330 LEDLKRQLEE-ETKAKNALAHALQSARHDSDLLREQFEEEQEAKAElqrILSKANSEVAQWRTKYEtdaiqRTEELEEAK 1408
Cdd:PRK02224 189 LDQLKAQIEEkEEKDLHERLNGLESELAELDEEIERYEEQREQARE---TRDEADEVLEEHEERRE-----ELETLEAEI 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1409 KKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAALDKKQRNFDKILAEWKQKFEESQT----- 1483
Cdd:PRK02224 261 EDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVaaqah 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1484 --ELESSQKEARSLSTELFKLKNA-------YEESLDHLETFKRENKNLQEEISDLTEQLGESGKSIHELEKIRKQLDQE 1554
Cdd:PRK02224 341 neEAESLREDADDLEERAEELREEaaeleseLEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1555 KMEIQSALEEAEATLEHEEGKILHAQLELHQIK-----------------ADSERKLAEKDEEMEQAKRNYQRMVDTLQT 1617
Cdd:PRK02224 421 RDELREREAELEATLRTARERVEEAEALLEAGKcpecgqpvegsphvetiEEDRERVEELEAELEDLEEEVEEVEERLER 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1618 SLEA-ETRSRNEALRIKKKMEGDL-NEMEIQLSQANRQAAEAQKQVKILQSYLKDTQIQLDDALRASEDLKENIAIVERR 1695
Cdd:PRK02224 501 AEDLvEAEDRIERLEERREDLEELiAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSK 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1696 NTLLQAELEELRSLVEQTERARKLsEQELIETSERVQLLHSQNTSLINQKKKMESDLSQLQTEMEEA-VQECRNAEEKAK 1774
Cdd:PRK02224 581 LAELKERIESLERIRTLLAAIADA-EDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEArIEEAREDKERAE 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1775 KAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQQRLDeaeqiALKGGKKQLQKLEARVRELDN---ELEAE-QKR 1850
Cdd:PRK02224 660 EYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERRE-----ALENRVEALEALYDEAEELESmygDLRAElRQR 734
|
....*...
gi 1072253241 1851 NAESVKGM 1858
Cdd:PRK02224 735 NVETLERM 742
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
866-1871 |
2.53e-17 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 89.02 E-value: 2.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 866 EMQTMKEEFQKLKEALEKSEARRKDLEEKMVSLLQEK-NDLQLQVQAEQDNLADADERCEQLIKNKIQLEAKLKEQTERL 944
Cdd:pfam15921 114 DLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTvHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSIL 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 945 EDEEEmnaeltAKKRKLEDECSELKKDIDDLELTLAKVEKEkhatenkvknLTEEMAGLDEIIVKLTKEKKALQEAHQQA 1024
Cdd:pfam15921 194 VDFEE------ASGKKIYEHDSMSTMHFRSLGSAISKILRE----------LDTEISYLKGRIFPVEDQLEALKSESQNK 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1025 LD-DLQAEEDKVNTL-TKAKAKLEQQVDDLEGSLEQEKKIRMDLERVKRKLEGDVKLSQESLMDLENDKQQLEEKLK--K 1100
Cdd:pfam15921 258 IElLLQQHQDRIEQLiSEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELReaK 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1101 KDFEvsqlntriedeqnvciqlqKKMKELQARIEELEEELEAERTARAKVEKLRCDLSRELEEISERLEEAGGATSVQME 1180
Cdd:pfam15921 338 RMYE-------------------DKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKE 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1181 LNKK-------REAEFLKLRRDLEESTLHSEATAASLRKKHADSVAELSEQIDNLQRVKQKLEKEKS---EFKLELDDVT 1250
Cdd:pfam15921 399 QNKRlwdrdtgNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSltaQLESTKEMLR 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1251 SNMEQMVKAKANLEKLCRSLEDQANEHRTKSEENQRTVNELSSLRAKLQTENGELSRRLDEKESLvsqmtRGKQTytqHL 1330
Cdd:pfam15921 479 KVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHL-----RNVQT---EC 550
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1331 EDLKRQLEEETKAknalahalqsarhdSDLLREQFEEEQEAKAELQRILSKANSEVAQwrtkYETDAIQRTEELEEAK-- 1408
Cdd:pfam15921 551 EALKLQMAEKDKV--------------IEILRQQIENMTQLVGQHGRTAGAMQVEKAQ----LEKEINDRRLELQEFKil 612
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1409 --------KKLAQRLQEAE-EAVEAVNAKCSSLEKTK------HRLQNEIEDLMVDLERSNAAAAALDKKQRN----FDK 1469
Cdd:pfam15921 613 kdkkdakiRELEARVSDLElEKVKLVNAGSERLRAVKdikqerDQLLNEVKTSRNELNSLSEDYEVLKRNFRNkseeMET 692
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1470 ILAEWKQKFEESQTELESSQKEARSLS-TELFKLKNAYeeSLDHLETFKRENKN-LQEEISDLTEQLGESGKSIHELEKI 1547
Cdd:pfam15921 693 TTNKLKMQLKSAQSELEQTRNTLKSMEgSDGHAMKVAM--GMQKQITAKRGQIDaLQSKIQFLEEAMTNANKEKHFLKEE 770
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1548 RKQLDQEKMEIQSALEEAEATLEheegkILHAQlelhqikadsERKLAEKDEEME----QAKRNYQRMVDTLQtsleaet 1623
Cdd:pfam15921 771 KNKLSQELSTVATEKNKMAGELE-----VLRSQ----------ERRLKEKVANMEvaldKASLQFAECQDIIQ------- 828
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1624 RSRNEALRIKKKMEGDLNEMEIQLSQANRQ-AAEAQKQVKILQSYLKDTQIQLDDALRASEDLKENiAIVERRNTLLQAE 1702
Cdd:pfam15921 829 RQEQESVRLKLQHTLDVKELQGPGYTSNSSmKPRLLQPASFTRTHSNVPSSQSTASFLSHHSRKTN-ALKEDPTRDLKQL 907
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1703 LEELRSLVEQTE-----------------RARKLSEQELIETSERVQLLHSQNTSLINQKKKMESDLSQ----LQTEMEE 1761
Cdd:pfam15921 908 LQELRSVINEEPtvqlskaedkgrapslgALDDRVRDCIIESSLRSDICHSSSNSLQTEGSKSSETCSRepvlLHAGELE 987
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1762 AVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLerMKKNMEQTIKDLQQ-----------RLDEAEQIALKGGKKQL 1830
Cdd:pfam15921 988 DPSSCFTFPSTASPSVKNSASRSFHSSPKKSPVHSL--LTSSAEGSIGSSSQyrsaktihspdSVKDSQSLPIETTGKTC 1065
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|.
gi 1072253241 1831 QKLEARVRELDNELEAEQKRNAESVKGMRKYERRIKELTYQ 1871
Cdd:pfam15921 1066 RKLQNRLESLQTLVEDLQLKNQAMSSMIRNQEKRIQKVKDQ 1106
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
910-1552 |
3.85e-17 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 88.20 E-value: 3.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 910 QAEQDNLADADERCEQLIKNKIQLEaKLKEQTERLedeEEMNAELTAKKRKLEDECSElKKDIDDLeltLAKVEKEKHAT 989
Cdd:PRK03918 134 QGEIDAILESDESREKVVRQILGLD-DYENAYKNL---GEVIKEIKRRIERLEKFIKR-TENIEEL---IKEKEKELEEV 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 990 ENKVKNLTEEMAGLDEIIVKLTKEKKALqEAHQQALDDLQAEEDKVNtltKAKAKLEQQVDDLEGSLEQEKKIRMDLERV 1069
Cdd:PRK03918 206 LREINEISSELPELREELEKLEKEVKEL-EELKEEIEELEKELESLE---GSKRKLEEKIRELEERIEELKKEIEELEEK 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1070 KRKLEgDVKLSQESLMDLEndkqQLEEKLKKKDFEVSQLNTRIEDEQNVCIQLQKKMKELQARIEeleeeleaertaraK 1149
Cdd:PRK03918 282 VKELK-ELKEKAEEYIKLS----EFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE--------------E 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1150 VEKLRCDLSRELEEISERLEEAGGATSVQMELNKKReaeflKLRRDLEESTLHSEATAASLRKKhadsvaELSEQIDNLQ 1229
Cdd:PRK03918 343 LKKKLKELEKRLEELEERHELYEEAKAKKEELERLK-----KRLTGLTPEKLEKELEELEKAKE------EIEEEISKIT 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1230 RVKQKLEKEKSEFKLelddvtsNMEQMVKAKANLEKLCRSLEDqanEHRTK-SEENQRTVNELSSLRAKLQTENGELSRR 1308
Cdd:PRK03918 412 ARIGELKKEIKELKK-------AIEELKKAKGKCPVCGRELTE---EHRKElLEEYTAELKRIEKELKEIEEKERKLRKE 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1309 LDEKESLVSQMTRGKQTYTqhLEDLKRQLEEETKAKNalahaLQSARHDSDLLREQFEEEQEAKAELQRILSKANSEVAq 1388
Cdd:PRK03918 482 LRELEKVLKKESELIKLKE--LAEQLKELEEKLKKYN-----LEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE- 553
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1389 wrtkYETDAIQRTEELEEAKKKLAQRLQEAEE----AVEAVNAKCSSLEKTKHR---LQNEIEDLMVDLERSNAAAAALD 1461
Cdd:PRK03918 554 ----LKKKLAELEKKLDELEEELAELLKELEElgfeSVEELEERLKELEPFYNEyleLKDAEKELEREEKELKKLEEELD 629
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1462 KKQRNFDKILAEWKQKFEE-SQTELESSQKEARSLSTELFKLKNAYEESLDHLETFKRENKNLQEEISDLTEQLGESGKS 1540
Cdd:PRK03918 630 KAFEELAETEKRLEELRKElEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKA 709
|
650
....*....|..
gi 1072253241 1541 IHELEKIRKQLD 1552
Cdd:PRK03918 710 KKELEKLEKALE 721
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
901-1446 |
5.68e-17 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 87.40 E-value: 5.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 901 EKNDLQLQVQAEQDNLADADERCEQLIKNKIQLEAKLKEQTERLEDEEEMNAELTakkrkledecsELKKDIDDLELTLA 980
Cdd:PRK02224 200 EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELE-----------TLEAEIEDLRETIA 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 981 KVEKEKHATENKVKNLTEEMAGLDEIIVKLTKEkKALQEAHQQALDDLQAEedkvntltkakakLEQQVDDLEGSLEQEk 1060
Cdd:PRK02224 269 ETEREREELAEEVRDLRERLEELEEERDDLLAE-AGLDDADAEAVEARREE-------------LEDRDEELRDRLEEC- 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1061 kiRMDLERVKRKLEGdvklSQESLMDLENDKQQLEEKLKKKDFEVSQLNTRIEDEQNVCIQLQKKMKELQARIEELEeel 1140
Cdd:PRK02224 334 --RVAAQAHNEEAES----LREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAP--- 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1141 eaerTARAKVEKLRCDLSRELEEISERLEEAggATSVQMELNKKREAEFL-------KLRRDLEEStlhseataaslrkK 1213
Cdd:PRK02224 405 ----VDLGNAEDFLEELREERDELREREAEL--EATLRTARERVEEAEALleagkcpECGQPVEGS-------------P 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1214 HADSVAELSEQIDNLQRVKQKLEKEKSEFKLELDDVtsnmEQMVKAKANLEKL---CRSLEDQANEHRTKSEENQRTVNE 1290
Cdd:PRK02224 466 HVETIEEDRERVEELEAELEDLEEEVEEVEERLERA----EDLVEAEDRIERLeerREDLEELIAERRETIEEKRERAEE 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1291 LSSLRAKLQTENGELSRRLDEKESLVSQMTRGKQTYTQHLEDLKRQLEEETKAKNALAhALQSARHDSDLLREQFEEEQE 1370
Cdd:PRK02224 542 LRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLA-AIADAEDEIERLREKREALAE 620
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1072253241 1371 AKAELQRILSKANSEVAQWRTKYETDAIqrtEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDL 1446
Cdd:PRK02224 621 LNDERRERLAEKRERKRELEAEFDEARI---EEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEEL 693
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
865-1788 |
1.15e-16 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 87.02 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 865 KEMQTMKEEFQKLKEALEKSEARRKDLEEKMVSLLQEKnDLQLQVQAEQDNLADADERCEQLIKNKIQLEAKLKEQTERL 944
Cdd:TIGR00606 200 QKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSR-EIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRK 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 945 EDEEEMNAELTAKKRKLEDECSELKKDIDdleltlakvekekHATENKVKNLTEEMAGLDEIIVKLTKEKKALQEAH--- 1021
Cdd:TIGR00606 279 KQMEKDNSELELKMEKVFQGTDEQLNDLY-------------HNHQRTVREKERELVDCQRELEKLNKERRLLNQEKtel 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1022 --QQALDDLQAEEDKVNTLTKAKAKLEQQ----VDDLEGSLEQEKKIRMDLERVKRKLEGDVKLSQESLMDLENDKQQLE 1095
Cdd:TIGR00606 346 lvEQGRLQLQADRHQEHIRARDSLIQSLAtrleLDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQ 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1096 EKLKKKDFEVSQLNTRIEDEQnvcIQLQKKMKELQARIEELEEELEAERTARAKVEKLRcdlsRELEEISERLEEAGGAT 1175
Cdd:TIGR00606 426 EQADEIRDEKKGLGRTIELKK---EILEKKQEELKFVIKELQQLEGSSDRILELDQELR----KAERELSKAEKNSLTET 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1176 svqmelnKKREAEFLKLRRDLEESTLHSEATAASLRKKHADSVAELSEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQ 1255
Cdd:TIGR00606 499 -------LKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPN 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1256 mvkaKANLEKLCRSLEDQANEHRTKSEENQRTVNELSSLRAKLQTENGELSRRLDEKESLVSQMTrGKQTYTQHLEDLKR 1335
Cdd:TIGR00606 572 ----KKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVC-GSQDEESDLERLKE 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1336 QLEEETKAKNALAHAlqSARHDSdLLREQFEEEQEAKAELQRILsKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRL 1415
Cdd:TIGR00606 647 EIEKSSKQRAMLAGA--TAVYSQ-FITQLTDENQSCCPVCQRVF-QTEAELQEFISDLQSKLRLAPDKLKSTESELKKKE 722
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1416 QEAEEAVEAVNAKCSSL---EKTKHRLQNEIEDLMVDLERSNaaaAALDKKQRNFDKILAEWKQK---------FEESQT 1483
Cdd:TIGR00606 723 KRRDEMLGLAPGRQSIIdlkEKEIPELRNKLQKVNRDIQRLK---NDIEEQETLLGTIMPEEESAkvcltdvtiMERFQM 799
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1484 ELESSQKEARSLSTEL--FKLKNAYEESLDHLETFKRENKNLQEEISDLTEQLGESGKSIHELEKIRKQLDQEKMEIQSA 1561
Cdd:TIGR00606 800 ELKDVERKIAQQAAKLqgSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTN 879
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1562 LEEAEATLEHEEGKILHAQLELHQIKadserKLAEKDEEMEQAKRNYQRMVDTLQTSLEAETR-SRNEALRIKKKM---- 1636
Cdd:TIGR00606 880 LQRRQQFEEQLVELSTEVQSLIREIK-----DAKEQDSPLETFLEKDQQEKEELISSKETSNKkAQDKVNDIKEKVknih 954
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1637 --------------EGDLNEMEIQLSQANRQAAEAQKQVKILQSYLKDTQIQLDDALRASEDLKENIAIVERRNTLLQAE 1702
Cdd:TIGR00606 955 gymkdienkiqdgkDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVE 1034
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1703 LEELRSLVEQTERARKLSEQELIETSERVQLLHSQNTSLINQKKKMESDLSQLQTEMEEavQECRNAEEKAKKAITDAAM 1782
Cdd:TIGR00606 1035 EELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELRE--PQFRDAEEKYREMMIVMRT 1112
|
....*.
gi 1072253241 1783 MAEELK 1788
Cdd:TIGR00606 1113 TELVNK 1118
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
934-1824 |
1.52e-16 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 86.18 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 934 EAKLKEQTERLEDEEEMNAEL-TAKKRKLEDECSELKKDIDDLELTLAKVEKEKHatenkvknlteemagLDEIIVKLTK 1012
Cdd:pfam02463 180 EETENLAELIIDLEELKLQELkLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKL---------------NEERIDLLQE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1013 EKKALQEAHQQALDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKIRMDLERVKRKLEGDVKLSQESLMDLENDKQ 1092
Cdd:pfam02463 245 LLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKK 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1093 QLEEKLKKKDFEVSQLNTRIEDEQNVCIQLQKKMKELQARieeleeeLEAERTARAKVEKLRCDLSRELEEISERLEEAg 1172
Cdd:pfam02463 325 KAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKL-------QEKLEQLEEELLAKKKLESERLSSAAKLKEEE- 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1173 gatsVQMELNKKREAEFLKLRRDLEESTLHSEATAASLRKKHADSVAELSEQIDNLQRVKQKLEKEKsefklelddvtsn 1252
Cdd:pfam02463 397 ----LELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELK------------- 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1253 meqmvkakanLEKLCRSLEDQANEHRTKSEENQRTVNELSSLRAKLQTENGELSRRLDEKESLVSQMTRGKQT-YTQHLE 1331
Cdd:pfam02463 460 ----------LLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGrIISAHG 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1332 DLKRQLEEETKAKNALAHALQSARHDSDLLREQFEEEQEAKAELQRILSKAN----SEVAQWRTKYETDAIQRTEELEEA 1407
Cdd:pfam02463 530 RLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRllipKLKLPLKSIAVLEIDPILNLAQLD 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1408 KKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLM--VDLERSNAAAAALDKKQRNFDKILAEWKQKFEESQTEL 1485
Cdd:pfam02463 610 KATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRkgVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESEL 689
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1486 ESSQKEARSLSTELFKLKNAYEESLDHLETFKRENKNLQEEISDLTEQLGESGKSIHELEKIRKQLDQEKMEIQSALEEA 1565
Cdd:pfam02463 690 AKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSEL 769
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1566 EATLEHEEGKILHAQLELHQIKADSERKLAEKDEEMEQAKRNY----QRMVDTLQTSLEAETRSRNEALRIKKKMEGDLN 1641
Cdd:pfam02463 770 SLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEeaelLEEEQLLIEQEEKIKEEELEELALELKEEQKLE 849
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1642 EMEIQLsqANRQAAEAQKQVKILQSYLKDTQIQLDDALRASEDLKENIaiverrNTLLQAELEELRSLVEQTERARKLSE 1721
Cdd:pfam02463 850 KLAEEE--LERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKE------KEEKKELEEESQKLNLLEEKENEIEE 921
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1722 QELIETSERVQLLHSQNTSLINQKKKMESDLSQLQTEMEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDtsahLERMK 1801
Cdd:pfam02463 922 RIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNK----DELEK 997
|
890 900
....*....|....*....|...
gi 1072253241 1802 KNMEQTIKDLQQRLDEAEQIALK 1824
Cdd:pfam02463 998 ERLEEEKKKLIRAIIEETCQRLK 1020
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
990-1689 |
6.89e-16 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 83.92 E-value: 6.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 990 ENKVKNLTEEMAGLDEIIVKLTKEKKALQeahqqalDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKIRMDLERV 1069
Cdd:TIGR04523 32 DTEEKQLEKKLKTIKNELKNKEKELKNLD-------KNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1070 KRKLEGDVKLSQESLMDLENDKQQLEEKLKKKDFEVSQLNTRIEDEQNVCIQLQKKMKELQARIeeleeeleaertarak 1149
Cdd:TIGR04523 105 LSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQK---------------- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1150 vEKLRCDLSRELEEISerleeaggatsvqmelNKKREAEFLKLRRDLEESTLHSEATAASLRKKHADSVAELSEQIDNLQ 1229
Cdd:TIGR04523 169 -EELENELNLLEKEKL----------------NIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1230 RVKQKLEKEKSEFKLELDdvtSNMEQMVKAKANLEKLCRSLEDQANEHRTKSEENQRTVNELSSLRAKLQTENGELSRRL 1309
Cdd:TIGR04523 232 DNIEKKQQEINEKTTEIS---NTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDW 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1310 DEKesLVSQMTRGKQtytqHLEDLKRQLEEETKAKNALAHALQSARHDSDLLREQFEEEQEAKAELQRILSKANSEVAQW 1389
Cdd:TIGR04523 309 NKE--LKSELKNQEK----KLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSY 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1390 RtkyetdaiQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAALDKKQRNFDK 1469
Cdd:TIGR04523 383 K--------QEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKEL 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1470 ILAEWKQKFEESQTELESSQKEARSLSTELFKLKNAYEESLDHLETFKRENKNLQEEISDLTEQLGESGKSIHELEKIRK 1549
Cdd:TIGR04523 455 IIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKK 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1550 QLDQEKMEIQSALEEAEATLEHE--EGKILHAQLELHQIKADSERKLAEKDEEMEQAKrNYQRMVDTLQTSLEAETRSRN 1627
Cdd:TIGR04523 535 EKESKISDLEDELNKDDFELKKEnlEKEIDEKNKEIEELKQTQKSLKKKQEEKQELID-QKEKEKKDLIKEIEEKEKKIS 613
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1072253241 1628 EALRIKKKMEGDLNEMEIQLSQANRQAAEAQKQVKILQSYLKDTQIQLDDALRASEDLKENI 1689
Cdd:TIGR04523 614 SLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKI 675
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
852-1272 |
1.95e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 82.42 E-value: 1.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 852 FKIKPLLKSAETEKEMQTMKEEFQKLKEA---LEKSEARRKDLEEKMVSLLQEKNDLQLQVQAEQDNLADADE----RCE 924
Cdd:PRK03918 301 FYEEYLDELREIEKRLSRLEEEINGIEERikeLEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEElerlKKR 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 925 QLIKNKIQLEAKLKEQTERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLE-----LTLAKVEKEKHATEN-------K 992
Cdd:PRK03918 381 LTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKkakgkCPVCGRELTEEHRKElleeytaE 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 993 VKNLTEEMAGLDEIIVKLTKEKKALQEA---------HQQALDDLQAEEDKVNTLTkaKAKLEQQVDDLEGSLEQEKKIR 1063
Cdd:PRK03918 461 LKRIEKELKEIEEKERKLRKELRELEKVlkkeselikLKELAEQLKELEEKLKKYN--LEELEKKAEEYEKLKEKLIKLK 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1064 MDLERVKRKLegdvklsqESLMDLENDKQQLEEKLKKKDFEVSQLNTRIEDEQNVCI-QLQKKMKELQARIEELEEELEA 1142
Cdd:PRK03918 539 GEIKSLKKEL--------EKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVeELEERLKELEPFYNEYLELKDA 610
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1143 ERTARAKVEKLRcDLSRELEEISERLEEAggatsvqmelnkkrEAEFLKLRRDLEE-STLHSEATAASLRKKHadsvAEL 1221
Cdd:PRK03918 611 EKELEREEKELK-KLEEELDKAFEELAET--------------EKRLEELRKELEElEKKYSEEEYEELREEY----LEL 671
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1072253241 1222 SEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQMVKAKANLEKLCRSLED 1272
Cdd:PRK03918 672 SRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALER 722
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1224-1902 |
2.41e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 82.03 E-value: 2.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1224 QIDNLQRVKQKLEKEKSEFKLELDdvtsNMEQMVKAKANLEKLCRSLEDqanehrtKSEENQRTVNELSSLRAKLQTENG 1303
Cdd:PRK03918 156 GLDDYENAYKNLGEVIKEIKRRIE----RLEKFIKRTENIEELIKEKEK-------ELEEVLREINEISSELPELREELE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1304 ELSRRLDEKESLVSQmtrgkqtytqhLEDLKRQLEEETKAKNALAHALQSARHDSDLLREQFEEEQEAKAELQRILSKAn 1383
Cdd:PRK03918 225 KLEKEVKELEELKEE-----------IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKA- 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1384 sevaqwrTKYETdAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLqNEIEDLMVDLERSnaaAAALDKK 1463
Cdd:PRK03918 293 -------EEYIK-LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL-EELKKKLKELEKR---LEELEER 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1464 QRNFDKILAEwkqkfeesQTELESSQKEARSLSTElfKLKNAYEEsldhletFKRENKNLQEEISDLTEQLGEsgksihe 1543
Cdd:PRK03918 361 HELYEEAKAK--------KEELERLKKRLTGLTPE--KLEKELEE-------LEKAKEEIEEEISKITARIGE------- 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1544 LEKIRKQLDQEKMEIQSALEE-----AEATLEHEEGKILHAQLELhqikADSERKLAEKDEEMEQAKRNYQRmvdtLQTS 1618
Cdd:PRK03918 417 LKKEIKELKKAIEELKKAKGKcpvcgRELTEEHRKELLEEYTAEL----KRIEKELKEIEEKERKLRKELRE----LEKV 488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1619 LEAETRsrneaLRIKKKMEGDLNEMEIQLSQANRQAAEAQKQ----VKILQSYLKDTQIQLDDALRASEDLKENIAIVER 1694
Cdd:PRK03918 489 LKKESE-----LIKLKELAEQLKELEEKLKKYNLEELEKKAEeyekLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEK 563
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1695 RntlLQAELEELRSLVEQTERARKLSEQELIETSERVQLLHSQNTSLINQKKKMESDLSQLQTEMEEAvqecrnaeEKAK 1774
Cdd:PRK03918 564 K---LDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEEL--------DKAF 632
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1775 KAITDAAMMAEELKKEQDtsahlERMKKNMEQTIKDLQQRLDEAEQiALKGGKKQLQKLEARVRELDNELEAEQkrnaES 1854
Cdd:PRK03918 633 EELAETEKRLEELRKELE-----ELEKKYSEEEYEELREEYLELSR-ELAGLRAELEELEKRREEIKKTLEKLK----EE 702
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1072253241 1855 VKGMRKYERRIKELtyqteedRKNLARLQDLVDklqlKVKTYKRQAEE 1902
Cdd:PRK03918 703 LEEREKAKKELEKL-------EKALERVEELRE----KVKKYKALLKE 739
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1399-1944 |
2.95e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 82.03 E-value: 2.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1399 QRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKhrlqNEIEDLMVDLERSNAAAAALDKKQRNFDKILAEWKQKF 1478
Cdd:PRK03918 200 KELEEVLREINEISSELPELREELEKLEKEVKELEELK----EEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEI 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1479 EESQtELESSQKEARSLSTELFKLKNAYEESLDHLETFKRENKNLQEEISDLTEQLGESGKSIHELEKIRKqldqEKMEI 1558
Cdd:PRK03918 276 EELE-EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKK----KLKEL 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1559 QSALEEAEATLE-HEEGKILHAQLELH--QIKADSERKLAEKDEEMEQAKRNYQRMVDTLQT---SLEAETRSRNEALRI 1632
Cdd:PRK03918 351 EKRLEELEERHElYEEAKAKKEELERLkkRLTGLTPEKLEKELEELEKAKEEIEEEISKITArigELKKEIKELKKAIEE 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1633 KKKMEGDLNEMEIQLSQANRQA--AEAQKQVKILQSYLKDTQIQLDDALRASEDLkENIAIVERRNTLLQAELEELRSLV 1710
Cdd:PRK03918 431 LKKAKGKCPVCGRELTEEHRKEllEEYTAELKRIEKELKEIEEKERKLRKELREL-EKVLKKESELIKLKELAEQLKELE 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1711 EQTErarKLSEQELIETSERVQLLHSQNTSLINQKKKMESDLSQLqtemeeavqecrNAEEKAKKAITDAAMMAEELKKE 1790
Cdd:PRK03918 510 EKLK---KYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKL------------EELKKKLAELEKKLDELEEELAE 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1791 QdtsahLERMKKNMEQTIKDLQQRLDEAEQ-----IALKGGKKQLQKLEARVRELDNELEAEQKRNAESVKGMRKYERRI 1865
Cdd:PRK03918 575 L-----LKELEELGFESVEELEERLKELEPfyneyLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKEL 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1866 KELTYQ-TEEDRKNLARLQDLVDKLQLKVKTYKRQAEESEEQANTSLSKFRKVQHELDEAEERAD---IAESQVNKLRAK 1941
Cdd:PRK03918 650 EELEKKySEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEkleKALERVEELREK 729
|
...
gi 1072253241 1942 SRD 1944
Cdd:PRK03918 730 VKK 732
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
861-1473 |
3.12e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 82.04 E-value: 3.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 861 AETEKEMQTMKEEFQKLKEALEKSEARRKDLEEKMVSLLQEKNDLQLQVQAEQDNLADADERCEQLIKNKIQLEAKLKEQ 940
Cdd:TIGR02169 374 EEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 941 TERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKN-------LTEEMAGLDEIIVKLTKE 1013
Cdd:TIGR02169 454 EWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGgraveevLKASIQGVHGTVAQLGSV 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1014 K----KALQEAHQQALDDLQAEEDKVNT------------------LTKAKAKL---------------------EQQ-- 1048
Cdd:TIGR02169 534 GeryaTAIEVAAGNRLNNVVVEDDAVAKeaiellkrrkagratflpLNKMRDERrdlsilsedgvigfavdlvefDPKye 613
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1049 ------------VDDLEGSLEQEKKIRM----------------------DLERVKRKLEGDVKLSQESLMDLENDKQQL 1094
Cdd:TIGR02169 614 pafkyvfgdtlvVEDIEAARRLMGKYRMvtlegelfeksgamtggsraprGGILFSRSEPAELQRLRERLEGLKRELSSL 693
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1095 EEKLKKKDFEVSQLNTRIEDEQNVCIQLQKKMKELQARIeeleeeleaeRTARAKVEKLRcdlsRELEEISERLEEAgga 1174
Cdd:TIGR02169 694 QSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEE----------EKLKERLEELE----EDLSSLEQEIENV--- 756
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1175 tsvqmelnkkrEAEFLKLRRDLEEStlhsEATAASLRKKHADSVAELS-EQIDNLQRVKQKLEKEKSEFKLELDDVTSNM 1253
Cdd:TIGR02169 757 -----------KSELKELEARIEEL----EEDLHKLEEALNDLEARLShSRIPEIQAELSKLEEEVSRIEARLREIEQKL 821
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1254 EQMVKAKANLEKLCRSLEDQANEHRTKSEENQRTVNElsslrakLQTENGELSRRLDEKESLVSQMTRGKQTYTQHLEDL 1333
Cdd:TIGR02169 822 NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN-------LNGKKEELEEELEELEAALRDLESRLGDLKKERDEL 894
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1334 KRQLEEETKAKNALAHALQSARHDSDLLREQFEEEQEAKAELQRILSKANSEVAQwrTKYETDAIQRTEELEEAKKKLAQ 1413
Cdd:TIGR02169 895 EAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEE--ELSLEDVQAELQRVEEEIRALEP 972
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1072253241 1414 RLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDL-----MVDLERSNAAAAALDKKQRNFDKILAE 1473
Cdd:TIGR02169 973 VNMLAIQEYEEVLKRLDELKEKRAKLEEERKAIlerieEYEKKKREVFMEAFEAINENFNEIFAE 1037
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1626-1941 |
3.23e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 81.91 E-value: 3.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1626 RNEALRIKKKMEGDLN-------EMEIQLSQANRQAAEAQKqVKILQSYLKDTQIQLddALRASEDLKENIAIVERRNTL 1698
Cdd:COG1196 174 KEEAERKLEATEENLErledilgELERQLEPLERQAEKAER-YRELKEELKELEAEL--LLLKLRELEAELEELEAELEE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1699 LQAELE----ELRSLVEQTERARklseQELIETSERVQLLHSQNTSLINQKKKMESDLSQLQTEMEEAVQECRNAEEKAK 1774
Cdd:COG1196 251 LEAELEeleaELAELEAELEELR----LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1775 KAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQQRLDEAEQIALKGGKKQLQKLEARVRELDNELEAEQKRNAES 1854
Cdd:COG1196 327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1855 VKgMRKYERRIKELTYQTEEDRKNLARLQDLVDKLQLKVKTYKRQAEESEEQANTSLSKFRKVQHELDEAEERADIAESQ 1934
Cdd:COG1196 407 EA-EEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
|
....*..
gi 1072253241 1935 VNKLRAK 1941
Cdd:COG1196 486 LAEAAAR 492
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
872-1747 |
3.52e-15 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 81.94 E-value: 3.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 872 EEFQKLKEALEKsearrkdLEEKMVSLLQEKNDLQLQVQAEQDNLADADERCEQLIKNKIQLEAKLKEQTERLE-DEEEM 950
Cdd:pfam02463 166 RLKRKKKEALKK-------LIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLkLNEER 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 951 NAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIVKLTKEKKALQEAHQQALDDLQA 1030
Cdd:pfam02463 239 IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1031 EEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKIRMDLERVKrklegdVKLSQESLMDLENDKQQLEEKLKKKDFEVSQLNT 1110
Cdd:pfam02463 319 SEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEE------EELEKLQEKLEQLEEELLAKKKLESERLSSAAKL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1111 RIEDEQNVCIQLQKKMKELQARIEELEEELEAERTARAKVEKLRCDLSRELEEISERLEEAGGATSVQMELNKKREAEFL 1190
Cdd:pfam02463 393 KEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSED 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1191 KLRRDLEESTLHSEATAASLRKKHADSVAELSEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQMVKAKANLEKLCRSL 1270
Cdd:pfam02463 473 LLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVE 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1271 EDQANEHRTKSEENQRTVNELSSLRAKLQTENGelsrrlDEKESLVSQMTRGKQTYTQHLEDLKRQLEEETKAKNALAHA 1350
Cdd:pfam02463 553 VSATADEVEERQKLVRALTELPLGARKLRLLIP------KLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVE 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1351 LQSARHDSDLLREqfeeeqeaKAELQRILSKANSEVAQWRTKYETDaiQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCS 1430
Cdd:pfam02463 627 GILKDTELTKLKE--------SAKAKESGLRKGVSLEEGLAEKSEV--KASLSELTKELLEIQELQEKAESELAKEEILR 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1431 SLEKTKHRLQNEIEDL-MVDLERSNAAAAALDKKQRNFDKILAEWKQKFEESQTELESSQKEARSLSTELFKLKNaYEES 1509
Cdd:pfam02463 697 RQLEIKKKEQREKEELkKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSL-KEKE 775
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1510 LDHLETFKRENKNLQEEISDLTEQLgESGKSIHELEKIRKQLDQEKMEIQSALEEAEATLEHEEGKILHAQLELHQIKAD 1589
Cdd:pfam02463 776 LAEEREKTEKLKVEEEKEEKLKAQE-EELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEE 854
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1590 SERKLAEKDEEMEQAKRNYQRMVDTLQTSLEAETRSRNEALRIKKKmegdlneMEIQLSQANRQAAEAQKQVKILQSYLK 1669
Cdd:pfam02463 855 ELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKK-------ELEEESQKLNLLEEKENEIEERIKEEA 927
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1670 DTQIQLDDALRASEDLkENIAIVERRNTLLQAELEELRSLVEQTERARKLSEQ--ELIETSERVQLLHSQNTSLINQKKK 1747
Cdd:pfam02463 928 EILLKYEEEPEELLLE-EADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAieEFEEKEERYNKDELEKERLEEEKKK 1006
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1432-1941 |
3.76e-15 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 81.70 E-value: 3.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1432 LEKTKHRLQNEIEDLMVDLERSNAaaaaLDKKQRNF-DKILAEWKQKFEESQTELESSQKEARSLSTELFKLKNAYEESL 1510
Cdd:pfam15921 76 IERVLEEYSHQVKDLQRRLNESNE----LHEKQKFYlRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1511 DHLETfkreNKNLQEEIsdlteqLGESGKSIHELEKIRKQLDQEKMEIQSAL---EEAEATLEHEEGKIlhAQLELHQIK 1587
Cdd:pfam15921 152 HELEA----AKCLKEDM------LEDSNTQIEQLRKMMLSHEGVLQEIRSILvdfEEASGKKIYEHDSM--STMHFRSLG 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1588 ADSERKLAEKDEEMEQAKRNYQRMVDTLQTsLEAETRSRNEAL--RIKKKMEGDLNEMEIQLSQANRQAAEAQKQVKILQ 1665
Cdd:pfam15921 220 SAISKILRELDTEISYLKGRIFPVEDQLEA-LKSESQNKIELLlqQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQ 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1666 SYLKDTQIQlddalrasedlkeniaiVERRNTLLQAELEELRSLVEQTE---RARKLSEQELIETSERVQLLHSqntsli 1742
Cdd:pfam15921 299 SQLEIIQEQ-----------------ARNQNSMYMRQLSDLESTVSQLRselREAKRMYEDKIEELEKQLVLAN------ 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1743 nqkkkmeSDLSQLQTEMEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQQRLDEAEQia 1822
Cdd:pfam15921 356 -------SELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNM-- 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1823 lkggkkQLQKLEARVRELDNELEAEQKRNAESVKGMRKYERRIKELTYQTEEDRKnlaRLQDLVDKLqlkvkTYKRQAEE 1902
Cdd:pfam15921 427 ------EVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKE---MLRKVVEEL-----TAKKMTLE 492
|
490 500 510
....*....|....*....|....*....|....*....
gi 1072253241 1903 SEEQANTSLSKfrkvqhELDEAEERADIAESQVNKLRAK 1941
Cdd:pfam15921 493 SSERTVSDLTA------SLQEKERAIEATNAEITKLRSR 525
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
865-1555 |
4.61e-15 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 81.22 E-value: 4.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 865 KEMQTMKEEFQKLKEALEKSEARRKDLEEKMVSLLQEKNDLQLQVQAEQDNLADADERCEQL---IKNKIQLEAKLKEQT 941
Cdd:TIGR04523 47 NELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKInseIKNDKEQKNKLEVEL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 942 ERLEDEEEMNAELTAKK----RKLEDECSELKKDIDDLEltlakveKEKHATENKVKNLTEEMAGLDEIIVKLTKEKKAL 1017
Cdd:TIGR04523 127 NKLEKQKKENKKNIDKFlteiKKKEKELEKLNNKYNDLK-------KQKEELENELNLLEKEKLNIQKNIDKIKNKLLKL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1018 QeahqQALDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKirmDLERVKRKLegdvKLSQESLMDLENDKQQLEEK 1097
Cdd:TIGR04523 200 E----LLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQ---EINEKTTEI----SNTQTQLNQLKDEQNKIKKQ 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1098 LKKKDFEVSQLNTRIedeqnvcIQLQKKMKELQARIEELEEEleaertaraKVEKLRCDLSRELEEISERLEEAGGATSV 1177
Cdd:TIGR04523 269 LSEKQKELEQNNKKI-------KELEKQLNQLKSEISDLNNQ---------KEQDWNKELKSELKNQEKKLEEIQNQISQ 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1178 QMELNKKREAEFLKLRRDLEESTLHSEATAASLRKKHaDSVAELSEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQMV 1257
Cdd:TIGR04523 333 NNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQ-NEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKD 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1258 KAKANLEKLCRSLEDQANEHRTKSEENQRTVNELSSLRAKLQTENGELSRRLDEKESLVSQMTRGKQTYTQHLEDLKRQL 1337
Cdd:TIGR04523 412 EQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKEL 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1338 EEETKaknalahalqsarhdsdllreQFEEEQEAKAELQRILSKANSEVAQwrtkyetdAIQRTEELEEAKKKLAQRLQE 1417
Cdd:TIGR04523 492 KSKEK---------------------ELKKLNEEKKELEEKVKDLTKKISS--------LKEKIEKLESEKKEKESKISD 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1418 AEEAVEAV--NAKCSSLEKTKHRLQNEIEDLMVD---LERSNAAAAAL-DKKQRNFDKI---LAEWKQKFEESQTELESS 1488
Cdd:TIGR04523 543 LEDELNKDdfELKKENLEKEIDEKNKEIEELKQTqksLKKKQEEKQELiDQKEKEKKDLikeIEEKEKKISSLEKELEKA 622
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1072253241 1489 QKEARSLSTELFKLKNAYEESLDHLETFKRENKNLQEEISDLTEQLGESGKSIHELEKIRKQLDQEK 1555
Cdd:TIGR04523 623 KKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKEL 689
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1270-1923 |
5.14e-15 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 81.32 E-value: 5.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1270 LEDQANEHRTKSEENQRTVNELSSLRAK----LQTENGELSRRLDEKESLVSQMTRGKQTYTQHLEDLKRQLE----EET 1341
Cdd:pfam15921 76 IERVLEEYSHQVKDLQRRLNESNELHEKqkfyLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQntvhELE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1342 KAKNALAHALQSARHDSDLLREQFEEEQEAKAELQRILskANSEVAQWRTKYETDAIQrTEELEEAKKKLAQRLQEAEEA 1421
Cdd:pfam15921 156 AAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSIL--VDFEEASGKKIYEHDSMS-TMHFRSLGSAISKILRELDTE 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1422 VEAVNAKC----SSLEKTKHRLQNEIEDLmvdlersnaaaaaLDKKQRNFDKILAEWKQKFEESQTELESSQKEARSLST 1497
Cdd:pfam15921 233 ISYLKGRIfpveDQLEALKSESQNKIELL-------------LQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1498 ELFKLKnayEESLDHLETFKRENKNLQEEISDLTEQLGESGKSIHE-LEKIRKQLDQEKMEIQSALEEAEaTLEHEEGKI 1576
Cdd:pfam15921 300 QLEIIQ---EQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDkIEELEKQLVLANSELTEARTERD-QFSQESGNL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1577 lhaQLELHQIKADSERKLAEKDEEMEQAKRNYQR------MVDTLQTSLEAETR--SRNEALRIKKKMEGDlNEMEIQLS 1648
Cdd:pfam15921 376 ---DDQLQKLLADLHKREKELSLEKEQNKRLWDRdtgnsiTIDHLRRELDDRNMevQRLEALLKAMKSECQ-GQMERQMA 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1649 qANRQAAEAQKQVKILQSYLKDTQIQLDDALRASEDLKENIAIVERRNTLLQAELEElrslveqTERARKLSEQELIETS 1728
Cdd:pfam15921 452 -AIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQE-------KERAIEATNAEITKLR 523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1729 ERVQLLHSQNTSLINQkkkmESDLSQLQTEMEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTI 1808
Cdd:pfam15921 524 SRVDLKLQELQHLKNE----GDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEI 599
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1809 KDlqQRLDEAEQIALKGGK-KQLQKLEARVRELdnELEAEQKRNA--ESVKGMRKYERRIKELTYQTEEDRKNLARLQDL 1885
Cdd:pfam15921 600 ND--RRLELQEFKILKDKKdAKIRELEARVSDL--ELEKVKLVNAgsERLRAVKDIKQERDQLLNEVKTSRNELNSLSED 675
|
650 660 670
....*....|....*....|....*....|....*...
gi 1072253241 1886 VDKLQlkvKTYKRQAEESEEQANTSLSKFRKVQHELDE 1923
Cdd:pfam15921 676 YEVLK---RNFRNKSEEMETTTNKLKMQLKSAQSELEQ 710
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1157-1818 |
6.79e-15 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 80.93 E-value: 6.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1157 LSRELEEISERLEEAGGATSVQMELNKKRE----AEFLKLRRDLEESTLHSEATAaSLRKKHADSVAELSEQidnLQRVK 1232
Cdd:pfam15921 76 IERVLEEYSHQVKDLQRRLNESNELHEKQKfylrQSVIDLQTKLQEMQMERDAMA-DIRRRESQSQEDLRNQ---LQNTV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1233 QKLEKEKSEFKLELDDVTSNMEQMVKAKANLEKLCRSLE------DQANEHRTKSEENQRTV------NELSSLRAKLQT 1300
Cdd:pfam15921 152 HELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRsilvdfEEASGKKIYEHDSMSTMhfrslgSAISKILRELDT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1301 ENGELSRRL----DEKESLVSQMTRGKQTYTQHLEDLKRQLEEETKAK-NALAHALQSARHDSDLLREQFEEEQEAK--- 1372
Cdd:pfam15921 232 EISYLKGRIfpveDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVEiTGLTEKASSARSQANSIQSQLEIIQEQArnq 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1373 --------AELQRILSKANSEVAQWRTKYEtDAIQRTE--------ELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTK 1436
Cdd:pfam15921 312 nsmymrqlSDLESTVSQLRSELREAKRMYE-DKIEELEkqlvlansELTEARTERDQFSQESGNLDDQLQKLLADLHKRE 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1437 HRLQNEIEDLMVDLERSNAAAAALDKKQRNFD-------KILAEWKQKFEESQTELE----------SSQKEARSLSTEL 1499
Cdd:pfam15921 391 KELSLEKEQNKRLWDRDTGNSITIDHLRRELDdrnmevqRLEALLKAMKSECQGQMErqmaaiqgknESLEKVSSLTAQL 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1500 FKLKNAYEESLDHLETFKRENKNLQEEISDLTEQLGESGKSIH----ELEKIRKQLDQEKMEIQSaleeaeatLEHEEGK 1575
Cdd:pfam15921 471 ESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEatnaEITKLRSRVDLKLQELQH--------LKNEGDH 542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1576 ILHAQLELHQIKAdserKLAEKDEEMEQAKRNYQRMVDTL-------------QTSLEAETRSRNEALR----IKKKMEG 1638
Cdd:pfam15921 543 LRNVQTECEALKL----QMAEKDKVIEILRQQIENMTQLVgqhgrtagamqveKAQLEKEINDRRLELQefkiLKDKKDA 618
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1639 DLNEME----------IQLSQANRQAAEAQKQVKI---------------LQSYLKDTQIQLDDALRASEDLKENIAIVE 1693
Cdd:pfam15921 619 KIRELEarvsdlelekVKLVNAGSERLRAVKDIKQerdqllnevktsrneLNSLSEDYEVLKRNFRNKSEEMETTTNKLK 698
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1694 RRNTLLQAELEELRSLVEQTERarklSEQELIETSERVQllhSQNTSLINQKKKMESDLSQLQTEMEEAVQECRNAEEKA 1773
Cdd:pfam15921 699 MQLKSAQSELEQTRNTLKSMEG----SDGHAMKVAMGMQ---KQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEK 771
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 1072253241 1774 KKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQQRLDEA 1818
Cdd:pfam15921 772 NKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKA 816
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
864-1621 |
1.03e-14 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 80.48 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 864 EKEMQTMKEEFQKLKEALEKSEARRKDLEEKMVSLLQEKNDLQLQVQAEQDNLADAD------------ERCEQLIKNKI 931
Cdd:TIGR00606 311 QRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDsliqslatrlelDGFERGPFSER 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 932 QLEAKLKEQTERLEDEEEMNAELTA--------KKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGL 1003
Cdd:TIGR00606 391 QIKNFHTLVIERQEDEAKTAAQLCAdlqskerlKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSS 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1004 DEIIVK----------------------LTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKK 1061
Cdd:TIGR00606 471 DRILELdqelrkaerelskaeknsltetLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQ 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1062 IRMDLERVKRKLEG------DVKLSQESLMDLENDKQQLEEKLKKKDFEVSQLntriEDEQNvciQLQKKMKELQARIEE 1135
Cdd:TIGR00606 551 IRKIKSRHSDELTSllgyfpNKKQLEDWLHSKSKEINQTRDRLAKLNKELASL----EQNKN---HINNELESKEEQLSS 623
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1136 LEEELEAERTARAKVEKLRcDLSRELEEISERLEEAGGATSVQ----MELNKKREAEFLKLRRDLEestlhSEATAASLR 1211
Cdd:TIGR00606 624 YEDKLFDVCGSQDEESDLE-RLKEEIEKSSKQRAMLAGATAVYsqfiTQLTDENQSCCPVCQRVFQ-----TEAELQEFI 697
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1212 KKHADSVAELSEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQMVKAKANLEKLCRSLEDQANEHRTKSEENQR---TV 1288
Cdd:TIGR00606 698 SDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETllgTI 777
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1289 NELSSLRAKLQTENGELSR---RLDEKESLVSQMTRGKQTytqhlEDLKRQLEEETKAKNALAHALQSARHDSDLLREQF 1365
Cdd:TIGR00606 778 MPEEESAKVCLTDVTIMERfqmELKDVERKIAQQAAKLQG-----SDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLI 852
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1366 EEEQEAKAELQRILSKANSEVAQWRTkyetdAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIED 1445
Cdd:TIGR00606 853 QDQQEQIQHLKSKTNELKSEKLQIGT-----NLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEE 927
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1446 LMVDLERSNAAAA-ALDKKQRNFDKILAEWKQKFEESQTELESSQKEARslsTELFKLKNAYEESLDHLETFKRENKNLQ 1524
Cdd:TIGR00606 928 LISSKETSNKKAQdKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKE---TELNTVNAQLEECEKHQEKINEDMRLMR 1004
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1525 EEISDLTEQ---------LGESGKSIHELEKIRKQLDQEKMEIQ--------SALEEAEATLEHEEGKILHAQLELHQIK 1587
Cdd:TIGR00606 1005 QDIDTQKIQerwlqdnltLRKRENELKEVEEELKQHLKEMGQMQvlqmkqehQKLEENIDLIKRNHVLALGRQKGYEKEI 1084
|
810 820 830
....*....|....*....|....*....|....
gi 1072253241 1588 ADSERKLAEKdeEMEQAKRNYQRMVDTLQTSLEA 1621
Cdd:TIGR00606 1085 KHFKKELREP--QFRDAEEKYREMMIVMRTTELV 1116
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
857-1554 |
1.25e-14 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 80.01 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 857 LLKSAETEKEMQTMKEEFQKLKEALEKSEARRKDLEEKMVSLLQEKNDLQLQVQAEQDNLADADERCEQLIKNKIQLEAK 936
Cdd:TIGR00618 169 LMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQK 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 937 LKEQTERLEDEEEMnAELTAKKRKLEDECSELKKDIDDLELT--LAKVEKEKHATENKVKNLTEEMAGLDEIIVKLTKEK 1014
Cdd:TIGR00618 249 REAQEEQLKKQQLL-KQLRARIEELRAQEAVLEETQERINRArkAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLL 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1015 KALQEAHQQALdDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKIRMDLERVkRKLEGDVKLSQESLMDLENDKQQL 1094
Cdd:TIGR00618 328 MKRAAHVKQQS-SIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHI-HTLQQQKTTLTQKLQSLCKELDIL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1095 EEKLKKKDFEVSQLN----------TRIEDEQNVCIQLQKKM-KELQARIEELEEELEAERTARAKVEKLrcdlsRELEE 1163
Cdd:TIGR00618 406 QREQATIDTRTSAFRdlqgqlahakKQQELQQRYAELCAAAItCTAQCEKLEKIHLQESAQSLKEREQQL-----QTKEQ 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1164 ISERLEEAGgatsvqmELNKKREAEFLKLRRDLEESTLHSEA--------------------TAASLRKKHADSVAELSE 1223
Cdd:TIGR00618 481 IHLQETRKK-------AVVLARLLELQEEPCPLCGSCIHPNParqdidnpgpltrrmqrgeqTYAQLETSEEDVYHQLTS 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1224 QIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQMVKAKANLEKLCRSLEDQANEHRTKSEENQRTVNELSSLRAKLQT--E 1301
Cdd:TIGR00618 554 ERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVrlH 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1302 NGELSRRLDEKESLVS--QMTRGKQTYTQHLEDLKRQLEEETKAKNALAHALQSARHDSDLLREQFEEEQEAKAELQRIL 1379
Cdd:TIGR00618 634 LQQCSQELALKLTALHalQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHI 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1380 SKANSEVAQWRTKYETdaiqRTEELEEAKKKLAQRLQEAEEavEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNaAAAA 1459
Cdd:TIGR00618 714 EEYDREFNEIENASSS----LGSDLAAREDALNQSLKELMH--QARTVLKARTEAHFNNNEEVTAALQTGAELSH-LAAE 786
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1460 LDKKQRNFDKILAEWKQKFEESQTELESSQKEarsLSTELFKLKNAYEESLDHLEtfkrENKNLQEEISDLTEQLGESGK 1539
Cdd:TIGR00618 787 IQFFNRLREEDTHLLKTLEAEIGQEIPSDEDI---LNLQCETLVQEEEQFLSRLE----EKSATLGEITHQLLKYEECSK 859
|
730
....*....|....*
gi 1072253241 1540 SIHELEKIRKQLDQE 1554
Cdd:TIGR00618 860 QLAQLTQEQAKIIQL 874
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1362-1953 |
3.03e-14 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 78.96 E-value: 3.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1362 REQFEEEQEAKAELQRILSKANSEVAQWRTKYET----DAIQRteELEEAK-KKLAQRLQEAEEAVEAVNAKCSSLEKTK 1436
Cdd:TIGR02169 176 LEELEEVEENIERLDLIIDEKRQQLERLRREREKaeryQALLK--EKREYEgYELLKEKEALERQKEAIERQLASLEEEL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1437 HRLQNEIEDLMvdlERSNAAAAALDKkqrnfdkILAEWKQKFEESQTELessQKEARSLSTELFKLKNAYEESLDHLETF 1516
Cdd:TIGR02169 254 EKLTEEISELE---KRLEEIEQLLEE-------LNKKIKDLGEEEQLRV---KEKIGELEAEIASLERSIAEKERELEDA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1517 KRENKNLQEEISDLTEQLGESGKSIHELEKIRKQLDQEKMEIQSALEEAEATLEHEEGKILHAQLELhqikADSERKLAE 1596
Cdd:TIGR02169 321 EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL----KDYREKLEK 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1597 KDEEMEQAKRNYQRMVDTLQTSLEAETRSRNEALRIkkkmEGDLNEMEIQLSqanrqaaEAQKQVKILQSYLKDTQIQLD 1676
Cdd:TIGR02169 397 LKREINELKRELDRLQEELQRLSEELADLNAAIAGI----EAKINELEEEKE-------DKALEIKKQEWKLEQLAADLS 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1677 DALRASEDLKENIAIVERRNTLLQAELEEL---RSLVEQTERARKLSEQ--------------ELIETSER--------- 1730
Cdd:TIGR02169 466 KYEQELYDLKEEYDRVEKELSKLQRELAEAeaqARASEERVRGGRAVEEvlkasiqgvhgtvaQLGSVGERyataievaa 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1731 ------------------VQLLHSQNTSL-----INQKKKMESDLSQLQTE----------------------------- 1758
Cdd:TIGR02169 546 gnrlnnvvveddavakeaIELLKRRKAGRatflpLNKMRDERRDLSILSEDgvigfavdlvefdpkyepafkyvfgdtlv 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1759 ---MEEAVQECRNAE-------------------EKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQQRLD 1816
Cdd:TIGR02169 626 vedIEAARRLMGKYRmvtlegelfeksgamtggsRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLD 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1817 EAeQIALKGGKKQLQKLEARVRELDNELEAEQKRNAESvkgmrkyERRIKELTYQTEEDRKNLARLQDLVDKLQLKVKTY 1896
Cdd:TIGR02169 706 EL-SQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL-------EEDLSSLEQEIENVKSELKELEARIEELEEDLHKL 777
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 1072253241 1897 KRQAEESEeqANTSLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDVSTKKSLNE 1953
Cdd:TIGR02169 778 EEALNDLE--ARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLE 832
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1461-1942 |
4.82e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 77.77 E-value: 4.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1461 DKKQRNFDKILAEWKQKFEESQTELE--SSQKE-ARSLSTELFKLKNAYEESLDHLETFKRENKNLQEEISDLTEQLGES 1537
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIEryEEQREqARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREEL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1538 GKSIHELEKIRKQLDQEKMEIQsaleeAEATLEHEEGKILHAQLElhqikaDSERKLAEKDEEMEQAKRNYQRMVDTLQT 1617
Cdd:PRK02224 278 AEEVRDLRERLEELEEERDDLL-----AEAGLDDADAEAVEARRE------ELEDRDEELRDRLEECRVAAQAHNEEAES 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1618 SLE--AETRSRNEALRIK-KKMEGDLNEMEIQLSQANRQAAEAQKQVKILQSYLKDTQIQLDDALRASEDLKENIAIVER 1694
Cdd:PRK02224 347 LREdaDDLEERAEELREEaAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRE 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1695 RNTLLQAELEELRSLVEQTER---ARKLSE--QElIETSERVQLLHSQNtsliNQKKKMESDLSQLQTEMEEAvqecrna 1769
Cdd:PRK02224 427 REAELEATLRTARERVEEAEAlleAGKCPEcgQP-VEGSPHVETIEEDR----ERVEELEAELEDLEEEVEEV------- 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1770 EEKAKKAitdaammaEELKKEQDTSAHLERMKKNMEQTIKDLQQRLDEAEQialkggkkQLQKLEARVRELDNELEAEQK 1849
Cdd:PRK02224 495 EERLERA--------EDLVEAEDRIERLEERREDLEELIAERRETIEEKRE--------RAEELRERAAELEAEAEEKRE 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1850 RNAESVKGMRKYERRIKELTYQTEE---DRKNLARLQDLVDKLQLKVKTYKRQAE------ESEEQANTSLSKFRKVQHE 1920
Cdd:PRK02224 559 AAAEAEEEAEEAREEVAELNSKLAElkeRIESLERIRTLLAAIADAEDEIERLREkrealaELNDERRERLAEKRERKRE 638
|
490 500
....*....|....*....|..
gi 1072253241 1921 LDEAEERADIAESQVNKLRAKS 1942
Cdd:PRK02224 639 LEAEFDEARIEEAREDKERAEE 660
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
918-1568 |
5.22e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 78.03 E-value: 5.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 918 DADERCEQLIKNKIQLEA------KLKEQTERLEDEEEMNAELTAKKRKLEdecselKKDIDDLELTLAKVEKEKHATEN 991
Cdd:COG4913 222 DTFEAADALVEHFDDLERahealeDAREQIELLEPIRELAERYAAARERLA------ELEYLRAALRLWFAQRRLELLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 992 KVKNLTEEMAGLDEIIVKLTKEKKALQEAHQQALDDLQAEEdkvntlTKAKAKLEQQVDDLEGSLEQEKKIRMDLERVKR 1071
Cdd:COG4913 296 ELEELRAELARLEAELERLEARLDALREELDELEAQIRGNG------GDRLEQLEREIERLERELEERERRRARLEALLA 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1072 KLEGDVKLSQESLMDLENDKQQLEEKLKKKDFEVSQLNTRIEDEQNvciQLQKKMKELQARIeeleeeleaertarAKVE 1151
Cdd:COG4913 370 ALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALR---DLRRELRELEAEI--------------ASLE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1152 KLRCDLSRELEEISERLEEAGGATSVQMELnkkrEAEFLKLRRDLE------ESTLHSEATAASLRKKHADSVAELSEQI 1225
Cdd:COG4913 433 RRKSNIPARLLALRDALAEALGLDEAELPF----VGELIEVRPEEErwrgaiERVLGGFALTLLVPPEHYAAALRWVNRL 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1226 D-----NLQRVKQKLEKEKSEF--------KLELDD--VTSNMEQMVKAKANLEKlCRSLEDQANEHR-------TKSEE 1283
Cdd:COG4913 509 HlrgrlVYERVRTGLPDPERPRldpdslagKLDFKPhpFRAWLEAELGRRFDYVC-VDSPEELRRHPRaitragqVKGNG 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1284 NQRTVNELSSLRAKLQT--ENGelsRRLDEKESLVSQMTRGKQTYTQHLEDLKRQLEEETKAKNALAHALQSARHDSDLL 1361
Cdd:COG4913 588 TRHEKDDRRRIRSRYVLgfDNR---AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVA 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1362 REQfEEEQEAKAELQRiLSKANSEVaqwrtkyetdaiqrtEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQN 1441
Cdd:COG4913 665 SAE-REIAELEAELER-LDASSDDL---------------AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEE 727
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1442 EIEDLMVDLER-----SNAAAAALDKK--QRNFDKILAEWKQKFEESQTELESsqkEARSLSTELFKLKNAYeesldhLE 1514
Cdd:COG4913 728 ELDELQDRLEAaedlaRLELRALLEERfaAALGDAVERELRENLEERIDALRA---RLNRAEEELERAMRAF------NR 798
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1072253241 1515 TFKRENKNLQEEISDLTE------QLGESGksIHELE-KIRKQL----DQEKMEIQSALEEAEAT 1568
Cdd:COG4913 799 EWPAETADLDADLESLPEylalldRLEEDG--LPEYEeRFKELLnensIEFVADLLSKLRRAIRE 861
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1031-1948 |
1.44e-13 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 76.62 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1031 EEDKVNTLTKAKAkLEQQVDDLEG------SLEQEKKIRMDLERVKRKLEGDVKLSQESLMDLENDKQQLEEKLKKKDFE 1104
Cdd:TIGR00606 158 QEDSNWPLSEGKA-LKQKFDEIFSatryikALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESS 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1105 vSQLNTRIEDEQNVCIQLQKKMKELQARIEELEEELEAERTARAKVEKLRCDLSRELEEISERLEEA-GGATSVQMELNK 1183
Cdd:TIGR00606 237 -REIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQlNDLYHNHQRTVR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1184 KREAEFLKLRRDLEEstLHSEATAASLRKKHAD---SVAELSEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQMVKAK 1260
Cdd:TIGR00606 316 EKERELVDCQRELEK--LNKERRLLNQEKTELLveqGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIK 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1261 ANLEKLCRSLEDQA-----------NEHRTKSEENQRTVNELSSLRAKLQTENGELSRRLDEKESLVSQMtrgkQTYTQH 1329
Cdd:TIGR00606 394 NFHTLVIERQEDEAktaaqlcadlqSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKEL----QQLEGS 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1330 LEDLKRQLEEETKAKNALAHALQSARHDSDLLREQFEeeQEAKAELQRILSKANSEVAQwrTKYETDAIQRTEELEEAKK 1409
Cdd:TIGR00606 470 SDRILELDQELRKAERELSKAEKNSLTETLKKEVKSL--QNEKADLDRKLRKLDQEMEQ--LNHHTTTRTQMEMLTKDKM 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1410 KLAQRL-----QEAEEAVEAVN--AKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAALDKKQ---RNFDKILAEWKQKFE 1479
Cdd:TIGR00606 546 DKDEQIrkiksRHSDELTSLLGyfPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKnhiNNELESKEEQLSSYE 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1480 ES----------QTELESSQKEARSLSTELFKLKNAYEESLDHLETFKREN--------------KNLQEEISDLTEQLG 1535
Cdd:TIGR00606 626 DKlfdvcgsqdeESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENqsccpvcqrvfqteAELQEFISDLQSKLR 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1536 ESGKSIHELEKIRKQLDQEKMEIQSALEEAEATLEHEEGKILHAQLELHQIKADSERklaEKDEEMEQAKrnyqrMVDTL 1615
Cdd:TIGR00606 706 LAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQR---LKNDIEEQET-----LLGTI 777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1616 QTSLEAETRSRNEALRIKK-KMEGDLNEMEIQLSQANRQAAEAQKQVKILQSYLKDTQIQLDDALRASEDLKENIAIVER 1694
Cdd:TIGR00606 778 MPEEESAKVCLTDVTIMERfQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQE 857
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1695 RNTLLQAELEELRS----LVEQTERARKLSEQeLIETSERVQLLHSQNTSLINQKKKMESDLSQLQTEMEEAVQecrNAE 1770
Cdd:TIGR00606 858 QIQHLKSKTNELKSeklqIGTNLQRRQQFEEQ-LVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELIS---SKE 933
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1771 EKAKKAITDAAMMAEELKK--------EQDTSAHLERMKKNMEQTIKDLQQRLDEAEQialkgGKKQLQKlEARVRELDN 1842
Cdd:TIGR00606 934 TSNKKAQDKVNDIKEKVKNihgymkdiENKIQDGKDDYLKQKETELNTVNAQLEECEK-----HQEKINE-DMRLMRQDI 1007
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1843 ELEAEQKRNAESVKGMRKYERRIKEL-----TYQTEEDRKNLARLQDLVDKLQLKVKTYKR-------QAEESEEQANTS 1910
Cdd:TIGR00606 1008 DTQKIQERWLQDNLTLRKRENELKEVeeelkQHLKEMGQMQVLQMKQEHQKLEENIDLIKRnhvlalgRQKGYEKEIKHF 1087
|
970 980 990
....*....|....*....|....*....|....*...
gi 1072253241 1911 LSKFRKVQHELDEAEERADIAESQVNKLRAKSRDVSTK 1948
Cdd:TIGR00606 1088 KKELREPQFRDAEEKYREMMIVMRTTELVNKDLDIYYK 1125
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
861-1545 |
1.56e-13 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 76.31 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 861 AETEKEMQTMKEEFQ-KLKEALEKSEARRKDLEEKMVSLLQEKNDLQLQVQAEQDNladADERCEQLIKNKIQLEAKLke 939
Cdd:pfam15921 252 SESQNKIELLLQQHQdRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQ---ARNQNSMYMRQLSDLESTV-- 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 940 qterledeEEMNAELTAKKRKLEDECSELKKD--IDDLELTLAKVEKEKHATENkvKNLTEEmagLDEIIVKLTKEKKAL 1017
Cdd:pfam15921 327 --------SQLRSELREAKRMYEDKIEELEKQlvLANSELTEARTERDQFSQES--GNLDDQ---LQKLLADLHKREKEL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1018 QEAHQQ--------------------ALDDLQAEEDKVNTLTKA-----KAKLEQQVDDLEG---SLEQEKKIRMDLERV 1069
Cdd:pfam15921 394 SLEKEQnkrlwdrdtgnsitidhlrrELDDRNMEVQRLEALLKAmksecQGQMERQMAAIQGkneSLEKVSSLTAQLEST 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1070 KRKLEGDV----------KLSQESLMDLENDKQQLEEKLKKKDFEVSQLNTRIEdeqnVCIQLQKKMKELQARIEELEEE 1139
Cdd:pfam15921 474 KEMLRKVVeeltakkmtlESSERTVSDLTASLQEKERAIEATNAEITKLRSRVD----LKLQELQHLKNEGDHLRNVQTE 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1140 LEAERTARAKVEKLRCDLSRELEEISERLEEAGGATSVQMELNKKREAEFLKLRRDLEESTLhseataasLRKKHADSVA 1219
Cdd:pfam15921 550 CEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKI--------LKDKKDAKIR 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1220 ELSEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQMVK----AKANLEKLCRSLEDQANEHRTKSEENQRTVN------ 1289
Cdd:pfam15921 622 ELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNevktSRNELNSLSEDYEVLKRNFRNKSEEMETTTNklkmql 701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1290 -----ELSSLRAKLQTENGELSRRLDEKESLVSQMT--RGK----QTYTQHLEDLKRQLEEE----TKAKNALAHALQSA 1354
Cdd:pfam15921 702 ksaqsELEQTRNTLKSMEGSDGHAMKVAMGMQKQITakRGQidalQSKIQFLEEAMTNANKEkhflKEEKNKLSQELSTV 781
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1355 RHDS-------DLLREQFEEEQEAKAELQRILSKANSEVAQWRtkyetDAIQRTEElEEAKKKLAQRLQEAE-------- 1419
Cdd:pfam15921 782 ATEKnkmagelEVLRSQERRLKEKVANMEVALDKASLQFAECQ-----DIIQRQEQ-ESVRLKLQHTLDVKElqgpgyts 855
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1420 -EAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAALDKKQRNFDKILAEWKQKFEESQTeLESSQKEARSLSTE 1498
Cdd:pfam15921 856 nSSMKPRLLQPASFTRTHSNVPSSQSTASFLSHHSRKTNALKEDPTRDLKQLLQELRSVINEEPT-VQLSKAEDKGRAPS 934
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 1072253241 1499 LFKLKNAYEESLDHLE----TFKRENKNLQEEISDLTEQLGESGKSIHELE 1545
Cdd:pfam15921 935 LGALDDRVRDCIIESSlrsdICHSSSNSLQTEGSKSSETCSREPVLLHAGE 985
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
922-1706 |
1.75e-13 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 76.16 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 922 RCEQLIKNKIQLEAKLKEQTERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHAT----ENKVKNLT 997
Cdd:TIGR00618 153 EFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERkqvlEKELKHLR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 998 EEMAGLDEIIVKLTKEKKALQEAH--QQALDDLQAEEDKVNTLTKAKAKLEQqvddlegsleqekkiRMDLERVKRKLEG 1075
Cdd:TIGR00618 233 EALQQTQQSHAYLTQKREAQEEQLkkQQLLKQLRARIEELRAQEAVLEETQE---------------RINRARKAAPLAA 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1076 DVKLSQESLMDLENDKQQLEEKLKKKDFEVSQLNTRIEDEQNVCIQLQKKMKELQARIEELEEeleaertarAKVEKLRC 1155
Cdd:TIGR00618 298 HIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDA---------HEVATSIR 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1156 DLSRELEEISERLEEAGGATSVQMELNKKREAEFLKLRRDL-EESTLHSEATAASLRKKHADSVAELSEQIDNLQRVK-Q 1233
Cdd:TIGR00618 369 EISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQaTIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAiT 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1234 KLEKEKSEFKLELDDVTSNMEQMVKAKANLEKLCRSLEDQANEHRTKSEENQRTVNELSSLRAKLQTEngelSRRLDEKE 1313
Cdd:TIGR00618 449 CTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPA----RQDIDNPG 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1314 SLVSQMTRGKQTYTQH---LEDLKRQLEEETKAKNALAHALQSARHDSDLLREQFEEEQEAKAELQRILSkansEVAQWR 1390
Cdd:TIGR00618 525 PLTRRMQRGEQTYAQLetsEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITV----RLQDLT 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1391 TKYETDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNaKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAALDKKQrnfdki 1470
Cdd:TIGR00618 601 EKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQ-CSQELALKLTALHALQLTLTQERVREHALSIRVLPKE------ 673
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1471 laewkqKFEESQTELESSQKEARSLSTELfklknayeESLDHLETFKREnknlqeeisdLTEQLGESGKSIHELEKIRKQ 1550
Cdd:TIGR00618 674 ------LLASRQLALQKMQSEKEQLTYWK--------EMLAQCQTLLRE----------LETHIEEYDREFNEIENASSS 729
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1551 LDQEKMEIQSALEEAEATLEHEEGKILHAQLELHQIKADSERKLAEKDEEMEQAKRNYQRMVDTLQTSLEaETRSRNEAL 1630
Cdd:TIGR00618 730 LGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTH-LLKTLEAEI 808
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1072253241 1631 RIKKKMEGDLNEMEIQLSQANRQaaeaqkQVKILQSYLKDTQIQLDDALRASEDLKENIAIVERRNTLLQAELEEL 1706
Cdd:TIGR00618 809 GQEIPSDEDILNLQCETLVQEEE------QFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1088-1818 |
1.96e-13 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 75.83 E-value: 1.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1088 ENDKQQLEEKLKKKDFEVSQLNTRIEDEQNVCIQLQKKMKELQARIEELEEELEA----ERTARAKVEKLRCDLSRELEE 1163
Cdd:TIGR04523 32 DTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDlndkLKKNKDKINKLNSDLSKINSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1164 ISerleeaggatsVQMELNKKREAEFLKLRRDLEESTLHSEATAASLRKKHADsVAELSEQIDNLQRVKQKLEKEKSEFK 1243
Cdd:TIGR04523 112 IK-----------NDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKE-LEKLNNKYNDLKKQKEELENELNLLE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1244 LELDDVTSNMEQMVKAKANLEKLCRSLEdqanehrTKSEENqrtvNELSSLRAKLQTENGELSRRLDEKESLVSQMTRGK 1323
Cdd:TIGR04523 180 KEKLNIQKNIDKIKNKLLKLELLLSNLK-------KKIQKN----KSLESQISELKKQNNQLKDNIEKKQQEINEKTTEI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1324 QTYTQHLEDLKrqlEEETKAKNALAHALQSARHDSDLLREQFEEEQEAKAELQRILSKANSEvaqWRTKYETDAIQRTEE 1403
Cdd:TIGR04523 249 SNTQTQLNQLK---DEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQD---WNKELKSELKNQEKK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1404 LEEAKKKLAQrlqeAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAALDKKQRNFDKILAEWKQKFEESQT 1483
Cdd:TIGR04523 323 LEEIQNQISQ----NNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLES 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1484 ELESSQKEARSLSTELFKLKNAYEESLDHLETFKRENKNLQEEISDLTEQLGESGKSIHELEKIRKQLDQEKMEIQSALE 1563
Cdd:TIGR04523 399 KIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSIN 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1564 EAEATLEHEEGKILHAQLELHQIKA---DSERKLAEKDEEMEQAKRNyQRMVDTLQTSLEAETRSRNEALrIKKKMEGDL 1640
Cdd:TIGR04523 479 KIKQNLEQKQKELKSKEKELKKLNEekkELEEKVKDLTKKISSLKEK-IEKLESEKKEKESKISDLEDEL-NKDDFELKK 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1641 NEMEIQLSQANRQAaeaqKQVKILQSYLKDTQIQLDDALRASEDLKENI-----------AIVERRNTLLQAELEELRSL 1709
Cdd:TIGR04523 557 ENLEKEIDEKNKEI----EELKQTQKSLKKKQEEKQELIDQKEKEKKDLikeieekekkiSSLEKELEKAKKENEKLSSI 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1710 VEQTERARKLSEQELIETSERVQLLHSQNTSLINQKKKMESDLSQLQTEMEEAVQECRNAEEKA---KKAITDAAMMAEE 1786
Cdd:TIGR04523 633 IKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKELSLHYKKYitrMIRIKDLPKLEEK 712
|
730 740 750
....*....|....*....|....*....|..
gi 1072253241 1787 LKKEQDTSAHLERMKKNMEQTIKDLQQRLDEA 1818
Cdd:TIGR04523 713 YKEIEKELKKLDEFSKELENIIKNFNKKFDDA 744
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1216-1889 |
2.24e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 76.11 E-value: 2.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1216 DSVAELSEQIDNLQRVKQKLEKEKSEFKLeLDDVTSNMEQMVKAKANLEKLcRSLEDQAN--EHRTKSEENQRTVNELSS 1293
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAREQIEL-LEPIRELAERYAAARERLAEL-EYLRAALRlwFAQRRLELLEAELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1294 LRAKLQTENGELSRRLDEKESLVSQMtrgKQTYTQH----LEDLKRQLEEETKAKNALAHALQSARHDSDLLREQFEEEQ 1369
Cdd:COG4913 303 ELARLEAELERLEARLDALREELDEL---EAQIRGNggdrLEQLEREIERLERELEERERRRARLEALLAALGLPLPASA 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1370 EAKAELQRILSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQE-----------AEEAVEAVNAKCSSLEKTKHR 1438
Cdd:COG4913 380 EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEiaslerrksniPARLLALRDALAEALGLDEAE 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1439 L----------------QNEIE--------DLMVDLERSNAAAAALDK---KQR-NFDKIlaewkqkfEESQTELESSQK 1490
Cdd:COG4913 460 LpfvgelievrpeeerwRGAIErvlggfalTLLVPPEHYAAALRWVNRlhlRGRlVYERV--------RTGLPDPERPRL 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1491 EARSLSTELFKLKNAYEESLDHL-------------ETFKRENKNlqeeisdLTEQ-LGESGKSIHELeKIRKQLDQEkm 1556
Cdd:COG4913 532 DPDSLAGKLDFKPHPFRAWLEAElgrrfdyvcvdspEELRRHPRA-------ITRAgQVKGNGTRHEK-DDRRRIRSR-- 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1557 eiqsaleeaeatleheegkilhaqlelHQIKADSERKLAEKDEEMEQAKRNY---QRMVDTLQTSLEAETRSRNEALRIK 1633
Cdd:COG4913 602 ---------------------------YVLGFDNRAKLAALEAELAELEEELaeaEERLEALEAELDALQERREALQRLA 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1634 kkmegDLNEMEIQLSQANRQAAEAQKQ----------VKILQSYLKDTQIQLDDALRASEDLKENIAIVERRNTLLQAEL 1703
Cdd:COG4913 655 -----EYSWDEIDVASAEREIAELEAElerldassddLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL 729
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1704 EELRSLVEQTERARKLSEQELIEtsERVQLLHSQNtSLINQKKKMESDLSQLQTEMEEAVQECRNAEEKAKK-------- 1775
Cdd:COG4913 730 DELQDRLEAAEDLARLELRALLE--ERFAAALGDA-VERELRENLEERIDALRARLNRAEEELERAMRAFNRewpaetad 806
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1776 ------AITDAAMMAEELkKEQDTSAHLERMK----KNMEQTIKDLQQRLDEAEQIAlkggKKQLQKLEARVRELD-NE- 1843
Cdd:COG4913 807 ldadleSLPEYLALLDRL-EEDGLPEYEERFKellnENSIEFVADLLSKLRRAIREI----KERIDPLNDSLKRIPfGPg 881
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 1072253241 1844 ----LEAEQKRNAEsvkgMRKYERRIKELT----YQTEEDR-KNLARLQDLVDKL 1889
Cdd:COG4913 882 rylrLEARPRPDPE----VREFRQELRAVTsgasLFDEELSeARFAALKRLIERL 932
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
858-1533 |
2.44e-13 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 75.98 E-value: 2.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 858 LKSAETEKEmqtmkeefqklkealeksearRKDLEEKMvsllqekNDLQLQVQAEQDNLADADERCEQLIKNKIQLEAKL 937
Cdd:pfam01576 419 ARLSESERQ---------------------RAELAEKL-------SKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQL 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 938 KEQTERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIVKLTKEKKAL 1017
Cdd:pfam01576 471 QDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRL 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1018 QEAHQQALDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKIRMDLERVKRKLegDVKLSQESLMDLEN--DKQQLE 1095
Cdd:pfam01576 551 QRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKF--DQMLAEEKAISARYaeERDRAE 628
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1096 EKLKKKDFEVSQLNTRIEDEQNVCIQLQKKMKELQARIEELEEELEAERTARAKVEKLRCDLSRELEEISERLE----EA 1171
Cdd:pfam01576 629 AEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEeledEL 708
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1172 GGATSVQMELNKKREAEFLKLRRDLEESTLHSEATAASLRKKHADSVAELSE---QIDNLQRVKQKLEKEKSEFKLELDD 1248
Cdd:pfam01576 709 QATEDAKLRLEVNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDerkQRAQAVAAKKKLELDLKELEAQIDA 788
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1249 VTSNMEQMVKakaNLEKLcrsledqanehRTKSEENQRTVNELSSLRAKLQTENGELSRRLDEKESLVSQMT-------R 1321
Cdd:pfam01576 789 ANKGREEAVK---QLKKL-----------QAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQedlaaseR 854
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1322 GKQTYTQHLEDLKRQLEEETKAKNALAHALQSARHDSDLLREQFEEEQEAKAELQRILSKANSEVAQWRTKY--ETDAIQ 1399
Cdd:pfam01576 855 ARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELaaERSTSQ 934
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1400 RTE----ELEEAKKKLAQRLQEAEEAVEavnakcSSLEKTKHRLQNEIEDLMVDLERSNAAAAALDKKQRNFDKILAEWK 1475
Cdd:pfam01576 935 KSEsarqQLERQNKELKAKLQEMEGTVK------SKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVL 1008
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 1072253241 1476 QKFEESQTELESSQKEARSLSTELFKLKNAYEESLDHLETFKRENKNLQEEISDLTEQ 1533
Cdd:pfam01576 1009 LQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATES 1066
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1222-1947 |
2.92e-13 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 75.39 E-value: 2.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1222 SEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQMVKAKANLEKLCRSLEDQANEHRtKSEENQRTVNELSSLRAKLQTE 1301
Cdd:TIGR00618 183 LMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQ-QSHAYLTQKREAQEEQLKKQQL 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1302 NGELSRRLDEKESLVSQmtrgkqtytqhLEDLKRQLEEETKAKNALAHALQSARHDSDLlREQFEEEQEAKAELQRILSK 1381
Cdd:TIGR00618 262 LKQLRARIEELRAQEAV-----------LEETQERINRARKAAPLAAHIKAVTQIEQQA-QRIHTELQSKMRSRAKLLMK 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1382 ANSEVAQwrtkyETDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEiEDLMVDLERSNAAAAALD 1461
Cdd:TIGR00618 330 RAAHVKQ-----QSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQ-QQKTTLTQKLQSLCKELD 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1462 KKQRNFDKILAEwKQKFEESQTELESSQKEARSLSTELFKLKNAYEESLDHLETFKRENKNLQEEISDLTEQLGEsgksi 1541
Cdd:TIGR00618 404 ILQREQATIDTR-TSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQT----- 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1542 heLEKIRKQLDQEKMEIQSALEEAEATLEHEEGKILHaqLELHQIKADSERKLAEKDEEMEQAKRNYQRMVDTLQTSLEA 1621
Cdd:TIGR00618 478 --KEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIH--PNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTS 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1622 EtrsRNEALRIKKKMEGDLNEMEIQLSQANRQAAEAQKQVKILQSYLKDTQIQLDDALRASEDLKENIAIVERRNTLLQA 1701
Cdd:TIGR00618 554 E---RKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDV 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1702 ELEELRSLVEQTERARKLSEQELIETSERVQllHSQNTSLINQKKKMESDLSQLQTEMEEAVQECRNAEEKAKKAitdaA 1781
Cdd:TIGR00618 631 RLHLQQCSQELALKLTALHALQLTLTQERVR--EHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQ----T 704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1782 MMAEELKKEQDTSAHLERMKKNMEQTIKDLQQRLDEAEQIALKGGKKQLQKLEARVRELDN---ELEAEQKRNAESVKGM 1858
Cdd:TIGR00618 705 LLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNnneEVTAALQTGAELSHLA 784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1859 RKYERRIKELTYQTEEDRKNLARLQDLVDKLQLKVKTYKRQAEESEEQANTSLSKFRKVQHELDEAEERADIAESQVNKL 1938
Cdd:TIGR00618 785 AEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQL 864
|
....*....
gi 1072253241 1939 RAKSRDVST 1947
Cdd:TIGR00618 865 TQEQAKIIQ 873
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1212-1716 |
3.50e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 75.34 E-value: 3.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1212 KKHADSVAELSEQIDNLQRVKQKLEKEKSEFKLELddvtsnmeqMVKAKANLEKLCRSLEDQANEHRTKSEENQRTVNEL 1291
Cdd:COG4913 258 RELAERYAAARERLAELEYLRAALRLWFAQRRLEL---------LEAELEELRAELARLEAELERLEARLDALREELDEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1292 SSLRAKLQTEN-GELSRRLDEKESLVSQMTRGKQTYTQHLEDLKRQLEEETKAKNALAHALQSARHDsdlLREQFEEEQE 1370
Cdd:COG4913 329 EAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEA---LEEELEALEE 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1371 AKAELQRILSKANSEVAQWRTkyETDAIQRT-----EELEEAKKKLAQRLQEAEEAVEAVnakCSSLE-KTKHRL-QNEI 1443
Cdd:COG4913 406 ALAEAEAALRDLRRELRELEA--EIASLERRksnipARLLALRDALAEALGLDEAELPFV---GELIEvRPEEERwRGAI 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1444 E--------DLMVDLERSNAAAAALDK---KQR-NFDKIlaewkqkfEESQTELESSQKEARSLSTELFKLKNAYEESLD 1511
Cdd:COG4913 481 ErvlggfalTLLVPPEHYAAALRWVNRlhlRGRlVYERV--------RTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLE 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1512 HL-------------ETFKRENKNL-------------------------------QEEISDLTEQLGESGKSIHELEKI 1547
Cdd:COG4913 553 AElgrrfdyvcvdspEELRRHPRAItragqvkgngtrhekddrrrirsryvlgfdnRAKLAALEAELAELEEELAEAEER 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1548 RKQLDQEKMEIQSALEEAEATLEHEEGKILHAQLElhqikadseRKLAEKDEEMEQAKRNyQRMVDTLQTSLEAETRSRN 1627
Cdd:COG4913 633 LEALEAELDALQERREALQRLAEYSWDEIDVASAE---------REIAELEAELERLDAS-SDDLAALEEQLEELEAELE 702
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1628 EALRIKKKMEGDLNEMEIQLSQANRQAAEAQKQVKILQSYLKDTQIQLDDALRASEDLKENIAIVERRntlLQAELEELR 1707
Cdd:COG4913 703 ELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELREN---LEERIDALR 779
|
....*....
gi 1072253241 1708 SLVEQTERA 1716
Cdd:COG4913 780 ARLNRAEEE 788
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
861-1318 |
7.16e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 74.31 E-value: 7.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 861 AETEKEMQTMKEEFQKLKEALEKSEARRKDLEEKM-------VSLLQEKNDLQLQVQAEQDNLAD-------ADERCEQL 926
Cdd:PRK02224 268 AETEREREELAEEVRDLRERLEELEEERDDLLAEAglddadaEAVEARREELEDRDEELRDRLEEcrvaaqaHNEEAESL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 927 IKNKIQLE---AKLKEQTERLEDEEEmNAELTAKKRklEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGL 1003
Cdd:PRK02224 348 REDADDLEeraEELREEAAELESELE-EAREAVEDR--REEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDEL 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1004 DEIIVKLTKEKKALQEAHQQALDDLQA-----------EEDKVNTLTKAkaklEQQVDDLEGSLEQekkIRMDLERVKRK 1072
Cdd:PRK02224 425 REREAELEATLRTARERVEEAEALLEAgkcpecgqpveGSPHVETIEED----RERVEELEAELED---LEEEVEEVEER 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1073 LEgdvklSQESLMDLENDKQQLEEKLKKKDFEVSQLNTRIEDEQNVCIQLQKKMKELQARIEELEEELEAERTARAKVEK 1152
Cdd:PRK02224 498 LE-----RAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEARE 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1153 LRCDLSRELEEISERLEEAGGATSVQMEL-NKKREAEFLKLRR-DLEESTLHSEATAASLRKKHADSVAELSEqiDNLQR 1230
Cdd:PRK02224 573 EVAELNSKLAELKERIESLERIRTLLAAIaDAEDEIERLREKReALAELNDERRERLAEKRERKRELEAEFDE--ARIEE 650
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1231 VKQKlekeKSEFKLELDDVTSNMEQMVKAKANLEKLCRSLE---DQANEHRTKSEENQRTVNELSS-------------- 1293
Cdd:PRK02224 651 ARED----KERAEEYLEQVEEKLDELREERDDLQAEIGAVEnelEELEELRERREALENRVEALEAlydeaeelesmygd 726
|
490 500
....*....|....*....|....*.
gi 1072253241 1294 LRAKLQTEN-GELSRRLDEKESLVSQ 1318
Cdd:PRK02224 727 LRAELRQRNvETLERMLNETFDLVYQ 752
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1213-1927 |
8.35e-13 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 74.10 E-value: 8.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1213 KHADSVAELSEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQMVKAKANLEKLCRSLEDQANEHRtkseenQRTVNELS 1292
Cdd:pfam12128 238 KIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKR------DELNGELS 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1293 SLRAKLQTENGELSRrLDEKESLVSQMtrGKQTYTQHLEDL---KRQLEEETKAKNALAHALQSARHDSDLLReqfeeeQ 1369
Cdd:pfam12128 312 AADAAVAKDRSELEA-LEDQHGAFLDA--DIETAAADQEQLpswQSELENLEERLKALTGKHQDVTAKYNRRR------S 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1370 EAKAELQRILSKANSEVAQwrtKYETDAIQRTEElEEAKKKLAQRLQEAEEAVEAvnakcsSLEKTKHRLQNEIEDLMVd 1449
Cdd:pfam12128 383 KIKEQNNRDIAGIKDKLAK---IREARDRQLAVA-EDDLQALESELREQLEAGKL------EFNEEEYRLKSRLGELKL- 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1450 leRSNAAAAALDKK--QRNFDKILaewkqkfEESQTELESSQKEARSLSTELFKLKNAYEESLDHLETFKRENKNLQEEI 1527
Cdd:pfam12128 452 --RLNQATATPELLlqLENFDERI-------ERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSAL 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1528 SDLTEQLGESGKSIHELEKIRKQLDQEKMEIQSALEEAEATLEHEE--GKILHAQLELHQIKADSERKLAEKDEEMEQAK 1605
Cdd:pfam12128 523 DELELQLFPQAGTLLHFLRKEAPDWEQSIGKVISPELLHRTDLDPEvwDGSVGGELNLYGVKLDLKRIDVPEWAASEEEL 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1606 RnyqRMVDTLQTSLEAEtRSRNEALrikkkmegdlnemEIQLSQANRQAAEAQKQVKILQSYLK---DTQIQLDDALRaS 1682
Cdd:pfam12128 603 R---ERLDKAEEALQSA-REKQAAA-------------EEQLVQANGELEKASREETFARTALKnarLDLRRLFDEKQ-S 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1683 EDLKENIAIVERRntllQAELEELRSLVEQteraRKLSEQELIETSERVQLLHSQNTSLINQKKK-MESDLSqlqtEMEE 1761
Cdd:pfam12128 665 EKDKKNKALAERK----DSANERLNSLEAQ----LKQLDKKHQAWLEEQKEQKREARTEKQAYWQvVEGALD----AQLA 732
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1762 AVQECRNAEEKAKKAITDA--AMMAEELKK---EQDTSAHLERMKKNMEQTIKDLQQRLDEAEQ----------IALKGG 1826
Cdd:pfam12128 733 LLKAAIAARRSGAKAELKAleTWYKRDLASlgvDPDVIAKLKREIRTLERKIERIAVRRQEVLRyfdwyqetwlQRRPRL 812
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1827 KKQLQKLEARVRELDNELeaeqKRNAESVKGMR-KYERRIKELTYQTEEDRKNLARLQDLVDKL-QLKVKTYKRQAEESE 1904
Cdd:pfam12128 813 ATQLSNIERAISELQQQL----ARLIADTKLRRaKLEMERKASEKQQVRLSENLRGLRCEMSKLaTLKEDANSEQAQGSI 888
|
730 740
....*....|....*....|...
gi 1072253241 1905 EQANTSLSKFRKVQHELDEAEER 1927
Cdd:pfam12128 889 GERLAQLEDLKLKRDYLSESVKK 911
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1391-1945 |
1.50e-12 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 73.29 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1391 TKYETDAIQRTEELEEAKkklaQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEdlmvdlersnaAAAALDKKQRNFDKI 1470
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVK----ERQQKAESELKELEKKHQQLCEEKNALQEQLQ-----------AETELCAEAEEMRAR 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1471 LAEWKQKFEESQTELESSQKEARSLSTELfklknayeesldhletfKRENKNLQEEISDLTEQLGESgksihelEKIRKQ 1550
Cdd:pfam01576 66 LAARKQELEEILHELESRLEEEEERSQQL-----------------QNEKKKMQQHIQDLEEQLDEE-------EAARQK 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1551 LDQEKMEIQSALEEAEA---TLEHEEGKILHAQLELHQIKADSERKLAEKDEE---MEQAKRNYQRMVDTLQTSLEAETR 1624
Cdd:pfam01576 122 LQLEKVTTEAKIKKLEEdilLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKaksLSKLKNKHEAMISDLEERLKKEEK 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1625 SRNEALRIKKKMEGDLNEMEIQLSQANRQAAEAQKQVKILQSYLKDTQIQLDDALRASEDLKENIAIVERRNTLLQAELE 1704
Cdd:pfam01576 202 GRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLE 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1705 ELRSLVEQTERARKLSEQELieTSERVQLLHSQNTSLINQ--KKKMESDLSQLQTEMEEavqECRNAEekakkaitdaam 1782
Cdd:pfam01576 282 SERAARNKAEKQRRDLGEEL--EALKTELEDTLDTTAAQQelRSKREQEVTELKKALEE---ETRSHE------------ 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1783 maeelkkeqdtsAHLERMKKNMEQTIKDLQQRLDEAEQiALKGGKKQLQKLEARVRELDNELEAEQKRNAESVKGMRKYE 1862
Cdd:pfam01576 345 ------------AQLQEMRQKHTQALEELTEQLEQAKR-NKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLE 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1863 RRIKELTYQTEEDRKNLARLQDLVDKLQLKVKTykrqaeeseeqantslskfrkVQHELDEAEERADIAESQVNKLRAKS 1942
Cdd:pfam01576 412 GQLQELQARLSESERQRAELAEKLSKLQSELES---------------------VSSLLNEAEGKNIKLSKDVSSLESQL 470
|
...
gi 1072253241 1943 RDV 1945
Cdd:pfam01576 471 QDT 473
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1361-1940 |
1.64e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 72.77 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1361 LREQFEEEQEAkaELQRILSKANSEVAqwrtkyETDAIqrTEELEEAKKKLAQRLQEAEEAVEAVNAKcsslektkhrlQ 1440
Cdd:PRK02224 192 LKAQIEEKEEK--DLHERLNGLESELA------ELDEE--IERYEEQREQARETRDEADEVLEEHEER-----------R 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1441 NEIEDLMVDLERSNAAAAALDKKQRNFDKILAEWKQKFEESQTELESSQKEArslstelfKLKNAYEESL-DHLETFKRE 1519
Cdd:PRK02224 251 EELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEA--------GLDDADAEAVeARREELEDR 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1520 NKNLQEEISDLTEQLGESGKSIHELEKIRKQLDQEKMEIQSALEEAEATLEHEEGKIlhaqlelhqikADSERKLAEKDE 1599
Cdd:PRK02224 323 DEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAV-----------EDRREEIEELEE 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1600 EMEQAKRNyqrmVDTLQTSLEAETRSRNEALRIKKKMEGDLNEMEIQLSQA------NRQAAEAQKQVKILQSyLKDTQI 1673
Cdd:PRK02224 392 EIEELRER----FGDAPVDLGNAEDFLEELREERDELREREAELEATLRTArerveeAEALLEAGKCPECGQP-VEGSPH 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1674 --QLDDALRASEDLKENIAIVERRNTLLQAELEELRSLVEQTERARKLSEQEliETSErvQLLHSQNTSLINQKKKMES- 1750
Cdd:PRK02224 467 veTIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERR--EDLE--ELIAERRETIEEKRERAEEl 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1751 --DLSQLQTEMEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERmkknmeqtIKDLQQRLDEAEQialkggkk 1828
Cdd:PRK02224 543 reRAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLER--------IRTLLAAIADAED-------- 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1829 qlqkleaRVRELDNELEAEQKRNAESVKGMRKYERRIKELTYQTEEDrknlaRLQDLVDKLQlKVKTYKRQAEES----E 1904
Cdd:PRK02224 607 -------EIERLREKREALAELNDERRERLAEKRERKRELEAEFDEA-----RIEEAREDKE-RAEEYLEQVEEKldelR 673
|
570 580 590
....*....|....*....|....*....|....*....
gi 1072253241 1905 EQANTSLSKFRKVQHELDEAE---ERADIAESQVNKLRA 1940
Cdd:PRK02224 674 EERDDLQAEIGAVENELEELEelrERREALENRVEALEA 712
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1328-1899 |
1.73e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 73.03 E-value: 1.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1328 QHLEDLKRQLEEETKAKNALAHALQSArhdsdllrEQFEEEQEAKAELQRILSKANSEVAQwrTKYETdAIQRTEELEEA 1407
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEPIRELA--------ERYAAARERLAELEYLRAALRLWFAQ--RRLEL-LEAELEELRAE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1408 KKKLAQRLQEAEEAVEAVNAKCSSLE--------KTKHRLQNEIEDLMVDLERSNAAAAALDKKQRNFDKILAEWKQKFE 1479
Cdd:COG4913 304 LARLEAELERLEARLDALREELDELEaqirgnggDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFA 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1480 ESQTELessQKEARSLSTELFKLKNAYEESLDHLETFKRENKNLQEEISDLteqlgESGKSI--HELEKIRKqldqekmE 1557
Cdd:COG4913 384 ALRAEA---AALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASL-----ERRKSNipARLLALRD-------A 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1558 IQSALEEAEATLeheegKILHaqlELHQIKADSE--RKLAEK------------DEEMEQAKRNYQRM-----VDT--LQ 1616
Cdd:COG4913 449 LAEALGLDEAEL-----PFVG---ELIEVRPEEErwRGAIERvlggfaltllvpPEHYAAALRWVNRLhlrgrLVYerVR 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1617 TSLEAETRSRNEALRIKKKMEGDLN------EMEI-------------QLSQA------------NRQAAEAQKQVKILQ 1665
Cdd:COG4913 521 TGLPDPERPRLDPDSLAGKLDFKPHpfrawlEAELgrrfdyvcvdspeELRRHpraitragqvkgNGTRHEKDDRRRIRS 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1666 SYL--KDTQIQLDDALRASEDLKENIAIVERRNTLLQAELEELRSLVEQTERARKLSEQELietseRVQLLHSQNTSLIN 1743
Cdd:COG4913 601 RYVlgFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEI-----DVASAEREIAELEA 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1744 QKKKME---SDLSQLQTEMEEAVQECRNAEEKAKKAITDAAMMAEELkkeqdtsahlermkKNMEQTIKDLQQRLDEAEQ 1820
Cdd:COG4913 676 ELERLDassDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKEL--------------EQAEEELDELQDRLEAAED 741
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1072253241 1821 IALKGgkkQLQKLEARVRELDNELEAEQKRnaesvkgmRKYERRIKELTyqteedrknlARLQDLVDKLQLKVKTYKRQ 1899
Cdd:COG4913 742 LARLE---LRALLEERFAAALGDAVERELR--------ENLEERIDALR----------ARLNRAEEELERAMRAFNRE 799
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
849-1629 |
3.21e-12 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 72.39 E-value: 3.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 849 KLYFKIKPLLKSAETEKEMQTMKEEFQKLKEALEKSE--ARRKDLEEKMVSLLQEKNDLQLQVQAEQDNLADAD------ 920
Cdd:TIGR00606 455 ELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEknSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNhhtttr 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 921 ERCEQLIKNKIQLEAKLKEQTERLEDEEEMNAELTAKKRKLEDECSELKKDID-------DLELTLAKVEKEKHATENKV 993
Cdd:TIGR00606 535 TQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINqtrdrlaKLNKELASLEQNKNHINNEL 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 994 KNLTEEMAGLDEIIVKLTKekkalQEAHQQALDDLQAEEDKVNT----LTKAKAKLEQQVDDLEGSLEQEKKIRMDLERV 1069
Cdd:TIGR00606 615 ESKEEQLSSYEDKLFDVCG-----SQDEESDLERLKEEIEKSSKqramLAGATAVYSQFITQLTDENQSCCPVCQRVFQT 689
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1070 KRKLEGDVKLSQESLMDLENDKQQLEEKLKKKDFEVSQLNTRIEDEQNVCIQLQKKMKELQARIEELEEELEAERTARAK 1149
Cdd:TIGR00606 690 EAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEE 769
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1150 VEKLRCDLSRELEEISERLEEAGGATSVQMELNKkreaeflklrrdleestlhseataasLRKKHADSVAELseQIDNLQ 1229
Cdd:TIGR00606 770 QETLLGTIMPEEESAKVCLTDVTIMERFQMELKD--------------------------VERKIAQQAAKL--QGSDLD 821
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1230 RVKQKLEKEKSEFKLELDDVTSNMEQMVKAKANLEKLCRSLEDQANE---HRTKSEENQRTVNELSSLRAKLQTENGELS 1306
Cdd:TIGR00606 822 RTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNElksEKLQIGTNLQRRQQFEEQLVELSTEVQSLI 901
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1307 RRLDEKESLVSQMTRGKQTYTQHLEDLKRQLEEETKAknalahalqsARHDSDLLREQFEEEQEAKAELQRILSKANSEV 1386
Cdd:TIGR00606 902 REIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKK----------AQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDY 971
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1387 AQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQneIEDLMVDLERSNAAAaaldKKQRN 1466
Cdd:TIGR00606 972 LKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRK--RENELKEVEEELKQH----LKEMG 1045
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1467 FDKILaEWKQKFEESQTELESSQKEARSLSTELfklkNAYEESLDHLETFKREN--KNLQEEISDLTEQLGESGKSIHEL 1544
Cdd:TIGR00606 1046 QMQVL-QMKQEHQKLEENIDLIKRNHVLALGRQ----KGYEKEIKHFKKELREPqfRDAEEKYREMMIVMRTTELVNKDL 1120
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1545 EKIRKQLDQEKMEIQS-ALEEAEATLEHEEGKILHAQ-LELHQIKADSERKLAEKDEemeqaKRNYQRMVDTLQTSLEAE 1622
Cdd:TIGR00606 1121 DIYYKTLDQAIMKFHSmKMEEINKIIRDLWRSTYRGQdIEYIEIRSDADENVSASDK-----RRNYNYRVVMLKGDTALD 1195
|
....*..
gi 1072253241 1623 TRSRNEA 1629
Cdd:TIGR00606 1196 MRGRCSA 1202
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1255-1922 |
4.31e-12 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 71.68 E-value: 4.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1255 QMVKAKANLEKLCRSLEDQANEHRTKSEENQRTVNELSSLRAKLQTENGELSRRLDEKeslvsqmtrgkqtyTQHLEDLK 1334
Cdd:pfam05483 82 KLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEE--------------IQENKDLI 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1335 RQLEEETKAKNALAHALQSARHDSDLLREQFEEEQEAKAELQRILSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQR 1414
Cdd:pfam05483 148 KENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1415 LQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAALDKKQRNFDKILAEWKQKFEESQTELESsqkears 1494
Cdd:pfam05483 228 EEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELED------- 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1495 lstelfkLKNAYEESLDHLETFKRENKNLQEEISDLTEqlgESGKSIHELEKIRKQLDQEKMEIQSALEEAEATLEHEEG 1574
Cdd:pfam05483 301 -------IKMSLQRSMSTQKALEEDLQIATKTICQLTE---EKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQ 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1575 KILHAQLELHQIKADSERKLAEKdEEMEQAKRNYQRMVDTLQTSLEAETRSRNEalriKKKMEGDLNEMEIQLSQANRQA 1654
Cdd:pfam05483 371 RLEKNEDQLKIITMELQKKSSEL-EEMTKFKNNKEVELEELKKILAEDEKLLDE----KKQFEKIAEELKGKEQELIFLL 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1655 AEAQKQVKILQSYLKDTQIQLDDALRASEDLKENIAIVERRNTLLQAELEELrslveqterarKLSEQELI-ETSERVQL 1733
Cdd:pfam05483 446 QAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKL-----------LLENKELTqEASDMTLE 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1734 LHSQNTSLINQKKKMESDLSQLQTEMEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQQ 1813
Cdd:pfam05483 515 LKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILEN 594
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1814 RLDEAeqialkggKKQLQKLEARVRELDNELEAEQKRNAESVKGMRKYERRIKELTYQTEEDRKNLARLQDLVDKLQLKV 1893
Cdd:pfam05483 595 KCNNL--------KKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDK 666
|
650 660
....*....|....*....|....*....
gi 1072253241 1894 KTYKRQAEESEEQANTSLSKFRKVQHELD 1922
Cdd:pfam05483 667 KISEEKLLEEVEKAKAIADEAVKLQKEID 695
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
942-1644 |
4.81e-12 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 71.29 E-value: 4.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 942 ERLEDEEEMNAE-LTAKKRKLEDECSELKKDIDDLELTL----AKVEKEKHATENKVKNLTEEMAGLDEIIVKLTKEkka 1016
Cdd:pfam05483 63 EGLKDSDFENSEgLSRLYSKLYKEAEKIKKWKVSIEAELkqkeNKLQENRKIIEAQRKAIQELQFENEKVSLKLEEE--- 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1017 LQEaHQQALDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKIRMDLE-------------RVK---RKLEGDVKLs 1080
Cdd:pfam05483 140 IQE-NKDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNnniekmilafeelRVQaenARLEMHFKL- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1081 QESLMDLENDKQQLEEKLKKKDFEVSQLNTRIEDEQNVCIQLQKKMKELQARIEELEEELEAERTARAKVEKLRCDLSRE 1160
Cdd:pfam05483 218 KEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKE 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1161 LEEISERLEEaggATSVQMELNKKREAEFLKLRRDLEESTLHSEATAASlRKKHADSVAELSEQIDNLQRV----KQKLE 1236
Cdd:pfam05483 298 LEDIKMSLQR---SMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKA-KAAHSFVVTEFEATTCSLEELlrteQQRLE 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1237 KEKSEFKL---ELDDVTSNMEQMVKAKANLEKLCRSLEDQANEHRTKSEENQRTVNELSSLRAKLQTENGELSRRLDEKE 1313
Cdd:pfam05483 374 KNEDQLKIitmELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIH 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1314 SLVSQMT---RGKQTYTQHLEDLKRQLEEET-KAKNALAHALQSARHDSDLLREQFEEEQEAKAELQRILSKANSE---V 1386
Cdd:pfam05483 454 DLEIQLTaikTSEEHYLKEVEDLKTELEKEKlKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEermL 533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1387 AQWRTKYETDaIQRTEELEEAKKKLAQ-------RLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAA 1459
Cdd:pfam05483 534 KQIENLEEKE-MNLRDELESVREEFIQkgdevkcKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEE 612
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1460 LDKKQRNFdkilaewKQKFEESQTELESSQKEARSLSTELFKLKNAYEESLDHLETfKRENKNLQEEisDLTEQLGESGK 1539
Cdd:pfam05483 613 LHQENKAL-------KKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQK-EIEDKKISEE--KLLEEVEKAKA 682
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1540 SIHELEKIRKQLD---QEKMEIQSALEEAEatlEHEEGKILHAQlelhqikaDSERKLAeKDEEMEQAkrnyqrmvdTLQ 1616
Cdd:pfam05483 683 IADEAVKLQKEIDkrcQHKIAEMVALMEKH---KHQYDKIIEER--------DSELGLY-KNKEQEQS---------SAK 741
|
730 740
....*....|....*....|....*....
gi 1072253241 1617 TSLEAETRS-RNEALRIKKKMEGDLNEME 1644
Cdd:pfam05483 742 AALEIELSNiKAELLSLKKQLEIEKEEKE 770
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
859-1670 |
7.13e-12 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 71.16 E-value: 7.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 859 KSAETEKEMQTMKEEFQKLKEALEKSEARRKdlEEKMVSLLQEKNDLQLQvqaeqdnladadERCEQLIKNKIQLEAKLK 938
Cdd:pfam02463 245 LLRDEQEEIESSKQEIEKEEEKLAQVLKENK--EEEKEKKLQEEELKLLA------------KEEEELKSELLKLERRKV 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 939 EQTERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLEltlAKVEKEKHATENKVKNLTEEMAGLDEIIVKLTKEKKALQ 1018
Cdd:pfam02463 311 DDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELE---IKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLS 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1019 EAHQQALDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKIRMDLERVKRKLEGDVKLSQESLMDlendkqqLEEKL 1098
Cdd:pfam02463 388 SAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEK-------QELKL 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1099 KKKDFEVSQLNTRIEDEQNVCIQLQKKmKELQARIEELEEELEAERTARAKVEKLRCDLSRELEEISERLEEAGGATSVQ 1178
Cdd:pfam02463 461 LKDELELKKSEDLLKETQLVKLQEQLE-LLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVE 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1179 MELNKKreaeflklrrdleeSTLHSEATAASLRKKHADSVAELSEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQMVK 1258
Cdd:pfam02463 540 NYKVAI--------------STAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNL 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1259 AKANLEKLCRSLEDQANEHRTKSEENQRTVNELSSLRAKLQTENGELSRRLDEKESLVSQMTRGKQTYTQHLEDLKRQLE 1338
Cdd:pfam02463 606 AQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKA 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1339 EETKAKNALAHALQS----ARHDSDLLREQFEEEQEAKAELQRILSKANSEVAQWRTKYETDAIQrtEELEEAKKKLAQR 1414
Cdd:pfam02463 686 ESELAKEEILRRQLEikkkEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEE--EEEKSRLKKEEKE 763
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1415 LQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAALDKKQRNFDKILAEwKQKFEESQTELESSQKEARS 1494
Cdd:pfam02463 764 EEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQL-LIEQEEKIKEEELEELALEL 842
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1495 LSTELFKLKNAYEESLDHLETFKRENKNLQEEISDLTEQLGESGKSIHELEKIRKQLDQEKMEIQSALEEAEATLEHEEG 1574
Cdd:pfam02463 843 KEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEER 922
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1575 KILHAQLELHQIKADSERKLAEKDEE--MEQAKRNYQRMVDTLQTSLEAETRSRNEALRIKKKMEGDLNEMEIQLSQANR 1652
Cdd:pfam02463 923 IKEEAEILLKYEEEPEELLLEEADEKekEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEE 1002
|
810
....*....|....*...
gi 1072253241 1653 QAAEAQKQVKILQSYLKD 1670
Cdd:pfam02463 1003 EKKKLIRAIIEETCQRLK 1020
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1352-1927 |
7.55e-12 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 70.52 E-value: 7.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1352 QSARHDSDLlreqfeEEQEAKAELQRILSKANSEVAQWRTKYETDAIQRTEELEEAKKKL-AQR--LQEAEEAVEAVNAK 1428
Cdd:pfam05483 62 QEGLKDSDF------ENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIeAQRkaIQELQFENEKVSLK 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1429 CSSLEKTKHRL--QNEIEDLMVDLERSNAAAAALDKKQRNFDK-----ILAEWKQKFEESQTELESSQKEARSLSTEL-F 1500
Cdd:pfam05483 136 LEEEIQENKDLikENNATRHLCNLLKETCARSAEKTKKYEYEReetrqVYMDLNNNIEKMILAFEELRVQAENARLEMhF 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1501 KLKNAYEESLDHLETFKRENKNLQEEISDLTEQLGESGKSIHELEKIRKQLDQEKMEIQSALEEAEATLEHEEGKILHAQ 1580
Cdd:pfam05483 216 KLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLT 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1581 LELHQIKADSERKLAEK---DEEMEQAKRNYQRMVDTLQTSLEAETRSRNEALRIKKKMEGDLNEMEIQLSQANRQAAEA 1657
Cdd:pfam05483 296 KELEDIKMSLQRSMSTQkalEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKN 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1658 QKQVKILQSYLKDTQIQLDDALRASE----DLKENIAIVERRNTLLQAE------LEELRSLVEQTERARKLSEQELIET 1727
Cdd:pfam05483 376 EDQLKIITMELQKKSSELEEMTKFKNnkevELEELKKILAEDEKLLDEKkqfekiAEELKGKEQELIFLLQAREKEIHDL 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1728 SERVQLLHSQNTSLINQKKKMESDLSQLQTEMEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQT 1807
Cdd:pfam05483 456 EIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQ 535
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1808 IKDLQQR---LDEAEQIALKGGKKQLQKLEARVRELDNELEAEQKRNAESVKGMRKYERRIKELTYQTEEDRKNlarlqd 1884
Cdd:pfam05483 536 IENLEEKemnLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKN------ 609
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1072253241 1885 lVDKLQLKVKTYKRQAEESEEQANTSLSKFRKVQHELDEAEER 1927
Cdd:pfam05483 610 -IEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQK 651
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
862-1446 |
1.22e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 70.33 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 862 ETEKEMQTMKEEFQKLKEA---LEKSEARRKDLE------EKMVSLLQEKNDLQ-----LQVQAEQDNLADADERCEQLI 927
Cdd:COG4913 222 DTFEAADALVEHFDDLERAheaLEDAREQIELLEpirelaERYAAARERLAELEylraaLRLWFAQRRLELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 928 KNKIQLEAKLKEQTERLEDEEEMNAELTAKKRKLE-DECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEI 1006
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1007 IVKLTKEKKALQEAHQQALDDLQAE----EDKVNTLTKAKAKLEQQVDDLEGS--------------------------- 1055
Cdd:COG4913 382 FAALRAEAAALLEALEEELEALEEAlaeaEAALRDLRRELRELEAEIASLERRksniparllalrdalaealgldeaelp 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1056 --------LEQEKKIRMDLERV-----------------------KRKLEG-----DVKLSQESLMDLENDKQQLEEKLK 1099
Cdd:COG4913 462 fvgelievRPEEERWRGAIERVlggfaltllvppehyaaalrwvnRLHLRGrlvyeRVRTGLPDPERPRLDPDSLAGKLD 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1100 KKDFEVSQ-LNTRIEDEQNV-C-------------IQLQKKMKELQARIEELEEELEAER-----TARAKVEKLRcdlsR 1159
Cdd:COG4913 542 FKPHPFRAwLEAELGRRFDYvCvdspeelrrhpraITRAGQVKGNGTRHEKDDRRRIRSRyvlgfDNRAKLAALE----A 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1160 ELEEISERLEEAGGATSvqmELNKKREAeflkLRRDLEESTLHSEATAASLRkkhadsVAELSEQIDNLQRVKQKLEKEK 1239
Cdd:COG4913 618 ELAELEEELAEAEERLE---ALEAELDA----LQERREALQRLAEYSWDEID------VASAEREIAELEAELERLDASS 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1240 SEFklelddvtsnmeqmvkakanleklcRSLEDQANEHRTKSEENQRTVNELSSLRAKLQTENGELSRRLDEKESLVSQM 1319
Cdd:COG4913 685 DDL-------------------------AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1320 T-RGKQTYTQHLEDLKRQLEEETKAKnALAHALQSARhdSDLLREQFEEEQEAKAELQRILSKANSEVAQWRTKYET--- 1395
Cdd:COG4913 740 EdLARLELRALLEERFAAALGDAVER-ELRENLEERI--DALRARLNRAEEELERAMRAFNREWPAETADLDADLESlpe 816
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 1072253241 1396 -DAI---QRTEELEEAKKKLAQRLQEAEEavEAVNAKCSSLEKTKHRLQNEIEDL 1446
Cdd:COG4913 817 yLALldrLEEDGLPEYEERFKELLNENSI--EFVADLLSKLRRAIREIKERIDPL 869
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
853-1345 |
1.30e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 70.56 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 853 KIKPLLKSAETEKEMQTMK---EEFQKLKEALEKSEARRKDLEEKMVSLLQEKNDLQLQVQAEQDNLADADERCEQLIKN 929
Cdd:PTZ00121 1445 KADEAKKKAEEAKKAEEAKkkaEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKA 1524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 930 KIQLEAKLKEQTERLEDEEEMNAELTAKK----RKLED--ECSELKKDIDDLELTLAKVEKEKHATENKVknltEEMAGL 1003
Cdd:PTZ00121 1525 DEAKKAEEAKKADEAKKAEEKKKADELKKaeelKKAEEkkKAEEAKKAEEDKNMALRKAEEAKKAEEARI----EEVMKL 1600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1004 DEIIVKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKIRMDLERVKRKLEGDVKLSQEs 1083
Cdd:PTZ00121 1601 YEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEE- 1679
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1084 LMDLENDKQQLEEKLKKKDFE---VSQLNTRIEDEQNVCIQLQKKMKElqarieeleeeleaertARAKVEKLRcdlsRE 1160
Cdd:PTZ00121 1680 AKKAEEDEKKAAEALKKEAEEakkAEELKKKEAEEKKKAEELKKAEEE-----------------NKIKAEEAK----KE 1738
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1161 LEEISERLEEAggatsvqmelnKKREAEflklRRDLEESTLHSEATAASLRKKHADSVAELSEQIDNLQR--VKQKLEKE 1238
Cdd:PTZ00121 1739 AEEDKKKAEEA-----------KKDEEE----KKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRmeVDKKIKDI 1803
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1239 KSEFKLELDDVTSNMEQMVKAKANLEKLCRSLEDQANEHRTKSEENQRTVNELSSLRAKLQTENGELSRRLDEKESLVSQ 1318
Cdd:PTZ00121 1804 FDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEE 1883
|
490 500
....*....|....*....|....*..
gi 1072253241 1319 MTRGKQTYTQHLEDLKRQLEEETKAKN 1345
Cdd:PTZ00121 1884 IEEADEIEKIDKDDIEREIPNNNMAGK 1910
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1333-1715 |
2.38e-11 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 68.38 E-value: 2.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1333 LKRQLEEETKAKNALAHALQSARHDSDLLREQFEEEQEA----KAELQRILSKANSEVAQWRTKYEtDAIQRTEELEEAK 1408
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQwerqRRELESRVAELKEELRQSREKHE-ELEEKYKELSASS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1409 KKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERsnaaaaaLDKKQRNFDKILAEWKQKFEESQTELESS 1488
Cdd:pfam07888 111 EELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELER-------MKERAKKAGAQRKEEEAERKQLQAKLQQT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1489 QKEARSLSTELFKLKNAYEESLDHLETfkrenknLQEEISDLTEQLGESGKSIHELEKIRKQLD--QEKMEI-QSALEEA 1565
Cdd:pfam07888 184 EEELRSLSKEFQELRNSLAQRDTQVLQ-------LQDTITTLTQKLTTAHRKEAENEALLEELRslQERLNAsERKVEGL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1566 EATLEHEEGKILHAQLELHQIK---ADSERKLAEKDEEMEQAKRNYQRMVDTLQTSLEAETRSRNEALRIKKKMEGDLNE 1642
Cdd:pfam07888 257 GEELSSMAAQRDRTQAELHQARlqaAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQE 336
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1072253241 1643 MEIQlsqanRQAAEAQkqvkiLQSYLKDTQIQLDDALRASEDLKENIAIVERRNTLLQAELEELRSLVEQTER 1715
Cdd:pfam07888 337 ERME-----REKLEVE-----LGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQ 399
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1149-1856 |
3.15e-11 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 68.59 E-value: 3.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1149 KVEKLRCDLSRELEEISERLEEAGGATSVQ----MELNKKREAEFLKLRRDLEESTLHSEATAASlrkKHADSVaeLSEQ 1224
Cdd:pfam05483 89 KIKKWKVSIEAELKQKENKLQENRKIIEAQrkaiQELQFENEKVSLKLEEEIQENKDLIKENNAT---RHLCNL--LKET 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1225 IDNLQRVKQKLEKEKSEFKLELDDVTSNMEQMVKAkanLEKLCRSLEDQANEHRTKSEENQRTVNELSSlraklqtengE 1304
Cdd:pfam05483 164 CARSAEKTKKYEYEREETRQVYMDLNNNIEKMILA---FEELRVQAENARLEMHFKLKEDHEKIQHLEE----------E 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1305 LSRRLDEKESLVSQMTRGKQTYTQHLEDLKRQLEEETKAKNALAhalQSARHDSDLLREQFEEEQEAKAELQRILSKANS 1384
Cdd:pfam05483 231 YKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLE---EKTKLQDENLKELIEKKDHLTKELEDIKMSLQR 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1385 EVAQWRTkyetdaiqRTEELEEAKKKLAQRLQEAEEAVEAVNAKcssleKTKHRLQ-NEIEDLMVDLERSNAAAAALDKK 1463
Cdd:pfam05483 308 SMSTQKA--------LEEDLQIATKTICQLTEEKEAQMEELNKA-----KAAHSFVvTEFEATTCSLEELLRTEQQRLEK 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1464 QRNFDKILAEWKQKfeeSQTELESSQKEARSLSTELFKLKNAYEES---LDHLETFKRENKNLQEEISDLTEQLGESGKS 1540
Cdd:pfam05483 375 NEDQLKIITMELQK---KSSELEEMTKFKNNKEVELEELKKILAEDeklLDEKKQFEKIAEELKGKEQELIFLLQAREKE 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1541 IHELEKIRKQLDQEKMEIQSALEEAEATLEHEE----------GKILHAQLELHQIKADSERKLAEKDEEMEQAKRNYQR 1610
Cdd:pfam05483 452 IHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKlknieltahcDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEER 531
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1611 MVDTLQTSLEAETRSRNEALRIKKKMEGDLNEMEIQLSQANRQAAEAQKQVKILQSYLKDTQIQLDDALRASEDLKENIA 1690
Cdd:pfam05483 532 MLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIE 611
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1691 IVERRNTLLQAELEELRSLVEQTERARKLSEQELIETSERVQLLHSQNTSLINQKKKMESDL----SQLQTEMEEAVQEC 1766
Cdd:pfam05483 612 ELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLleevEKAKAIADEAVKLQ 691
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1767 RNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQQRLDEAEQIALKGGKKQLQKLEARV---RELDNE 1843
Cdd:pfam05483 692 KEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLeieKEEKEK 771
|
730
....*....|...
gi 1072253241 1844 LEAEQKRNAESVK 1856
Cdd:pfam05483 772 LKMEAKENTAILK 784
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1144-1687 |
5.18e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.02 E-value: 5.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1144 RTARAKVEKLRcdlsrELEEISERLEEAGGATSVQMELNKKREAEFLKLRRDLEESTLHSEATAAslrKKHADSVAELSE 1223
Cdd:COG4913 245 EDAREQIELLE-----PIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAEL---ARLEAELERLEA 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1224 QIDNLQRVKQKLE--------KEKSEFKLELDDVTSNMEQMVKAKANLEKLCRSLEDQANEHRTKSEENQRTV------- 1288
Cdd:COG4913 317 RLDALREELDELEaqirgnggDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAaalleal 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1289 ----NELSSLRAKLQTENGELSRRLDEKESLVSQMTRGKQTYTQHLEDLKRQLEEET----------------------- 1341
Cdd:COG4913 397 eeelEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALgldeaelpfvgelievrpeeerw 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1342 -----------------------------------------KAKNALAHALQSARHDSDLLREQFEEEQEAKAELQRILS 1380
Cdd:COG4913 477 rgaiervlggfaltllvppehyaaalrwvnrlhlrgrlvyeRVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEAELG 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1381 ------KANSE---------------VAQWRTKYE--------------TDAIQRTEELEEAKKKLAQRLQEAEEAVEAV 1425
Cdd:COG4913 557 rrfdyvCVDSPeelrrhpraitragqVKGNGTRHEkddrrrirsryvlgFDNRAKLAALEAELAELEEELAEAEERLEAL 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1426 NAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAaldkkqrnfdkiLAEWKQKFEesqtELESSQKEARSLSTELFKLKNA 1505
Cdd:COG4913 637 EAELDALQERREALQRLAEYSWDEIDVASAERE------------IAELEAELE----RLDASSDDLAALEEQLEELEAE 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1506 YEESLDHLETFKRENKNLQEEISDLTEQLGESGKSIHELEKIRKQLDQEKMEIQSAlEEAEATLEHEEGKILHAQLELHQ 1585
Cdd:COG4913 701 LEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFA-AALGDAVERELRENLEERIDALR 779
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1586 IKADSERKLAEKdeEMEQAKRNYQRMVDTLQTSLEAE-------TRSRNEAL-RIKKKMEGDLNEMEIQ-----LSQANR 1652
Cdd:COG4913 780 ARLNRAEEELER--AMRAFNREWPAETADLDADLESLpeylallDRLEEDGLpEYEERFKELLNENSIEfvadlLSKLRR 857
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1072253241 1653 QAAEAQKQVKILQSYLK------DTQIQLDDALRASEDLKE 1687
Cdd:COG4913 858 AIREIKERIDPLNDSLKripfgpGRYLRLEARPRPDPEVRE 898
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1374-1793 |
6.57e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 67.49 E-value: 6.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1374 ELQRILSKANSEVAQWRTKYET--DAIQRTEELEEAKKKLAQRLQEAEEAVEAVnakcsSLEKTKHRLQNEIEDLMVDLE 1451
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEEleELEEELEELEAELEELREELEKLEKLLQLL-----PLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1452 RSNAAAAALDKKQRNFDKILAEWKQKFEESQTELESSQKEARSlstELFKLKNAYEESLDHLETFKRENKNLQEEISDLT 1531
Cdd:COG4717 150 ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE---ELQDLAEELEELQQRLAELEEELEEAQEELEELE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1532 EQLgESGKSIHELEKIRKQLDQEK---------MEIQSALEEAEATLEHEEGK------ILHAQLELHQIKADSERKLAE 1596
Cdd:COG4717 227 EEL-EQLENELEAAALEERLKEARlllliaaalLALLGLGGSLLSLILTIAGVlflvlgLLALLFLLLAREKASLGKEAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1597 KDEEMEQAKRNYQRMVDTLQTSLEAETRSRNEALRIKKKMEGDLNEMEIQLSQANRQAAEAQKQVKIlQSYLKDTQIQLD 1676
Cdd:COG4717 306 ELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEI-AALLAEAGVEDE 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1677 DALRASEDLKENIAIVERRNTLLQAELEELRSLVEQTERARKLS---------EQELIETSERVQLLHSQNTSLINQKKK 1747
Cdd:COG4717 385 EELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEeleeeleelEEELEELEEELEELREELAELEAELEQ 464
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1072253241 1748 MESD--LSQLQTEMEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDT 1793
Cdd:COG4717 465 LEEDgeLAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
865-1273 |
7.40e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 67.10 E-value: 7.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 865 KEMQTMKEEFQKLKEALEKSEARRKDLEEKMVSLLQEKNDLQLQVQAEQD--NLADADERCEQLIKNKIQLEAKLKEQTE 942
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLyqELEALEAELAELPERLEELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 943 RLEDEEEMNAELTAKKRKLEDEC-----------SELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIVKLT 1011
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLeqlslateeelQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1012 KEKKALQE-----------AHQQALDDLQAEEDKV---------------NTLTKAKAKLEQQVDDLEGSLEQEKKIRMD 1065
Cdd:COG4717 241 LEERLKEArlllliaaallALLGLGGSLLSLILTIagvlflvlgllallfLLLAREKASLGKEAEELQALPALEELEEEE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1066 LERVKRKLEGDVKLSQESLMDLENDKQQLEEKLKKKDFEVSQLntriedeqnvciQLQKKMKELQARIEELEEELEAERT 1145
Cdd:COG4717 321 LEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL------------QLEELEQEIAALLAEAGVEDEEELR 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1146 ARAKVEKLRCDLSRELEEISERLEEAGGATSVQMELNKKR--EAEFLKLRRDLEEstlhSEATAASLRKKHADSVAELS- 1222
Cdd:COG4717 389 AALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEelEEELEELEEELEE----LEEELEELREELAELEAELEq 464
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1072253241 1223 -EQIDNLQRVKQKLEKEKSEFKLELDDVTSNMeqmvKAKANLEKLCRSLEDQ 1273
Cdd:COG4717 465 lEEDGELAELLQELEELKAELRELAEEWAALK----LALELLEEAREEYREE 512
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
878-1227 |
7.90e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 67.63 E-value: 7.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 878 KEALEKSEARRKDLEEKMVSLLQEKNDLQLQVQAEQDnLADADERCEQLIKNKI---QLEAKLKEQTERLEDEEEMNAEL 954
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQE-RREALQRLAEYSWDEIdvaSAEREIAELEAELERLDASSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 955 takkRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIVKLTKEKKALQEAHqqaLDDLQAEEDK 1034
Cdd:COG4913 688 ----AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL---LEERFAAALG 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1035 VNTLTKAKAKLEQQVDDLEGSLEQ-EKKIRMDLERVKRKLEGDVKLSQESLMDLEndkqqleeklkkkDFEvsQLNTRIE 1113
Cdd:COG4913 761 DAVERELRENLEERIDALRARLNRaEEELERAMRAFNREWPAETADLDADLESLP-------------EYL--ALLDRLE 825
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1114 DEQnvCIQLQKKMKELQarieeleeeleaERTARAKVEKLRCDLSRELEEISERLEEA---------GGATSVQMELNKK 1184
Cdd:COG4913 826 EDG--LPEYEERFKELL------------NENSIEFVADLLSKLRRAIREIKERIDPLndslkripfGPGRYLRLEARPR 891
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1072253241 1185 REAEFLKLRRDLEESTLHSEATAASLRKKHADSVAELSEQIDN 1227
Cdd:COG4913 892 PDPEVREFRQELRAVTSGASLFDEELSEARFAALKRLIERLRS 934
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1502-1932 |
8.94e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 67.10 E-value: 8.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1502 LKNAYEESLDHLETFK-RENKNLQEEISDLTEQLGESGKSIHELEKIRKQLDQEKMEIQsALEEAEATLEHEEGKI--LH 1578
Cdd:COG4717 47 LLERLEKEADELFKPQgRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELE-ELEAELEELREELEKLekLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1579 AQLELHQIKADSERKLAEKDEEMEQAKRNYQRMVDTLQTSLEAETRSRNEALRIKKKMEGDLNEMEIQLSQANRQAAEAQ 1658
Cdd:COG4717 126 QLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1659 KQVKILQSYLKDTQIQLDDALRASEDLKENIAIVERRNTLLQAELE-----ELRSLVEQTERARKLSEQELIETSERVQL 1733
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLlliaaALLALLGLGGSLLSLILTIAGVLFLVLGL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1734 LHSQNTSLINQKKKMESDLSQLQtemeeAVQECRNAEEKAKKAITDAAMMAEELKKEqdtsaHLERMKKNMEQTIKDLQQ 1813
Cdd:COG4717 286 LALLFLLLAREKASLGKEAEELQ-----ALPALEELEEEELEELLAALGLPPDLSPE-----ELLELLDRIEELQELLRE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1814 RLDEAEQIALKGGKKQLQKLEARVrelDNELEAEQKRNAESVKGMRKYERRIKELTYQTEEDRKNLARLQDLVDKLQLKV 1893
Cdd:COG4717 356 AEELEEELQLEELEQEIAALLAEA---GVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEE 432
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1072253241 1894 K--TYKRQAEESEEQANTSLSKFRKVQHELDEAEERADIAE 1932
Cdd:COG4717 433 EleELEEELEELEEELEELREELAELEAELEQLEEDGELAE 473
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1559-1953 |
9.47e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 67.37 E-value: 9.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1559 QSALEEAEATLEHEEGKILHAQL-ELHQIKADSERKLAEKDEEMEQAKRNYQRMVDTLQTslEAETRSRNEALrikkkmE 1637
Cdd:PRK02224 186 RGSLDQLKAQIEEKEEKDLHERLnGLESELAELDEEIERYEEQREQARETRDEADEVLEE--HEERREELETL------E 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1638 GDLNEMEIQLSQANRQAAEAQKQVKILQSYLKDTQIQLDDALRASEDLKENIAIVERRNTLLQAELEELRSLVEQTERAR 1717
Cdd:PRK02224 258 AEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAA 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1718 KLSEQELIETSERVQLLHSQNTSLINQKKKMESDLSQLQTEME---EAVQECRNAEEKAKKAITDAAM----MAEELKKE 1790
Cdd:PRK02224 338 QAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEdrrEEIEELEEEIEELRERFGDAPVdlgnAEDFLEEL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1791 QDTSAHLERMKKNMEQTIKDLQQRLDEAEQIaLKGGK---------------------KQLQKLEARVRELDNELEAEQK 1849
Cdd:PRK02224 418 REERDELREREAELEATLRTARERVEEAEAL-LEAGKcpecgqpvegsphvetieedrERVEELEAELEDLEEEVEEVEE 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1850 RnAESVKGMRKYERRIKELtyqtEEDRKNLARLqdlvdklqlkVKTYKRQAEESEEQANTSLSKFRKVQHELDEAEERAD 1929
Cdd:PRK02224 497 R-LERAEDLVEAEDRIERL----EERREDLEEL----------IAERRETIEEKRERAEELRERAAELEAEAEEKREAAA 561
|
410 420
....*....|....*....|....
gi 1072253241 1930 IAESQVNKLRAKSRDVSTKKSLNE 1953
Cdd:PRK02224 562 EAEEEAEEAREEVAELNSKLAELK 585
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
932-1148 |
1.43e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 65.17 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 932 QLEAKLKEQTERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIVKLT 1011
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1012 KEKK----ALQEAHQQALDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKIRMDLERVKRKLEGDVKLSQESLMDL 1087
Cdd:COG4942 104 EELAellrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1072253241 1088 ENDKQQLEEKLKKKDFEVSQLNTRIEDEQNVCIQLQKKMKELQARIEELEEELEAERTARA 1148
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
873-1764 |
1.59e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 66.52 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 873 EFQKLKEALEKSEARRKDLEEKMVSLLQEKNDLQLQVQAEQDNLADADERCEQliKNKIQ--------LEAKLKEQTERL 944
Cdd:PRK04863 294 ELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQ--QEKIEryqadleeLEERLEEQNEVV 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 945 EDEEEMNAELTAKKRKLEDECSELKKDIDDL-------------------------------ELTLAKVEKEKHATENKV 993
Cdd:PRK04863 372 EEADEQQEENEARAEAAEEEVDELKSQLADYqqaldvqqtraiqyqqavqalerakqlcglpDLTADNAEDWLEEFQAKE 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 994 KNLTEEMAGL-------DEIIVKLTKEKKALQ---------EAHQQALDDL-QAEEDKVntLTKAKAKLEQQVDDLEGSL 1056
Cdd:PRK04863 452 QEATEELLSLeqklsvaQAAHSQFEQAYQLVRkiagevsrsEAWDVARELLrRLREQRH--LAEQLQQLRMRLSELEQRL 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1057 EQEKkirmDLERVKRKLEGDVKLSQESLMDLENDKQQLEEKLKKKDFEVSQLNTRIEDeqnvciqLQKKMKELQARIEEL 1136
Cdd:PRK04863 530 RQQQ----RAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMA-------LRQQLEQLQARIQRL 598
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1137 EEELEAERTARAKVEKLRcDLSRELEEISERLEEAggatsVQMELNKKREAEFlkLRRDLEEstlhseataaslRKKhad 1216
Cdd:PRK04863 599 AARAPAWLAAQDALARLR-EQSGEEFEDSQDVTEY-----MQQLLERERELTV--ERDELAA------------RKQ--- 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1217 svaELSEQIDNLQ--------RVKQKLEKEKSEFKLEL-DDVTsnmeqmvkakanleklcrsLEDQAN-EHRTKSEENQR 1286
Cdd:PRK04863 656 ---ALDEEIERLSqpggsedpRLNALAERFGGVLLSEIyDDVS-------------------LEDAPYfSALYGPARHAI 713
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1287 TVNELSSLRAKLQTE------------------NGELSRRLDEKESLVSQMTR-------------GKQTYTQHLEDLKR 1335
Cdd:PRK04863 714 VVPDLSDAAEQLAGLedcpedlyliegdpdsfdDSVFSVEELEKAVVVKIADRqwrysrfpevplfGRAAREKRIEQLRA 793
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1336 QLEE--ETKAKNAL-AHALQSARHD-SDLLREQ----FEEEQEAK-AELQRILSKANSEVAQwrtkyetdaiqrteeLEE 1406
Cdd:PRK04863 794 EREElaERYATLSFdVQKLQRLHQAfSRFIGSHlavaFEADPEAElRQLNRRRVELERALAD---------------HES 858
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1407 AKKKLAQRLQEAEEAVEAVN--AKCSSLEKTKHrLQNEIEDLMVDLERSNAAAAALDKKQRNFDKI-------------L 1471
Cdd:PRK04863 859 QEQQQRSQLEQAKEGLSALNrlLPRLNLLADET-LADRVEEIREQLDEAEEAKRFVQQHGNALAQLepivsvlqsdpeqF 937
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1472 AEWKQKFEESQTELESSQKEARSLsTELFKLKN--AYEESLDHLetfkrenknlqEEISDLTEQLGESGKsihELEKIRK 1549
Cdd:PRK04863 938 EQLKQDYQQAQQTQRDAKQQAFAL-TEVVQRRAhfSYEDAAEML-----------AKNSDLNEKLRQRLE---QAEQERT 1002
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1550 QLDQEKMEIQSALEEAEATL-----EHEEGKILHAQL--ELHQI----KADSERKLAEKDEEMEQAKR-NYQR--MVDTL 1615
Cdd:PRK04863 1003 RAREQLRQAQAQLAQYNQVLaslksSYDAKRQMLQELkqELQDLgvpaDSGAEERARARRDELHARLSaNRSRrnQLEKQ 1082
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1616 QTSLEAETRSRNEALRikkKMEGDLNEMEIQLSQAN-------RQAAEAQKQVKILQ---SYLKDTQIQ----------- 1674
Cdd:PRK04863 1083 LTFCEAEMDNLTKKLR---KLERDYHEMREQVVNAKagwcavlRLVKDNGVERRLHRrelAYLSADELRsmsdkalgalr 1159
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1675 --------LDDALRASEDLKeniaIVERRNTLLQAELEELRslveqtERARklseQELIETSERVQLLhsqntslinqkK 1746
Cdd:PRK04863 1160 lavadnehLRDVLRLSEDPK----RPERKVQFYIAVYQHLR------ERIR----QDIIRTDDPVEAI-----------E 1214
|
1050
....*....|....*...
gi 1072253241 1747 KMESDLSQLQTEMEEAVQ 1764
Cdd:PRK04863 1215 QMEIELSRLTEELTSREQ 1232
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1499-1927 |
1.72e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 66.24 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1499 LFKLKNAYEESLDHLETFKRENKNLQEEISDLTEQLGESGKSIHELEKIRKQLDQEKMEIQSALEEAEAT------LEHE 1572
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELkeeieeLEKE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1573 EGKILHAQLELHQIKADSERKLAEKDEEMEQAKRNYQRMvdtlqTSLEAETRSRNEALRIKKKMEGDLNEMEIQLSQANR 1652
Cdd:PRK03918 247 LESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL-----KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1653 QAAEAQKQVKilqsylkdtqiQLDDALRASEDLKENIAIVERRNTLLQAELEELRSLVEQTERARKLSEQELIETSERVQ 1732
Cdd:PRK03918 322 EINGIEERIK-----------ELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLE 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1733 llhSQNTSLINQKKKMESDLSQLQT---EMEEAVQECRNAEEKAKKAITDAAMMAEELKKEqdtsaHLERMKKNMEQTIK 1809
Cdd:PRK03918 391 ---KELEELEKAKEEIEEEISKITArigELKKEIKELKKAIEELKKAKGKCPVCGRELTEE-----HRKELLEEYTAELK 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1810 DLQQRLDEAEqialkggkKQLQKLEARVRELDNELEAEQK--RNAESVKGMRKYERRIKELTYQT-EEDRKNLARLQDLV 1886
Cdd:PRK03918 463 RIEKELKEIE--------EKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKKYNLEElEKKAEEYEKLKEKL 534
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1072253241 1887 DKLQLKVKTYKRQAEESEEQANtslsKFRKVQHELDEAEER 1927
Cdd:PRK03918 535 IKLKGEIKSLKKELEKLEELKK----KLAELEKKLDELEEE 571
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
881-1686 |
1.87e-10 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 66.51 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 881 LEKSEARRKDLEEKmvslLQEKND-LQLQVQAEQdnLADADERCEQLIKnkiQLEAKLKEQTERLEDEEEMNAELTAKKR 959
Cdd:COG3096 315 LEELSARESDLEQD----YQAASDhLNLVQTALR--QQEKIERYQEDLE---ELTERLEEQEEVVEEAAEQLAEAEARLE 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 960 KLEDECSELKKDIDDL-------------------------------ELTLAKVEKEKHATENKVKNLTEEMAGLD---- 1004
Cdd:COG3096 386 AAEEEVDSLKSQLADYqqaldvqqtraiqyqqavqalekaralcglpDLTPENAEDYLAAFRAKEQQATEEVLELEqkls 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1005 -------------EIIVKLTKEKKAlQEAHQQALDDLQAEEDKVNTLTKAKAkLEQQVDDLEGSLEQEKKIRMDLERVKR 1071
Cdd:COG3096 466 vadaarrqfekayELVCKIAGEVER-SQAWQTARELLRRYRSQQALAQRLQQ-LRAQLAELEQRLRQQQNAERLLEEFCQ 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1072 KLEGDVklsqESLMDLENDKQQLEEKLKkkdfevsQLNTRIEDEQNVCIQLQKKMKELQARIEELEEELEAERTARAKVE 1151
Cdd:COG3096 544 RIGQQL----DAAEELEELLAELEAQLE-------ELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALE 612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1152 KLRcdlsrelEEISERLEEAGGATS-VQMELNKKREAEFL-------KLRRDLEESTLHSEATAASLR-KKHADS----- 1217
Cdd:COG3096 613 RLR-------EQSGEALADSQEVTAaMQQLLEREREATVErdelaarKQALESQIERLSQPGGAEDPRlLALAERlggvl 685
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1218 VAELSEQI---------------------DNLQRVKQKLEK-EKSEFKLEL--------DDVTSNMEQMVKA-------- 1259
Cdd:COG3096 686 LSEIYDDVtledapyfsalygparhaivvPDLSAVKEQLAGlEDCPEDLYLiegdpdsfDDSVFDAEELEDAvvvklsdr 765
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1260 ------------------KANLEKLCRSLEDQANEHRTKS---EENQRTVNELSSL----------------RAKLQTEN 1302
Cdd:COG3096 766 qwrysrfpevplfgraarEKRLEELRAERDELAEQYAKASfdvQKLQRLHQAFSQFvgghlavafapdpeaeLAALRQRR 845
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1303 GELSRRLdekESLVSQMTRGKQTYTQ---HLEDLKRQLEEetkaKNALAHALQSARHDSdlLREQFEEEQEAKAELQRil 1379
Cdd:COG3096 846 SELEREL---AQHRAQEQQLRQQLDQlkeQLQLLNKLLPQ----ANLLADETLADRLEE--LREELDAAQEAQAFIQQ-- 914
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1380 skanseVAQWRTKYET--DAIQRTEELEEAkkkLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQN-EIEDLMVDLERSNAA 1456
Cdd:COG3096 915 ------HGKALAQLEPlvAVLQSDPEQFEQ---LQADYLQAKEQQRRLKQQIFALSEVVQRRPHfSYEDAVGLLGENSDL 985
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1457 AAALdkKQRnfdkiLAEWKQKFEESQTELESSQKEARSLSTELFKLKNAYEESLDHLETFKRENKNLQEEISDLTEQLGE 1536
Cdd:COG3096 986 NEKL--RAR-----LEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAEAEERAR 1058
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1537 SGksihelekiRKQLDQEKMEIQSALEEAEATLEHEEGKILHAQLELHQikadSERKLAEKDEEMEQAKRNY---QRMVd 1613
Cdd:COG3096 1059 IR---------RDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRK----AERDYKQEREQVVQAKAGWcavLRLA- 1124
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1072253241 1614 tlqtsleaetRSRNealrikkkMEGDLNEMEIQLSQANRQAAEAQKQVKILQSYLKDTQiQLDDALRASEDLK 1686
Cdd:COG3096 1125 ----------RDND--------VERRLHRRELAYLSADELRSMSDKALGALRLAVADNE-HLRDALRLSEDPR 1178
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1258-1723 |
1.98e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.94 E-value: 1.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1258 KAKANLEKLcRSLEDQANEHRTKSEENQRTVNELSSLRAKLQtengELSRRLDEKESLVSQMTRGKQTYT--QHLEDLKR 1335
Cdd:COG4717 65 KPELNLKEL-KELEEELKEAEEKEEEYAELQEELEELEEELE----ELEAELEELREELEKLEKLLQLLPlyQELEALEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1336 QLEEETKAKNALAHALQSARHDSDLLREQFEEEQEAKAELQRILSKANSEVAQwrtkYETDAIQRTEELEEAKKKLAQRL 1415
Cdd:COG4717 140 ELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE----ELQDLAEELEELQQRLAELEEEL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1416 QEAEEAVEAVNAKCSSLEKTK--HRLQNEIEDLMVDLERSNAAAAALDKKQRNFDKILAEWKQKFEESQTELessqkear 1493
Cdd:COG4717 216 EEAQEELEELEEELEQLENELeaAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLA-------- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1494 SLSTELFKLKNAYEESLDHLETFKRENKNLQEEISDLTEQLG-ESGKSIHELEKIRKQLDQEKmEIQSALEEAEATLEHE 1572
Cdd:COG4717 288 LLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGlPPDLSPEELLELLDRIEELQ-ELLREAEELEEELQLE 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1573 EGKILHAQLeLHQIKADSERKLAEKDEEMEQAKRNYQRmVDTLQTSLEAETRSRNEALRikkkmEGDLNEMEIQLSQANR 1652
Cdd:COG4717 367 ELEQEIAAL-LAEAGVEDEEELRAALEQAEEYQELKEE-LEELEEQLEELLGELEELLE-----ALDEEELEEELEELEE 439
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1072253241 1653 QAAEAQKQVKILQSYLKDTQIQLDDALRASE--DLKENIAIVERRNTLLQAELEELRSLVEQTERARKLSEQE 1723
Cdd:COG4717 440 ELEELEEELEELREELAELEAELEQLEEDGElaELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1229-1914 |
2.42e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 65.81 E-value: 2.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1229 QRVKQKLEKEKSEFK---LELDDVTSNMEQMVKAKANLEKLCRSLEDQANEHRTKSEENQRTVNELSSLRAKLqteNGEL 1305
Cdd:TIGR04523 36 KQLEKKLKTIKNELKnkeKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKI---NSEI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1306 SRRLDEKESLVSQMTRGKQTYTQHLEDLKRQLEEETKAKNALAhalqSARHDSDLLREQFEEEQEAKAELQRILSKANSE 1385
Cdd:TIGR04523 113 KNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELE----KLNNKYNDLKKQKEELENELNLLEKEKLNIQKN 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1386 VAQWRTKYetdaiQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAALDKKQR 1465
Cdd:TIGR04523 189 IDKIKNKL-----LKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQN 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1466 NFDKILAEWKQKFEESQTELESSQKEARSLSTELFKLKNAYEESLDhlETFKRENKNLQEEISDLTEQLGESGKSIHELE 1545
Cdd:TIGR04523 264 KIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWN--KELKSELKNQEKKLEEIQNQISQNNKIISQLN 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1546 KIRKQLDQEKMEIQSALEEAEatleheegkilhaqlelhqikadseRKLAEKDEEMEQAKRNYQRMVDTLQtSLEAETRS 1625
Cdd:TIGR04523 342 EQISQLKKELTNSESENSEKQ-------------------------RELEEKQNEIEKLKKENQSYKQEIK-NLESQIND 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1626 RNEALRIKKKMEgdlNEMEIQLSQANRQAAEAQKQVKILQSYLKDTQIQLDDALRASEDLKENIAIVERRNTLLQAELEE 1705
Cdd:TIGR04523 396 LESKIQNQEKLN---QQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1706 LRSLVEQTERARKLSEQELIETSERVQLLHSQNTSLINQKKKMESDLSQLQTEMEEAVQECRNAEEKAKKAITDAAMMAE 1785
Cdd:TIGR04523 473 LSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDF 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1786 ELKKEQdtsahLERMKKNMEQTIKDLQQrldeaEQIALKGGKKQLQklearvrELDNELEAEQKrnaESVKGMRKYERRI 1865
Cdd:TIGR04523 553 ELKKEN-----LEKEIDEKNKEIEELKQ-----TQKSLKKKQEEKQ-------ELIDQKEKEKK---DLIKEIEEKEKKI 612
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1072253241 1866 KELTYQTEEDRKNLARLQDLVDKLQLKVKTYKRQAEESEEQANTSLSKF 1914
Cdd:TIGR04523 613 SSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKW 661
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1402-1936 |
2.47e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.09 E-value: 2.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1402 EELEEAKKKLaQRLQEAEEAVEAVNAKCSSLEKTKHRLQ-NEIEDLMVDLERSNAAAAALDKKQRNFDKILAEWKQKFEE 1480
Cdd:COG4913 235 DDLERAHEAL-EDAREQIELLEPIRELAERYAAARERLAeLEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1481 SQTELESSQKEARSLSTELFKL----KNAYEESLDHLETFKRENKNLQEEISDLTEQLGESGK-SIHELEKIRKQLDQEK 1555
Cdd:COG4913 314 LEARLDALREELDELEAQIRGNggdrLEQLEREIERLERELEERERRRARLEALLAALGLPLPaSAEEFAALRAEAAALL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1556 MEIQSALEEAEAtleheegkilhAQLELHQIKADSERKLAEKDEE---MEQAKRNYQRMVDTLQTSLEAETRSRNEALRI 1632
Cdd:COG4913 394 EALEEELEALEE-----------ALAEAEAALRDLRRELRELEAEiasLERRKSNIPARLLALRDALAEALGLDEAELPF 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1633 KkkmeGDLneMEIQLSQAN-RQAAEAqkqvkilqsYLKDTQIQLddaLRASEDLKENIAIVERRNtllqaeleeLRSLVe 1711
Cdd:COG4913 463 V----GEL--IEVRPEEERwRGAIER---------VLGGFALTL---LVPPEHYAAALRWVNRLH---------LRGRL- 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1712 QTERARKLSEQELIETSERVQLLHsqntslinqkkKMESDLSQLQTEMEEAVQE------CRNAEE--KAKKAITDAAMM 1783
Cdd:COG4913 515 VYERVRTGLPDPERPRLDPDSLAG-----------KLDFKPHPFRAWLEAELGRrfdyvcVDSPEElrRHPRAITRAGQV 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1784 AEELKK-EQDTSAHLER---MKKNMEQTIKDLQQRLDEAEQiALKGGKKQLQKLEARVRELDNELEAEQK--RNAESVKG 1857
Cdd:COG4913 584 KGNGTRhEKDDRRRIRSryvLGFDNRAKLAALEAELAELEE-ELAEAEERLEALEAELDALQERREALQRlaEYSWDEID 662
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1072253241 1858 MRKYERRIKELtyqtEEDRKNLARLQDLVDKLQLKVKTYKRQAEESEEQANTSLSKFRKVQHELDEAEERADIAESQVN 1936
Cdd:COG4913 663 VASAEREIAEL----EAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE 737
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
870-1444 |
3.51e-10 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 65.13 E-value: 3.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 870 MKEEFQKLKEaLEKSEARRKDLEEKMVSLLQekndlqLQVQAEQDNLADADERCEQLIKNKIQLEAKLKEQTERLEDEEE 949
Cdd:pfam05483 217 LKEDHEKIQH-LEEEYKKEINDKEKQVSLLL------IQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 950 MNAELTakkrkledecselkKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIVKLTKEKKALQEAHQQALDDLQ 1029
Cdd:pfam05483 290 KKDHLT--------------KELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1030 AEEDKVNTLTKAkaklEQQvdDLEGSLEQEKKIRMDLERVKRKLEGDVKLSQESLMDLENDKQQLEEKLKKKDfEVSQLN 1109
Cdd:pfam05483 356 ATTCSLEELLRT----EQQ--RLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLD-EKKQFE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1110 TRIED----EQNVCIQLQKKMKELQARIEELEEELEAERTARAKVEKLRCDLSRELEEISERLEEAGGATSVQMELNKKR 1185
Cdd:pfam05483 429 KIAEElkgkEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEA 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1186 EAEFLKLRRDLEESTLHSEATAASLrkKHADSVAELSEQI-DNLQRVKQKLEKEKSEFKLELDDVTSNMEQMVKAKANLE 1264
Cdd:pfam05483 509 SDMTLELKKHQEDIINCKKQEERML--KQIENLEEKEMNLrDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKE 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1265 KLCRSLEDQANEHRTKSEENQRTVNEL----SSLRAKLQTENGELSRRLDEKESLVSQMTRGKQTYTQHLEDLKRQLEEE 1340
Cdd:pfam05483 587 KQMKILENKCNNLKKQIENKNKNIEELhqenKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDK 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1341 TKAKNALAHALQSARHDSDllrEQFEEEQEAKAELQRILSKANSEVAQWRTKYETDAIQRTEELEEAKkklaQRLQEAEE 1420
Cdd:pfam05483 667 KISEEKLLEEVEKAKAIAD---EAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYK----NKEQEQSS 739
|
570 580
....*....|....*....|....
gi 1072253241 1421 AVEAVNAKCSSLEKTKHRLQNEIE 1444
Cdd:pfam05483 740 AKAALEIELSNIKAELLSLKKQLE 763
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
859-1061 |
4.14e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 64.01 E-value: 4.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 859 KSAETEKEMQTMKEEFQKLKEALEKSEARRKDLEEKMVSLLQEKNDLQLQVQAEQDNLADADERCEQLIKNKIQLEAKLK 938
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 939 EQTERL----------------------EDEEEMNAELTAKKRKLEdecsELKKDIDDLELTLAKVEKEKHATENKVKNL 996
Cdd:COG4942 101 AQKEELaellralyrlgrqpplalllspEDFLDAVRRLQYLKYLAP----ARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1072253241 997 TEEMAGLDEIIVKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKK 1061
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
932-1361 |
4.76e-10 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 64.15 E-value: 4.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 932 QLEAKLKEQTERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIVKLT 1011
Cdd:pfam07888 35 RLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1012 KEKKALQEAHQQALDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKIRMDLERVKRKLEGDVKLSQESLMDLENDK 1091
Cdd:pfam07888 115 EEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1092 QQLEEKLKKKDFEVSQLNTRIEDEQNVCIQLQKKMKELQARIEELEEELEAERTARAKVEKLRCDLSreleeiserlEEA 1171
Cdd:pfam07888 195 QELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELS----------SMA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1172 GGATSVQMELNKKR-EAEFLKLRrdLEESTLH---SEATAASLRKKHADSVAELSEQIDNLQRVKQKLEKEKSEfkleld 1247
Cdd:pfam07888 265 AQRDRTQAELHQARlQAAQLTLQ--LADASLAlreGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQE------ 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1248 dvtsnmEQMVKAKANLEklcrsLEDQANEHRTKSEENQRtvnELSSLRAKLQTENgelsrrlDEKESLVSQmtrgKQTYT 1327
Cdd:pfam07888 337 ------ERMEREKLEVE-----LGREKDCNRVQLSESRR---ELQELKASLRVAQ-------KEKEQLQAE----KQELL 391
|
410 420 430
....*....|....*....|....*....|....
gi 1072253241 1328 QHLEDLKRQLEEETKAKNALAHALQSARHDSDLL 1361
Cdd:pfam07888 392 EYIRQLEQRLETVADAKWSEAALTSTERPDSPLS 425
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
887-1950 |
6.19e-10 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 65.07 E-value: 6.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 887 RRKDLEEKMVSLLQEKNDlqlQVQAEQDNLADADERCEQLIKNKIqlEAKLKEQTERLEDEEEMNAELTAKKRKLEDECS 966
Cdd:TIGR01612 501 RMKDFKDIIDFMELYKPD---EVPSKNIIGFDIDQNIKAKLYKEI--EAGLKESYELAKNWKKLIHEIKKELEEENEDSI 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 967 ELKKDIDDLELTLAKVEKE-------KHATENKVKNLTEEmaglDEIIVKLTKEKKALqEAHQQALDDL------QAEED 1033
Cdd:TIGR01612 576 HLEKEIKDLFDKYLEIDDEiiyinklKLELKEKIKNISDK----NEYIKKAIDLKKII-ENNNAYIDELakispyQVPEH 650
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1034 KVNT---LTKAKAKLEQ-QVDDLE------GSLEQEKKI-----RMDLERVKRKLEGDVKLSQE--------SLMDLEND 1090
Cdd:TIGR01612 651 LKNKdkiYSTIKSELSKiYEDDIDalynelSSIVKENAIdntedKAKLDDLKSKIDKEYDKIQNmetatvelHLSNIENK 730
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1091 KQQLEE---KLKKKDF-EVS-QLNTRIEDEQNvciqlqkKMKELQARIEELEEELEAERTARAKVEKLRCDLSRELEEIS 1165
Cdd:TIGR01612 731 KNELLDiivEIKKHIHgEINkDLNKILEDFKN-------KEKELSNKINDYAKEKDELNKYKSKISEIKNHYNDQINIDN 803
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1166 ERLEEAGGATSVQMELNKK---REAEFLKL---RRDLEESTLHSEATAASLRKKHADSVAELSEQIDNL-QRVKQKLEKE 1238
Cdd:TIGR01612 804 IKDEDAKQNYDKSKEYIKTisiKEDEIFKIineMKFMKDDFLNKVDKFINFENNCKEKIDSEHEQFAELtNKIKAEISDD 883
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1239 K--------SEFKLELDDVTSNMEQMVKAKANLE------KLCRSLEDQANEHRTKseenQRTVNELSSLRAKLQTENGE 1304
Cdd:TIGR01612 884 KlndyekkfNDSKSLINEINKSIEEEYQNINTLKkvdeyiKICENTKESIEKFHNK----QNILKEILNKNIDTIKESNL 959
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1305 LSRRLDEK--ESLVSQMTRGKQTYTQ-HLEDLKRQLEEETKAKNALAHALqsARHDSDLLREQFEEEQEAKAELQRILSK 1381
Cdd:TIGR01612 960 IEKSYKDKfdNTLIDKINELDKAFKDaSLNDYEAKNNELIKYFNDLKANL--GKNKENMLYHQFDEKEKATNDIEQKIED 1037
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1382 ANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQeaEEAVEAVNAKCSSLEKTKHRLQ----------------NEIED 1445
Cdd:TIGR01612 1038 ANKNIPNIEIAIHTSIYNIIDEIEKEIGKNIELLN--KEILEEAEINITNFNEIKEKLKhynfddfgkeenikyaDEINK 1115
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1446 LMVDLErsnaaaaALDKKQRNFDKILAEWKQKFEESQTELESSQKEARSLSTELFKLKN--AYEESLDHLETFKRENKNL 1523
Cdd:TIGR01612 1116 IKDDIK-------NLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDVADKAISNDDpeEIEKKIENIVTKIDKKKNI 1188
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1524 QEEISDLTEQLGESGKSIHELEKIR---------------KQLDQEKMEIQSALEEAEATLEheegkilhaqlELHQIKA 1588
Cdd:TIGR01612 1189 YDEIKKLLNEIAEIEKDKTSLEEVKginlsygknlgklflEKIDEEKKKSEHMIKAMEAYIE-----------DLDEIKE 1257
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1589 DSERKLAEKDEEMEQAKR---------NYQRMVDTLQTSLEAETRSRNEALRIKKKM--EGDLNEMEIQLsqaNRQAAEA 1657
Cdd:TIGR01612 1258 KSPEIENEMGIEMDIKAEmetfnishdDDKDHHIISKKHDENISDIREKSLKIIEDFseESDINDIKKEL---QKNLLDA 1334
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1658 QKQVKILQSYLKDTQ-----IQLDDALRASEDLKENIAIVERRNTLLQAE----------------LEELRSLVEQTERA 1716
Cdd:TIGR01612 1335 QKHNSDINLYLNEIAniyniLKLNKIKKIIDEVKEYTKEIEENNKNIKDEldkseklikkikddinLEECKSKIESTLDD 1414
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1717 RKLSE--QELIETSERVQLLHSQNTSLINQKKKMESDLSQLQTEMEEAVQECRN-AEEKAKKAITDAAMMAEELKKEQDT 1793
Cdd:TIGR01612 1415 KDIDEciKKIKELKNHILSEESNIDTYFKNADENNENVLLLFKNIEMADNKSQHiLKIKKDNATNDHDFNINELKEHIDK 1494
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1794 S-----------AHLERMKKNMEQTIKDLQQRLDEAEQIALKGG----KKQLQKLEARVRELDNELEAEQKRNAESVKGM 1858
Cdd:TIGR01612 1495 SkgckdeadknaKAIEKNKELFEQYKKDVTELLNKYSALAIKNKfaktKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEI 1574
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1859 RKYERRIKELTYQTEEDRKNLARLQDLVDKLQ---LKVKTYKRQAE------ESEEQANTSLSkFRKVQHELDEAEERAD 1929
Cdd:TIGR01612 1575 KKEKFRIEDDAAKNDKSNKAAIDIQLSLENFEnkfLKISDIKKKINdclketESIEKKISSFS-IDSQDTELKENGDNLN 1653
|
1210 1220
....*....|....*....|.
gi 1072253241 1930 IAESQVNKLRAKSRDVSTKKS 1950
Cdd:TIGR01612 1654 SLQEFLESLKDQKKNIEDKKK 1674
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1122-1813 |
8.62e-10 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 64.07 E-value: 8.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1122 LQKKMKELQARIEELEEE-LEAERTARAKVEKLRCD--LSRELEEISERLEEAGGATSVQMELN---KKREAEFLKLRrd 1195
Cdd:pfam10174 135 LRKTLEEMELRIETQKQTlGARDESIKKLLEMLQSKglPKKSGEEDWERTRRIAEAEMQLGHLEvllDQKEKENIHLR-- 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1196 lEESTLHSEATAASLRKKHADSVAELSE-QIDNLQRVKQKLEKE----KSEFKLELDDVTSNMEQMVKAKANlEKLCRSL 1270
Cdd:pfam10174 213 -EELHRRNQLQPDPAKTKALQTVIEMKDtKISSLERNIRDLEDEvqmlKTNGLLHTEDREEEIKQMEVYKSH-SKFMKNK 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1271 EDQANEHRTKSEenqrtvNELSSLRAKLQTENGELSrrlDEKeslvsqmtrgkqtytQHLEDLKRQLeeetKAKNALAHA 1350
Cdd:pfam10174 291 IDQLKQELSKKE------SELLALQTKLETLTNQNS---DCK---------------QHIEVLKESL----TAKEQRAAI 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1351 LQSarhDSDLLREQFEEEQeakaelqRILSKansevaqwrtkyETDAIQRteeLEEAKKKLAQRLQEAEEAVEAVNAKCS 1430
Cdd:pfam10174 343 LQT---EVDALRLRLEEKE-------SFLNK------------KTKQLQD---LTEEKSTLAGEIRDLKDMLDVKERKIN 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1431 SLEKTKHRLQNEIEDLMVDLERSNAAAAALDKKQRNFDKILAEWKQKFEESQTELESSQKEARSLSTELfklknayeesL 1510
Cdd:pfam10174 398 VLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRER----------L 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1511 DHLETFKRENKNLQEEISDLTEQLGESGKSIHELEKIRKQLDQEKMEIQSALEEAEATLEH--EEGKILHAQLELHQIKA 1588
Cdd:pfam10174 468 EELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQkkEECSKLENQLKKAHNAE 547
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1589 DSERKLAEKDEEMEQAKRNYQRMVD---TLQTSLEAETRSRNEALRIKKKMEGDLNEMEIQLSQANRQAAEAQKQVKILQ 1665
Cdd:pfam10174 548 EAVRTNPEINDRIRLLEQEVARYKEesgKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQ 627
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1666 SYLKDTQIQ-LDDALRASEDLKENIAiverrntllQAELEELRSLVEQTerarklsEQELIETSERV----QLLHSQNTS 1740
Cdd:pfam10174 628 QEMKKKGAQlLEEARRREDNLADNSQ---------QLQLEELMGALEKT-------RQELDATKARLsstqQSLAEKDGH 691
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1072253241 1741 LIN----QKKKMESDLSQLQTEMEEAVqecrnAEEKAKKAITDaaMMAEELKKEQDTSAHLERMKKNMEQTIKDLQQ 1813
Cdd:pfam10174 692 LTNlraeRRKQLEEILEMKQEALLAAI-----SEKDANIALLE--LSSSKKKKTQEEVMALKREKDRLVHQLKQQTQ 761
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1633-1854 |
8.77e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.86 E-value: 8.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1633 KKKMEGDLNEMEIQLSQANRQAAEAQKQVKILQSYLKDTQIQLDDALRASEDLKENIAIVERRNTLLQAELEELR-SLVE 1711
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRaELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1712 QTER-ARKLSEQELIETSERVQLLHSQNTS--LINQKKKMESDLSQLQTEMEEAVQECRNAEEKAKKAITDAAMMAEELK 1788
Cdd:COG4942 102 QKEElAELLRALYRLGRQPPLALLLSPEDFldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1072253241 1789 KEQDTSAHLERMKKNMEQTIKDLQQRLDEAEQiALKGGKKQLQKLEARVRELDNELEAEQKRNAES 1854
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAELAA-ELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1400-1941 |
1.06e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 63.50 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1400 RTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMvdlERSNAAAAALDKKQRNFDKILAEWKQKFE 1479
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILE---QQIKDLNDKLKKNKDKINKLNSDLSKINS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1480 ESQTELESSQKearsLSTELFKLKNAYEESLDHLETFKRENKNLQEEISDLTEQLGESGKSIHELEKIRKQLDQEKMEIQ 1559
Cdd:TIGR04523 111 EIKNDKEQKNK----LEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1560 SALEEA---EATLEHE--------------EGKILHAQLELHQIKADSERKLAEKDEEMEQAKRNYQRMVDTLQ------ 1616
Cdd:TIGR04523 187 KNIDKIknkLLKLELLlsnlkkkiqknkslESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDeqnkik 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1617 TSLEAETRSRNEALRIKKKMEGDLNEMEIQLSQANRQAA-----EAQKQVKILQSYLKDTQIQLDDALRASEDLKENIAI 1691
Cdd:TIGR04523 267 KQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEqdwnkELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQ 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1692 VERRNTLLQAELEELRSLVEQTERARKLSEQELIETSERVQLLHSQNTSLINQKKKMESDLSQLQTEMEEAVQECRNAEE 1771
Cdd:TIGR04523 347 LKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1772 KAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQQRLD-------------EAEQIALKGGKKQLQKLEARVR 1838
Cdd:TIGR04523 427 EIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKvlsrsinkikqnlEQKQKELKSKEKELKKLNEEKK 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1839 ELDNELEAEQKRNAESVKGMRKYERRIKELTYQTEEDRKNLARLQDLVDKLQL-KVKTYKRQAEESEEQANTSLSKfrkv 1917
Cdd:TIGR04523 507 ELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLeKEIDEKNKEIEELKQTQKSLKK---- 582
|
570 580
....*....|....*....|....
gi 1072253241 1918 qhELDEAEERADIAESQVNKLRAK 1941
Cdd:TIGR04523 583 --KQEEKQELIDQKEKEKKDLIKE 604
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
853-1289 |
1.06e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.01 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 853 KIKPLLKSAETEKEMQTMKEEFQKLKEALEKSEARRKDLEEKMVSLLQEKNDLQLQVQAEQDNLADADERCEQLIKNKIQ 932
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYE 1602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 933 LEAKLKEQTERLEDEEEMNAEltakkrkledecsELKKDiddlELTLAKVEKEKHATENKVKNLTEEMAGLDEIIVKLTK 1012
Cdd:PTZ00121 1603 EEKKMKAEEAKKAEEAKIKAE-------------ELKKA----EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAE 1665
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1013 EKKALQEAHQQALDDLQAEEDkvntltkaKAKLEQQVDDLEGSLEQEKKIRMDLERVKRKLEGDVKLSQESLMDLENDKQ 1092
Cdd:PTZ00121 1666 EAKKAEEDKKKAEEAKKAEED--------EKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKK 1737
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1093 QLEEKLKKKDfevsqlNTRIEDEQNVCIQLQKKMKELQARIEELEEELEAERTARAKVEKLRCDLSRELEEI---SERLE 1169
Cdd:PTZ00121 1738 EAEEDKKKAE------EAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIfdnFANII 1811
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1170 EAGGATSVQMELNKKREAEFLKLRRDLEESTLHS-------EATAASLRKKHADSVAELSEQIDNLQRVKQKLEKEKSEF 1242
Cdd:PTZ00121 1812 EGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEadafekhKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIE 1891
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1072253241 1243 KLELDDVTSNMEQMVKAKANLEKLCRSLEDQANEHRTKSEENQRTVN 1289
Cdd:PTZ00121 1892 KIDKDDIEREIPNNNMAGKNNDIIDDKLDKDEYIKRDAEETREEIIK 1938
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
910-1549 |
1.52e-09 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 63.38 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 910 QAEQDNLADADERCEQLIKNKI----QLEA---KLKEQTERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKV 982
Cdd:PRK01156 137 QGEMDSLISGDPAQRKKILDEIleinSLERnydKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSIT 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 983 EKEKHATENKVKNLTEEMAGLDEiivkltkekkalqeahqqALDDLQAEEDKVNTLTKAKAKLEqqvDDLEGSLEQEKKI 1062
Cdd:PRK01156 217 LKEIERLSIEYNNAMDDYNNLKS------------------ALNELSSLEDMKNRYESEIKTAE---SDLSMELEKNNYY 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1063 RMDLERVKRKLEGDVKLSQESLMDLENDKQQLEEKlkkkdfevSQLNTRIEDEQNVCIQLQKKMKELQArieeleeelea 1142
Cdd:PRK01156 276 KELEERHMKIINDPVYKNRNYINDYFKYKNDIENK--------KQILSNIDAEINKYHAIIKKLSVLQK----------- 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1143 ERTARAKVEKLRCDLSRELEEISERLEEAGGATSVQMELNKKREAEFLKLRR---DLEESTLHSEATAASLRKKHadsvA 1219
Cdd:PRK01156 337 DYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERmsaFISEILKIQEIDPDAIKKEL----N 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1220 ELSEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEqMVKAKANLEKLCRSLEDQANEHRTK--SEENQRTVNELSSLRAK 1297
Cdd:PRK01156 413 EINVKLQDISSKVSSLNQRIRALRENLDELSRNME-MLNGQSVCPVCGTTLGEEKSNHIINhyNEKKSRLEEKIREIEIE 491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1298 LQTENGELSRRLDEKESLVSQMTRGKQTYTQHLEDLKRQLEEETKAKNALAHALQSARHDSDLLREQFEEEQEAKAElqr 1377
Cdd:PRK01156 492 VKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKRT--- 568
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1378 ILSKANSEvaqwRTKYETDAIQ-RTEELEEAKKKLAQRLQEAEEAVEAVNakcSSLEKTKHRLQNEIEDL---MVDLERS 1453
Cdd:PRK01156 569 SWLNALAV----ISLIDIETNRsRSNEIKKQLNDLESRLQEIEIGFPDDK---SYIDKSIREIENEANNLnnkYNEIQEN 641
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1454 NAAAAALDKKQRNFDKILAEwKQKFEESQTELESsqkEARSLSTELFKLKNAYEESLDHLETFKRENKNLQEEISDLTEQ 1533
Cdd:PRK01156 642 KILIEKLRGKIDNYKKQIAE-IDSIIPDLKEITS---RINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDR 717
|
650
....*....|....*.
gi 1072253241 1534 LGESGKSIHELEKIRK 1549
Cdd:PRK01156 718 INDINETLESMKKIKK 733
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
49-91 |
1.82e-09 |
|
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the N-terminus of many but not all myosins. The function of this domain is unknown.
Pssm-ID: 460670 Cd Length: 45 Bit Score: 54.74 E-value: 1.82e-09
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1072253241 49 DMKKDIFVPDDTEEYVKAKVTSREGDNVTAETEHGKKVNVKDS 91
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVETEDGKTVTVKKD 43
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
876-1576 |
2.24e-09 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 62.93 E-value: 2.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 876 KLKEALEKSEARRKDLEEKMVSLLQEKNDLQLQVQAEQDnladadeRCEQLIKNKIQLEAKLKEQTERLEDEEEMNAELT 955
Cdd:pfam12128 183 KIAKAMHSKEGKFRDVKSMIVAILEDDGVVPPKSRLNRQ-------QVEHWIRDIQAIAGIMKIRPEFTKLQQEFNTLES 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 956 AkkrklEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEM-AGLDEIIVKLTKEKKALQEAHQQALDDLQAEEDK 1034
Cdd:pfam12128 256 A-----ELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLdDQWKEKRDELNGELSAADAAVAKDRSELEALEDQ 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1035 vntltkAKAKLEQQVDDLEGSLEQEKKIRMDLERVKRKLEGdvklsqesLMDLENDKQQLEEKLKKKdfEVSQLNTRIED 1114
Cdd:pfam12128 331 ------HGAFLDADIETAAADQEQLPSWQSELENLEERLKA--------LTGKHQDVTAKYNRRRSK--IKEQNNRDIAG 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1115 EQnvciQLQKKMKELQARIEELEEELEAERTA--RAKVEKLRCDLSRELEEISERLEEAGG------ATSVQMELNKKRE 1186
Cdd:pfam12128 395 IK----DKLAKIREARDRQLAVAEDDLQALESelREQLEAGKLEFNEEEYRLKSRLGELKLrlnqatATPELLLQLENFD 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1187 AEFLKLRRDLEESTLHSEATAASLRK----------KHADSVAELSEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQM 1256
Cdd:pfam12128 471 ERIERAREEQEAANAEVERLQSELRQarkrrdqaseALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEAPDWEQS 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1257 VKAKANLEKLCRS-LEDQANEHRTKSEENQRTVN----------------ELSSLRAKLQTENGELSRRLDEKESLVSQ- 1318
Cdd:pfam12128 551 IGKVISPELLHRTdLDPEVWDGSVGGELNLYGVKldlkridvpewaaseeELRERLDKAEEALQSAREKQAAAEEQLVQa 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1319 ----------MTRGKQTYTQHLEDLKRQLEEETKAKNALAHALQSARHDSDLLREQFEEEQEA-KAELQRILSKANSEVA 1387
Cdd:pfam12128 631 ngelekasreETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQlDKKHQAWLEEQKEQKR 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1388 QWRTKYEtdaiQRTEELEEAKK-KLAQRLQEAEEAVEAVNAKCSSLEKTKHR--------------LQNEIEDLMVDLER 1452
Cdd:pfam12128 711 EARTEKQ----AYWQVVEGALDaQLALLKAAIAARRSGAKAELKALETWYKRdlaslgvdpdviakLKREIRTLERKIER 786
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1453 ---SNAAAAALDKKQR--------NFDKILAEWKQKFEESQTELESSQKEARSLSTELFKLKNAYEESLDHLETFKRENK 1521
Cdd:pfam12128 787 iavRRQEVLRYFDWYQetwlqrrpRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLR 866
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 1072253241 1522 NLQEEISDLTEQlGESGKSIHELEKIRKQLDQEKMEIQSALEEAEATLEHEEGKI 1576
Cdd:pfam12128 867 CEMSKLATLKED-ANSEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHFKNVI 920
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1254-1902 |
2.35e-09 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 62.90 E-value: 2.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1254 EQMVKAKANLEKLcrslEDQANEHRTKSEENQRTVNElsSLRAKLQTENGELSRRLDEKESLvSQMTRGKQTYTQHLEDL 1333
Cdd:PRK10246 191 EQHKSARTELEKL----QAQASGVALLTPEQVQSLTA--SLQVLTDEEKQLLTAQQQQQQSL-NWLTRLDELQQEASRRQ 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1334 KRQL---EEETKAKNALAhALQSArHDSDLLREQFEEEQEAKAELQRILSKANS------EVAQWRTKYETDAIQRTEEL 1404
Cdd:PRK10246 264 QALQqalAAEEKAQPQLA-ALSLA-QPARQLRPHWERIQEQSAALAHTRQQIEEvntrlqSTMALRARIRHHAAKQSAEL 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1405 EEAKKKLAQRLQEAE------EAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNA------------AAAALDK--KQ 1464
Cdd:PRK10246 342 QAQQQSLNTWLAEHDrfrqwnNELAGWRAQFSQQTSDREQLRQWQQQLTHAEQKLNAlpaitltltadeVAAALAQhaEQ 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1465 RNFDKILAEWKQKFEESQTELESSQKEARSLSTELFKLKnayeeslDHLETFKRENKNLQEEISDLtEQLGESGKSIHEL 1544
Cdd:PRK10246 422 RPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRN-------AALNEMRQRYKEKTQQLADV-KTICEQEARIKDL 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1545 EKIRKQLDQEK------------MEIQSALE-----------EAEATLEHEEGKILHAQLE--LHQIKADSE--RKLAEK 1597
Cdd:PRK10246 494 EAQRAQLQAGQpcplcgstshpaVEAYQALEpgvnqsrldalEKEVKKLGEEGAALRGQLDalTKQLQRDESeaQSLRQE 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1598 DEEMEQAkrnYQRMVDTLQTSLEaetrsrnealrIKKKMEGDLNEME------IQLSQA---NRQAAEAQKQVKILQSYL 1668
Cdd:PRK10246 574 EQALTQQ---WQAVCASLNITLQ-----------PQDDIQPWLDAQEeherqlRLLSQRhelQGQIAAHNQQIIQYQQQI 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1669 KDTQIQLDDALRA-----SEDLKENIAIVER------------RNTLLQAELEELRSLVE-------QTERARKLSEQEL 1724
Cdd:PRK10246 640 EQRQQQLLTALAGyaltlPQEDEEASWLATRqqeaqswqqrqnELTALQNRIQQLTPLLEtlpqsddLPHSEETVALDNW 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1725 IETSERVQLLHSQNTSLINQKKKMESDLSQLQTEMEEAVQECRNAEEKAKKAitdaAMMAEElkkeqdTSAHLERMKKNM 1804
Cdd:PRK10246 720 RQVHEQCLSLHSQLQTLQQQDVLEAQRLQKAQAQFDTALQASVFDDQQAFLA----ALLDEE------TLTQLEQLKQNL 789
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1805 EQTIKDLQQRLDEAEQialkggkKQLQKLEARVRELDNELEAE--QKRNAESVKGMRKYERRIKELTYQTEEDRKNLARL 1882
Cdd:PRK10246 790 ENQRQQAQTLVTQTAQ-------ALAQHQQHRPDGLDLTVTVEqiQQELAQLAQQLRENTTRQGEIRQQLKQDADNRQQQ 862
|
730 740
....*....|....*....|
gi 1072253241 1883 QDLVdklqLKVKTYKRQAEE 1902
Cdd:PRK10246 863 QALM----QQIAQATQQVED 878
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
859-1321 |
2.94e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 62.35 E-value: 2.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 859 KSAETEKEMQTMKEEFQKLKEALEKsearrkdleekmvsLLQEKNDLQLQVQAEQDNLADADercEQLIKNKIQLEAKLK 938
Cdd:TIGR04523 212 KNKSLESQISELKKQNNQLKDNIEK--------------KQQEINEKTTEISNTQTQLNQLK---DEQNKIKKQLSEKQK 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 939 EqterLEDEEEMNAELTAKKRKLEDECSELKKD-----IDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIVKLTKE 1013
Cdd:TIGR04523 275 E----LEQNNKKIKELEKQLNQLKSEISDLNNQkeqdwNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKE 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1014 KKALQEAHQQALDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEqekkirmDLERvkrklegdvklsqeSLMDLENDKQQ 1093
Cdd:TIGR04523 351 LTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQIN-------DLES--------------KIQNQEKLNQQ 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1094 LEEKLKKKDFEVSQLNTRIEDEQNVCIQLQKKMKELQARIEELEEELEAERTARAKVEKLRCDLSRELEEISERLEEagg 1173
Cdd:TIGR04523 410 KDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQ--- 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1174 atsVQMELNKKrEAEFLKLRRDLEESTlhseataaslrkkhaDSVAELSEQIDNLQRVKQKLEKEKSEFKLELDDVTSNM 1253
Cdd:TIGR04523 487 ---KQKELKSK-EKELKKLNEEKKELE---------------EKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDEL 547
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1254 EQM--VKAKANLEKLCRSLEDQANEHRTKSEENQRTVNELSSLRAKLQTENGELSRRLDEKESLVSQMTR 1321
Cdd:TIGR04523 548 NKDdfELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEK 617
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
858-1095 |
3.30e-09 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 61.96 E-value: 3.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 858 LKSAETEKEMQTMKEEFQKLKEALEKSEARRKDLEEKMVSLlqeknDLQLQVQAEQDNLADADERCEQLIKNKIQLEAKL 937
Cdd:COG3206 168 LRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLV-----DLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 938 KEQTERLEDEEEMNAELTAkkrklEDECSELKKDIDDLELTLAkvEKEKHATEN--KVKNLTEEMAGLdeiivkltkeKK 1015
Cdd:COG3206 243 AALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAELEAELA--ELSARYTPNhpDVIALRAQIAAL----------RA 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1016 ALQEAHQQALDDLQAEedkVNTLTKAKAKLEQQVDDLEGSLEQEKKIRMDLERVKRklegDVKLSQESLMDLENDKQQLE 1095
Cdd:COG3206 306 QLQQEAQRILASLEAE---LEALQAREASLQAQLAQLEARLAELPELEAELRRLER----EVEVARELYESLLQRLEEAR 378
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1028-1379 |
3.45e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 62.24 E-value: 3.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1028 LQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKIRMDLERVKRKLEGDVKLSQeslmdLENDKQQLEEKLKkkdfevsq 1107
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVAS-----AEREIAELEAELE-------- 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1108 lntRIEDEQNVCIQLQKKMKELQARIEELEEELEAERTARAKVEKLRCDLSRELEEISERLEEAGGATSVQmelnkkrea 1187
Cdd:COG4913 679 ---RLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE--------- 746
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1188 eflkLRRDLEE--STLHSEATAASLRKKHADSVAELSEQIDNLQrvkQKLEKEKSEFKLELDDVTSNMEQMVKAKANLEK 1265
Cdd:COG4913 747 ----LRALLEErfAAALGDAVERELRENLEERIDALRARLNRAE---EELERAMRAFNREWPAETADLDADLESLPEYLA 819
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1266 LCRSLEDQ---ANEHRTKSEENQRTVNELSSLRAKLQTENGELSRRLDEKESLVSQMTRGKQTYTQhLEDLKRQLEEETK 1342
Cdd:COG4913 820 LLDRLEEDglpEYEERFKELLNENSIEFVADLLSKLRRAIREIKERIDPLNDSLKRIPFGPGRYLR-LEARPRPDPEVRE 898
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1343 AKNALAHALQSARHDSDLLREQF-------------EEEQEAKAELQRIL 1379
Cdd:COG4913 899 FRQELRAVTSGASLFDEELSEARfaalkrlierlrsEEEESDRRWRARVL 948
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1194-1924 |
3.86e-09 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 62.28 E-value: 3.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1194 RDLEESTLHSEAtAASLRKKHADSVAELSEQIDNLQRVKQKL-EKEKSEFKLELDDVTSN--MEQMVKAKANLEKLCRSL 1270
Cdd:COG3096 275 RHANERRELSER-ALELRRELFGARRQLAEEQYRLVEMARELeELSARESDLEQDYQAASdhLNLVQTALRQQEKIERYQ 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1271 ED--QANEhrtKSEENQRTVNELSSLRAKLQTEngeLSRRLDEKESLVSQMTrgkqTYTQHLEDLKRQLEEETKAKNALA 1348
Cdd:COG3096 354 EDleELTE---RLEEQEEVVEEAAEQLAEAEAR---LEAAEEEVDSLKSQLA----DYQQALDVQQTRAIQYQQAVQALE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1349 HAlQSARHDSDLLREQFEEEQEA-KAELQrilskansevaqwrtkyetdaiQRTEELEEAKKKLA------QRLQEAEEA 1421
Cdd:COG3096 424 KA-RALCGLPDLTPENAEDYLAAfRAKEQ----------------------QATEEVLELEQKLSvadaarRQFEKAYEL 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1422 VEAVNAkcsslektkhrlqneiedlmvDLERSNA--AAAALDKKQRNFdKILAEWKQKFEESQTELE---SSQKEARSLS 1496
Cdd:COG3096 481 VCKIAG---------------------EVERSQAwqTARELLRRYRSQ-QALAQRLQQLRAQLAELEqrlRQQQNAERLL 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1497 TELFKLKNAYEESLDHLETFKREnknLQEEISDLTEQLGESGKSIHELekiRKQLDQEKMEIQSALEEAEATLEheegki 1576
Cdd:COG3096 539 EEFCQRIGQQLDAAEELEELLAE---LEAQLEELEEQAAEAVEQRSEL---RQQLEQLRARIKELAARAPAWLA------ 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1577 lhAQLELHQIKADSERKLAekdeemeqakrNYQRMVDTLQTSLEAE---TRSRNEALRIKKKMEGDLNEmeiqLSQAN-- 1651
Cdd:COG3096 607 --AQDALERLREQSGEALA-----------DSQEVTAAMQQLLEREreaTVERDELAARKQALESQIER----LSQPGga 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1652 ---RQAAEAQKQVKILQSYLKDtQIQLDDA-------------------------LRASEDLKENIAIVERR-----NTL 1698
Cdd:COG3096 670 edpRLLALAERLGGVLLSEIYD-DVTLEDApyfsalygparhaivvpdlsavkeqLAGLEDCPEDLYLIEGDpdsfdDSV 748
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1699 LQAELEELRSLVEQTERA-------------RKLSEQELIETS-ERVQLLHSQNTSLINQKK--KMESDLSQL------- 1755
Cdd:COG3096 749 FDAEELEDAVVVKLSDRQwrysrfpevplfgRAAREKRLEELRaERDELAEQYAKASFDVQKlqRLHQAFSQFvgghlav 828
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1756 ----------------QTEMEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLErmKKNMEQTIKDLQQRLDEAE 1819
Cdd:COG3096 829 afapdpeaelaalrqrRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLA--DETLADRLEELREELDAAQ 906
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1820 Q----IALKGgkKQLQKLEARVRELDN-------------ELEAEQKRNAESVKGMRKYERRIKELTYQTEEDRknLARL 1882
Cdd:COG3096 907 EaqafIQQHG--KALAQLEPLVAVLQSdpeqfeqlqadylQAKEQQRRLKQQIFALSEVVQRRPHFSYEDAVGL--LGEN 982
|
810 820 830 840
....*....|....*....|....*....|....*....|..
gi 1072253241 1883 QDLVDKLQLKVktykRQAEESEEQANTSLskfRKVQHELDEA 1924
Cdd:COG3096 983 SDLNEKLRARL----EQAEEARREAREQL---RQAQAQYSQY 1017
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1049-1886 |
4.09e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 61.90 E-value: 4.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1049 VDDLEGSLeqeKKIRMDLE--RVKRKLEGDVK-LSQESL-------MDLENDKQQLEEKLKKKDFEVSQLNTRIEDEQNV 1118
Cdd:PRK04863 232 FQDMEAAL---RENRMTLEaiRVTQSDRDLFKhLITESTnyvaadyMRHANERRVHLEEALELRRELYTSRRQLAAEQYR 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1119 CIQLQKKM-------KELQARIEELEEELEAERTARAKVEKL-RCdlSRELEEISERLEEAGGATSVQMELNKKREAEFl 1190
Cdd:PRK04863 309 LVEMARELaelneaeSDLEQDYQAASDHLNLVQTALRQQEKIeRY--QADLEELEERLEEQNEVVEEADEQQEENEARA- 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1191 klrRDLEESTLhseataaSLRKKHADSVAELSEQ----------IDNLQRVKQ----------KLEKEKSEFKLELDDVT 1250
Cdd:PRK04863 386 ---EAAEEEVD-------ELKSQLADYQQALDVQqtraiqyqqaVQALERAKQlcglpdltadNAEDWLEEFQAKEQEAT 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1251 SNMEQmvkakanLEKLCRSLEDQANEHRTKSEENQRTVNELSSLRAKLQTEngELSRRLDEKESLVSQMtrgkQTYTQHL 1330
Cdd:PRK04863 456 EELLS-------LEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWDVAR--ELLRRLREQRHLAEQL----QQLRMRL 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1331 EDLKRQLEEETKAKNALAHALQsaRHDSDLLRE-QFEEEQEAKAELQRILSKANSEVAQWRTKYEtdaiQRTEELEEAKK 1409
Cdd:PRK04863 523 SELEQRLRQQQRAERLLAEFCK--RLGKNLDDEdELEQLQEELEARLESLSESVSEARERRMALR----QQLEQLQARIQ 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1410 KLAQRLQE---AEEAVEAVNAKCSSLEKTKHRLQNEIEDLmvdLERSNAAAAALDKkqrnfdkiLAEWKQKFEESQTELe 1486
Cdd:PRK04863 597 RLAARAPAwlaAQDALARLREQSGEEFEDSQDVTEYMQQL---LERERELTVERDE--------LAARKQALDEEIERL- 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1487 sSQKEARSLST--------------ELFK---LKNA-YEESL----------DHLETFKRENKNLQEEISDL------TE 1532
Cdd:PRK04863 665 -SQPGGSEDPRlnalaerfggvllsEIYDdvsLEDApYFSALygparhaivvPDLSDAAEQLAGLEDCPEDLyliegdPD 743
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1533 QLGESGKSIHELEK-IRKQLDQEKMEIQSALEEAEATLEHEEgkilhAQLELHQIKADS-ERKLAEKDEEMEQAKRNYQR 1610
Cdd:PRK04863 744 SFDDSVFSVEELEKaVVVKIADRQWRYSRFPEVPLFGRAARE-----KRIEQLRAEREElAERYATLSFDVQKLQRLHQA 818
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1611 MVDTLQTSL--------EAETRSRNEALRikkKMEGDLNEMEIQLSQANRQAAEAQKQVKILQSYLKDTQI--------- 1673
Cdd:PRK04863 819 FSRFIGSHLavafeadpEAELRQLNRRRV---ELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLladetladr 895
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1674 ------QLDDALRASEDLKEN---IAIVERRNTLLQA---ELEELRSLVEQTERARKLSEQELIETSERVQLLH----SQ 1737
Cdd:PRK04863 896 veeireQLDEAEEAKRFVQQHgnaLAQLEPIVSVLQSdpeQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAhfsyED 975
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1738 NTSLINQkkkmESDLS-QLQTEMEEAVQECRNAEEKAKKA---ITDAAMMAEELKKEQDTsahLERMKKNMEQTIKDLQQ 1813
Cdd:PRK04863 976 AAEMLAK----NSDLNeKLRQRLEQAEQERTRAREQLRQAqaqLAQYNQVLASLKSSYDA---KRQMLQELKQELQDLGV 1048
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1072253241 1814 RLDEAEQIALKGGKKQLQKLEARVRELDNELEAE---QKRNAES-VKGMRKYERRIKELTYQTEEDRKNLARLQDLV 1886
Cdd:PRK04863 1049 PADSGAEERARARRDELHARLSANRSRRNQLEKQltfCEAEMDNlTKKLRKLERDYHEMREQVVNAKAGWCAVLRLV 1125
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
859-1531 |
5.08e-09 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 61.78 E-value: 5.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 859 KSAETEKEMQTMKEEFQKLKEALEKSEARRK-----DLEEKMVSLLQE---KNDLQLQ-------------VQAEQDNL- 916
Cdd:pfam12128 302 KRDELNGELSAADAAVAKDRSELEALEDQHGafldaDIETAAADQEQLpswQSELENLeerlkaltgkhqdVTAKYNRRr 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 917 ADADERCEQLIKNKIQLEAKLKEQTERLEDEEE---------MNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKH 987
Cdd:pfam12128 382 SKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEddlqaleseLREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPE 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 988 ATENKvKNLTEEMAGLDEIIVKLTKEKKALQE-------AHQQALDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSL-EQE 1059
Cdd:pfam12128 462 LLLQL-ENFDERIERAREEQEAANAEVERLQSelrqarkRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLlHFL 540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1060 KKIRMDLERVKRKLEGDVKLSQESL---MDLENDKQQLEEKLKKKDFEVSQLNTRIEDEQNVCIQLQKKMKELQARIEEL 1136
Cdd:pfam12128 541 RKEAPDWEQSIGKVISPELLHRTDLdpeVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQ 620
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1137 EEELEAERTARAKVEKLRCDLSRELEEIsERLEEAGGATSVQMELNKKREAEFLKLRRDLEESTLHS-EATAASLRKKHA 1215
Cdd:pfam12128 621 AAAEEQLVQANGELEKASREETFARTAL-KNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSlEAQLKQLDKKHQ 699
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1216 DSVAELSEQidnlqrvKQKLEKEKSEFKLELDDVTSNMEQMVKAKANLEKLCRSLEDQANEHRTKSEENQRTVNELSSlr 1295
Cdd:pfam12128 700 AWLEEQKEQ-------KREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVI-- 770
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1296 AKLQTENGELSRRLDEKESLVSQMTRGKQ----TYTQHLEDLKRQLEEETKAKNALAHALQSARHDSDLLREQFEEEQEA 1371
Cdd:pfam12128 771 AKLKREIRTLERKIERIAVRRQEVLRYFDwyqeTWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKA 850
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1372 KAELQRILSKANSEVAQWRTKYETDAIQRTEelEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVD-- 1449
Cdd:pfam12128 851 SEKQQVRLSENLRGLRCEMSKLATLKEDANS--EQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHFKNVIADHSGSgl 928
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1450 ---LERSNAAAAALDKKQRNFDKILAEWKQKFEESQTELESSQKEARSLSTelfKLKNAYEESLDHLETFKRE----NKN 1522
Cdd:pfam12128 929 aetWESLREEDHYQNDKGIRLLDYRKLVPYLEQWFDVRVPQSIMVLREQVS---ILGVDLTEFYDVLADFDRRiasfSRE 1005
|
....*....
gi 1072253241 1523 LQEEISDLT 1531
Cdd:pfam12128 1006 LQREVGEEA 1014
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1657-1927 |
8.46e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.85 E-value: 8.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1657 AQKQVKILQSYLKDTQIQLDDALRASEDLKENIAIVERRNTLLQAELEELRSLVEQTERA-RKLSE--QELIETSERVQL 1733
Cdd:PRK03918 163 AYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREElEKLEKevKELEELKEEIEE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1734 LHSQNTSLINQKKKMESDLSQLQTEMEEAVQECRNAEEKAKKaitdaammAEELKKEQDTSAHLERMKKNMEQTIKDLQQ 1813
Cdd:PRK03918 243 LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKE--------LKELKEKAEEYIKLSEFYEEYLDELREIEK 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1814 RLDEAEQiALKGGKKQLQKLE---ARVRELDNELEAEQKRNAESVKGMRKYErRIKELTYQTEEDRKNLARLQ-DLVDKL 1889
Cdd:PRK03918 315 RLSRLEE-EINGIEERIKELEekeERLEELKKKLKELEKRLEELEERHELYE-EAKAKKEELERLKKRLTGLTpEKLEKE 392
|
250 260 270
....*....|....*....|....*....|....*...
gi 1072253241 1890 QLKVKTYKRQAEESEEQANTSLSKFRKVQHELDEAEER 1927
Cdd:PRK03918 393 LEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE 430
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
865-1152 |
8.55e-09 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 60.89 E-value: 8.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 865 KEMQTMKEEFQ--KLKEALEKSEARRKDLEEKmvSLLQEKNDLQLQVQAEQDNLADADERCEQLIKnkiQLEAKLKEQTE 942
Cdd:pfam05483 471 KEVEDLKTELEkeKLKNIELTAHCDKLLLENK--ELTQEASDMTLELKKHQEDIINCKKQEERMLK---QIENLEEKEMN 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 943 RLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIVKLTKEKKALQEAHQ 1022
Cdd:pfam05483 546 LRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGS 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1023 QALDDLQAEEDKVNT----LTKAKAKLEQQVDDLEGSLE----QEKKIRMDLERVKRKLEGDVKLSQ-----------ES 1083
Cdd:pfam05483 626 AENKQLNAYEIKVNKleleLASAKQKFEEIIDNYQKEIEdkkiSEEKLLEEVEKAKAIADEAVKLQKeidkrcqhkiaEM 705
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1072253241 1084 LMDLENDKQQLEEKLKKKDFEVSQLNTRIEDEQNVCIQLQKKMKELQARIEELEEELEAERTARAKVEK 1152
Cdd:pfam05483 706 VALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKM 774
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1455-1695 |
1.38e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.01 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1455 AAAAALDKKQRNFDKILAEWKQKFEESQTELESSQKEARSLSTELFKLKNAYEESLDHLETFKRENKNLQEEISDLTEQl 1534
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1535 gesgksiheLEKIRKQLDQEKMEIQSALEEAEATLEHEEGKILhaqlelhqIKADSERKLAEKDEEMEQAKRNYQRMVDT 1614
Cdd:COG4942 92 ---------IAELRAELEAQKEELAELLRALYRLGRQPPLALL--------LSPEDFLDAVRRLQYLKYLAPARREQAEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1615 LQTSLEAETRSRNEALRIKKKMEGDLNEMEIQLSQANRQAAEAQKQVKILQSYLKDTQIQLDDALRASEDLKENIAIVER 1694
Cdd:COG4942 155 LRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
.
gi 1072253241 1695 R 1695
Cdd:COG4942 235 E 235
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1080-1308 |
1.93e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.62 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1080 SQESLMDLENDKQQLEEKLKKKDFEVSQLNTRIEDEQNVCIQLQKKMKELQARIEELEEELEAERTARAKVEKLRCDLSR 1159
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1160 ELEEISERLEEAGGAtsvqMELNKKREAEFLKLRRDLEESTLHSEATAASLRKKHADSVAELSEQIDNLQRVKQKLEKEK 1239
Cdd:COG4942 98 ELEAQKEELAELLRA----LYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1072253241 1240 SEFKLELDDVTSNMEQMVKAKANLEKLCRSLEDQANEHRTKSEENQRTVNELSSLRAKLQTENGELSRR 1308
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1232-1459 |
2.97e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.24 E-value: 2.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1232 KQKLEKEKSEFKLELDDVTSNMEQMVKAKANLEKLCRSLEDQANEHRTKSEENQRTVNELSSLRAKLQTENGELSRRLDE 1311
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1312 KESLVSQMTRGKQTYTQH--LEDLKRQleeetKAKNALAHALQSARHDSDLLREQFEEEQEAKAELQRILSKANSEVAQW 1389
Cdd:COG4942 102 QKEELAELLRALYRLGRQppLALLLSP-----EDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1390 RTKYETDAIQRtEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAA 1459
Cdd:COG4942 177 EALLAELEEER-AALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
862-1249 |
3.96e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 58.49 E-value: 3.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 862 ETEKEMQTMKEEFQKLKEALEKSEARRKDLEEKMVSLLQEKNDLQLQV-----QAEQDNLADADERCEQLIKNKIQLEAK 936
Cdd:TIGR04523 250 NTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEIsdlnnQKEQDWNKELKSELKNQEKKLEEIQNQ 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 937 LKEQTERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIVKLTKEKKA 1016
Cdd:TIGR04523 330 ISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1017 LQEAHQQALDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKIRMDLERVKRKLEGDVKLSQESLMDLENDKQQLEE 1096
Cdd:TIGR04523 410 KDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQK 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1097 KLKKKDFEVSQLNTRIEDEQNVCIQLQKKMKELQARIEE----LEEELEAERTARAKVEKLRCDLSREL---------EE 1163
Cdd:TIGR04523 490 ELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKleseKKEKESKISDLEDELNKDDFELKKENlekeideknKE 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1164 ISERLEEAGGATSVQMELN---KKREAEFLKLRRDLEEstlhSEATAASLRKKHADSVAE---LSEQIDNLQRVKQKLEK 1237
Cdd:TIGR04523 570 IEELKQTQKSLKKKQEEKQeliDQKEKEKKDLIKEIEE----KEKKISSLEKELEKAKKEnekLSSIIKNIKSKKNKLKQ 645
|
410
....*....|..
gi 1072253241 1238 EKSEFKLELDDV 1249
Cdd:TIGR04523 646 EVKQIKETIKEI 657
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1499-1938 |
4.15e-08 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 58.33 E-value: 4.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1499 LFKLKNAYEEsLDHLETFKRE--NKNLQEEISDLtEQLGESGKSIHELEKIRKQ----LDQEKMEIQSALEEAEATLEhe 1572
Cdd:pfam06160 2 LLLRKKIYKE-IDELEERKNElmNLPVQEELSKV-KKLNLTGETQEKFEEWRKKwddiVTKSLPDIEELLFEAEELND-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1573 EGKILHAQlelhqikadseRKLAEKDEEMEQAKRNYQRMVDTLQTSLEAETRSRNEALRIKKK----------------- 1635
Cdd:pfam06160 78 KYRFKKAK-----------KALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKyrelrktllanrfsygp 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1636 ----MEGDLNEMEIQLSQ-----ANRQAAEAQKQVKILQSYLKDTQIQLDDalrasedlkenI-AIVERRNTLLQAELEE 1705
Cdd:pfam06160 147 aideLEKQLAEIEEEFSQfeeltESGDYLEAREVLEKLEEETDALEELMED-----------IpPLYEELKTELPDQLEE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1706 LRSLVEQTERAR-KLSEQELIETSERVQLLHSQNTSLINQK--KKMESDLSQLQTEMEEaVQECRNAEEKAKKaitdaam 1782
Cdd:pfam06160 216 LKEGYREMEEEGyALEHLNVDKEIQQLEEQLEENLALLENLelDEAEEALEEIEERIDQ-LYDLLEKEVDAKK------- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1783 maeELKKEQDT-SAHLERMKKNMEQTIKDLQQ-----RLDEAEQIALKGGKKQLQKLEARVRELDNELEAEQKRNAESVK 1856
Cdd:pfam06160 288 ---YVEKNLPEiEDYLEHAEEQNKELKEELERvqqsyTLNENELERVRGLEKQLEELEKRYDEIVERLEEKEVAYSELQE 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1857 GMRKYERRIKELTYQTEEDRKNLARL-------QDLVDKLQLKVKTYKR-------------------QAEESEEQANTS 1910
Cdd:pfam06160 365 ELEEILEQLEEIEEEQEEFKESLQSLrkdeleaREKLDEFKLELREIKRlveksnlpglpesyldyffDVSDEIEDLADE 444
|
490 500 510
....*....|....*....|....*....|..
gi 1072253241 1911 LSKFR----KVQHELDEAEERADIAESQVNKL 1938
Cdd:pfam06160 445 LNEVPlnmdEVNRLLDEAQDDVDTLYEKTEEL 476
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
927-1420 |
4.77e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.24 E-value: 4.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 927 IKNKIQLEAkLKEQTERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEK--HATENKVKNLTEEMAGLD 1004
Cdd:COG4717 67 ELNLKELKE-LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLqlLPLYQELEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1005 EIIVKLTKEKKALQEAHQQalddlqaeedkvntltkaKAKLEQQVDDLEGSLEQEkkirmdLERVKRKLEGDVKLSQESL 1084
Cdd:COG4717 146 ERLEELEERLEELRELEEE------------------LEELEAELAELQEELEEL------LEQLSLATEEELQDLAEEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1085 MDLENDKQQLEEKLKkkdfevsqlntriedeqnvciQLQKKMKELQARIEELEEELEAERTAR--------AKVEKLRCD 1156
Cdd:COG4717 202 EELQQRLAELEEELE---------------------EAQEELEELEEELEQLENELEAAALEErlkearllLLIAAALLA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1157 LSRELEEISERLEEAGGATSVQMEL----------------NKKREAEFLKLRRDLEESTLHSEATAASL-RKKHADSVA 1219
Cdd:COG4717 261 LLGLGGSLLSLILTIAGVLFLVLGLlallflllarekaslgKEAEELQALPALEELEEEELEELLAALGLpPDLSPEELL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1220 ELSEQIDNLQRVKQKLEKEKSEFKLElddvtsnmEQMVKAKANLEKLCRSLEDQANEHRTKSEENQRTVNELSSLRAKLQ 1299
Cdd:COG4717 341 ELLDRIEELQELLREAEELEEELQLE--------ELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1300 TENGELSRRLDEKESlvSQMTRGKQTYTQHLEDLKRQLEEETKAKNALAHALQSARHDSDLlreqfeeeQEAKAELQRIL 1379
Cdd:COG4717 413 ELLGELEELLEALDE--EELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGEL--------AELLQELEELK 482
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1072253241 1380 SKANSEVAQWRT-KYETDAIQRTEELEEaKKKLAQRLQEAEE 1420
Cdd:COG4717 483 AELRELAEEWAAlKLALELLEEAREEYR-EERLPPVLERASE 523
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
869-1051 |
5.45e-08 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 55.70 E-value: 5.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 869 TMKEEFQKLKEaLEKSEARRKDLEEKMVSLLQEKNDLQLQVQAEQDNLADADERCEQLIKNKIQLEAKLKEQTERLE-DE 947
Cdd:COG1579 1 AMPEDLRALLD-LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKkYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 948 EEMNAELTAKkrkledECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIVKLTKEKKALQEAHQQALDD 1027
Cdd:COG1579 80 EQLGNVRNNK------EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE 153
|
170 180
....*....|....*....|....
gi 1072253241 1028 LQAEEDKvntLTKAKAKLEQQVDD 1051
Cdd:COG1579 154 LEAELEE---LEAEREELAAKIPP 174
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1399-1846 |
6.93e-08 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 57.39 E-value: 6.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1399 QRTEELE-------EAKKKLAQ---RLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAALDKKQRNFD 1468
Cdd:pfam05622 14 QRCHELDqqvsllqEEKNSLQQenkKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFRLETARDDYRIKCEELE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1469 KILAEWKQKFEEsqteLESSQKEARSLSTELFKLKNA-------------YEESLDHLETFKRENKNLQEEISDLTEQLG 1535
Cdd:pfam05622 94 KEVLELQHRNEE----LTSLAEEAQALKDEMDILRESsdkvkkleatvetYKKKLEDLGDLRRQVKLLEERNAEYMQRTL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1536 ESGKSIHELEKIRKQLDQEKMEIQsaleEAEATLEHEEGKILHAQLELHQIKA-------DSERKLAEKD---EEMEQAK 1605
Cdd:pfam05622 170 QLEEELKKANALRGQLETYKRQVQ----ELHGKLSEESKKADKLEFEYKKLEEklealqkEKERLIIERDtlrETNEELR 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1606 RNYQRMVDTLQTSLEAETRSRNEALRIKKKMEGDLNEMEIQLSQANRQAAEAQKQVKilQSYLKDTQIQLDDALRASEDL 1685
Cdd:pfam05622 246 CAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLRLGQEGSY--RERLTELQQLLEDANRRKNEL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1686 KENIAIVERRNTLLQAELEELRslveqteraRKLSEQElietservqllhSQNTSLINQKKKMESDLSQLQTEMEEAVQE 1765
Cdd:pfam05622 324 ETQNRLANQRILELQQQVEELQ---------KALQEQG------------SKAEDSSLLKQKLEEHLEKLHEAQSELQKK 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1766 CRNAEEKAKKAITDAAMMAEEL-----KKEQDTSAHLERMKKNMEQT---IKDLQQRLDEAEQIALKGGKKQLQKLEARV 1837
Cdd:pfam05622 383 KEQIEELEPKQDSNLAQKIDELqealrKKDEDMKAMEERYKKYVEKAksvIKTLDPKQNPASPPEIQALKNQLLEKDKKI 462
|
....*....
gi 1072253241 1838 RELDNELEA 1846
Cdd:pfam05622 463 EHLERDFEK 471
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1637-1854 |
8.46e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 56.76 E-value: 8.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1637 EGDLNEMEIQLSQANRQAAEAQKQVKILQSYLKDTQIQLDDALRASEDLKENIAIVERRNTLLQAELEELRSLVEqtERA 1716
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG--ERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1717 RKLSEQELIETSERVqLLHSQNTS-LINQkkkmESDLSQLQTEMEEAVQECRNAEEKAKKAitdaammAEELKKEQDTsa 1795
Cdd:COG3883 93 RALYRSGGSVSYLDV-LLGSESFSdFLDR----LSALSKIADADADLLEELKADKAELEAK-------KAELEAKLAE-- 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1072253241 1796 hLERMKKNMEQTIKDLQQRLDEAEQiALKGGKKQLQKLEARVRELDNELEAEQKRNAES 1854
Cdd:COG3883 159 -LEALKAELEAAKAELEAQQAEQEA-LLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
872-1446 |
8.56e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 57.66 E-value: 8.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 872 EEFQKLKEALEKSEARRKDLEEkmvsllqeknDLQLQVQAEQdNLADADERCEQLIKNKIQLEAKLKEQTERLEDEEEMN 951
Cdd:PRK04863 506 REQRHLAEQLQQLRMRLSELEQ----------RLRQQQRAER-LLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESV 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 952 AELTAKKRKLEDECSELKKDIDdlelTLAKVEKEKHATENKVKNLTEEMAGLDEiivkltkEKKALQEAHQQALDDLQAE 1031
Cdd:PRK04863 575 SEARERRMALRQQLEQLQARIQ----RLAARAPAWLAAQDALARLREQSGEEFE-------DSQDVTEYMQQLLEREREL 643
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1032 EDKVNTLTKAKAKLEQQVDDL---EGSlEQEKKIRM--------------------------------------DLERVK 1070
Cdd:PRK04863 644 TVERDELAARKQALDEEIERLsqpGGS-EDPRLNALaerfggvllseiyddvsledapyfsalygparhaivvpDLSDAA 722
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1071 RKLEGDVKLSQESLMdLENDKQQLEEKLkkkdFEVSQLntriedEQNVCIQLQKKmkelQARIEELEEELEAERTARakv 1150
Cdd:PRK04863 723 EQLAGLEDCPEDLYL-IEGDPDSFDDSV----FSVEEL------EKAVVVKIADR----QWRYSRFPEVPLFGRAAR--- 784
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1151 EKLRCDLSRELEEISERLEEAG----------------GATSVQMELNKKREAEFLKLRRDLEEStlhsEATAASLRKKH 1214
Cdd:PRK04863 785 EKRIEQLRAEREELAERYATLSfdvqklqrlhqafsrfIGSHLAVAFEADPEAELRQLNRRRVEL----ERALADHESQE 860
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1215 AdsvaELSEQIDNLQRVKQKLEKEKSEFKLeLDDVTSNMEQMVKAkanlEKLCRSLEDQANEHRtkseeNQRTVNELSSL 1294
Cdd:PRK04863 861 Q----QQRSQLEQAKEGLSALNRLLPRLNL-LADETLADRVEEIR----EQLDEAEEAKRFVQQ-----HGNALAQLEPI 926
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1295 RAKLQT---ENGELSRRLDEKESLVSQMTRGKQTYTQ------HL--EDLKRQLEEETKAKNALAHALQSARHDSDLLRE 1363
Cdd:PRK04863 927 VSVLQSdpeQFEQLKQDYQQAQQTQRDAKQQAFALTEvvqrraHFsyEDAAEMLAKNSDLNEKLRQRLEQAEQERTRARE 1006
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1364 QFEEEQEAKAELQRILSKANSEvaqWRTKYET--DAIQRTEEL-----EEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTK 1436
Cdd:PRK04863 1007 QLRQAQAQLAQYNQVLASLKSS---YDAKRQMlqELKQELQDLgvpadSGAEERARARRDELHARLSANRSRRNQLEKQL 1083
|
650
....*....|
gi 1072253241 1437 HRLQNEIEDL 1446
Cdd:PRK04863 1084 TFCEAEMDNL 1093
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
669-693 |
1.11e-07 |
|
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: 53.50 E-value: 1.11e-07
10 20
....*....|....*....|....*
gi 1072253241 669 HRENLNKLMTNLRATHPHFVRCIIP 693
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1274-1941 |
1.13e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 57.27 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1274 ANEHRTKSEENQRTVNELSSLRAKLQTEN---GELSRRLDEkeslvsqMTRGKQTYTQHLEDLKRQLEeetKAKNALAHA 1350
Cdd:PRK04863 278 ANERRVHLEEALELRRELYTSRRQLAAEQyrlVEMARELAE-------LNEAESDLEQDYQAASDHLN---LVQTALRQQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1351 LQSARHDSDL--LREQFEEEQEAKAElqrilskANSEVAQWRTKYEtdaiQRTEELEEAKKKLA---QRL---------- 1415
Cdd:PRK04863 348 EKIERYQADLeeLEERLEEQNEVVEE-------ADEQQEENEARAE----AAEEEVDELKSQLAdyqQALdvqqtraiqy 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1416 QEAEEAVEAVNAKC-------SSLEKTKHRLQNEIEDL---MVDLER----SNAAAAALDK------------------- 1462
Cdd:PRK04863 417 QQAVQALERAKQLCglpdltaDNAEDWLEEFQAKEQEAteeLLSLEQklsvAQAAHSQFEQayqlvrkiagevsrseawd 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1463 ----------KQRNFDKILAEWKQKFEESQTELESsQKEARSLSTELFKLKNAYEESLDHLETFKREnknLQEEISDLTE 1532
Cdd:PRK04863 497 varellrrlrEQRHLAEQLQQLRMRLSELEQRLRQ-QQRAERLLAEFCKRLGKNLDDEDELEQLQEE---LEARLESLSE 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1533 QLGESGKSIHELEKIRKQLDQEKMEIQS------ALEEAEATLEHEEGKIL---HAQLELHQIKADSERKLAEKDEEMEQ 1603
Cdd:PRK04863 573 SVSEARERRMALRQQLEQLQARIQRLAArapawlAAQDALARLREQSGEEFedsQDVTEYMQQLLERERELTVERDELAA 652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1604 AKRNYQRMVDTLQtslEAETRSRNEALRIKKKMEGDL-----NEMEIQ----LSQANRQAAEAqkqvkILQSYLKDTQIQ 1674
Cdd:PRK04863 653 RKQALDEEIERLS---QPGGSEDPRLNALAERFGGVLlseiyDDVSLEdapyFSALYGPARHA-----IVVPDLSDAAEQ 724
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1675 LDdalrASEDLKENIAIVER-----RNTLLQAELEELRSLVEQTERARKLS---EQELIETSERVQLLHSQNTSLinqkk 1746
Cdd:PRK04863 725 LA----GLEDCPEDLYLIEGdpdsfDDSVFSVEELEKAVVVKIADRQWRYSrfpEVPLFGRAAREKRIEQLRAER----- 795
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1747 kmeSDLSQLQTEMEEAVQECRNAEEKAKKAITDAAMMA------EELKKEQDTSAHLERMKKNMEQTIKDLQQRLDeaeq 1820
Cdd:PRK04863 796 ---EELAERYATLSFDVQKLQRLHQAFSRFIGSHLAVAfeadpeAELRQLNRRRVELERALADHESQEQQQRSQLE---- 868
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1821 iALKGGKKQLQKLEARVRELDN--------ELEAEQKRNAESVKGMRKYERRIKELTYQT---EEDRKNLARLQDLVDKL 1889
Cdd:PRK04863 869 -QAKEGLSALNRLLPRLNLLADetladrveEIREQLDEAEEAKRFVQQHGNALAQLEPIVsvlQSDPEQFEQLKQDYQQA 947
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 1072253241 1890 QLKVKTYKRQAEeseeqantSLSKFRKVQHELDEAEERADIAESQ--VNKLRAK 1941
Cdd:PRK04863 948 QQTQRDAKQQAF--------ALTEVVQRRAHFSYEDAAEMLAKNSdlNEKLRQR 993
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1222-1431 |
1.39e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.93 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1222 SEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQMVKAKANLEKLCRSLEDQANEHRTKSEENQRTVNEL----SSLRAK 1297
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELekeiAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1298 LQTENGELSRRL---------DEKESLVS-----QMTRGKQTYTQHLEDLKRQLEEETKAKNALAHALQSARHDSDLLRE 1363
Cdd:COG4942 99 LEAQKEELAELLralyrlgrqPPLALLLSpedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1072253241 1364 QFEEEQEAKAELQRILSKANSEVAQWRTKYETDAiQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSS 1431
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELA-AELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1048-1621 |
1.59e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 56.83 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1048 QVDDL-EGSLEQEKKIRMDLERVKRKLEGDVKLSQ--ESLMDLENDKQQLEEKLKKKDFEVSQLNTRIEDEQNVCIQLQK 1124
Cdd:PRK01156 139 EMDSLiSGDPAQRKKILDEILEINSLERNYDKLKDviDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLK 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1125 KMKELQARIEELEEELEAERTA--------------RAKVEKLRCDLSRELEE---ISERLEEAGGATSVQMELNKKREA 1187
Cdd:PRK01156 219 EIERLSIEYNNAMDDYNNLKSAlnelssledmknryESEIKTAESDLSMELEKnnyYKELEERHMKIINDPVYKNRNYIN 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1188 EFLKLRRDLEESTLHSEATAASLRKKHaDSVAELSE-QIDNLQRVKQKleKEKSEFKLELDDVTSNMEQMVKAKANLEKL 1266
Cdd:PRK01156 299 DYFKYKNDIENKKQILSNIDAEINKYH-AIIKKLSVlQKDYNDYIKKK--SRYDDLNNQILELEGYEMDYNSYLKSIESL 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1267 CRSLEDQANEHRTKSEENQRTVNELSSLRAKLQTENGELSRRLDEKESLVSQMTRGKQTYTQHLEDLKRQLEEETKAKNA 1346
Cdd:PRK01156 376 KKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVC 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1347 LAHALQSARHDSDLLREQFEEE----QEAKAELQRILSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQ--------- 1413
Cdd:PRK01156 456 PVCGTTLGEEKSNHIINHYNEKksrlEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESaradledik 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1414 ----RLQEAEEAVEAVNAKCSSLEKTKHRLQNEiEDLMVDLERSNAAAAALDKKQRNFDKILAEWKQKFEESQTELESSQ 1489
Cdd:PRK01156 536 ikinELKDKHDKYEEIKNRYKSLKLEDLDSKRT-SWLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDK 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1490 KEARSLSTELFKLKNAYEESLDHLETFKRENKNLQEEISDLTEQLGEsgksihelekiRKQLDQEKMEIQSALEEAEATL 1569
Cdd:PRK01156 615 SYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAE-----------IDSIIPDLKEITSRINDIEDNL 683
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1072253241 1570 EHEEGKILHAQLELHQIKADSErKLAEKDEEMEQAKRNYQRMVDTLQTSLEA 1621
Cdd:PRK01156 684 KKSRKALDDAKANRARLESTIE-ILRTRINELSDRINDINETLESMKKIKKA 734
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1683-1950 |
1.75e-07 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 56.06 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1683 EDLKENIAIVERRNTLLQAELEELrslveQTERARKLSEQELI--ETSERVQLLHSQNTSLINQKKKMESDLSQLQTEME 1760
Cdd:pfam07888 16 EEGGTDMLLVVPRAELLQNRLEEC-----LQERAELLQAQEAAnrQREKEKERYKRDREQWERQRRELESRVAELKEELR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1761 EAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQQRLDEAEqIALKGGKKQLQKLEARVREL 1840
Cdd:pfam07888 91 QSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERE-TELERMKERAKKAGAQRKEE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1841 DNELEAEQKRNAESVKGMRKYERRIKELTYQTEEDRKNLARLQDLVDKLQLKVKTYKRQAEESEEQANtslskfrkvqhE 1920
Cdd:pfam07888 170 EAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLE-----------E 238
|
250 260 270
....*....|....*....|....*....|
gi 1072253241 1921 LDEAEERADIAESQVNKLRAKSRDVSTKKS 1950
Cdd:pfam07888 239 LRSLQERLNASERKVEGLGEELSSMAAQRD 268
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
940-1176 |
2.06e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.54 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 940 QTERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIVKLTKEKKALQE 1019
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1020 ahqqaldDLQAEEDKVNTLTKAKAKLEQQvDDLEGSLEQEKKirMDLERVKRKLEGDVKLSQESLMDLENDKQQLEEKLK 1099
Cdd:COG4942 98 -------ELEAQKEELAELLRALYRLGRQ-PPLALLLSPEDF--LDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1072253241 1100 KKDFEVSQLNTRIEDEQNVCIQLQKKMKELQARIEELEEELEAERTARAKVEKLRCDLSRELEEISERLEEAGGATS 1176
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
870-1306 |
2.20e-07 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 55.98 E-value: 2.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 870 MKEEFQKLKEALEKSEARRKDLEEKMVSLLQEKNDLQLQVQAEQDNLADADERCEQLiknkiqlEAKLKEQTERLEDEEE 949
Cdd:pfam10174 287 MKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAIL-------QTEVDALRLRLEEKES 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 950 MNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIVKLTKEKKALQEAHQQA----- 1024
Cdd:pfam10174 360 FLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTdtalt 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1025 -LDDLQAEEDKV-NTLTKAKAKLEQQVDDlegSLEQEKKIRMDLERVKRKLEGDVKLSQESLMDLENDKQQLEEKLKKKD 1102
Cdd:pfam10174 440 tLEEALSEKERIiERLKEQREREDRERLE---ELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKD 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1103 FEVSQLNTRIEDEQNVCIQLQKKMKELQarieeleEELEAERTARAKVEKLRCdlsreLE-EISERLEEAGGAtsvQMEL 1181
Cdd:pfam10174 517 SKLKSLEIAVEQKKEECSKLENQLKKAH-------NAEEAVRTNPEINDRIRL-----LEqEVARYKEESGKA---QAEV 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1182 NKkreaeFLKLRRDLEESTLHSEATAASLRKKHADSVAELSEQIDNLQrVKQKLEKEKSEFKLELDDVTSNMEQMVKAKA 1261
Cdd:pfam10174 582 ER-----LLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIK-HGQQEMKKKGAQLLEEARRREDNLADNSQQL 655
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1072253241 1262 NLEKLCRSLEdqanehRTKSEENQrTVNELSSLRAKLQTENGELS 1306
Cdd:pfam10174 656 QLEELMGALE------KTRQELDA-TKARLSSTQQSLAEKDGHLT 693
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
876-1585 |
2.26e-07 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 55.98 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 876 KLKEALEKSEARRKD-LEEKMVSLLQEKNDLQLQVQAEQDNLADADERCEQLIKNKIQLEAKLKEQTERLEDEEEMNAEL 954
Cdd:pfam10174 42 KKERALRKEEAARISvLKEQYRVTQEENQHLQLTIQALQDELRAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 955 TAKKRKLEDECSELKKDIDDLELtlaKVEKEKHATENKvknlteemaglDEIIvkltkeKKALQEAHQQALDDLQAEEDk 1034
Cdd:pfam10174 122 QSEHERQAKELFLLRKTLEEMEL---RIETQKQTLGAR-----------DESI------KKLLEMLQSKGLPKKSGEED- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1035 vNTLTKAKAKLEQQVDDLEGSLEQEKKIRMDL-ERVKRKLEGDVKLSQESLMdlendkQQLEEKLKKKDFEVSQLNTRIE 1113
Cdd:pfam10174 181 -WERTRRIAEAEMQLGHLEVLLDQKEKENIHLrEELHRRNQLQPDPAKTKAL------QTVIEMKDTKISSLERNIRDLE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1114 DEQNV--------CIQLQKKMKELQArieeleeELEAERTARAKVEKLRCDLSR---ELEEISERLEEAGGATSvqmelN 1182
Cdd:pfam10174 254 DEVQMlktngllhTEDREEEIKQMEV-------YKSHSKFMKNKIDQLKQELSKkesELLALQTKLETLTNQNS-----D 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1183 KKREAEFLK---LRRDLEESTLHSEATAASLRKKHADSVaeLSEQIDNLQRvkqkLEKEKSEFKLELddvtSNMEQMVKA 1259
Cdd:pfam10174 322 CKQHIEVLKeslTAKEQRAAILQTEVDALRLRLEEKESF--LNKKTKQLQD----LTEEKSTLAGEI----RDLKDMLDV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1260 KAN----LEKLCRSLEDQANEHRTKSEENQRTVNELSSLRAKLQTENGELSRRLDEKESLVS----QMTRGKQTYTQHLE 1331
Cdd:pfam10174 392 KERkinvLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIErlkeQREREDRERLEELE 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1332 DLKRQLEEetkaknalahalqsARHDSDLLREQFEEEQEAKAELQRILSKANSEVAQWRTKYETDAIQRTEELEEAKK-- 1409
Cdd:pfam10174 472 SLKKENKD--------------LKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKle 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1410 ---KLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAALDKKQRNFDKILAEWKQKFEESQTELE 1486
Cdd:pfam10174 538 nqlKKAHNAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQN 617
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1487 SSQKEARSLSTELfKLKNAYEESLDHLETFKRENKNLQEEISDLTEqlgesgksihELEKIRKQLDQEKMEI---QSALE 1563
Cdd:pfam10174 618 KKVANIKHGQQEM-KKKGAQLLEEARRREDNLADNSQQLQLEELMG----------ALEKTRQELDATKARLsstQQSLA 686
|
730 740
....*....|....*....|....*
gi 1072253241 1564 EAEA---TLEHEEGKILHAQLELHQ 1585
Cdd:pfam10174 687 EKDGhltNLRAERRKQLEEILEMKQ 711
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1330-1944 |
3.19e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 55.68 E-value: 3.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1330 LEDLKRQLEEETKAKNALAHALQSARHDSDLLREQFEEEQEAKAELQRILSKANSEVAQWRTKYE--TDAIQRTEELEEA 1407
Cdd:PRK01156 171 LKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNnlKSALNELSSLEDM 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1408 KKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLqNEIEDLMVDLERSNAAAAALDKKQrnfdkiLAEWKQKFEESQTELES 1487
Cdd:PRK01156 251 KNRYESEIKTAESDLSMELEKNNYYKELEERH-MKIINDPVYKNRNYINDYFKYKND------IENKKQILSNIDAEINK 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1488 SQKEARSLStELFKLKNAYEESldhletfKRENKNLQEEISDLTEQLGESGKSIHELEKIRKQLDQEKMEIQSALEEAEA 1567
Cdd:PRK01156 324 YHAIIKKLS-VLQKDYNDYIKK-------KSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1568 TLEHEE--GKILHAQLE-----LHQIKAD------SERKLAEKDEEMEQ--AKRNYQRMVDTLQTSL--EAETRSRNEAL 1630
Cdd:PRK01156 396 ILKIQEidPDAIKKELNeinvkLQDISSKvsslnqRIRALRENLDELSRnmEMLNGQSVCPVCGTTLgeEKSNHIINHYN 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1631 RIKKKMEGDLNEMEIQLSQANrqaaEAQKQVKILQSYLKDTQI--------QLDDALRASEDLKENIAIVERRNTLLQAE 1702
Cdd:PRK01156 476 EKKSRLEEKIREIEIEVKDID----EKIVDLKKRKEYLESEEInksineynKIESARADLEDIKIKINELKDKHDKYEEI 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1703 LEELRSLveqterarklseqelietseRVQLLHSQNTSLINQKKKMES-DLSQLQTEMEEAVQECRNAEEKakkaitdaa 1781
Cdd:PRK01156 552 KNRYKSL--------------------KLEDLDSKRTSWLNALAVISLiDIETNRSRSNEIKKQLNDLESR--------- 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1782 mMAEELKKEQDTSAHLERMKKNMEQTIKDLQQRLDEAEqiALKGGKKQLQKLEARVRELDNELEAEQKRNAESVKGMRKY 1861
Cdd:PRK01156 603 -LQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQ--ENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDI 679
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1862 ERRIKELTYQTEEDRKNLARLQDLVDKLQLKVKTYK------RQAEESEEQANTSLSKFRKVQHELDEAEERADIAESQV 1935
Cdd:PRK01156 680 EDNLKKSRKALDDAKANRARLESTIEILRTRINELSdrindiNETLESMKKIKKAIGDLKRLREAFDKSGVPAMIRKSAS 759
|
....*....
gi 1072253241 1936 NKLRAKSRD 1944
Cdd:PRK01156 760 QAMTSLTRK 768
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1603-1825 |
3.87e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.38 E-value: 3.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1603 QAKRNYQRMVDTLQTSLEAETRSRNEALRIKKKMEGDLNEMEIQLSQANRQAAEAQKQVKILQSYLKDTQIQLDDALRAS 1682
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1683 EDLKENIA----------IVERRNTLLQAE----LEELRSLVEQTERARKLSEQELIETSERvqlLHSQNTSLINQKKKM 1748
Cdd:COG4942 100 EAQKEELAellralyrlgRQPPLALLLSPEdfldAVRRLQYLKYLAPARREQAEELRADLAE---LAALRAELEAERAEL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1072253241 1749 ESDLSQLQTEMEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQQRLDEAEQIALKG 1825
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKG 253
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1519-1937 |
4.55e-07 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 55.30 E-value: 4.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1519 ENKNLQEEISDLTEQLGESGKSIHELEKIRKQLDQ--EKM-EIQSALEEAEATLEHEEGKILhAQLELHQIkadsERKLA 1595
Cdd:PRK11281 57 EDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQapAKLrQAQAELEALKDDNDEETRETL-STLSLRQL----ESRLA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1596 EKDEEMEQAKRN---YQRMVDTLQTSLEaetRSRNEalrikkkmegdLNEMEIQLSQANRQAaeaqKQVKILQSYLKDTQ 1672
Cdd:PRK11281 132 QTLDQLQNAQNDlaeYNSQLVSLQTQPE---RAQAA-----------LYANSQRLQQIRNLL----KGGKVGGKALRPSQ 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1673 IQLDDALRASEDLKeniaIVERR-----NTLLQAELEELRSLVeqTERARKLSEQelietserVQLLhsQNtsLINQKKK 1747
Cdd:PRK11281 194 RVLLQAEQALLNAQ----NDLQRkslegNTQLQDLLQKQRDYL--TARIQRLEHQ--------LQLL--QE--AINSKRL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1748 MESdlsqlqtemEEAVQECRNAEEKAKkaITDAAMMAEELKKEQDTSAHL----ERMKKNMEQTIKdLQQRLDEA----- 1818
Cdd:PRK11281 256 TLS---------EKTVQEAQSQDEAAR--IQANPLVAQELEINLQLSQRLlkatEKLNTLTQQNLR-VKNWLDRLtqser 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1819 ---EQI-ALKGG-------KKQLQKLEArvRELDNELeaeqkrnAESVKGMRKYerrIKELTYQteedRKNLARLQDLVD 1887
Cdd:PRK11281 324 nikEQIsVLKGSlllsrilYQQQQALPS--ADLIEGL-------ADRIADLRLE---QFEINQQ----RDALFQPDAYID 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1888 KLQlkvktyKRQAEESEEQANTSLskfrkvqheLDEAEERADIAEsQVNK 1937
Cdd:PRK11281 388 KLE------AGHKSEVTDEVRDAL---------LQLLDERRELLD-QLNK 421
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1343-1495 |
5.32e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 54.40 E-value: 5.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1343 AKNALAHALQSARHDSDLLREqfEEEQEAKAELQRILSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRlqeaeeaV 1422
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILE--EAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQK-------E 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1072253241 1423 EAVNAKCSSLEKTKHRLQNEIEDlmvdlersnaaaaaLDKKQRNFDKILAEWKQKFEESQTELES----SQKEARSL 1495
Cdd:PRK12704 96 ENLDRKLELLEKREEELEKKEKE--------------LEQKQQELEKKEEELEELIEEQLQELERisglTAEEAKEI 158
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1647-1915 |
5.35e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.00 E-value: 5.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1647 LSQANRQAAEAQKQvkilqsyLKDTQIQLDDALRASEDLKENIAIVERRNTLLQAELEELRSLVEQTERARKLSEQELie 1726
Cdd:COG4942 15 AAAQADAAAEAEAE-------LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1727 tservqllhsqnTSLINQKKKMESDLSQLQTEMEEAVqecRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQ 1806
Cdd:COG4942 86 ------------AELEKEIAELRAELEAQKEELAELL---RALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARRE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1807 TIKDLQQRLDEAEQI--ALKGGKKQLQKLEARVRELDNELEAEQKRNAESVKgmrKYERRIKELTYQTEEDRKNLARLQD 1884
Cdd:COG4942 151 QAEELRADLAELAALraELEAERAELEALLAELEEERAALEALKAERQKLLA---RLEKELAELAAELAELQQEAEELEA 227
|
250 260 270
....*....|....*....|....*....|.
gi 1072253241 1885 LVDKLQlkvktyKRQAEESEEQANTSLSKFR 1915
Cdd:COG4942 228 LIARLE------AEAAAAAERTPAAGFAALK 252
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
1212-1503 |
6.34e-07 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 54.47 E-value: 6.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1212 KKHADSVAELSEQIDNLQRVKQKLEKEKSEF---KLELDDVTSNMEQMVKAKANLEKLCRSLEDQANEHRTKSEENQRTV 1288
Cdd:pfam09726 346 RSHSHNSGSVTSSSSSKNSKKQKGPGGKSGArhkDPAENCIPNNQLSKPDALVRLEQDIKKLKAELQASRQTEQELRSQI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1289 NELSSLRAKLQTENGELSRRLDEKESLVSQMTRGKQTYTQHLEDLKRQLEEETKAKNALAHALQSARHdsdllREQFEEE 1368
Cdd:pfam09726 426 SSLTSLERSLKSELGQLRQENDLLQTKLHNAVSAKQKDKQTVQQLEKRLKAEQEARASAEKQLAEEKK-----RKKEEEA 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1369 QEAKAELQRILSKANSevaqwrtkyeTDAI-QRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRlQNEIEDLM 1447
Cdd:pfam09726 501 TAARAVALAAASRGEC----------TESLkQRKRELESEIKKLTHDIKLKEEQIRELEIKVQELRKYKES-EKDTEVLM 569
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1072253241 1448 vdlersNAAAAALDKKQRNFDKILAEWKQKFE------ESQTELESSQKEARSLSTELFKLK 1503
Cdd:pfam09726 570 ------SALSAMQDKNQHLENSLSAETRIKLDlfsalgDAKRQLEIAQGQIYQKDQEIKDLK 625
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1272-1488 |
6.84e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.61 E-value: 6.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1272 DQANEHRTKSEENQRTVNELSSLRAKLQTENGELSRRLDEKESLVSQMTRGKQTYTQHLEDLKRQLEEETKAKNALAHAL 1351
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1352 QSARHD-SDLLREQFEEEQEAKAELqrILSKANSEVAQWRTKY----------ETDAIQRT-EELEEAKKKLAQRLQEAE 1419
Cdd:COG4942 100 EAQKEElAELLRALYRLGRQPPLAL--LLSPEDFLDAVRRLQYlkylaparreQAEELRADlAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1072253241 1420 EAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAALDKKQRNFDKILAEWKQKFEESQTELESS 1488
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1369-1607 |
6.84e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.61 E-value: 6.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1369 QEAKAELQRILSKANSEVAQwrtkyetdAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMv 1448
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAE--------LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1449 dlERSNAAAAALDKKQRNFDKILAEWKQKFEESQTELESSQKEARSLSTELFKLKNAYEESLDHLETFKRENKNLQEEIS 1528
Cdd:COG4942 90 --KEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1072253241 1529 DLTEQLGESGKSIHELEKIRKQLDQEKMEIQSALEEAEATLEHEEgkilhAQLELHQIKADSERKLAEKDEEMEQAKRN 1607
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELA-----AELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1751-1950 |
1.14e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1751 DLSQLQTEMEEAvQECRNAEEKAKKAitdaammAEELKKEQDTSAHLERMKK-----NMEQTIKDLQQRLDEAEQiALKG 1825
Cdd:COG4913 236 DLERAHEALEDA-REQIELLEPIREL-------AERYAAARERLAELEYLRAalrlwFAQRRLELLEAELEELRA-ELAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1826 GKKQLQKLEARVRELDNEL-EAEQKRNAESVKGMRKYERRIKELTYQTEEDRKNLARLQDLVDKLQLKV----KTYKRQA 1900
Cdd:COG4913 307 LEAELERLEARLDALREELdELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLpasaEEFAALR 386
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1901 EESEEQANTSLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDVSTKKS 1950
Cdd:COG4913 387 AEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKS 436
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1698-1948 |
1.20e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.91 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1698 LLQAELEELRSLVEQ-------TERaRKLSEQELIETSERVQLLHSQNTSLINQKKKMesdlsQLQTEMEEAVQECRNAE 1770
Cdd:TIGR02168 149 IIEAKPEERRAIFEEaagiskyKER-RKETERKLERTRENLDRLEDILNELERQLKSL-----ERQAEKAERYKELKAEL 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1771 EKAKKAItdAAMMAEELKKEQDTsahLERMKKNMEQTIKDLQQRLDEAEQialkggkkQLQKLEARVRELDNELEAEQKR 1850
Cdd:TIGR02168 223 RELELAL--LVLRLEELREELEE---LQEELKEAEEELEELTAELQELEE--------KLEELRLEVSELEEEIEELQKE 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1851 NAESVKGMRKYERRIKELTYQTEEDRKNLARLQDLVDKLQLKVKTYKRQAEESEEQANTSLSKFRKVQHELDEAEERADI 1930
Cdd:TIGR02168 290 LYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEE 369
|
250
....*....|....*...
gi 1072253241 1931 AESQVNKLRAKSRDVSTK 1948
Cdd:TIGR02168 370 LESRLEELEEQLETLRSK 387
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1683-1915 |
1.24e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.48 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1683 EDLKENIAIVERRNTLLQAELEELRSLVEQTERARK--LSEQELIETSERVQLLHSQNTSLINQKKKMESDLSQLQTEME 1760
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1761 eAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQ---TIKDLQQRLDEAEQialkggkkqlqKLEARV 1837
Cdd:COG3206 244 -ALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPnhpDVIALRAQIAALRA-----------QLQQEA 311
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1072253241 1838 RELDNELEAEQKRNAESVKGMRKYERRIKELTYQTEEDRKNLARLQDLVDKLQLKVKTYKRQAEESEEQANTSLSKFR 1915
Cdd:COG3206 312 QRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVR 389
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1399-1629 |
1.34e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.84 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1399 QRTEELEEAKKKLAQ---RLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAALDKKQRNFDKILAEWK 1475
Cdd:COG4942 24 EAEAELEQLQQEIAElekELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1476 QKFEESqteLESSQKEARSLSTELFKLKNAYEESLDHLETFKRENKNLQEEISDLTEQLgesgksiHELEKIRKQLDQEK 1555
Cdd:COG4942 104 EELAEL---LRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL-------AELAALRAELEAER 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1072253241 1556 meiqSALEEAEATLEHEEGKILHAQLELHQIKADSERKLAEKDEEMEQAKRNYQRMVDTLQtSLEAETRSRNEA 1629
Cdd:COG4942 174 ----AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA-RLEAEAAAAAER 242
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
849-1163 |
1.47e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.53 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 849 KLYFKIKPLLKSAETEKEMQTMKEEFQKLKEALEKSEARRKDLEEKMVSLLQEKNDLQLQVQAEQDNLADADERCEQLIK 928
Cdd:PRK03918 477 KLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKK 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 929 NKIQLEAKLKEQTERLEDEEEMNAELTAKKRK-LEDECSELKKdIDDLELTLAKVEKEKHATENKVKNLTEEmagLDEII 1007
Cdd:PRK03918 557 KLAELEKKLDELEEELAELLKELEELGFESVEeLEERLKELEP-FYNEYLELKDAEKELEREEKELKKLEEE---LDKAF 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1008 VKLTKEKKALQEAHQQaLDDLQAEEDKvntltkakakleqqvDDLEGSLEQEKKIRMDLERVKRKLEGDVKLSQESLMDL 1087
Cdd:PRK03918 633 EELAETEKRLEELRKE-LEELEKKYSE---------------EEYEELREEYLELSRELAGLRAELEELEKRREEIKKTL 696
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1072253241 1088 ENDKQQLEEkLKKKDFEVSQLNTRIEDEQNvciqLQKKMKELQARIeeleeeleaERTARAKVEKLRCDLSRELEE 1163
Cdd:PRK03918 697 EKLKEELEE-REKAKKELEKLEKALERVEE----LREKVKKYKALL---------KERALSKVGEIASEIFEELTE 758
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1484-1938 |
1.54e-06 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 53.21 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1484 ELESSQKEARSLSTELFKLKNAYEESLDHLEtfkRENKNLQEEISD----LTEQLGESGKSIHELEKIRKQLDQEKMEIQ 1559
Cdd:pfam05557 62 KREAEAEEALREQAELNRLKKKYLEALNKKL---NEKESQLADAREviscLKNELSELRRQIQRAELELQSTNSELEELQ 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1560 SALEEAEATLEHEEgkILHAQLEL-HQIKADSERKLAEKDEEMEQakrnyqrmvdtlQTSLEAETRSRNEALRIKKKMEG 1638
Cdd:pfam05557 139 ERLDLLKAKASEAE--QLRQNLEKqQSSLAEAEQRIKELEFEIQS------------QEQDSEIVKNSKSELARIPELEK 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1639 DLNemeiQLSQANRQAAEAQKQVKILQSYLKDTQIQLDdalrASEDLKENIAIVERRNTLLQAELEELRSLVEQTerarK 1718
Cdd:pfam05557 205 ELE----RLREHNKHLNENIENKLLLKEEVEDLKRKLE----REEKYREEAATLELEKEKLEQELQSWVKLAQDT----G 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1719 LSEQELIETSERVQLLHSQNTSLINQKKKMESDLSQLQTEMEEAVQECRNAEEKakkaitdaammAEELKKEqdtsahle 1798
Cdd:pfam05557 273 LNLRSPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKK-----------IEDLNKK-------- 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1799 rmKKNMEQTIKDLQQRLDEAeqialkggKKQLQKLEARVRELDNELEAEQ------KRNAESVKGMRKYERRIKELTYQT 1872
Cdd:pfam05557 334 --LKRHKALVRRLQRRVLLL--------TKERDGYRAILESYDKELTMSNyspqllERIEEAEDMTQKMQAHNEEMEAQL 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1072253241 1873 EEDRKNLARLQDLVDKLQLKVKTYKRQAEESEEQANTSL--SKFRKVQH---ELDEAEERADIAESQVNKL 1938
Cdd:pfam05557 404 SVAEEELGGYKQQAQTLERELQALRQQESLADPSYSKEEvdSLRRKLETlelERQRLREQKNELEMELERR 474
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1003-1442 |
1.61e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1003 LDEIIVKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKIRMDLERVKRKLEGDVKLsQE 1082
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL-LP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1083 SLMDLENDKQQLE------EKLKKKDFEVSQLNTRIEDEQNVCIQLQKKMKEL--------QARIEELEEELEAERTARA 1148
Cdd:COG4717 130 LYQELEALEAELAelperlEELEERLEELRELEEELEELEAELAELQEELEELleqlslatEEELQDLAEELEELQQRLA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1149 KVEKLRCDLSRELEEISERLEEAGGATSVQMELNKKREAE-----------FLKLRRDLEESTLHSEATAAS-------- 1209
Cdd:COG4717 210 ELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARlllliaaallaLLGLGGSLLSLILTIAGVLFLvlgllall 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1210 ---LRKKHADSVAELSEQIDNLQR---VKQKLEKEKSEFKLELDDVTSNMEQMVKAKANLEKLCRSLEDQANEHRTKSEE 1283
Cdd:COG4717 290 fllLAREKASLGKEAEELQALPALeelEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1284 nqrtvNELSSLRAKLQTENGE-LSRRLDEKESlvsqmtrgKQTYTQHLEDLKRQLEEETKAKNALAhalqsARHDSDLLR 1362
Cdd:COG4717 370 -----QEIAALLAEAGVEDEEeLRAALEQAEE--------YQELKEELEELEEQLEELLGELEELL-----EALDEEELE 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1363 EQFEEEQEAKAELQRILSKANSEVAqwRTKYETDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKC---SSLEKTKHRL 1439
Cdd:COG4717 432 EELEELEEELEELEEELEELREELA--ELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKlalELLEEAREEY 509
|
...
gi 1072253241 1440 QNE 1442
Cdd:COG4717 510 REE 512
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
987-1170 |
1.65e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.46 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 987 HATENKVKNLTEEMAGLDEIIVKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSL----EQEKKI 1062
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELaeleKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1063 RMDLERVKRKLEG--------------DVKLSQESLMDLENDKQQLEEKLKKKDFEVSQLNTRIEDEQNVCIQLQKKMKE 1128
Cdd:COG4942 96 RAELEAQKEELAEllralyrlgrqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1072253241 1129 LQARIEELEEELEAERTARAKVEKLRCDLSRELEEISERLEE 1170
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1292-1845 |
2.11e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 53.03 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1292 SSLRAKLQTENGELSRRLDEKESLV--SQMTRGKQTYTQHLEDLKRQLEEETKAKNA---LAHALQSARHDSDLL----- 1361
Cdd:COG3096 214 RSLRDYLLPENSGVRKAFQDMEAALreNRMTLEAIRVTQSDRDLFKHLITEATNYVAadyMRHANERRELSERALelrre 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1362 ----REQFEEEQEAKAELQRILskansevaqwrtkyetdaiqrtEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKH 1437
Cdd:COG3096 294 lfgaRRQLAEEQYRLVEMAREL----------------------EELSARESDLEQDYQAASDHLNLVQTALRQQEKIER 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1438 RlQNEIEDLMVDLERSNAAAAALDKKQrnfdkilaewkqkfEESQTELESSQKEARSLSTELFKlknaYEESLDHLETfk 1517
Cdd:COG3096 352 Y-QEDLEELTERLEEQEEVVEEAAEQL--------------AEAEARLEAAEEEVDSLKSQLAD----YQQALDVQQT-- 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1518 renKNLQEEisdlteqlgesgKSIHELEKIRKQLDQEKMEIQSAlEEAEATLEHEEGKILHAQLELHQikadserKLAEK 1597
Cdd:COG3096 411 ---RAIQYQ------------QAVQALEKARALCGLPDLTPENA-EDYLAAFRAKEQQATEEVLELEQ-------KLSVA 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1598 DEemeqAKRNYqrmvdtlqtsleaetrsrNEALRIKKKMEGdlnemEIQLSQANRQAAEAqkqvkilqsylkdtqiqldd 1677
Cdd:COG3096 468 DA----ARRQF------------------EKAYELVCKIAG-----EVERSQAWQTAREL-------------------- 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1678 aLRASEDLKeniAIVERRNTLlQAELEELRSLVEQTERARKLSEqeliETSERVQLLHSQNTSLINQKKKMESDLSQLQT 1757
Cdd:COG3096 501 -LRRYRSQQ---ALAQRLQQL-RAQLAELEQRLRQQQNAERLLE----EFCQRIGQQLDAAEELEELLAELEAQLEELEE 571
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1758 EMEEAVQ---ECRNAEEKAKKAITDAAMMAEELKKEQDTsahLERMKKNMEQTIKDLQQrLDEAEQIAL---KGGKKQLQ 1831
Cdd:COG3096 572 QAAEAVEqrsELRQQLEQLRARIKELAARAPAWLAAQDA---LERLREQSGEALADSQE-VTAAMQQLLereREATVERD 647
|
570
....*....|....
gi 1072253241 1832 KLEARVRELDNELE 1845
Cdd:COG3096 648 ELAARKQALESQIE 661
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
851-1426 |
2.19e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 52.98 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 851 YFKIKPLLKSAETE-KEMQTMKEEFQKLKEALEKSEARRKDLEEKMVSLLQEKNDLQLQVQAEQDNLADADE---RCEQL 926
Cdd:PRK01156 168 YDKLKDVIDMLRAEiSNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSalnELSSL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 927 IKNKIQLEAKLKEQTERLEDEEEMNAELTAKKRKLedecselkkdiddLELTLAKVEKEKHATeNKVKNLTEEMAGLDEI 1006
Cdd:PRK01156 248 EDMKNRYESEIKTAESDLSMELEKNNYYKELEERH-------------MKIINDPVYKNRNYI-NDYFKYKNDIENKKQI 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1007 IVKLTKEKKALQEAHQQaLDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKIRMDLERVKRKLEgdvklsqESLMD 1086
Cdd:PRK01156 314 LSNIDAEINKYHAIIKK-LSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIE-------EYSKN 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1087 LENDKQQLEEKLKKKDFEVSQLNTRIEDEQNVCIQLQKKMKELQARIEELEEELEAERTARA------------------ 1148
Cdd:PRK01156 386 IERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEmlngqsvcpvcgttlgee 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1149 KVEKLRCDLSRELEEISERLEEAGGATSvqmELNKKREAEFLKLRRDLEESTLHSEATAASLRKKHADsVAELSEQIDNL 1228
Cdd:PRK01156 466 KSNHIINHYNEKKSRLEEKIREIEIEVK---DIDEKIVDLKKRKEYLESEEINKSINEYNKIESARAD-LEDIKIKINEL 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1229 QRVKQKLEKEKSEFK-LELDDVTSNMEQMVKAKANLEKL-CRSLEDQANEHRTKSEENQRTVNELSSLRAKLQTENGELS 1306
Cdd:PRK01156 542 KDKHDKYEEIKNRYKsLKLEDLDSKRTSWLNALAVISLIdIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSI 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1307 RRLDEKESLVsqmtRGKQTYTQHLEDLKRQLEEETKAKNALAHALQSARHDSDLLREQFEEEQEAKAELQRILSKANSEV 1386
Cdd:PRK01156 622 REIENEANNL----NNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANR 697
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1072253241 1387 AQWRTKYETDaIQRTEELEEAKKKLAQRLQEAEEAVEAVN 1426
Cdd:PRK01156 698 ARLESTIEIL-RTRINELSDRINDINETLESMKKIKKAIG 736
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1760-1935 |
2.34e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 52.55 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1760 EEAVQECRNAE--EKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQQRLDEAEQialkggkkQLQKLEARV 1837
Cdd:COG2433 379 EEALEELIEKElpEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDE--------RIERLEREL 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1838 RELDNELEAEQKRNAEsvkgMRKYERRIKELTYQTEEDRKNLARLQDLVDKLqlkvktykRQAEESEEQANTS----LSK 1913
Cdd:COG2433 451 SEARSEERREIRKDRE----ISRLDREIERLERELEEERERIEELKRKLERL--------KELWKLEHSGELVpvkvVEK 518
|
170 180
....*....|....*....|..
gi 1072253241 1914 FRKvqHELDEAEERADIAESQV 1935
Cdd:COG2433 519 FTK--EAIRRLEEEYGLKEGDV 538
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1750-1944 |
2.62e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.07 E-value: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1750 SDLSQLQTEMEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQQRLDEAEQiALKGGKKQ 1829
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK-EIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1830 LQKLEARVRELDNELEAEQKRN-----------AESVKGMRKYERRIKELTYQTEEDRKNLARLQDLVDKLQLKVKTYKR 1898
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1072253241 1899 QAEESEEQANTSLSKFRKVQHELDEAEERADIAESQVNKLRAKSRD 1944
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1081-1661 |
2.65e-06 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 52.44 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1081 QESLMDLENDKQQLEEKLKKKDFEVSQLNTRIEDEQNVCIQLQKKMKELQARIeeleeeleaertarakveklrcdlsre 1160
Cdd:pfam05557 5 IESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRI--------------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1161 lEEISERLEEAGGATSVQMELNKKREAEFLKLRRDLEESTLhSEATAASLRKKHADSVAELSEQIDNLQRVKQKLEKEKS 1240
Cdd:pfam05557 58 -RLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKES-QLADAREVISCLKNELSELRRQIQRAELELQSTNSELE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1241 EFKLELDDVTSNMEQMVKAKANLEKLCRSLEDQANEHRTKSEENQRTVN---ELSSLRAKLQT--ENGELSRRLDEKESL 1315
Cdd:pfam05557 136 ELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQdseIVKNSKSELARipELEKELERLREHNKH 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1316 VSQMTRGKQTYTQHLEDLKRQLeeetkaknalahalqsarhdsdllrEQFEEEQEAKAELQRILSKANSEVAQWRTKYET 1395
Cdd:pfam05557 216 LNENIENKLLLKEEVEDLKRKL-------------------------EREEKYREEAATLELEKEKLEQELQSWVKLAQD 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1396 DA--IQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNE-------IEDLMVDLERSNAAAAALDK---- 1462
Cdd:pfam05557 271 TGlnLRSPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQElaqylkkIEDLNKKLKRHKALVRRLQRrvll 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1463 --KQRNFDKILAEwkqKFEESQTELESSQKEA---RSLSTELFKLKNAYEESLDHLETFKRENKNLQEEISDL------- 1530
Cdd:pfam05557 351 ltKERDGYRAILE---SYDKELTMSNYSPQLLeriEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLerelqal 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1531 --TEQLGESGKSIHELEKIRKQLDQEKMEIQSaLEEAEATLEheegkilhAQLELHQIKADSERK----LAEKDEEMEQA 1604
Cdd:pfam05557 428 rqQESLADPSYSKEEVDSLRRKLETLELERQR-LREQKNELE--------MELERRCLQGDYDPKktkvLHLSMNPAAEA 498
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 1072253241 1605 KRNYQRMVDTLQTSLEAeTRSRNEALRIKKKMEGDLNEMEIQLsqANRQAAEAQKQV 1661
Cdd:pfam05557 499 YQQRKNQLEKLQAEIER-LKRLLKKLEDDLEQVLRLPETTSTM--NFKEVLDLRKEL 552
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1396-1722 |
2.80e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 52.61 E-value: 2.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1396 DAIQRTEELEEAKKKLAQRLQEAEE---AVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAAlDKKQRNFDKILA 1472
Cdd:PRK11281 46 DALNKQKLLEAEDKLVQQDLEQTLAlldKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDE-ETRETLSTLSLR 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1473 EWKQKFEESQTELESSQKEARSLSTELFKLKNAYEesldhletfkrenkNLQEEISDLTEQLGEsgksihelekIRKQLD 1552
Cdd:PRK11281 125 QLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPE--------------RAQAALYANSQRLQQ----------IRNLLK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1553 QEKMEiQSALEEAEATLEHEEGKILHAQLELHQIKADSERKLaekdEEMEQAKRNY--------QRMVDTLQTSleaetr 1624
Cdd:PRK11281 181 GGKVG-GKALRPSQRVLLQAEQALLNAQNDLQRKSLEGNTQL----QDLLQKQRDYltariqrlEHQLQLLQEA------ 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1625 srnealrikkkmegdLNEMEIQLSQAN-RQAAEAQKQVKILQSYLkdTQIQLDDALRASEDLkenIAIVERRNTLLQAEL 1703
Cdd:PRK11281 250 ---------------INSKRLTLSEKTvQEAQSQDEAARIQANPL--VAQELEINLQLSQRL---LKATEKLNTLTQQNL 309
|
330 340
....*....|....*....|..
gi 1072253241 1704 E---ELRSLVeQTERArkLSEQ 1722
Cdd:PRK11281 310 RvknWLDRLT-QSERN--IKEQ 328
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1482-1869 |
2.83e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 52.20 E-value: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1482 QTELESSQKEARSLSTELFKLKNAYEESLDHLET----FKRENKNLQEEISDLTEQLGESGKSIHELEKIRKqldqEKME 1557
Cdd:pfam07888 33 QNRLEECLQERAELLQAQEAANRQREKEKERYKRdreqWERQRRELESRVAELKEELRQSREKHEELEEKYK----ELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1558 IQSALEEAEATLEHEEGKILHAQLELHQ-IKADSERKLaEKDEEMEQAKRNYQRMVDTLQtsleaETRSRNEALRIK-KK 1635
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEdIKTLTQRVL-ERETELERMKERAKKAGAQRK-----EEEAERKQLQAKlQQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1636 MEGDLNEMEIQLSQANRQAAEAQKQVKILQSYLKDTQIQLDDAlrasedlkeniaivERRNTLLQAELEELRSLveqter 1715
Cdd:pfam07888 183 TEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTA--------------HRKEAENEALLEELRSL------ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1716 arklseQELIETSER-VQLLHSQNTSLINQKKKMESDLSQLQTEMEE----------AVQECRNAEEKAKKAITDAAMMA 1784
Cdd:pfam07888 243 ------QERLNASERkVEGLGEELSSMAAQRDRTQAELHQARLQAAQltlqladaslALREGRARWAQERETLQQSAEAD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1785 EElkKEQDTSAHLERMKKNMEQTIKDLQQ------RLDEAEQIALKGGKKQLQKLEARVRELDNELEAEQKRNAESVKGM 1858
Cdd:pfam07888 317 KD--RIEKLSAELQRLEERLQEERMEREKlevelgREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYI 394
|
410
....*....|.
gi 1072253241 1859 RKYERRIKELT 1869
Cdd:pfam07888 395 RQLEQRLETVA 405
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1277-1789 |
3.96e-06 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 51.95 E-value: 3.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1277 HRTKSEENQRTVN-ELSslraKLQTENGELSRRLDEKESLVSQMTRGKQTYTQHLEDLKRQLEeetKAKnalaHALQSAR 1355
Cdd:pfam05701 29 HRIQTVERRKLVElELE----KVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEELKLNLE---RAQ----TEEAQAK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1356 HDSDLLREQFEEEQEAKAELQRILSKANSEVAQWR-TKYETDAIQRTEELEEAKKKLAQRLQEAEEAV---EAVNAKCSS 1431
Cdd:pfam05701 98 QDSELAKLRVEEMEQGIADEASVAAKAQLEVAKARhAAAVAELKSVKEELESLRKEYASLVSERDIAIkraEEAVSASKE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1432 LEKTKHRLQNEIEDLMVDLErsNAAAAALDKKQRNFDKILAeWKQKFEESQTELESSQKEARSLSTELFKLKNAYEEsld 1511
Cdd:pfam05701 178 IEKTVEELTIELIATKESLE--SAHAAHLEAEEHRIGAALA-REQDKLNWEKELKQAEEELQRLNQQLLSAKDLKSK--- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1512 hLETFKRENKNLQEEISDLTEqlgesGKSIHELEKiRKQLDQEKMEIQSALEEAEATLEHEEGKILHAQLELHQIKADSE 1591
Cdd:pfam05701 252 -LETASALLLDLKAELAAYME-----SKLKEEADG-EGNEKKTSTSIQAALASAKKELEEVKANIEKAKDEVNCLRVAAA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1592 RKLAEKDEEMEQAKRNYQR--MVDTLQTSLEAE---TRSRNEALRIKKKMEGD-LNEMEIQLSQANRQAAEAQKQVKILQ 1665
Cdd:pfam05701 325 SLRSELEKEKAELASLRQRegMASIAVSSLEAElnrTKSEIALVQAKEKEAREkMVELPKQLQQAAQEAEEAKSLAQAAR 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1666 SYLKD--------------TQIQLDDALRASEDLK--ENIAIVERRnTLLQAELEELRSLVEQTERARKLSEQELIETSE 1729
Cdd:pfam05701 405 EELRKakeeaeqakaaastVESRLEAVLKEIEAAKasEKLALAAIK-ALQESESSAESTNQEDSPRGVTLSLEEYYELSK 483
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1072253241 1730 RVQ----LLH---SQNTSLINQKKKMES----DLSQLQTEMEEAVQECRNAEEKAKKAITDAAMMAEELKK 1789
Cdd:pfam05701 484 RAHeaeeLANkrvAEAVSQIEEAKESELrsleKLEEVNREMEERKEALKIALEKAEKAKEGKLAAEQELRK 554
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1525-1921 |
4.19e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 51.89 E-value: 4.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1525 EEISDLTEQLGESGKSIHELEKIRKQLDQEKMEIQ-SALEEAEATLEHEEGKILHAQLELHQIKA--DSERKLAEKDEEM 1601
Cdd:TIGR00618 179 TQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMpDTYHERKQVLEKELKHLREALQQTQQSHAylTQKREAQEEQLKK 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1602 EQAKRNYQRMVDTLQTsLEAETRSRNEALRIKKKMEGDLNEMEiQLSQANRQAAEAQKQVKILQSYLKDTQIQLDDALRA 1681
Cdd:TIGR00618 259 QQLLKQLRARIEELRA-QEAVLEETQERINRARKAAPLAAHIK-AVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQ 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1682 SEDLKENiaivERRNTLLQAELEELRSLVEQTERARKLSEQELIETsERVQLLHSQNTSLINQKKKMESDLSQLQTEmeE 1761
Cdd:TIGR00618 337 QSSIEEQ----RRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLT-QHIHTLQQQKTTLTQKLQSLCKELDILQRE--Q 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1762 AVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIK-----DLQQRLDEAEQiaLKGGKKQLQKLEAR 1836
Cdd:TIGR00618 410 ATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEkihlqESAQSLKEREQ--QLQTKEQIHLQETR 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1837 VRELDNELEAEQKRNAESVKGMRKYERRIKELTYQTEEDRKNLARLQDLVDKLQLKVKTYKRQAEESEEQANTSLSKFRK 1916
Cdd:TIGR00618 488 KKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQE 567
|
....*
gi 1072253241 1917 VQHEL 1921
Cdd:TIGR00618 568 IQQSF 572
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1355-1735 |
5.24e-06 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 51.30 E-value: 5.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1355 RHDSDLLREQFEEEQEAKAELQRILSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQE-AEEAVEAVNAKCSSLE 1433
Cdd:pfam09731 70 SVVSAVTGESKEPKEEKKQVKIPRQSGVSSEVAEEEKEATKDAAEAKAQLPKSEQEKEKALEEvLKEAISKAESATAVAK 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1434 KTKHRLQNEIEDLMVDLERSNAAAAALDKKQRNFDKILAEWKQKFEESQTELESSQKEARSLSTELFKLKNAyEESLDHL 1513
Cdd:pfam09731 150 EAKDDAIQAVKAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETP-PKLPEHL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1514 ETFKRENKNLQEEISDLTEqlgesgksIHELEKIRKQLDQEKM-----EIQSALEEAEATLEHEEGK-ILHAQLELHQI- 1586
Cdd:pfam09731 229 DNVEEKVEKAQSLAKLVDQ--------YKELVASERIVFQQELvsifpDIIPVLKEDNLLSNDDLNSlIAHAHREIDQLs 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1587 ----------KADSERKLAEKDEEMEQAKRNYQRMVDTLQTSLEAETRSRNEA--LRIKKKMEgdlNEMEIQLSQANRQA 1654
Cdd:pfam09731 301 kklaelkkreEKHIERALEKQKEELDKLAEELSARLEEVRAADEAQLRLEFERerEEIRESYE---EKLRTELERQAEAH 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1655 AEAQKQVKILQsylkdtQIQLDdaLRASEDLKENIAiVERRNTLLQaeLEELRSLVEQTERArKLSEQELIETSERVQLL 1734
Cdd:pfam09731 378 EEHLKDVLVEQ------EIELQ--REFLQDIKEKVE-EERAGRLLK--LNELLANLKGLEKA-TSSHSEVEDENRKAQQL 445
|
.
gi 1072253241 1735 H 1735
Cdd:pfam09731 446 W 446
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1469-1674 |
6.19e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.17 E-value: 6.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1469 KILAEWKQKFEESQTEL--ESSQKEARSLSTELFKLKNAYEESLDHLETFKRENK--NLQEEISDLTEQLGESGKSIHEL 1544
Cdd:COG3206 152 AVANALAEAYLEQNLELrrEEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1545 EKIRKQLDQEKMEIQSAL----EEAEATLEHEEGKILHAQLelhqikADSERKLAEK--------------DEEMEQAKR 1606
Cdd:COG3206 232 RAELAEAEARLAALRAQLgsgpDALPELLQSPVIQQLRAQL------AELEAELAELsarytpnhpdvialRAQIAALRA 305
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1072253241 1607 NYQRMVDTLQTSLEAE---TRSRNEALR-----IKKKMEgDLNEMEIQLSQANRQAAEAQKQVKILQSYLKDTQIQ 1674
Cdd:COG3206 306 QLQQEAQRILASLEAEleaLQAREASLQaqlaqLEARLA-ELPELEAELRRLEREVEVARELYESLLQRLEEARLA 380
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
871-1417 |
8.21e-06 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 50.91 E-value: 8.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 871 KEEFQKLKEALEKSEARRKDLEEKMVSLLQE-----KNDLQLQVQAEQDNLADADERCEQLIKNKIQLEAKLKEQTERL- 944
Cdd:pfam07111 114 QAEAEGLRAALAGAEMVRKNLEEGSQRELEEiqrlhQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLa 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 945 --------------EDEEEMNAELT-----------------------AKKRKLEDECSELKKDIDDL----ELTLAKVE 983
Cdd:pfam07111 194 eaqkeaellrkqlsKTQEELEAQVTlveslrkyvgeqvppevhsqtweLERQELLDTMQHLQEDRADLqatvELLQVRVQ 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 984 KEKHATENKVKNLTEEMAGLDEIIVKLTKEKKALQEAHQQA----LDDLQAEE----DKVNTLTKAKAKLEQQVDD---- 1051
Cdd:pfam07111 274 SLTHMLALQEEELTRKIQPSDSLEPEFPKKCRSLLNRWREKvfalMVQLKAQDlehrDSVKQLRGQVAELQEQVTSqsqe 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1052 ---LEGSLeQEKKIRMDLERVKRK-LEGDVKLSQESLMDLENDKQQLEEKLKkkdFEVSQLNTriedeqnVCIQLQKKMK 1127
Cdd:pfam07111 354 qaiLQRAL-QDKAAEVEVERMSAKgLQMELSRAQEARRRQQQQTASAEEQLK---FVVNAMSS-------TQIWLETTMT 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1128 ELQARIEELEEELEAERTARAKVEKLRCDLSRELEEISERLEEAGGA-------TSVQMELNKKREaeflklrrdleest 1200
Cdd:pfam07111 423 RVEQAVARIPSLSNRLSYAVRKVHTIKGLMARKVALAQLRQESCPPPppappvdADLSLELEQLRE-------------- 488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1201 lhseataaslRKKHADSVAELSEQIDNlQRVKQKLEKEKSEfKLELDDVTSNMEQmvkakaNLEKLCRSLEDQANEHRTK 1280
Cdd:pfam07111 489 ----------ERNRLDAELQLSAHLIQ-QEVGRAREQGEAE-RQQLSEVAQQLEQ------ELQRAQESLASVGQQLEVA 550
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1281 SEENQRTVNELSSLRAKLQTENGELSRRLDEKESLVSQMTRgkqtytQHLEDLKRQLEEetkAKNALAHALQSARHdsdl 1360
Cdd:pfam07111 551 RQGQQESTEEAASLRQELTQQQEIYGQALQEKVAEVETRLR------EQLSDTKRRLNE---ARREQAKAVVSLRQ---- 617
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 1072253241 1361 LREQFEEEQEAKAELQRILSKANSEVAQWRTKyetdaiqRTEELEEAKKKLAQRLQE 1417
Cdd:pfam07111 618 IQHRATQEKERNQELRRLQDEARKEEGQRLAR-------RVQELERDKNLMLATLQQ 667
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
861-1032 |
9.17e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 9.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 861 AETEKEMQTMKEEFQKLKEALEKSEA----RRKDLEEKMVSLLQEKNDLQ-LQVQAEQDNLADADERCEQLikNKIQlea 935
Cdd:COG3883 54 NELQAELEALQAEIDKLQAEIAEAEAeieeRREELGERARALYRSGGSVSyLDVLLGSESFSDFLDRLSAL--SKIA--- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 936 klKEQTERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIVKLTKEKK 1015
Cdd:COG3883 129 --DADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
|
170
....*....|....*..
gi 1072253241 1016 ALQEAHQQALDDLQAEE 1032
Cdd:COG3883 207 AAEAAAAAAAAAAAAAA 223
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1412-1657 |
9.20e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.15 E-value: 9.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1412 AQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAALDKKQRNFDKILAEwkqkfeeSQTELESSQKE 1491
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA-------LEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1492 ARSLSTELFKLKNAYEESLDHLETFKRENKNLQEEISDLTEQLGESGKSIHELEKIRKQLDQEKMEIQSALEEAEATLEH 1571
Cdd:COG4942 92 IAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1572 EegkilhaqlelHQIKADSERKLAEKDEEMEQAKRNYQRMVDTLQTSLEAETRSRNEALRIKKKMEGDLNEMEIQLSQAN 1651
Cdd:COG4942 172 E-----------RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
....*.
gi 1072253241 1652 RQAAEA 1657
Cdd:COG4942 241 ERTPAA 246
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1591-1820 |
9.63e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.79 E-value: 9.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1591 ERKLAEKDEEMEQAKRNYQRMVDTLQTSLEaETRSRNEALRIKKKM---EGDLNEMEIQLSQANRQAAEAQKQVKILQSY 1667
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELE-EAEAALEEFRQKNGLvdlSEEAKLLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1668 LKDTQIQLDDALRASEDLKENIAIVERRNTLLQAELEelrsLVEQTERARklseqeliETSERVQLLHSQNTSLinqKKK 1747
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAE----LAELSARYT--------PNHPDVIALRAQIAAL---RAQ 306
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1072253241 1748 MESDLSQLQTEMEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQQRLDEAEQ 1820
Cdd:COG3206 307 LQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARL 379
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1436-1814 |
9.76e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 50.89 E-value: 9.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1436 KHRLQNEIEDLMVDLERSNAAAAALDKKQRNFDK---ILAEWKQKFEESQTELESSQKEARslstelfklknayeesldh 1512
Cdd:pfam17380 298 QERLRQEKEEKAREVERRRKLEEAEKARQAEMDRqaaIYAEQERMAMERERELERIRQEER------------------- 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1513 letfKRENKNLQEEisdlteQLGESGKSIHELEKIRKQLDQEKMEIQSALEEAEATLEHEEgkilhaqlelhqikaDSER 1592
Cdd:pfam17380 359 ----KRELERIRQE------EIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEE---------------ERQR 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1593 KLAEKDEEMEQAKRNyqrmvdtlqtsleaETRSRNEALRIKKKmegdlnEMEIQLSQANRQAAEAQKQVKILQSYLKDTQ 1672
Cdd:pfam17380 414 KIQQQKVEMEQIRAE--------------QEEARQREVRRLEE------ERAREMERVRLEEQERQQQVERLRQQEEERK 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1673 IQLDDALRASEDLKEniaIVERRNTLLQAELEELRSLVEQTERARKLSEQELIEtservqllhSQNTSLINQKKKMESDL 1752
Cdd:pfam17380 474 RKKLELEKEKRDRKR---AEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEE---------RQKAIYEEERRREAEEE 541
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1072253241 1753 SQLQTEMEEavqecrnaeekaKKAITDAAMMAEELKKEQDTsahLERMKKNMEQTIKDLQQR 1814
Cdd:pfam17380 542 RRKQQEMEE------------RRRIQEQMRKATEERSRLEA---MEREREMMRQIVESEKAR 588
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1772-1944 |
1.07e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1772 KAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQQRLDEAEqialkggkKQLQKLEARVRELDNELEAEQKRN 1851
Cdd:COG1196 219 KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELE--------AELEELRLELEELELELEEAQAEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1852 AESVKGMRKYERRIKELTYQTEEDRKNLARLQDLVDKLQLKVKTYKRQAEESEEQANTSLSKFRKVQHELDEAEERADIA 1931
Cdd:COG1196 291 YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370
|
170
....*....|...
gi 1072253241 1932 ESQVNKLRAKSRD 1944
Cdd:COG1196 371 EAELAEAEEELEE 383
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
990-1376 |
1.16e-05 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 50.34 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 990 ENKVKNLTEEMAGLDEIIVKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKIRMDLERV 1069
Cdd:COG5185 172 LNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQT 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1070 ----KRKLEGDVKLSQESLMDLENDKQQLEEKLKKKDFEVSQLNTRIED--EQNVCIQLQKKMKELQARIEELEEELEAE 1143
Cdd:COG5185 252 sdklEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEytKSIDIKKATESLEEQLAAAEAEQELEESK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1144 RTARAKVEKLRCDLSRELEEISERLEEAGGATSvqmelNKKREAEFLKLRRDLEESTLHSEATAASLRKKHADSVAELSE 1223
Cdd:COG5185 332 RETETGIQNLTAEIEQGQESLTENLEAIKEEIE-----NIVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1224 QIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQMVKAKANLEKlcrslEDQANEHRTKSEENQRTVNELSSLRAKLQTENG 1303
Cdd:COG5185 407 ILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELIS-----ELNKVMREADEESQSRLEEAYDEINRSVRSKKE 481
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1072253241 1304 ELSRRLDEKESLVSQMTRGKQTYTQHLEdlkRQLEEETKAKNALAHALQSARHDSDLLREQFEEEQEAKAELQ 1376
Cdd:COG5185 482 DLNEELTQIESRVSTLKATLEKLRAKLE---RQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASELI 551
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1507-1847 |
1.21e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 50.07 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1507 EESLDHLETFKRENKNLQEEISDLTEQLGESGKSIHELEKIRKQ-------LDQEKMEIQSALEEAEATLEHEEGKILHA 1579
Cdd:pfam19220 16 ADRLEDLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQeraaygkLRRELAGLTRRLSAAEGELEELVARLAKL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1580 QLELHQIKADSERKLAEKDEEMEQAKRnyqrmvdtLQTSLEAETRSR------NEALRIK-KKMEGDLNEMEIQLSQANR 1652
Cdd:pfam19220 96 EAALREAEAAKEELRIELRDKTAQAEA--------LERQLAAETEQNraleeeNKALREEaQAAEKALQRAEGELATARE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1653 QAAEAQKQVKILQSYLKDTQIQLDDALRASEDLKEniaivERRNTLLQAELEELRSLVEQTERARKLSEQELIETSERVQ 1732
Cdd:pfam19220 168 RLALLEQENRRLQALSEEQAAELAELTRRLAELET-----QLDATRARLRALEGQLAAEQAERERAEAQLEEAVEAHRAE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1733 L--LHSQNTSLINQKKKMESDLSQLQTEMEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQ---- 1806
Cdd:pfam19220 243 RasLRMKLEALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRarae 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1072253241 1807 ------------------------TIKDLQQRLDEAEQIALKggkkQLQKLEARVRELDNELEAE 1847
Cdd:pfam19220 323 leeraemltkalaakdaaleraeeRIASLSDRIAELTKRFEV----ERAALEQANRRLKEELQRE 383
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1144-1884 |
1.40e-05 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 50.59 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1144 RTARAKVEKLRCDLSRELEEI---SERL--EEAGGATSVQMELNkkreAEFLKLRRDLEESTLHSEATAASlrkkHADsv 1218
Cdd:NF041483 79 RNAQIQADQLRADAERELRDAraqTQRIlqEHAEHQARLQAELH----TEAVQRRQQLDQELAERRQTVES----HVN-- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1219 aelseqiDNLQRVKQKLEKEKSEFKLELDDVTSNMEQMVKAKanleklcrsledQANEHRTKSEENQRTVNELSSLRAKL 1298
Cdd:NF041483 149 -------ENVAWAEQLRARTESQARRLLDESRAEAEQALAAA------------RAEAERLAEEARQRLGSEAESARAEA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1299 QTengELSRRLDEKESLVSQMTRGKQTYTQHLEDLKRQLEEETKAknALAHALQSARHDSDLLREQFEEEQEAKAELQRI 1378
Cdd:NF041483 210 EA---ILRRARKDAERLLNAASTQAQEATDHAEQLRSSTAAESDQ--ARRQAAELSRAAEQRMQEAEEALREARAEAEKV 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1379 LSKANSEVAQWRTKYETDAIQRTeelEEAKKKLAQRLQEAEEAVEAVNAKCsslEKTKHRLQNEIEDLMVDLE---RSNA 1455
Cdd:NF041483 285 VAEAKEAAAKQLASAESANEQRT---RTAKEEIARLVGEATKEAEALKAEA---EQALADARAEAEKLVAEAAekaRTVA 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1456 A---AAALDKKQRNFDKIL--------AEWKQKFEESQTELESSQKEARSLSTELF----KLKNAYEeslDHLETFKREN 1520
Cdd:NF041483 359 AedtAAQLAKAARTAEEVLtkasedakATTRAAAEEAERIRREAEAEADRLRGEAAdqaeQLKGAAK---DDTKEYRAKT 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1521 KNLQEEISDL---TEQLgeSGKSIHELEKIRKQLDQEKMEiqsALEEAEATLEHEEGKILHAQLELHQ-IKADSERKLAE 1596
Cdd:NF041483 436 VELQEEARRLrgeAEQL--RAEAVAEGERIRGEARREAVQ---QIEEAARTAEELLTKAKADADELRStATAESERVRTE 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1597 KDEEMEQAKRNYQrmvdtlqtslEAETRSRNEALRIKKKMEgdlNEMEIQLSQANRQAAEAQKQVkilQSYLKDTQIQLD 1676
Cdd:NF041483 511 AIERATTLRRQAE----------ETLERTRAEAERLRAEAE---EQAEEVRAAAERAARELREET---ERAIAARQAEAA 574
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1677 DAL-RASEDLKENIAIVERRNTLLQAELEELRS-LVEQTERARKlseqeliETSERVQLLHSQntslinqkkkMESDLSQ 1754
Cdd:NF041483 575 EELtRLHTEAEERLTAAEEALADARAEAERIRReAAEETERLRT-------EAAERIRTLQAQ----------AEQEAER 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1755 LQTE-MEEAVQECRNAEEKAKKAITDAAMMAEELKKE-QDTS--------AHLERMKKNMEQTIKDLQQ----RLDEAEQ 1820
Cdd:NF041483 638 LRTEaAADASAARAEGENVAVRLRSEAAAEAERLKSEaQESAdrvraeaaAAAERVGTEAAEALAAAQEeaarRRREAEE 717
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1072253241 1821 IaLKGGKKQLQKLEARVRELDNELEAEQKR-----NAESVKGMRKYERRIKELTYQTEED----RKNLARLQD 1884
Cdd:NF041483 718 T-LGSARAEADQERERAREQSEELLASARKrveeaQAEAQRLVEEADRRATELVSAAEQTaqqvRDSVAGLQE 789
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1275-1570 |
1.84e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 48.76 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1275 NEHRTKSEENQRTVNELSSLRAkLQTENGELSRRLDEKESLVS-QMTRGKQTYTQHLEDLKRQLEEETKAKNALAHALQS 1353
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRF-LEQQNKLLETKISELRQKKGaEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1354 ARHDSDLLREQFEEE----QEAKAELQrILSKANSEVAQWRTKYETDAIQRTEEL-------EEAKKKLAQRLQEAEEAV 1422
Cdd:pfam00038 80 LRLAAEDFRQKYEDElnlrTSAENDLV-GLRKDLDEATLARVDLEAKIESLKEELaflkknhEEEVRELQAQVSDTQVNV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1423 EAVNAKCSSLEKTKHRLQNEIEDLMvdlersnaaaaaldkkQRNFDKILAEWKQKFEESQTELESSQKEARSLSTELFKL 1502
Cdd:pfam00038 159 EMDAARKLDLTSALAEIRAQYEEIA----------------AKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITEL 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1072253241 1503 KNAYEESLDHLETFKRENKNLQEEISDLTEQLGesgksiHELEKIRKQLDQEKMEIQSALEEAEATLE 1570
Cdd:pfam00038 223 RRTIQSLEIELQSLKKQKASLERQLAETEERYE------LQLADYQELISELEAELQETRQEMARQLR 284
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1768-1945 |
1.86e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1768 NAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQQRLDEAEqIALKGGKKQLQKLEARVRELD---NEL 1844
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEIS-SELPELREELEKLEKEVKELEelkEEI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1845 EAEQKRNAESVKGMRKYERRIKELTYQTEEDRKNLARLQDLVDKLQlKVKTYKRQAEESEEQANTSLSKFRKVQHELDEA 1924
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRL 319
|
170 180
....*....|....*....|.
gi 1072253241 1925 EERADIAESQVNKLRAKSRDV 1945
Cdd:PRK03918 320 EEEINGIEERIKELEEKEERL 340
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1453-1682 |
1.97e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1453 SNAAAAALDKKQRNFDKILAEWKQKFEESQTELESSQKEARSLSTELFKLKNAYEESLDHLETFKRENKNLQEEISDLTE 1532
Cdd:COG3883 7 AAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1533 QLGE-------SGKSIHELEKIrkqLDQEkmEIQSALEEAEA--TLEHEEGKILHAQLELHQIKADSERKLAEKDEEMEQ 1603
Cdd:COG3883 87 ELGEraralyrSGGSVSYLDVL---LGSE--SFSDFLDRLSAlsKIADADADLLEELKADKAELEAKKAELEAKLAELEA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1072253241 1604 AKRNYQRMVDTLQTSLEAETRSRNEALRIKKKMEGDLNEMEIQLSQANRQAAEAQKQVKILQSYLKDTQIQLDDALRAS 1682
Cdd:COG3883 162 LKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1584-1901 |
2.21e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 49.74 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1584 HQiKADSERKLAEKDEEMEQAKRNYQRmvdtlqTSLEAETRSRNEALRIKKKMEGDLNEMEIQLSQANRQAAEAQKQVKi 1663
Cdd:pfam17380 280 HQ-KAVSERQQQEKFEKMEQERLRQEK------EEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELE- 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1664 lqsylkdtQIQLDDALRASEDLKENIAIVE---------------RRNTLLQAELEELRSL-VEQTERARKLSEQELIET 1727
Cdd:pfam17380 352 --------RIRQEERKRELERIRQEEIAMEisrmrelerlqmerqQKNERVRQELEAARKVkILEEERQRKIQQQKVEME 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1728 SERVQllhsqntslinQKKKMESDLSQLQTEMEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNM-EQ 1806
Cdd:pfam17380 424 QIRAE-----------QEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAeEQ 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1807 TIKDLQQRLDEAEQIALKGGKKQlQKLEARVRELDNEL-EAEQKRNAESVKGMRK---YERRIKELTYQTEEDRKNLARL 1882
Cdd:pfam17380 493 RRKILEKELEERKQAMIEEERKR-KLLEKEMEERQKAIyEEERRREAEEERRKQQemeERRRIQEQMRKATEERSRLEAM 571
|
330
....*....|....*....
gi 1072253241 1883 QDLVDKLQLKVKTYKRQAE 1901
Cdd:pfam17380 572 EREREMMRQIVESEKARAE 590
|
|
| CBD_MYO6-like |
cd21759 |
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, ... |
812-940 |
2.21e-05 |
|
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, which are actin-based motor molecules with ATPase activity, include unconventional myosins that serve in intracellular movements. Myosin-VI, also called unconventional myosin-6 (MYO6), is a reverse-direction motor protein that moves towards the minus-end of actin filaments. It is required for the structural integrity of the Golgi apparatus via the p53-dependent pro-survival pathway. Myosin-VI appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells. It modulates RNA polymerase II-dependent transcription. As part of the DISP (DOCK7-Induced Septin disPlacement) complex, Myosin-VI may regulate the association of septins with actin and thereby regulate the actin cytoskeleton. Myosin-VI is encoded by gene MYO6, the human homolog of the gene responsible for deafness in Snell's waltzer mice. It is mutated in autosomal dominant non-syndromic hearing loss. This family also includes Drosophila melanogaster unconventional myosin VI Jaguar (Jar; also called myosin heavy chain 95F (Mhc95F), or 95F MHC), which is a motor protein necessary for the morphogenesis of epithelial tissues during Drosophila development. Jar is required for basal protein targeting and correct spindle orientation in mitotic neuroblasts. It contributes to synaptic transmission and development at the Drosophila neuromuscular junction. Together with CLIP-190 (CAP-Gly domain-containing/cytoplasmic linker protein 190), Jar may coordinate the interaction between the actin and microtubule cytoskeleton. Jar may link endocytic vesicles to microtubules and possibly be involved in transport in the early embryo and in the dynamic process of dorsal closure; its function is believed to change during the life cycle. This model corresponds to the calmodulin (CaM) binding domain (CBD), which consists of three subdomains: a unique insert (Insert 2 or Ins2), an IQ motif, and a proximal tail domain (PTD, also known as lever arm extension or LAE).
Pssm-ID: 409646 [Multi-domain] Cd Length: 149 Bit Score: 46.35 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 812 GALSRIEFK-KIVERRDALLVIQWNIRAFMGVKnwpwmKLYFKIKPLLKSAETEKEMQTMKEEFQKLKEALEKSEARRKD 890
Cdd:cd21759 30 CALSVIKLKnKILYRREALIKIQKTVRGYLARK-----KHRPRIKGLRKIRALEKQLKEMEEIASQLKKDKDKWTKQVKE 104
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1072253241 891 LEEKMVSLLQE-KNDlqlqvqaEQDNLADADERCEQLIKNKIQLEAKLKEQ 940
Cdd:cd21759 105 LKKEIDALIKKiKTN-------DMITRKEIDKLYNALVKKVDKQLAELQKK 148
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1254-1796 |
2.25e-05 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 49.82 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1254 EQMVKAKANLEKLCRSLEDQANEHRTKSEENQRTVNELS--SLRAKLQTENGELSRRLDEKESLVSQMTRGKQTYTQHLE 1331
Cdd:NF041483 524 ETLERTRAEAERLRAEAEEQAEEVRAAAERAARELREETerAIAARQAEAAEELTRLHTEAEERLTAAEEALADARAEAE 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1332 DLKRQLEEETKAKNALA----HALQS-ARHDSDLLR-EQFEEEQEAKAELQRILSKANSEVAQWRTKYETDAIQRTEELE 1405
Cdd:NF041483 604 RIRREAAEETERLRTEAaeriRTLQAqAEQEAERLRtEAAADASAARAEGENVAVRLRSEAAAEAERLKSEAQESADRVR 683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1406 EAKKKLAQRLqeAEEAVEAVNAKcsslEKTKHRLQNEIEDLMvdlerSNAAAAALDKKQR---NFDKILAEWKQKFEESQ 1482
Cdd:NF041483 684 AEAAAAAERV--GTEAAEALAAA----QEEAARRRREAEETL-----GSARAEADQERERareQSEELLASARKRVEEAQ 752
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1483 TELESSQKEARSLSTELFklkNAYEEsldHLETFKRENKNLQEEISDltEQLGESGKSIHELEKIRKQLDQEKMEIQS-A 1561
Cdd:NF041483 753 AEAQRLVEEADRRATELV---SAAEQ---TAQQVRDSVAGLQEQAEE--EIAGLRSAAEHAAERTRTEAQEEADRVRSdA 824
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1562 LEEAEATLEHEEGKILHAQLELHQIKADSERKLAEKDEE--------MEQAKRNYQRMVDTLQTSLEAETRSRNEALRIK 1633
Cdd:NF041483 825 YAERERASEDANRLRREAQEETEAAKALAERTVSEAIAEaerlrsdaSEYAQRVRTEASDTLASAEQDAARTRADAREDA 904
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1634 KKMEGDlnemeiQLSQANRQAAEAQKQVKILQSYLKDTQIQLDDALRASEDLK--ENIAIVERRNTLLQAELEELRSLVE 1711
Cdd:NF041483 905 NRIRSD------AAAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVraDAAAQAEQLIAEATGEAERLRAEAA 978
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1712 QTERARKLSEQELIETSERVQLLHSQNTSLINQKKKMESDlSQLQTEMEEAVQECRNAEEKAKKAITDAAMMAEELKKEQ 1791
Cdd:NF041483 979 ETVGSAQQHAERIRTEAERVKAEAAAEAERLRTEAREEAD-RTLDEARKDANKRRSEAAEQADTLITEAAAEADQLTAKA 1057
|
....*
gi 1072253241 1792 DTSAH 1796
Cdd:NF041483 1058 QEEAL 1062
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1332-1622 |
2.35e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.24 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1332 DLKRQLEEETKAKNALAHALQSA-----RHDSDLLREQFEEEQEAKAelQRILSK-ANSEVAQWRTKYETDAIQRTEELE 1405
Cdd:COG3206 104 NLDEDPLGEEASREAAIERLRKNltvepVKGSNVIEISYTSPDPELA--AAVANAlAEAYLEQNLELRREEARKALEFLE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1406 EAKKKLAQRLQEAEEAVEAvnakcsslektkHRLQNEIEDLmvdlerSNAAAAALDKkqrnfdkiLAEWKQKFEESQTEL 1485
Cdd:COG3206 182 EQLPELRKELEEAEAALEE------------FRQKNGLVDL------SEEAKLLLQQ--------LSELESQLAEARAEL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1486 ESSQKEARSLSTELFKLKNAYEESLDH--LETFKRENKNLQEEISDLTEQLGESGKSI----HELEKIRKQLDQEKMEIQ 1559
Cdd:COG3206 236 AEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTPNHPDVialrAQIAALRAQLQQEAQRIL 315
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1072253241 1560 SALEEAEATLEHEEgKILHAQLELHQIKADS----ERKLAEKDEEMEQAKRNYQRMVDTLQTSLEAE 1622
Cdd:COG3206 316 ASLEAELEALQARE-ASLQAQLAQLEARLAElpelEAELRRLEREVEVARELYESLLQRLEEARLAE 381
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1521-1945 |
2.73e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.51 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1521 KNLQEEISDLTEQLGESGKSIHELEKIRKQLDQEKME---IQSALEEAEATLEHEEGKILHAQLELHQIKA--------D 1589
Cdd:PRK01156 176 DMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKShsiTLKEIERLSIEYNNAMDDYNNLKSALNELSSledmknryE 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1590 SERKLAEKDEEMEQAKRNY-----QRMVDTLQTSLEAETRSRNEALRIKKKMeGDLNEMEIQLSQANRQAAEAQKQVKIL 1664
Cdd:PRK01156 256 SEIKTAESDLSMELEKNNYykeleERHMKIINDPVYKNRNYINDYFKYKNDI-ENKKQILSNIDAEINKYHAIIKKLSVL 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1665 QSYLKDTQIQLddalRASEDLKENIAIVERRNTLLQAELEELRSLVEQTERARKLSEQELIETSERVQLLHSQNTSLINQ 1744
Cdd:PRK01156 335 QKDYNDYIKKK----SRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKE 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1745 KKKMESDLSQLQTEMEEAVQECRNAEEKaKKAITDAAMMAEELKKEQDTSAHLERMKKNmeQTIKDLQQRLDEAEQialk 1824
Cdd:PRK01156 411 LNEINVKLQDISSKVSSLNQRIRALREN-LDELSRNMEMLNGQSVCPVCGTTLGEEKSN--HIINHYNEKKSRLEE---- 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1825 ggkkQLQKLEARVRELDNELEAEQKR----NAESVKGMRKYERRIKELTYQTEEDRKNLARLQDLVDKLQLKVKTYKRQA 1900
Cdd:PRK01156 484 ----KIREIEIEVKDIDEKIVDLKKRkeylESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLK 559
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1072253241 1901 EESEEQANTSLSKFRKVQH--ELDEAEERADIAESQVNKLRAKSRDV 1945
Cdd:PRK01156 560 LEDLDSKRTSWLNALAVISliDIETNRSRSNEIKKQLNDLESRLQEI 606
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
909-1116 |
3.07e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 909 VQAEqDNLADADERCEQLIKNKIQLEAKLKEQTERLEdeeemnaELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHA 988
Cdd:COG3883 12 AFAD-PQIQAKQKELSELQAELEAAQAELDALQAELE-------ELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 989 TENKVKNLTEEM--AGLDEIIVKLTKEKKALQEA--HQQALDDL-QAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKIR 1063
Cdd:COG3883 84 RREELGERARALyrSGGSVSYLDVLLGSESFSDFldRLSALSKIaDADADLLEELKADKAELEAKKAELEAKLAELEALK 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1072253241 1064 MDLERVKRKLEGDVKLSQESLMDLENDKQQLEEKLKKKDFEVSQLNTRIEDEQ 1116
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1074-1304 |
3.65e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 3.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1074 EGDVKLSQESLMDLENDKQQLEEKLKKKDFEVSQLNTRIEDEQNVCIQLQKKMKELQARIEeleeeleaerTARAKVEKL 1153
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA----------EAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1154 RcdlsrelEEISERL----EEAGGATSVQMELNKKREAEFL----------KLRRDLEESTLHSEATAASLRKKHADSVA 1219
Cdd:COG3883 85 R-------EELGERAralyRSGGSVSYLDVLLGSESFSDFLdrlsalskiaDADADLLEELKADKAELEAKKAELEAKLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1220 ELSEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQMVKAKANLEKLCRSLEDQANEHRTKSEENQRTVNELSSLRAKLQ 1299
Cdd:COG3883 158 ELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAA 237
|
....*
gi 1072253241 1300 TENGE 1304
Cdd:COG3883 238 AAAAA 242
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1363-1573 |
3.87e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 48.77 E-value: 3.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1363 EQFEEEQEAKAELQRILSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNE 1442
Cdd:PRK05771 43 ERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1443 IEDLM------VDL------ERSNAAAAALDKKQRNFDKILAEWKQKFEESQTELES------SQKEARSLSTELfkLKN 1504
Cdd:PRK05771 123 IERLEpwgnfdLDLslllgfKYVSVFVGTVPEDKLEELKLESDVENVEYISTDKGYVyvvvvvLKELSDEVEEEL--KKL 200
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1505 AYEE-SLDHLETFKRENKNLQEEISDLTEQLGEsgkSIHELEKIRKQLDQekmEIQSALEEAEATLEHEE 1573
Cdd:PRK05771 201 GFERlELEEEGTPSELIREIKEELEEIEKERES---LLEELKELAKKYLE---ELLALYEYLEIELERAE 264
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1467-1928 |
3.93e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 48.81 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1467 FDKILAEWKQKFEESQTELESSQKEARSLSTELFKLKNAYEESLdhletfkrenKNLQEEISDLTEQLGESGKSIHELEK 1546
Cdd:TIGR00618 178 YTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERK----------QVLEKELKHLREALQQTQQSHAYLTQ 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1547 IRKQLdQEKMEIQSALEEAEATLEHEEGKIlhAQLELHQIKADSERK---LAEKDEEMEQAKRNYQRMVDTLQ---TSLE 1620
Cdd:TIGR00618 248 KREAQ-EEQLKKQQLLKQLRARIEELRAQE--AVLEETQERINRARKaapLAAHIKAVTQIEQQAQRIHTELQskmRSRA 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1621 AETRSRNEALRIKKKMEGDLNEMEIQLSQANRQAAEAQKQVKILQSylKDTQIQLDDALRAsedLKENIAIVERRNTLLQ 1700
Cdd:TIGR00618 325 KLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREI--SCQQHTLTQHIHT---LQQQKTTLTQKLQSLC 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1701 AELEELRSLV------------EQTERARKLSEQELIETSERVQLLHSQNTSLI-NQKKKMESDLSQLQTEMEEAVQECR 1767
Cdd:TIGR00618 400 KELDILQREQatidtrtsafrdLQGQLAHAKKQQELQQRYAELCAAAITCTAQCeKLEKIHLQESAQSLKEREQQLQTKE 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1768 NAEEKAKKAITDAAMMAEELKKEQdtsahLERMKKNMEQTIKDLQQRLDEAEQIALKGGKKQLQKLEARVRELDNELEAE 1847
Cdd:TIGR00618 480 QIHLQETRKKAVVLARLLELQEEP-----CPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSE 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1848 QKRNAESVKGMR-------KYERRIKELTYQTEEDRKNLARLQDLVDKLQLKVKTYKRQAEESEEQANTSLSKFRKVQHE 1920
Cdd:TIGR00618 555 RKQRASLKEQMQeiqqsfsILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHL 634
|
....*...
gi 1072253241 1921 LDEAEERA 1928
Cdd:TIGR00618 635 QQCSQELA 642
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1693-1936 |
4.39e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 4.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1693 ERRNTLlqAELEELRSLVEQTERARklseQELIETSERVQLLhsqntslinqkkkmeSDLSQLQTEMEEAVQECRNAEE- 1771
Cdd:COG4913 219 EEPDTF--EAADALVEHFDDLERAH----EALEDAREQIELL---------------EPIRELAERYAAARERLAELEYl 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1772 ----KAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQQRLDEAEQIALKGGKKQLQKLEArvreldnELEAE 1847
Cdd:COG4913 278 raalRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLER-------EIERL 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1848 QKRNAESVKGMRKYERRIKELTYQTEEDRKNLARLQDLVDKLqlkVKTYKRQAEESEEQANTSLSKFRKVQHELDEAE-E 1926
Cdd:COG4913 351 ERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAAL---LEALEEELEALEEALAEAEAALRDLRRELRELEaE 427
|
250
....*....|
gi 1072253241 1927 RADIAESQVN 1936
Cdd:COG4913 428 IASLERRKSN 437
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
873-1048 |
5.21e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 5.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 873 EFQKLKEALEKSEARRKDLEEKMVSLLQEKNDLQLQVQAEQDNLADADERCEQLIKNKIQLEAKLKEQTERLED------ 946
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEraraly 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 947 ----------------------------------EEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENK 992
Cdd:COG3883 97 rsggsvsyldvllgsesfsdfldrlsalskiadaDADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1072253241 993 VKNLTEEMAGLDEIIVKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKAKLEQQ 1048
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
903-1096 |
5.21e-05 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 47.77 E-value: 5.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 903 NDLQLQVQAEQDNLADADERCEQLIKNKIQLEAKLKEQterledeEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKV 982
Cdd:PRK11637 43 SDNRDQLKSIQQDIAAKEKSVRQQQQQRASLLAQLKKQ-------EEAISQASRKLRETQNTLNQLNKQIDELNASIAKL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 983 EKEKHATEnkvKNLTEEM---------AGLDEIivkLTKEKKALQEAHQQALDDL-QAEEDKVNTLTKAKAKLEQQVDDL 1052
Cdd:PRK11637 116 EQQQAAQE---RLLAAQLdaafrqgehTGLQLI---LSGEESQRGERILAYFGYLnQARQETIAELKQTREELAAQKAEL 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1072253241 1053 EGSLEQEKKIRMDLERVKRKLEGDVKLSQESLMDLEN----DKQQLEE 1096
Cdd:PRK11637 190 EEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGLESslqkDQQQLSE 237
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
855-1200 |
5.56e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 48.20 E-value: 5.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 855 KPLLKSAETEKEMQTMKEEFQKLKEALEKSEARRKDLEEKMVSLlQEKNDLQLQVQAEQDNLADadERCEQLikNKIQLE 934
Cdd:pfam17380 282 KAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKAR-QAEMDRQAAIYAEQERMAM--EREREL--ERIRQE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 935 AKlKEQTERLEdEEEMNAELTaKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIivkltkeK 1014
Cdd:pfam17380 357 ER-KRELERIR-QEEIAMEIS-RMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQI-------R 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1015 KALQEAHQQALDDLqaEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKkirmdlERVKRKLEgdvklsqeslMDLENDKQQL 1094
Cdd:pfam17380 427 AEQEEARQREVRRL--EEERAREMERVRLEEQERQQQVERLRQQEE------ERKRKKLE----------LEKEKRDRKR 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1095 EEKLKKK--DFEVSQLNTRIEDEQNVCIQLQKKMKELQARIEELEEELEAERTARAKVEklrcdlSRELEEISERLEEAG 1172
Cdd:pfam17380 489 AEEQRRKilEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQE------MEERRRIQEQMRKAT 562
|
330 340 350
....*....|....*....|....*....|...
gi 1072253241 1173 GATSVQMELNKKRE-----AEFLKLRRDLEEST 1200
Cdd:pfam17380 563 EERSRLEAMEREREmmrqiVESEKARAEYEATT 595
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1767-1929 |
6.43e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.85 E-value: 6.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1767 RNAEEKAKKAITDAAMMAEELKKEQDTSAHlERMKKNMEQTIKDLQQRLDEAeqialkggKKQLQKLEARVRELDNELEA 1846
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKEALLEAK-EEIHKLRNEFEKELRERRNEL--------QKLEKRLLQKEENLDRKLEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1847 EQKRNAESVKGMRKYERRIKELTYQTEEdrknlarLQDLVDKLQLKVKTY---------KRQAEESEEQANTSLSKFRKV 1917
Cdd:PRK12704 105 LEKREEELEKKEKELEQKQQELEKKEEE-------LEELIEEQLQELERIsgltaeeakEILLEKVEEEARHEAAVLIKE 177
|
170
....*....|..
gi 1072253241 1918 QHEldEAEERAD 1929
Cdd:PRK12704 178 IEE--EAKEEAD 187
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
861-993 |
7.05e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.46 E-value: 7.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 861 AETEKEMQTMKEEFQKLKEALEKSEARRKDLEEKmvslLQEKNDLQLQVQAEQDNLADADE------RCEQLIKNKIQLE 934
Cdd:COG1579 34 AELEDELAALEARLEAAKTELEDLEKEIKRLELE----IEEVEARIKKYEEQLGNVRNNKEyealqkEIESLKRRISDLE 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1072253241 935 AKLKEQTERLEDEE----EMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKV 993
Cdd:COG1579 110 DEILELMERIEELEeelaELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
853-1074 |
7.15e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.11 E-value: 7.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 853 KIKPLLKSAETEKEMQTMKEEFQKLKEALEKSEARRKDLEEKMVSLLQEKNDLQLQVQAEQDNLADADERCEQLIKNKIQ 932
Cdd:PRK02224 497 RLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAE 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 933 LEAKLKEQTERLEDEEEMnAELTAKKRKLEDECSELKKDIDDleltLAKVEKEKhatENKVKNLTEEMAGLDEiivKLTK 1012
Cdd:PRK02224 577 LNSKLAELKERIESLERI-RTLLAAIADAEDEIERLREKREA----LAELNDER---RERLAEKRERKRELEA---EFDE 645
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1072253241 1013 EK-KALQEAHQQALDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKIRMDLERVKRKLE 1074
Cdd:PRK02224 646 ARiEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREALENRVE 708
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1503-1945 |
7.56e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 47.52 E-value: 7.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1503 KNAYEEsLDHLETFKRE--NKNLQEEISDLtEQLGESGKSIHELEKIRKQLDQ---EKM-EIQSALEEAEATLEheEGKI 1576
Cdd:PRK04778 25 KRNYKR-IDELEERKQEleNLPVNDELEKV-KKLNLTGQSEEKFEEWRQKWDEivtNSLpDIEEQLFEAEELND--KFRF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1577 LHAQLELHQIkadserklaekDEEMEQAKRNYQRMVDTLQTSLEAETRSRNEALRIKKK--------------------- 1635
Cdd:PRK04778 101 RKAKHEINEI-----------ESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLyrelrksllanrfsfgpalde 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1636 MEGDLNEMEIQLSQANRQAAEAQkqvkilqsYLK--DTQIQLDDALRASEDLKENI-AIVERRNTLLQAELEELRSLVEQ 1712
Cdd:PRK04778 170 LEKQLENLEEEFSQFVELTESGD--------YVEarEILDQLEEELAALEQIMEEIpELLKELQTELPDQLQELKAGYRE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1713 -TERARKLSEQELIETSERVQLLHSQNTSLINQK--KKMESDLSQLQTEMEEaVQECRNAEEKAKKaitdaammaeELKK 1789
Cdd:PRK04778 242 lVEEGYHLDHLDIEKEIQDLKEQIDENLALLEELdlDEAEEKNEEIQERIDQ-LYDILEREVKARK----------YVEK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1790 EQDT-SAHLERMKKNMEQTIKDLQQ-----RLDEAEQIALKGGKKQLQKLEARVRELDNELEAEQKRNAESVKGMRKYER 1863
Cdd:PRK04778 311 NSDTlPDFLEHAKEQNKELKEEIDRvkqsyTLNESELESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILK 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1864 RIKELTYQTEEDRKNLARL-------QDLVDKLQLKVKTYKRQAEES------EEQantsLSKFRKVQHELDEAEER--- 1927
Cdd:PRK04778 391 QLEEIEKEQEKLSEMLQGLrkdeleaREKLERYRNKLHEIKRYLEKSnlpglpEDY----LEMFFEVSDEIEALAEElee 466
|
490 500
....*....|....*....|....*....
gi 1072253241 1928 -----------ADIAESQVNKLRAKSRDV 1945
Cdd:PRK04778 467 kpinmeavnrlLEEATEDVETLEEETEEL 495
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1073-1734 |
7.84e-05 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 47.82 E-value: 7.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1073 LEGDVKLSQESlmdlENDKQQLEEkLKKKDFEVSQLNTriedeqnvcIQLQKKMKeLQARIEELEEELEAERTARAKVEK 1152
Cdd:pfam07111 55 LEGSQALSQQA----ELISRQLQE-LRRLEEEVRLLRE---------TSLQQKMR-LEAQAMELDALAVAEKAGQAEAEG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1153 LRCDLSRElEEISERLEEAggatsvqmelnKKREAEflklrrdlEESTLHSEATAaSLRKKHADSVAELSEQIDNLQRVK 1232
Cdd:pfam07111 120 LRAALAGA-EMVRKNLEEG-----------SQRELE--------EIQRLHQEQLS-SLTQAHEEALSSLTSKAEGLEKSL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1233 QKLEKEKSEFKLELDDVTSNME----QMVKAKANLE---KLCRSL----------EDQANEHRTKSEENQRTVNELSSLR 1295
Cdd:pfam07111 179 NSLETKRAGEAKQLAEAQKEAEllrkQLSKTQEELEaqvTLVESLrkyvgeqvppEVHSQTWELERQELLDTMQHLQEDR 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1296 AKLQT------------------ENGELSRRLDEKESLVSQMTRGKQTYTQHLEDLKRQLEEETKAKNaLAH--ALQSAR 1355
Cdd:pfam07111 259 ADLQAtvellqvrvqslthmlalQEEELTRKIQPSDSLEPEFPKKCRSLLNRWREKVFALMVQLKAQD-LEHrdSVKQLR 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1356 HDSDLLREQFEEEQEAKAELQRILSKANSEVAQWRTKYETDAIQrTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLekt 1435
Cdd:pfam07111 338 GQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQME-LSRAQEARRRQQQQTASAEEQLKFVVNAMSST--- 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1436 khrlQNEIEDLMVDLERSNAAAAALDKKQ----RNFDKILAEWKQKFEESQTELESS--QKEARSLSTELfklknayees 1509
Cdd:pfam07111 414 ----QIWLETTMTRVEQAVARIPSLSNRLsyavRKVHTIKGLMARKVALAQLRQESCppPPPAPPVDADL---------- 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1510 ldhletfKRENKNLQEEISDLTEQLGESGKSIHElekirkqldqekmEIQSALEEAEAtleheegkilhaqlelhqikad 1589
Cdd:pfam07111 480 -------SLELEQLREERNRLDAELQLSAHLIQQ-------------EVGRAREQGEA---------------------- 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1590 SERKLAEKDEEMEQAKRNYQRMVDTLQTSLEAETRSRNEALRIKKKMEGDLNEMEIQLSQA-NRQAAEAQKQvkiLQSYL 1668
Cdd:pfam07111 518 ERQQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEIYGQAlQEKVAEVETR---LREQL 594
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1072253241 1669 KDTQIQLDDALRASEDLKENIAIVERRNTLLQAELEELRSLVEQterARKLSEQELietSERVQLL 1734
Cdd:pfam07111 595 SDTKRRLNEARREQAKAVVSLRQIQHRATQEKERNQELRRLQDE---ARKEEGQRL---ARRVQEL 654
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
874-1446 |
7.88e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 48.02 E-value: 7.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 874 FQKLKEALEksEARR-KDLEEKMVSLLQEKNDLQLQVQAEQDNLADADERCEQL---IKNKIQLEAKLKEQTERLEDEEE 949
Cdd:COG3096 494 WQTARELLR--RYRSqQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIgqqLDAAEELEELLAELEAQLEELEE 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 950 MNAELTAKKRKLEDECSELKKDIDdlelTLAKVEKEKHATENKVKNLTEEmagLDEIIvkltKEKKALQEAHQQALDD-- 1027
Cdd:COG3096 572 QAAEAVEQRSELRQQLEQLRARIK----ELAARAPAWLAAQDALERLREQ---SGEAL----ADSQEVTAAMQQLLERer 640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1028 -LQAEEDKvntLTKAKAKLEQQVDDLE--GSLEQEKKIRM--------------------------------------DL 1066
Cdd:COG3096 641 eATVERDE---LAARKQALESQIERLSqpGGAEDPRLLALaerlggvllseiyddvtledapyfsalygparhaivvpDL 717
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1067 ERVKRKLEGdvklSQESLMDL---ENDKQQLEEKLkkkdFEVSQLntriedEQNVCIQLQKKmkelQARIEELEEELEAE 1143
Cdd:COG3096 718 SAVKEQLAG----LEDCPEDLyliEGDPDSFDDSV----FDAEEL------EDAVVVKLSDR----QWRYSRFPEVPLFG 779
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1144 RTARAK-VEKLRcdlsRELEEISERLEEAggATSVQmelnkkreaeflKLRRdLEES-----TLH--------SEATAAS 1209
Cdd:COG3096 780 RAAREKrLEELR----AERDELAEQYAKA--SFDVQ------------KLQR-LHQAfsqfvGGHlavafapdPEAELAA 840
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1210 LRKKHADSVAELSEQIDNLQRVKQKLEKEKSEFKLeLDDVTSNMeqMVKAKANLEKLCRSLE---DQANEHRTKSEENQR 1286
Cdd:COG3096 841 LRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQL-LNKLLPQA--NLLADETLADRLEELReelDAAQEAQAFIQQHGK 917
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1287 TVNELSSLRAKLQT---ENGELSRRLDEKESLVSQMTRGKQTYTQ------HL--EDLKRQLEEETKAKNALAHALQSAR 1355
Cdd:COG3096 918 ALAQLEPLVAVLQSdpeQFEQLQADYLQAKEQQRRLKQQIFALSEvvqrrpHFsyEDAVGLLGENSDLNEKLRARLEQAE 997
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1356 HDSDLLREQFEEEQEAKAELQRILSKANSevaQWRTKYET--DAIQRTEELE-----EAKKKLAQRLQEAEEAVEAVNAK 1428
Cdd:COG3096 998 EARREAREQLRQAQAQYSQYNQVLASLKS---SRDAKQQTlqELEQELEELGvqadaEAEERARIRRDELHEELSQNRSR 1074
|
650
....*....|....*...
gi 1072253241 1429 CSSLEKTKHRLQNEIEDL 1446
Cdd:COG3096 1075 RSQLEKQLTRCEAEMDSL 1092
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1312-1920 |
8.15e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 47.89 E-value: 8.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1312 KESLVSQMTRGKQTYTQHLEDLKRQLEEETKAKNALAHALQSARHDSDLLREQFE------------------------- 1366
Cdd:pfam10174 54 RISVLKEQYRVTQEENQHLQLTIQALQDELRAQRDLNQLLQQDFTTSPVDGEDKFstpelteenfrrlqseherqakelf 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1367 ------EEQEAKAELQRI--------------------LSKANSEVAQWRTKYETDAIQRTEELE---EAKKKLAQRLQE 1417
Cdd:pfam10174 134 llrktlEEMELRIETQKQtlgardesikkllemlqskgLPKKSGEEDWERTRRIAEAEMQLGHLEvllDQKEKENIHLRE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1418 A-----------------EEAVEAVNAKCSSLEKTKHRLQNEIEDLmvdleRSNAAAAALDK----KQRNFDKILAEW-K 1475
Cdd:pfam10174 214 ElhrrnqlqpdpaktkalQTVIEMKDTKISSLERNIRDLEDEVQML-----KTNGLLHTEDReeeiKQMEVYKSHSKFmK 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1476 QKFEESQTELESSQKEARSLSTELFKLKNAYEESLDHLETFK-------RENKNLQEEISDLTEQLGESGKSIHELEKIR 1548
Cdd:pfam10174 289 NKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKesltakeQRAAILQTEVDALRLRLEEKESFLNKKTKQL 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1549 KQLDQEKMEIQSALEEAEATLEHEEGKI--LHAQLE-LHQIKADSERKLAEKDEEMEQAKRNYQRMVDTLQTSLEAETRS 1625
Cdd:pfam10174 369 QDLTEEKSTLAGEIRDLKDMLDVKERKInvLQKKIEnLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEK 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1626 RNEALRIKKKMEGDLNEMEIQLSQANRQAAEAQKQVKILQSYLKDTQIQLDDALRASEDLKENIAIVERRNTLLQAEL-- 1703
Cdd:pfam10174 449 ERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVeq 528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1704 --EELRSLVEQTERARKLSEQELI--ETSERVQLLHSQNTSLINQKKKMESDLSQLQtemeEAVQECRNAEEKAKKAITD 1779
Cdd:pfam10174 529 kkEECSKLENQLKKAHNAEEAVRTnpEINDRIRLLEQEVARYKEESGKAQAEVERLL----GILREVENEKNDKDKKIAE 604
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1780 AAMMAEELKKEQDTSAHLERMKKNMEQ--TIKDLQQRLDEAEQIALKGGKKQLQKLEARVRELDNELEAEQKRNAESVKG 1857
Cdd:pfam10174 605 LESLTLRQMKEQNKKVANIKHGQQEMKkkGAQLLEEARRREDNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQS 684
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1072253241 1858 MRKYERrikELTYQTEEDRKNLARLqdlvdklqLKVKTYKRQAEESEEQANTSL-----SKFRKVQHE 1920
Cdd:pfam10174 685 LAEKDG---HLTNLRAERRKQLEEI--------LEMKQEALLAAISEKDANIALlelssSKKKKTQEE 741
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1396-1717 |
8.88e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 46.98 E-value: 8.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1396 DAIQRTEELEEAKKKLAQrlqeaeeAVEAVNAKCSSLEKTKHRLQNeiedLMVDLERSNAAAAALDKKQRNFDKILAEWK 1475
Cdd:pfam19220 14 EMADRLEDLRSLKADFSQ-------LIEPIEAILRELPQAKSRLLE----LEALLAQERAAYGKLRRELAGLTRRLSAAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1476 QKFEESQTELESSQKEARSLSTELFKLKNAYEESLDHLETFKR-------ENKNLQEEISDLTEQLGESGKSIHELEKIR 1548
Cdd:pfam19220 83 GELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALERqlaaeteQNRALEEENKALREEAQAAEKALQRAEGEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1549 KQ-------LDQEKMEIQSALEEAEATLEHEEGKI--LHAQLELHQIKADS-ERKLAEKDEEMEQAKRNYQRMVDTLQTS 1618
Cdd:pfam19220 163 ATarerlalLEQENRRLQALSEEQAAELAELTRRLaeLETQLDATRARLRAlEGQLAAEQAERERAEAQLEEAVEAHRAE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1619 LeAETRSRNEALrikkkmEGDLNEMEIQLSQANRQAAEAQKQVKILQSYLKDTQIQLDDAlrasedlkeniaivERRNTL 1698
Cdd:pfam19220 243 R-ASLRMKLEAL------TARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTL--------------ERRLAG 301
|
330
....*....|....*....
gi 1072253241 1699 LQAELEELRSLVEQTERAR 1717
Cdd:pfam19220 302 LEADLERRTQQFQEMQRAR 320
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
857-1131 |
8.94e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.81 E-value: 8.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 857 LLKSAETEKEMQTMKEEFQKLKEALEKSEARRKDLEEKMVSLLQEKNDLqlqVQAeqdnladADERCEQLIKNKIQLEAK 936
Cdd:pfam15921 589 QVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKL---VNA-------GSERLRAVKDIKQERDQL 658
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 937 LKEQTERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNlteeMAGLDEIIVKLTKEKKA 1016
Cdd:pfam15921 659 LNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKS----MEGSDGHAMKVAMGMQK 734
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1017 LQEAHQQALDDLQAeedKVNTLTKAKAKLEQQVDDLEgslEQEKKIRMDLERV---KRKLEGDVKLSQESLMDLENDKQQ 1093
Cdd:pfam15921 735 QITAKRGQIDALQS---KIQFLEEAMTNANKEKHFLK---EEKNKLSQELSTVateKNKMAGELEVLRSQERRLKEKVAN 808
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1072253241 1094 LEEKLKKKDFEVSQLNTRI--EDEQNVCIQLQKKM--KELQA 1131
Cdd:pfam15921 809 MEVALDKASLQFAECQDIIqrQEQESVRLKLQHTLdvKELQG 850
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1330-1586 |
9.00e-05 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 46.25 E-value: 9.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1330 LEDLKRQLEEETKAKNALAHALQSARHDSDLLREQFEEEQEakaELQRILSKAnsevaQWRTKYETDAIQRTEELEEAKK 1409
Cdd:pfam06008 21 LENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQK---KATQTLAKA-----QQVNAESERTLGHAKELAEAIK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1410 KLAQRLQEAEEAVEAVNAKCSSL-EKTKHRLQNEIEDLMVDLERSNaaaaaLDKKQRNFDKILAEWKQKFEESQTELESS 1488
Cdd:pfam06008 93 NLIDNIKEINEKVATLGENDFALpSSDLSRMLAEAQRMLGEIRSRD-----FGTQLQNAEAELKAAQDLLSRIQTWFQSP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1489 QKEARSLSTELFKLKNAYEESLDHLETFKRENKNLQEEISDLTeqlgesgksiHELEKIRKQLDQEKMEIQSALEEAEAT 1568
Cdd:pfam06008 168 QEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLN----------LANQANLREFQRKKEEVSEQKNQLEET 237
|
250
....*....|....*...
gi 1072253241 1569 LEHEEGKILHAQLELHQI 1586
Cdd:pfam06008 238 LKTARDSLDAANLLLQEI 255
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1405-1657 |
9.32e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 9.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1405 EEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAaaaLDKKQRNFDKILAEWKQKFEESQTE 1484
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAE---IDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1485 LESSQKEARSLS--TELFKLKNAYE--ESLDHLETFKRENKNLQEEISDLTEQLGESGKSI----HELEKIRKQLDQEKM 1556
Cdd:COG3883 92 ARALYRSGGSVSylDVLLGSESFSDflDRLSALSKIADADADLLEELKADKAELEAKKAELeaklAELEALKAELEAAKA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1557 EIQSALEEAEATLEHEEGKILHAQLELHQIKADSERKLAEKDEEMEQAKRNYQRMVDTLQTSLEAETRSRNEALRIKKKM 1636
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGA 251
|
250 260
....*....|....*....|.
gi 1072253241 1637 EGDLNEMEIQLSQANRQAAEA 1657
Cdd:COG3883 252 AGAAGAAAGSAGAAGAAAGAA 272
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
861-1241 |
9.70e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.20 E-value: 9.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 861 AETEKEMQTMKEEFQKLKEALEKSEARRKDLEEKMVSLLQEKNDLQLQVQAEQDNLADADERCEQLIKNKIQLEAKLKEQ 940
Cdd:pfam07888 76 RELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERM 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 941 TERLEdeeemnaELTAKKRKLEDECSelkkdidDLELTLAKVEKEKHatenkvknlteemagldeiivKLTKEKKALQEA 1020
Cdd:pfam07888 156 KERAK-------KAGAQRKEEEAERK-------QLQAKLQQTEEELR---------------------SLSKEFQELRNS 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1021 HQQALDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKIRMDLERVKRKLEGdvklSQESLMDLENDKQQLEEKLKK 1100
Cdd:pfam07888 201 LAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEG----LGEELSSMAAQRDRTQAELHQ 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1101 KDFEVSQLNTRIEDeqnvciqLQKKMKELQARieELEEELEAERTARAKVEKLRcDLSRELEEISERL-EEAGGATSVQM 1179
Cdd:pfam07888 277 ARLQAAQLTLQLAD-------ASLALREGRAR--WAQERETLQQSAEADKDRIE-KLSAELQRLEERLqEERMEREKLEV 346
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1072253241 1180 ELNKKREAEflklRRDLEESTLHSEATAASLR---KKHADSVAELSEQIDNLQRVKQKLEKEKSE 1241
Cdd:pfam07888 347 ELGREKDCN----RVQLSESRRELQELKASLRvaqKEKEQLQAEKQELLEYIRQLEQRLETVADA 407
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
892-1097 |
1.03e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 892 EEKMVSLLQEKNDLQLQVQAEQDNLADADERCEQLIKNKIQLEAKLKEQTERLedeEEMNAELTAKKRKLEDECSELKKD 971
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEI---DKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 972 IDDLELT------LAKVEKEKHATE--NKVKNLTEEMAGLDEIIVKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKA 1043
Cdd:COG3883 92 ARALYRSggsvsyLDVLLGSESFSDflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1072253241 1044 KLEQQVDDLEGSLEQEKKIRMDLERVKRKLEGDVKLSQESLMDLENDKQQLEEK 1097
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1010-1311 |
1.06e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.60 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1010 LTKEKKALQEAHQQALDDLqaeeDKVNTLTKAKAKLEQQVDDLEGSLeqeKKIRMDLERVKRKLEGDVK--LSQESLMDL 1087
Cdd:PRK11281 54 LEAEDKLVQQDLEQTLALL----DKIDRQKEETEQLKQQLAQAPAKL---RQAQAELEALKDDNDEETRetLSTLSLRQL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1088 E-------NDKQQLEEKLKKKDFEVSQLNTRIEDEQNVCIQLQKKMKELQARIEELEEELEAERTARakVEKLRCDLSRE 1160
Cdd:PRK11281 127 EsrlaqtlDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLKGGKVGGKALRPSQ--RVLLQAEQALL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1161 LEEISERLEEAGGATSVQMELNKKREAEFLKLRRDLEESTLHSEATAASLRKKHADSVAELSEQIDNLQRVKQKLEKEKS 1240
Cdd:PRK11281 205 NAQNDLQRKSLEGNTQLQDLLQKQRDYLTARIQRLEHQLQLLQEAINSKRLTLSEKTVQEAQSQDEAARIQANPLVAQEL 284
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1072253241 1241 EFKLELDDvtsnmeQMVKAKANLEKLcrsledqanehrtkSEENQRTVNELSSLrakLQTEngelsRRLDE 1311
Cdd:PRK11281 285 EINLQLSQ------RLLKATEKLNTL--------------TQQNLRVKNWLDRL---TQSE-----RNIKE 327
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1771-1953 |
1.13e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1771 EKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQQRLDEAEQIalkggkKQLQKLEARVRELDNELEAEQKR 1850
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKL------LQLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1851 naesvkgMRKYERRIKELT---YQTEEDRKNLARLQDLVDKLQLKVKTYKRQA-EESEEQANTSLSKFRKVQHELDEAEE 1926
Cdd:COG4717 148 -------LEELEERLEELReleEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQE 220
|
170 180
....*....|....*....|....*..
gi 1072253241 1927 RADIAESQVNKLRAKSRDVSTKKSLNE 1953
Cdd:COG4717 221 ELEELEEELEQLENELEAAALEERLKE 247
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1504-1948 |
1.29e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.94 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1504 NAYEESLDHLETFKRENKNLQEEISDLTEQLGESGKSIHELEKIRKQLDQEKMEIQSALEEAEATLEHEEGKILHAQLEl 1583
Cdd:TIGR04523 33 TEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSE- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1584 hqIKADSERKLAEKDE--EMEQAKRNYQRMVDTLQTSLeaetrsrnealrikKKMEGDLNEMEIQLSQANRQAAEAQKQV 1661
Cdd:TIGR04523 112 --IKNDKEQKNKLEVElnKLEKQKKENKKNIDKFLTEI--------------KKKEKELEKLNNKYNDLKKQKEELENEL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1662 KILQSYLKDTQIQLDDA---LRASEDLKENIAIVERRNTLLQAELEELRSLVEQTERARKLSEQELIETSERVQLLHSQN 1738
Cdd:TIGR04523 176 NLLEKEKLNIQKNIDKIknkLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1739 TSLINQKKKMESDLSQLQTEMEEAVQECRNAEEKAKKAITDAAMMAEElkKEQDTSAHLERMKKNMEQTIKDLQQRLDEA 1818
Cdd:TIGR04523 256 NQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQ--KEQDWNKELKSELKNQEKKLEEIQNQISQN 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1819 EQI------ALKGGKKQLQKLEARVRELDNELEAEQKRNAESVKGMRKYERRIKELTYQTEEDRKNLARLQDLVDKLQLK 1892
Cdd:TIGR04523 334 NKIisqlneQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQ 413
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1072253241 1893 VKTYKRQAEESEEQANTSLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDVSTK 1948
Cdd:TIGR04523 414 IKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQ 469
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
861-1107 |
1.36e-04 |
|
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.
Pssm-ID: 408741 [Multi-domain] Cd Length: 876 Bit Score: 47.07 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 861 AETEKEMQTMKEEFQKLKEALEKSEARRKDLEEKMVSLLQEKNDLQLQVQAEQdnladaderceqlikNKIQLEAKLKEQ 940
Cdd:pfam18971 603 AKSTGNYDEVKKAQKDLEKSLRKREHLEKEVEKKLESKSGNKNKMEAKAQANS---------------QKDEIFALINKE 667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 941 TERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIvKLTKEKKALQEA 1020
Cdd:pfam18971 668 ANRDARAIAYTQNLKGIKRELSDKLEKISKDLKDFSKSFDEFKNGKNKDFSKAEETLKALKGSVKDL-GINPEWISKVEN 746
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1021 HQQALDDLQAEEDK-VNTLTKAKAKLEQQVDDLEGSLEQEKKI-RMDLERVKRKLEGDVKLSQESLMDLEN-DKQQLEEK 1097
Cdd:pfam18971 747 LNAALNEFKNGKNKdFSKVTQAKSDLENSVKDVIINQKVTDKVdNLNQAVSVAKAMGDFSRVEQVLADLKNfSKEQLAQQ 826
|
250
....*....|.
gi 1072253241 1098 LKK-KDFEVSQ 1107
Cdd:pfam18971 827 AQKnEDFNTGK 837
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1458-1605 |
1.43e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.30 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1458 AALDKKQRNFDKILAEWKQKFEESQTELESSQKEARSLSTELFKLKNAYEESLDHLETFKRENKNL--QEEISDLTEQLG 1535
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnNKEYEALQKEIE 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1536 ESGKSIHELEKIRKQLDQEKMEIQSALEEAEATLEHEEGKILHAQLELHQIKADSERKLAEKDEEMEQAK 1605
Cdd:COG1579 100 SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELA 169
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1057-1721 |
1.62e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 46.72 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1057 EQEKKIRMDLERVKRKLEGDVKLSQESLmdlendkQQLEEKLKKKDFEVSQLNTRIEDEQ---NVCIQLQKKMKELQARI 1133
Cdd:PRK10246 191 EQHKSARTELEKLQAQASGVALLTPEQV-------QSLTASLQVLTDEEKQLLTAQQQQQqslNWLTRLDELQQEASRRQ 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1134 EELEEELEAERTARAKVEKLRCDL-SRELEEISERLEE---AGGATSVQMELNKKREAEFLKLRRDLEESTLHSEATAAS 1209
Cdd:PRK10246 264 QALQQALAAEEKAQPQLAALSLAQpARQLRPHWERIQEqsaALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSAELQA 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1210 LRKKHADSVAELseqiDNLQRVKQKLEKEKSEFKLElddvTSNMEQMVKAKANLEKLCRSLE-----------DQANEHR 1278
Cdd:PRK10246 344 QQQSLNTWLAEH----DRFRQWNNELAGWRAQFSQQ----TSDREQLRQWQQQLTHAEQKLNalpaitltltaDEVAAAL 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1279 TKSEENQRTVNELSSLRAKLQtengELSRRLDEKESLVSQMTRGKQTYTQHLEDLKRQLEEETKAKNALAHALQSARHDS 1358
Cdd:PRK10246 416 AQHAEQRPLRQRLVALHGQIV----PQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADVKTICEQEARIK 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1359 DLlreqfeEEQEAKAELQRIL----SKANSEVAQWRTKYETDAIQRTEELEEAKKKLA--------------QRLQEAEE 1420
Cdd:PRK10246 492 DL------EAQRAQLQAGQPCplcgSTSHPAVEAYQALEPGVNQSRLDALEKEVKKLGeegaalrgqldaltKQLQRDES 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1421 AVEAVNAKCSSLEKtkhRLQNEIEDLMVDLERSNAAAAALDKKQRnFDKILAEWKQKfEESQTELESSQKEARSLSTELF 1500
Cdd:PRK10246 566 EAQSLRQEEQALTQ---QWQAVCASLNITLQPQDDIQPWLDAQEE-HERQLRLLSQR-HELQGQIAAHNQQIIQYQQQIE 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1501 KLKNAYEESLDHLETFKRENKNLQEEISDLTEQLGESGKSIHELEKIRKQLDQ-----EKMEIQSALEEAEATLE----- 1570
Cdd:PRK10246 641 QRQQQLLTALAGYALTLPQEDEEASWLATRQQEAQSWQQRQNELTALQNRIQQltpllETLPQSDDLPHSEETVAldnwr 720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1571 --HEEGKILHAQLELHQIKADSERKLAEKDEEMEQAKRNYQRMVDT---LQTSLEAETRSRNEALriKKKMEGDLNEMEI 1645
Cdd:PRK10246 721 qvHEQCLSLHSQLQTLQQQDVLEAQRLQKAQAQFDTALQASVFDDQqafLAALLDEETLTQLEQL--KQNLENQRQQAQT 798
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1646 QLSQANRQAAEAQKQVKILQSYLKDTQiQLDDALRA-SEDLKENIAIV-ERRNTLLQAE--LEELRSLVEQTERARKLSE 1721
Cdd:PRK10246 799 LVTQTAQALAQHQQHRPDGLDLTVTVE-QIQQELAQlAQQLRENTTRQgEIRQQLKQDAdnRQQQQALMQQIAQATQQVE 877
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1205-1428 |
1.80e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1205 ATAASLRKKHADSVAELSEQIDNLQRVKQKLEKEKSEFKLELD----DVTSNMEQMVKAKANLEKLCRSLEDQANEHRTK 1280
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNelqaELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1281 SEENQRTVNELSSLRAKLQTEN-GELSRRLDekesLVSQMTRGKQTYTQHLEDLKRQLEEetkAKNALAHALQSARHDSD 1359
Cdd:COG3883 92 ARALYRSGGSVSYLDVLLGSESfSDFLDRLS----ALSKIADADADLLEELKADKAELEA---KKAELEAKLAELEALKA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1072253241 1360 LLREQFEEEQEAKAELQRILSKANSEVAQwrtkyetdAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAK 1428
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAA--------AEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1386-1525 |
1.93e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 46.36 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1386 VAQWRTKYETDA------IQRTEELEeakKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERsnAAAAA 1459
Cdd:PRK00409 504 IEEAKKLIGEDKeklnelIASLEELE---RELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEK--EAQQA 578
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1072253241 1460 LDKKQRNFDKILAEWKQKFEESQTELESSQ-KEARSlstelfKLKNAYEESLDHLETFKRENKNLQE 1525
Cdd:PRK00409 579 IKEAKKEADEIIKELRQLQKGGYASVKAHElIEARK------RLNKANEKKEKKKKKQKEKQEELKV 639
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
959-1646 |
1.98e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 46.58 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 959 RKLEDECSELKKDIDDLE---------------LTLAKVEKEKHATENKVKNLTEEMAGLDEIivkltKEKKALQEAHQQ 1023
Cdd:TIGR01612 1193 KKLLNEIAEIEKDKTSLEevkginlsygknlgkLFLEKIDEEKKKSEHMIKAMEAYIEDLDEI-----KEKSPEIENEMG 1267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1024 ALDDLQAEEDKVNTltkakakleqqvddlegSLEQEKKIRMDLERvkrklegdvklSQESLMDLENdkqqleeklkkKDF 1103
Cdd:TIGR01612 1268 IEMDIKAEMETFNI-----------------SHDDDKDHHIISKK-----------HDENISDIRE-----------KSL 1308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1104 EVSQLNTRIEDEQNVCIQLQKKMKELQarieeleeeleaertarakveKLRCDLSRELEEISERLEeaggatsvQMELNK 1183
Cdd:TIGR01612 1309 KIIEDFSEESDINDIKKELQKNLLDAQ---------------------KHNSDINLYLNEIANIYN--------ILKLNK 1359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1184 KReaeflKLRRDLEESTlhseataASLRKKHADSVAELSEQIDNLQRVKQ--KLEKEKSEFKLELDDvtSNMEQMVKAKA 1261
Cdd:TIGR01612 1360 IK-----KIIDEVKEYT-------KEIEENNKNIKDELDKSEKLIKKIKDdiNLEECKSKIESTLDD--KDIDECIKKIK 1425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1262 NLEKLCRSLEDQANEHRTKSEENQRTVNelsslrakLQTENGELSRRlDEKESLVSQMTRGKQTYTQHLEDLKRQLEEET 1341
Cdd:TIGR01612 1426 ELKNHILSEESNIDTYFKNADENNENVL--------LLFKNIEMADN-KSQHILKIKKDNATNDHDFNINELKEHIDKSK 1496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1342 KAKNAlAHALQSARHDSDLLREQFeeeqeaKAELQRILSKANS-EVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEE 1420
Cdd:TIGR01612 1497 GCKDE-ADKNAKAIEKNKELFEQY------KKDVTELLNKYSAlAIKNKFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQ 1569
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1421 aveavnaKCSSLEKTKHRlqneIEDLMVDLERSNAAAAALDKKQRNFDKIL---AEWKQKFEESQTELESSQKEARSLS- 1496
Cdd:TIGR01612 1570 -------KIKEIKKEKFR----IEDDAAKNDKSNKAAIDIQLSLENFENKFlkiSDIKKKINDCLKETESIEKKISSFSi 1638
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1497 ----TELFKLKNAYEESLDHLETFKRENKNLQEEISDLTEQLGESGK------------SIHELEKIRKQLDQEKMEIQS 1560
Cdd:TIGR01612 1639 dsqdTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELDELDSEIEKieidvdqhkknyEIGIIEKIKEIAIANKEEIES 1718
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1561 ALEEAEATLEHEEGKILHAQLElhqiKADSERKLAEKDEEM----EQAKRNYQRMVDTLQT-SLEAET---------RSR 1626
Cdd:TIGR01612 1719 IKELIEPTIENLISSFNTNDLE----GIDPNEKLEEYNTEIgdiyEEFIELYNIIAGCLETvSKEPITydeikntriNAQ 1794
|
730 740
....*....|....*....|...
gi 1072253241 1627 NEALR---IKKKMEGDLNEMEIQ 1646
Cdd:TIGR01612 1795 NEFLKiieIEKKSKSYLDDIEAK 1817
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
891-1195 |
2.07e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 46.46 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 891 LEEKMVSLLQEKNDLQLqVQAEQDNLADADERCEQLIKNKIQLEAKLkeqtERLEDEeeMNAELTAKKRKLEDECSELKK 970
Cdd:PRK05771 14 LKSYKDEVLEALHELGV-VHIEDLKEELSNERLRKLRSLLTKLSEAL----DKLRSY--LPKLNPLREEKKKVSVKSLEE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 971 DIDDLELTLAKVEKEkhatenkVKNLTEEMAGLDEIIVKLTKEKKALQEAHqqALD-DLQAEEDKVNTLTKAKAKLEQQV 1049
Cdd:PRK05771 87 LIKDVEEELEKIEKE-------IKELEEEISELENEIKELEQEIERLEPWG--NFDlDLSLLLGFKYVSVFVGTVPEDKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1050 DDLEGSLEQEKkirmdLERVKRKLEGDVKLsqesLMDLENDKQQLEEKLKKKDFEvsqlNTRIEDEQNVCIQLQKKMKEL 1129
Cdd:PRK05771 158 EELKLESDVEN-----VEYISTDKGYVYVV----VVVLKELSDEVEEELKKLGFE----RLELEEEGTPSELIREIKEEL 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1072253241 1130 qarieeleeeleaertarAKVEKLRCDLSRELEEISERLEEAGGATSVQMELNKKREAEFLKLRRD 1195
Cdd:PRK05771 225 ------------------EEIEKERESLLEELKELAKKYLEELLALYEYLEIELERAEALSKFLKT 272
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1615-1850 |
2.12e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 46.04 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1615 LQTSLEAETRSRNEALR----IKKKMEGDLNEMEIQLSQANRQAAEAQKQVKILQSYLKDTQIQLDDALRASEDLKE-NI 1689
Cdd:pfam07888 32 LQNRLEECLQERAELLQaqeaANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSAsSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1690 AIVERRNTLLQAELEELRSLVEQTERARKLSEQELiETSERVQLLHSQNTSLINQKKKMESDLSQLQTEMEEAVQECRNa 1769
Cdd:pfam07888 112 ELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVL-ERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRS- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1770 eekakkaitdaamMAEELKKEQDTSAHLERMKKNMEQTIKDLQQRLDEAEQIALkggkkQLQKLEARVRELDNELEAEQK 1849
Cdd:pfam07888 190 -------------LSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEA-----ENEALLEELRSLQERLNASER 251
|
.
gi 1072253241 1850 R 1850
Cdd:pfam07888 252 K 252
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1270-1427 |
2.18e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.92 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1270 LEDQANEHRTKSEENQRTVNELSSLRAKLQTENGELSRRLDEKESLVSQMTRGKQTYTQHLEDLKRQLEEETKAK--NAL 1347
Cdd:COG1579 15 LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyEAL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1348 AHALQSARHDSDLLREQFEEEQEAKAELQRILSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNA 1427
Cdd:COG1579 95 QKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1146-1828 |
2.27e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 46.36 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1146 ARAKVEKLRcdlsRELEEISERLEEAGGATSVQMELNKKREAEFLKLR--RDLEESTLHSEATAASLRKKHADSVAEL-S 1222
Cdd:NF041483 598 ARAEAERIR----REAAEETERLRTEAAERIRTLQAQAEQEAERLRTEaaADASAARAEGENVAVRLRSEAAAEAERLkS 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1223 EQIDNLQRVK-------QKLEKEKSEfkleldDVTSNMEQMVKAKANLEKLCRSLEDQANEHRTKSEENQRTVneLSSLR 1295
Cdd:NF041483 674 EAQESADRVRaeaaaaaERVGTEAAE------ALAAAQEEAARRRREAEETLGSARAEADQERERAREQSEEL--LASAR 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1296 AKLQTENGELSRRLDEKESLVSQMTRGKQTYTQHLED----LKRQLEEE-TKAKNALAHALQSAR----HDSDLLR-EQF 1365
Cdd:NF041483 746 KRVEEAQAEAQRLVEEADRRATELVSAAEQTAQQVRDsvagLQEQAEEEiAGLRSAAEHAAERTRteaqEEADRVRsDAY 825
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1366 EEEQEAKAELQRILSKANSEVAQWRTKYE---TDAIQRTEELEEAKKKLAQRLQ-EAEEAVEAVNAKCSSLEKTKHRLQN 1441
Cdd:NF041483 826 AERERASEDANRLRREAQEETEAAKALAErtvSEAIAEAERLRSDASEYAQRVRtEASDTLASAEQDAARTRADAREDAN 905
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1442 EIedlmvdleRSNAAAAAldkkQRNFDKILAEWKQKFEESQTELESSQKEARSLSTELFKLKNAYEESLdhLETFKRENK 1521
Cdd:NF041483 906 RI--------RSDAAAQA----DRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQL--IAEATGEAE 971
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1522 NLQEEISDLTeqlgesGKSIHELEKIRKQLDQEKMEIQSALEEAEAtleheegkilhaqlelhQIKADSERKLAEKDEEM 1601
Cdd:NF041483 972 RLRAEAAETV------GSAQQHAERIRTEAERVKAEAAAEAERLRT-----------------EAREEADRTLDEARKDA 1028
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1602 EQAKRNYQRMVDTLQTSLEAE-----TRSRNEALRIKKKMEGDLNEM-EIQLSQANRQAAEAQKQVkilQSYLKDTQIQL 1675
Cdd:NF041483 1029 NKRRSEAAEQADTLITEAAAEadqltAKAQEEALRTTTEAEAQADTMvGAARKEAERIVAEATVEG---NSLVEKARTDA 1105
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1676 DDALRASEdlKENIAIVERRNTL---LQAELEELRslveqtERARKLSEQELIETSERV-QLLHSQNTSLINQKKKMESD 1751
Cdd:NF041483 1106 DELLVGAR--RDATAIRERAEELrdrITGEIEELH------ERARRESAEQMKSAGERCdALVKAAEEQLAEAEAKAKEL 1177
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1752 LSQLQTE---------------MEEAVQE----CRNAEEKAKKAITDAAMMAEELKKEQDTsahLERMKKNMEQTIKDLQ 1812
Cdd:NF041483 1178 VSDANSEaskvriaavkkaeglLKEAEQKkaelVREAEKIKAEAEAEAKRTVEEGKRELDV---LVRRREDINAEISRVQ 1254
|
730
....*....|....*.
gi 1072253241 1813 QRLDEAEQIALKGGKK 1828
Cdd:NF041483 1255 DVLEALESFEAPSGGG 1270
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
1399-1816 |
2.76e-04 |
|
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.
Pssm-ID: 408741 [Multi-domain] Cd Length: 876 Bit Score: 45.92 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1399 QRTEELEEAKKKLaqrlqEAEEAVEAVNAKCSSL-EKTKHRLQNEIEDLMVDLER-----SNAAAAALDKKQRNFDKILA 1472
Cdd:pfam18971 390 QRALSQEEIRNKV-----DFMEFLAQNNTKLDNLsEKEKEKFQNEIEDFQKDSKAyldalGNDRIAFVSKKDTKHSALIT 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1473 EWKQKfEESQTELESSQKEARSLSTEL--------------------FKLKNAYEE---------SLDHLE--------- 1514
Cdd:pfam18971 465 EFNNG-DLSYTLKDYGKKADKALDREKnvtlqgslkhdgvmfvdysnFKYTNASKNpnkgvgatnGVSHLEagfnkvavf 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1515 -----------TFKRenKNLQEEISDLTEQLGESGKSIHELEKIRKQLDQEKMEIQSALEEAEATLEHEegkilhaqlel 1583
Cdd:pfam18971 544 nlpdlnnlaitSFVR--RNLENKLTAKGLSLQEANKLIKDFLSSNKELAGKALNFNKAVAEAKSTGNYD----------- 610
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1584 hqikadsERKLAEKDeeMEQAKRNYQRMVDTLQTSLEAETRSRNealRIKKKMEGDLNEMEIqLSQANRQAAEAQKQVKI 1663
Cdd:pfam18971 611 -------EVKKAQKD--LEKSLRKREHLEKEVEKKLESKSGNKN---KMEAKAQANSQKDEI-FALINKEANRDARAIAY 677
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1664 LQSyLKDTQIQLDDAL-RASEDLKEniaiverrntlLQAELEELR-------SLVEQTERARKLSEQELIETSERVQLLH 1735
Cdd:pfam18971 678 TQN-LKGIKRELSDKLeKISKDLKD-----------FSKSFDEFKngknkdfSKAEETLKALKGSVKDLGINPEWISKVE 745
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1736 SQNTSL---INQKKKMESDLSQLQTEMEEAV------QECRNAEEKAKKAITDAAMMAEELKKEQdTSAHLERMKKnmEQ 1806
Cdd:pfam18971 746 NLNAALnefKNGKNKDFSKVTQAKSDLENSVkdviinQKVTDKVDNLNQAVSVAKAMGDFSRVEQ-VLADLKNFSK--EQ 822
|
490
....*....|
gi 1072253241 1807 TIKDLQQRLD 1816
Cdd:pfam18971 823 LAQQAQKNED 832
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1122-1355 |
2.78e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1122 LQKKMKELQARIEEleeeleaertARAKVEKLR-----CDLSRELEEISERLEEAggatsvqmelnkkrEAEFLKLRRDL 1196
Cdd:COG3206 180 LEEQLPELRKELEE----------AEAALEEFRqknglVDLSEEAKLLLQQLSEL--------------ESQLAEARAEL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1197 EEstlhSEATAASLRKKHADSVAELSEQIDN--LQRVKQKLEKEKSEFKLELDDVTSNMEQMVKAKANLEKLCRSLEdqa 1274
Cdd:COG3206 236 AE----AEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQ--- 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1275 nehrtksEENQRTVNELSSLRAKLQTENGELSRRLDEKESLVSQMTRGKQTYTQhledLKRQLEEETKAKNALAHALQSA 1354
Cdd:COG3206 309 -------QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRR----LEREVEVARELYESLLQRLEEA 377
|
.
gi 1072253241 1355 R 1355
Cdd:COG3206 378 R 378
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1699-1935 |
2.87e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.53 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1699 LQAELEELRSLVEQTERARKLSEQELIETSERVQLLHSQNTSLINQKKKMESDLSQLQTEMEEAVQECRNAEEKAKKAIT 1778
Cdd:COG4942 32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1779 DAAMMAE----ELKKEQDTSAHLERMKKNMEQTIKDLQQRLDEaeqiaLKGGKKQLQKLEARVRELDNELEAEQKRNAEs 1854
Cdd:COG4942 112 ALYRLGRqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEE-----LRADLAELAALRAELEAERAELEALLAELEE- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1855 vkgmrkyerRIKELTYQTEEDRKNLARLQdlvdklqlkvktykRQAEESEEQANTSLSKFRKVQHELDEAEERADIAESQ 1934
Cdd:COG4942 186 ---------ERAALEALKAERQKLLARLE--------------KELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
.
gi 1072253241 1935 V 1935
Cdd:COG4942 243 T 243
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
861-1020 |
3.07e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 861 AETEKEMQTMKEEFQKLKEALEkseARRKDLEEKMVSLLQEKNDLQLQVQAEQDNLADAD--------------ERCEQL 926
Cdd:COG4942 79 AALEAELAELEKEIAELRAELE---AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVrrlqylkylaparrEQAEEL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 927 IKNKIQLEAKLKEQTERLEDEEEMNAELTAKKRKLEdecselkKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEI 1006
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEERAALE-------ALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
170
....*....|....
gi 1072253241 1007 IVKLTKEKKALQEA 1020
Cdd:COG4942 229 IARLEAEAAAAAER 242
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1549-1854 |
3.25e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 45.82 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1549 KQLDQEkmeiqsaLEEAEATLEHEEGKILHA-QLELHQIkadSERKLA-EKDEEMEQAKRNYQRMVDTLQTSLEAEtrsR 1626
Cdd:PRK10929 26 KQITQE-------LEQAKAAKTPAQAEIVEAlQSALNWL---EERKGSlERAKQYQQVIDNFPKLSAELRQQLNNE---R 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1627 NEALRIKKKMEGDlnEMEIQLSQANRQAAEAQKQVKILQsylkDTQIQLDDALrasedlkeniaiverrNTLLQaeleel 1706
Cdd:PRK10929 93 DEPRSVPPNMSTD--ALEQEILQVSSQLLEKSRQAQQEQ----DRAREISDSL----------------SQLPQ------ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1707 rslvEQTERARKLSEQElietsERVQLLHSQNTSLinqkkkMESDLSQLQtemeeavqecrnAEEKAKKAITDaammaeE 1786
Cdd:PRK10929 145 ----QQTEARRQLNEIE-----RRLQTLGTPNTPL------AQAQLTALQ------------AESAALKALVD------E 191
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1072253241 1787 LKkeqdtsahLERMKKNMEQTIKDLQQRLdeaeqialkgGKKQLQKLEARVRELDNELEAEQKRNAES 1854
Cdd:PRK10929 192 LE--------LAQLSANNRQELARLRSEL----------AKKRSQQLDAYLQALRNQLNSQRQREAER 241
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1346-1569 |
3.48e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1346 ALAHALQSARHDSDLLREQFEEEQEAKAELQRILSKAnsevaqwrtkyetdaiqrtEELEEAKKKLAQRLQEAEEAVEAV 1425
Cdd:COG3883 10 TPAFADPQIQAKQKELSELQAELEAAQAELDALQAEL-------------------EELNEEYNELQAELEALQAEIDKL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1426 NAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAALDK--KQRNFDKILAEWK--QKFEESQTELESSQKEARslsTELFK 1501
Cdd:COG3883 71 QAEIAEAEAEIEERREELGERARALYRSGGSVSYLDVllGSESFSDFLDRLSalSKIADADADLLEELKADK---AELEA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1072253241 1502 LKNAYEESLDHLETFKREnknLQEEISDLTEQLGESGKSIHELEKIRKQLDQEKMEIQSALEEAEATL 1569
Cdd:COG3883 148 KKAELEAKLAELEALKAE---LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
859-1132 |
3.50e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 45.66 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 859 KSAETEKEMQTMKEEFQKLKEALEKS-----EARRKDLEEkMVSLLQEKNDLQLQVQAEQDNLADADERCEQLIKNKI-- 931
Cdd:PLN02939 118 NSKDGEQLSDFQLEDLVGMIQNAEKNilllnQARLQALED-LEKILTEKEALQGKINILEMRLSETDARIKLAAQEKIhv 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 932 -----QLEAKLKEQTERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKekhaTENKVKNLTEEMAGLDEI 1006
Cdd:PLN02939 197 eileeQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAE----TEERVFKLEKERSLLDAS 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1007 IVKLTKEKKALQEAHQQaLDDLQAEE--DKVNTLTKAKAKLEQQVDDLEGSLEQEKkirmdlervkrklegdvklsqesl 1084
Cdd:PLN02939 273 LRELESKFIVAQEDVSK-LSPLQYDCwwEKVENLQDLLDRATNQVEKAALVLDQNQ------------------------ 327
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1072253241 1085 mDLENDKQQLEEKLKKKDfeVSQLNTRIEDeqnvciQLQKKMKELQAR 1132
Cdd:PLN02939 328 -DLRDKVDKLEASLKEAN--VSKFSSYKVE------LLQQKLKLLEER 366
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1351-1909 |
3.76e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 45.59 E-value: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1351 LQSARHDSDLLREQFEEE-QEAKAELQRILSKANSEVAQWRTKYETDAIQRTEELEE----------------------- 1406
Cdd:NF041483 78 LRNAQIQADQLRADAERElRDARAQTQRILQEHAEHQARLQAELHTEAVQRRQQLDQelaerrqtveshvnenvawaeql 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1407 -------AKKKLAQRLQEAEEAVEAVNAKCSSL-EKTKHRLQNEIEdlmvdlERSNAAAAALDKKQRNFDKILAEWKQKF 1478
Cdd:NF041483 158 rartesqARRLLDESRAEAEQALAAARAEAERLaEEARQRLGSEAE------SARAEAEAILRRARKDAERLLNAASTQA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1479 EESQTELE-------SSQKEARSLSTELFKlknAYEESLDHLETFKRENKNLQEEIsdLTEQLGESGKSIHELEKIRKQL 1551
Cdd:NF041483 232 QEATDHAEqlrsstaAESDQARRQAAELSR---AAEQRMQEAEEALREARAEAEKV--VAEAKEAAAKQLASAESANEQR 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1552 DQEKME-----IQSALEEAEATLEHEEGKILHAQLELHQIKADSERKLAEKDEE-----MEQAKRNYQRMVDTLQTSLEA 1621
Cdd:NF041483 307 TRTAKEeiarlVGEATKEAEALKAEAEQALADARAEAEKLVAEAAEKARTVAAEdtaaqLAKAARTAEEVLTKASEDAKA 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1622 ETRSRN-EALRIKKKMEgdlnemeiqlSQANRQAAEAQKQVKILQSYLKDtqiqlddalraseDLKENIAiverRNTLLQ 1700
Cdd:NF041483 387 TTRAAAeEAERIRREAE----------AEADRLRGEAADQAEQLKGAAKD-------------DTKEYRA----KTVELQ 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1701 AELEELRSLVEQTeRARKLSEQELIETSER---VQLLHSQNTSLINQKKKMESDLSQLQTemeeavqecrNAEEKAKKAI 1777
Cdd:NF041483 440 EEARRLRGEAEQL-RAEAVAEGERIRGEARreaVQQIEEAARTAEELLTKAKADADELRS----------TATAESERVR 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1778 TDAAMMAEELKKEQDTSahLERMKKNMEQTIKDLQQRLD----EAEQIALKGGKKQLQKLEARVRELDNEL-----EAEQ 1848
Cdd:NF041483 509 TEAIERATTLRRQAEET--LERTRAEAERLRAEAEEQAEevraAAERAARELREETERAIAARQAEAAEELtrlhtEAEE 586
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1072253241 1849 KRNA--ESVKGMRKYERRI-KELTYQTEEDRKNLARlqdlvdklqlKVKTYKRQAEESEEQANT 1909
Cdd:NF041483 587 RLTAaeEALADARAEAERIrREAAEETERLRTEAAE----------RIRTLQAQAEQEAERLRT 640
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1591-1918 |
4.33e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 45.35 E-value: 4.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1591 ERKLAEKDEEMEQAKRNYQRMVDTLQTSLEAETRSRNEALRIKKKMEGDLNEMEIQLsqANRQAAEAQKQVKILQSYLKD 1670
Cdd:pfam02463 171 KKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLL--YLDYLKLNEERIDLLQELLRD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1671 TQIQLDDALRASEDLKENIAIVERRNTLLQAELEELRSLVEQTERARKLSEQELIETSERVQLLHSQNTSLINQKKKMES 1750
Cdd:pfam02463 249 EQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEK 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1751 DLSQLQTEMEEA-----VQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHlermKKNMEQTIKDLQQRLDEAEQIALKG 1825
Cdd:pfam02463 329 ELKKEKEEIEELekelkELEIKREAEEEEEEELEKLQEKLEQLEEELLAKK----KLESERLSSAAKLKEEELELKSEEE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1826 GKKQLQKLEARVRELDNELEAEQKRNAESVKGMRKYERRIKELTYQTEEDRKNLARLQDLVDKLQLKVKTYKRQAEESEE 1905
Cdd:pfam02463 405 KEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQE 484
|
330
....*....|...
gi 1072253241 1906 QANTSLSKFRKVQ 1918
Cdd:pfam02463 485 QLELLLSRQKLEE 497
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1247-1497 |
4.36e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 4.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1247 DDVTSNMEQMVKAKANLEKLCRSLEDQANEHRTKSEENQRTVNELSSLRAKLQTENGELSRRLDEKESLVSQMTRGKQTY 1326
Cdd:COG3883 23 KELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1327 T--------QHLEDLKRQLEeetkaknalahALQS-ARHDSDLLREQfeeeQEAKAELQRILSKANSEVAqwrtkyetda 1397
Cdd:COG3883 103 SyldvllgsESFSDFLDRLS-----------ALSKiADADADLLEEL----KADKAELEAKKAELEAKLA---------- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1398 iqrteELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAALDKKQRNFDKILAEWKQK 1477
Cdd:COG3883 158 -----ELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
250 260
....*....|....*....|
gi 1072253241 1478 FEESQTELESSQKEARSLST 1497
Cdd:COG3883 233 AAAAAAAAAAAASAAGAGAA 252
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
863-1073 |
5.36e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 43.28 E-value: 5.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 863 TEKEMQTMKEEFQKLKEALEKSEARRKDLEEKMVSLLQEKNDLQLQ----VQAEQDNLAdadercEQLIKNKIQLEAKLK 938
Cdd:COG1842 28 LDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKarlaLEKGREDLA------REALERKAELEAQAE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 939 EQTERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVK-NLTEEMAGLDEIivkltKEKKAL 1017
Cdd:COG1842 102 ALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKAQEKVNEALSGiDSDDATSALERM-----EEKIEE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1072253241 1018 QEAHQQALDDLQAEEDkvntltkakakLEQQVDDLEGSLEQEKkirmDLERVKRKL 1073
Cdd:COG1842 177 MEARAEAAAELAAGDS-----------LDDELAELEADSEVED----ELAALKAKM 217
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
875-1108 |
5.99e-04 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 44.93 E-value: 5.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 875 QKLKEALEKSEARRKDLEEKMVSLLQEkndLQLQVQA------EQDNLADADERCEQLIKNKIQL----EAKLKEQterL 944
Cdd:PLN03188 1043 ESPEKKLEQERLRWTEAESKWISLAEE---LRTELDAsralaeKQKHELDTEKRCAEELKEAMQMamegHARMLEQ---Y 1116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 945 EDEEEMNAELTAKKRKLEDECSELKKD-------------IDDL--ELTLAKVEKEKHAT----ENK-----VKNLTEEM 1000
Cdd:PLN03188 1117 ADLEEKHIQLLARHRRIQEGIDDVKKAaaragvrgaeskfINALaaEISALKVEREKERRylrdENKslqaqLRDTAEAV 1196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1001 AGLDEIIVKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKAKLEQQVDDLEgslEQEKKIRMDLERVKRKLEGDVKLS 1080
Cdd:PLN03188 1197 QAAGELLVRLKEAEEALTVAQKRAMDAEQEAAEAYKQIDKLKRKHENEISTLN---QLVAESRLPKEAIRPACNDDCMAK 1273
|
250 260 270
....*....|....*....|....*....|..
gi 1072253241 1081 QESLMDLENDKQQLEEKL----KKKDFEVSQL 1108
Cdd:PLN03188 1274 YDAGEPLSEGDQQWREEFepfyKKEDGELSKL 1305
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1028-1165 |
6.10e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 6.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1028 LQAEEDKVNTLTKAKAKLEQQVDDLEgsLEQEKKIrmdlERVKRKLEGDVKLSQESLMDLENDKQQLEEKLKKKDFEVSQ 1107
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKEAL--LEAKEEI----HKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEK 107
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1072253241 1108 LNTRIEDEQNvciQLQKKMKELQARieeleeeleaertaRAKVEKLRCDLSRELEEIS 1165
Cdd:PRK12704 108 REEELEKKEK---ELEQKQQELEKK--------------EEELEELIEEQLQELERIS 148
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1050-1246 |
6.17e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.85 E-value: 6.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1050 DDLEGSLEQ-EKKI--RMDLERVK-RKLEGdvkLS-QESLMDLENDKQQLEEKLKKKDfevsqlntrIEDEQNVCIQLQK 1124
Cdd:COG2433 346 DAYKNKFERvEKKVppDVDRDEVKaRVIRG---LSiEEALEELIEKELPEEEPEAERE---------KEHEERELTEEEE 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1125 KMKELQARIEeleeeleaerTARAKVEKLRCDLsRELEEISERLEEaggatsvqmELNKKREAEFLKLRRDLEESTLhsE 1204
Cdd:COG2433 414 EIRRLEEQVE----------RLEAEVEELEAEL-EEKDERIERLER---------ELSEARSEERREIRKDREISRL--D 471
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1072253241 1205 ATAASLRKKhadsVAELSEQIDNLQRvkqKLEKEKSEFKLEL 1246
Cdd:COG2433 472 REIERLERE----LEEERERIEELKR---KLERLKELWKLEH 506
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
978-1188 |
6.27e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 6.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 978 TLAKVEKEKHATENKVKNLTEEMAGLDEIIVKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLE 1057
Cdd:COG3883 10 TPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1058 ------QEKKIRMD-----------------LERVKRKLEGDVKLsqesLMDLENDKQQLEEKLKKKDFEVSQLNTRIED 1114
Cdd:COG3883 90 eraralYRSGGSVSyldvllgsesfsdfldrLSALSKIADADADL----LEELKADKAELEAKKAELEAKLAELEALKAE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1072253241 1115 EQNVCIQLQKKMKELQARIeelEEELEAERTARAKVEKLRCDLSRELEEISERLEEAGGATSVQMELNKKREAE 1188
Cdd:COG3883 166 LEAAKAELEAQQAEQEALL---AQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
851-1169 |
6.95e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.44 E-value: 6.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 851 YFKIKPLLKSAE-----TEKEMQTMKEEFQKLKEALEKSEARRKDLEEKMvsllqekNDLQLQVQAEQDNLADADErceq 925
Cdd:PRK04778 100 FRKAKHEINEIEslldlIEEDIEQILEELQELLESEEKNREEVEQLKDLY-------RELRKSLLANRFSFGPALD---- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 926 liknkiQLEAKLKEQTERLEDEEEMNAE---LTAKK--RKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKN----L 996
Cdd:PRK04778 169 ------ELEKQLENLEEEFSQFVELTESgdyVEAREilDQLEEELAALEQIMEEIPELLKELQTELPDQLQELKAgyreL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 997 TEEMAGLDEiiVKLTKEKKALQEAHQQALDDLQ------AEE------DKVNTL-------TKAKAKLEQQVDDLEGSL- 1056
Cdd:PRK04778 243 VEEGYHLDH--LDIEKEIQDLKEQIDENLALLEeldldeAEEkneeiqERIDQLydilereVKARKYVEKNSDTLPDFLe 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1057 ---EQEKKIRMDLERVKRKL---EGDVKLS---QESLMDLENDKQQLEEKLKKKDFEVSQLNTRIEDEQNVCIQLQKKMK 1127
Cdd:PRK04778 321 hakEQNKELKEEIDRVKQSYtlnESELESVrqlEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQE 400
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1072253241 1128 ELQARIeelEEELEAERTARAKVEKLRcdlsRELEEISERLE 1169
Cdd:PRK04778 401 KLSEML---QGLRKDELEAREKLERYR----NKLHEIKRYLE 435
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
848-1009 |
7.01e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 43.85 E-value: 7.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 848 MKLYFKIKPLL--KSAETEKEMQTMKEEFQKLKEALEKSEARRKDLEEKMVSLLQEKNDLQLQVQAEQDNLADADERCEQ 925
Cdd:smart00787 139 MKLLEGLKEGLdeNLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQ 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 926 LIKNKIQLEAKLKEQTERLEDEEEmnaELTAKKRKLEDECSELKK-----------DIDDLELTLAKVEKEKHATENKVK 994
Cdd:smart00787 219 EIMIKVKKLEELEEELQELESKIE---DLTNKKSELNTEIAEAEKkleqcrgftfkEIEKLKEQLKLLQSLTGWKITKLS 295
|
170
....*....|....*
gi 1072253241 995 NLTEEMAGLDEIIVK 1009
Cdd:smart00787 296 GNTLSMTYDREINLV 310
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
1261-1574 |
7.24e-04 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 43.92 E-value: 7.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1261 ANLEKLCRSLEDQANEHRTKSEENQRTVNELSSLRaklqtengelsRRLDEKESLVSQMTRG-KQTYTQHLEDLKRQLEE 1339
Cdd:pfam04108 3 SSAQDLCRWANELLTDARSLLEELVVLLAKIAFLR-----------RGLSVQLANLEKVREGlEKVLNELKKDFKQLLKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1340 ETKAKNALAHALQSARhdSDLLREQFEEEQEAKAELQRILSKANSEVAQWRTKYETDAIQRT-EELEEAKKKLAQRLQEA 1418
Cdd:pfam04108 72 LDAALERLEETLDKLR--NTPVEPALPPGEEKQKTLLDFIDEDSVEILRDALKELIDELQAAqESLDSDLKRFDDDLRDL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1419 EEAVEAVNAKCSSLEKTKHRLQnEIEDLMVDLersnaaAAALDKKQRNFDKILAEWKQKFEESQTELESSQKEARSL--- 1495
Cdd:pfam04108 150 QKELESLSSPSESISLIPTLLK-ELESLEEEM------ASLLESLTNHYDQCVTAVKLTEGGRAEMLEVLENDARELddv 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1496 STELFK----LKNAYEESLDHLETFKRENKNLQEEISDLTEQLGESGKSIHELEKIRKQLDQEKMEIQSALEEAEATLEH 1571
Cdd:pfam04108 223 VPELQDrldeMENNYERLQKLLEQKNSLIDELLSALQLIAEIQSRLPEYLAALKEFEERWEEEKETIEDYLSELEDLREF 302
|
...
gi 1072253241 1572 EEG 1574
Cdd:pfam04108 303 YEG 305
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1022-1820 |
7.79e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.56 E-value: 7.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1022 QQALDDLQAEEDKVNTLTKAKAKLEQQVDDLEgsleqekkirmDLERVKRKLEGDVKLSQESLMDLENDKQQlEEKLKKK 1101
Cdd:COG3096 285 ERALELRRELFGARRQLAEEQYRLVEMARELE-----------ELSARESDLEQDYQAASDHLNLVQTALRQ-QEKIERY 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1102 DFEVSQLNTRIEDEQNVCIQLQKKMKELQARieeleeeleaERTARAKVEKLR---CDLSRELEEISERleeaggATSVQ 1178
Cdd:COG3096 353 QEDLEELTERLEEQEEVVEEAAEQLAEAEAR----------LEAAEEEVDSLKsqlADYQQALDVQQTR------AIQYQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1179 MELNKKREAEFLklrrdLEESTLhseaTAASLRKKHADSVAELSEQIDNLQRVKQKL---EKEKSEFK--LEL-----DD 1248
Cdd:COG3096 417 QAVQALEKARAL-----CGLPDL----TPENAEDYLAAFRAKEQQATEEVLELEQKLsvaDAARRQFEkaYELvckiaGE 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1249 VTSN-------------------MEQMVKAKANLEKLCRSLEDQANEHRTKSEENQRTVNELSSlRAKLQTENGELSRRL 1309
Cdd:COG3096 488 VERSqawqtarellrryrsqqalAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDA-AEELEELLAELEAQL 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1310 DEKESLVSQMTRGKQTYTQHLEDLKRQLEEETKAKNALAHALQSARHDSDLLREQFEEEQEAKAELQRILSKansevaqw 1389
Cdd:COG3096 567 EELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLER-------- 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1390 rtkyETDAIQRTEELEEAKKKLaqrLQEAEEAVEAVNAKCSSLEKTKHRLQNE----------IED-------------- 1445
Cdd:COG3096 639 ----EREATVERDELAARKQAL---ESQIERLSQPGGAEDPRLLALAERLGGVllseiyddvtLEDapyfsalygparha 711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1446 -LMVDLERSNAAAAALDKKQRNFDKILAEwKQKFEES---QTELE------SSQKEAR-SLSTELFKLKNAYEESldHLE 1514
Cdd:COG3096 712 iVVPDLSAVKEQLAGLEDCPEDLYLIEGD-PDSFDDSvfdAEELEdavvvkLSDRQWRySRFPEVPLFGRAAREK--RLE 788
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1515 TfkrenknLQEEISDLTEQLGESGKSIHELEKIRKQLDQ----------------EKMEIQSALEEAEATLEHEEGKILH 1578
Cdd:COG3096 789 E-------LRAERDELAEQYAKASFDVQKLQRLHQAFSQfvgghlavafapdpeaELAALRQRRSELERELAQHRAQEQQ 861
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1579 AQLELHQIKADSE--RKLAE-----KDEEMEQAKRNYQRMVDTLQTSlEAETRSRNEALRikkkmegdlnEMEIQLSqAN 1651
Cdd:COG3096 862 LRQQLDQLKEQLQllNKLLPqanllADETLADRLEELREELDAAQEA-QAFIQQHGKALA----------QLEPLVA-VL 929
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1652 RQAAEAQKQVKILQSYLKDTQIQLDDALRASEDLkeniaiVERRNTLLQAE----LEELRSLVEQTERARKLSEQELIET 1727
Cdd:COG3096 930 QSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEV------VQRRPHFSYEDavglLGENSDLNEKLRARLEQAEEARREA 1003
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1728 SERVQLLHSQNTSLiNQKkkmesdLSQLQTEMEEAVQECRNAEEKAK----KAITDAAMMAEELKKEQDTSAHLERMKKN 1803
Cdd:COG3096 1004 REQLRQAQAQYSQY-NQV------LASLKSSRDAKQQTLQELEQELEelgvQADAEAEERARIRRDELHEELSQNRSRRS 1076
|
890 900
....*....|....*....|....*
gi 1072253241 1804 --------MEQTIKDLQQRLDEAEQ 1820
Cdd:COG3096 1077 qlekqltrCEAEMDSLQKRLRKAER 1101
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1450-1723 |
7.82e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 44.56 E-value: 7.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1450 LERSNAAAAALDKKQRNFDKILAEWKQKFEESQ-TELESSQKEARSLSTELFKLKNAYEESLDhletfkrenkNLQEEIS 1528
Cdd:COG5185 277 SKRLNENANNLIKQFENTKEKIAEYTKSIDIKKaTESLEEQLAAAEAEQELEESKRETETGIQ----------NLTAEIE 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1529 DLTEQLGEsgksihELEKIRKQLDQekMEIQSALEEAEATLEHEEGKILHAQLELHQIKADSERKLAEKDEEMEQAKRNY 1608
Cdd:COG5185 347 QGQESLTE------NLEAIKEEIEN--IVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAA 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1609 QRMVDTLQTSLEAETRSRNEALRIKKKMEGDLNEMEiQLSQANRQAAEAQKQVKILQSYLKDTQIQLDDALRASEDLKEN 1688
Cdd:COG5185 419 DRQIEELQRQIEQATSSNEEVSKLLNELISELNKVM-READEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTL 497
|
250 260 270
....*....|....*....|....*....|....*
gi 1072253241 1689 IAIVERRNTLLQAELEELRSLVEQTERARKLSEQE 1723
Cdd:COG5185 498 KATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRA 532
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1720-1910 |
7.99e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 7.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1720 SEQELIETSERVQLLHSQNTSLINQKKKMESDLSQLQTEMEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDT-SAHLE 1798
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1799 RMKKNMEQT-----------IKDLQQRLDEAEQIAlKGGKKQLQKLEARVRELDNELEAEQKRNAESVKGMRKYERRIKE 1867
Cdd:COG3883 94 ALYRSGGSVsyldvllgsesFSDFLDRLSALSKIA-DADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1072253241 1868 LTYQTEEDRKNLARLQDLVDKLQLKVKTYKRQAEESEEQANTS 1910
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1029-1197 |
8.25e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 8.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1029 QAEEDKVNTLTKAKAKLEQQVDDLEGSLEQ-EKKirmdLERVKRK-----LEGDVKLSQESLMDLENDKQQLEEKLKKKD 1102
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEaEAA----LEEFRQKnglvdLSEEAKLLLQQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1103 FEVSQLNTRIEDEQN---------VCIQLQKKMKELQARIEELEEELEAE----RTARAKVEKLRCDLSRELEEISERLE 1169
Cdd:COG3206 240 ARLAALRAQLGSGPDalpellqspVIQQLRAQLAELEAELAELSARYTPNhpdvIALRAQIAALRAQLQQEAQRILASLE 319
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1072253241 1170 -EAGGATSVQMELNK-------------KREAEFLKLRRDLE 1197
Cdd:COG3206 320 aELEALQAREASLQAqlaqlearlaelpELEAELRRLEREVE 361
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1418-1660 |
8.42e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 8.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1418 AEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAALDKKqrnfdkiLAEWKQKFEESQTELESSQKEARSLST 1497
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAE-------LEALQAEIDKLQAEIAEAEAEIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1498 ELFK-LKNAYEE--SLDHLETFKrENKNLQEEIS--DLTEQLGESGKS-IHELEKIRKQLDQEKMEIQSALEEAEAtleh 1571
Cdd:COG3883 87 ELGErARALYRSggSVSYLDVLL-GSESFSDFLDrlSALSKIADADADlLEELKADKAELEAKKAELEAKLAELEA---- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1572 eegkilhAQLELHQIKADSERKLAEKDEEMEQAKRNYQRMVDTLQtSLEAETRSRNEALRIKKKMEGDLNEMEIQLSQAN 1651
Cdd:COG3883 162 -------LKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLA-ELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
....*....
gi 1072253241 1652 RQAAEAQKQ 1660
Cdd:COG3883 234 AAAAAAAAA 242
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
952-1075 |
8.44e-04 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 43.51 E-value: 8.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 952 AELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIV-KLTKEKKALQeahQQALDDLQA 1030
Cdd:cd22656 110 EELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKdLLTDEGGAIA---RKEIKDLQK 186
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1031 EEDKVNT--LTKAKAKLE---QQVDDLEGSLEQEKKIRMDLERVKRKLEG 1075
Cdd:cd22656 187 ELEKLNEeyAAKLKAKIDelkALIADDEAKLAAALRLIADLTAADTDLDN 236
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1691-1835 |
9.34e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.43 E-value: 9.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1691 IVERRNTLLQAELEELRSLVEQTERARKLSEQELIEtserVQLLHSQNTSLINQ-KKKMESDLSQLQTEMEEAVQECRNA 1769
Cdd:PRK00409 503 IIEEAKKLIGEDKEKLNELIASLEELERELEQKAEE----AEALLKEAEKLKEElEEKKEKLQEEEDKLLEEAEKEAQQA 578
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1072253241 1770 EEKAKKAITDAAMMAEELKKEQDTSAHlermkknmEQTIKDLQQRLDEAEQIALKGGKKQLQKLEA 1835
Cdd:PRK00409 579 IKEAKKEADEIIKELRQLQKGGYASVK--------AHELIEARKRLNKANEKKEKKKKKQKEKQEE 636
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1588-1795 |
9.75e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 9.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1588 ADSERKLAEKD-EEMEQAKRNYQRMVDTLQTSLEAETRSRNEALRIKKKMEGDLNEMEIQLSQANRQAAEAQKQVK--IL 1664
Cdd:COG3883 14 ADPQIQAKQKElSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGerAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1665 QSYLKDTQIQLDDALRASEDLKENI-------AIVERRNTLL------QAELEELRSLVEQTERARKLSEQELIETSERV 1731
Cdd:COG3883 94 ALYRSGGSVSYLDVLLGSESFSDFLdrlsalsKIADADADLLeelkadKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1072253241 1732 QLLHSQNTSLIN----QKKKMESDLSQLQTEMEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSA 1795
Cdd:COG3883 174 EAQQAEQEALLAqlsaEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1510-1816 |
1.16e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 43.37 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1510 LDHLETFKRENKNLQEEISDLTEQLGESGKSIH-----ELEKIRKQLDQekmeiqSALEEAEATLEheegkILHAQLELH 1584
Cdd:pfam00038 17 IDKVRFLEQQNKLLETKISELRQKKGAEPSRLYslyekEIEDLRRQLDT------LTVERARLQLE-----LDNLRLAAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1585 QIKADSERKLAEKdEEMEQAKRNYQRMVDTL---QTSLEAETRSRNEALRIKKKM-EGDLNEMEIQLSQANRQAAEAQKQ 1660
Cdd:pfam00038 86 DFRQKYEDELNLR-TSAENDLVGLRKDLDEAtlaRVDLEAKIESLKEELAFLKKNhEEEVRELQAQVSDTQVNVEMDAAR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1661 VKILQSYLKDTQIQLDD-ALRASEDLKENiaiverrntlLQAELEELRSLVEQTERARKLSEQELIETSERVQLLHSQNT 1739
Cdd:pfam00038 165 KLDLTSALAEIRAQYEEiAAKNREEAEEW----------YQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1740 SLINQKKKMESDLSQLQtemeeavqecrnaeekakkaitdaAMMAEELKKEQDTSAHLER----MKKNMEQTIKDLQQRL 1815
Cdd:pfam00038 235 SLKKQKASLERQLAETE------------------------ERYELQLADYQELISELEAelqeTRQEMARQLREYQELL 290
|
.
gi 1072253241 1816 D 1816
Cdd:pfam00038 291 N 291
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
870-1098 |
1.21e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 44.07 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 870 MKEEFQKLKEALEKSEARRKDLEEkmvslLQEKNDLqLQVQAEQDNLADADERCEQLiknKIQLEAKLKEQTERLEDEEE 949
Cdd:PLN03229 509 LMEKIEKLKDEFNKRLSRAPNYLS-----LKYKLDM-LNEFSRAKALSEKKSKAEKL---KAEINKKFKEVMDRPEIKEK 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 950 MNAeltakkRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMaGLDEIIVKltkeKKALQEAHQQALDDLQ 1029
Cdd:PLN03229 580 MEA------LKAEVASSGASSGDELDDDLKEKVEKMKKEIELELAGVLKSM-GLEVIGVT----KKNKDTAEQTPPPNLQ 648
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1072253241 1030 AEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKkirmdLERVKRKLEGDVKLSQEslmdLENDKQQLEEKL 1098
Cdd:PLN03229 649 EKIESLNEEINKKIERVIRSSDLKSKIELLK-----LEVAKASKTPDVTEKEK----IEALEQQIKQKI 708
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1019-1187 |
1.23e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1019 EAHQQALDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKIRM-------DLERVKRKLEGDVKLSQEslmDLENDK 1091
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEaakteleDLEKEIKRLELEIEEVEA---RIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1092 QQLEEKLKKKDFEvsQLNTRIEdeqnvciQLQKKMKELQARIEELEEELEAERTARAKVEKLRCDLSRELEEISERLEEA 1171
Cdd:COG1579 80 EQLGNVRNNKEYE--ALQKEIE-------SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE 150
|
170
....*....|....*..
gi 1072253241 1172 GGATSVQME-LNKKREA 1187
Cdd:COG1579 151 LAELEAELEeLEAEREE 167
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1607-1953 |
1.27e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1607 NYQRMVDTLQTSLEAETRSRNEAlriKKKMEGDLNEMEIQLSQANRQAAEAQKQVKILQSylkDTQIQLDDALRASEDLK 1686
Cdd:PTZ00121 1080 DFDAKEDNRADEATEEAFGKAEE---AKKTETGKAEEARKAEEAKKKAEDARKAEEARKA---EDARKAEEARKAEDAKR 1153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1687 ENIAiverRNTLLQAELEELRslveQTERARKLSE-QELIETSERVQLLHSQNTSLINQKKKMESdlsqlqtemEEAVQE 1765
Cdd:PTZ00121 1154 VEIA----RKAEDARKAEEAR----KAEDAKKAEAaRKAEEVRKAEELRKAEDARKAEAARKAEE---------ERKAEE 1216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1766 CRNAEEKAKkaiTDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQQRLDEAEQIALKGGKKQLQKLEAR----VRELD 1841
Cdd:PTZ00121 1217 ARKAEDAKK---AEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKkaeeKKKAD 1293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1842 NELEAEQKRNAESVKGMRKYERRIKELTYQTEEDRKNLARLQDLVDKLQLKVKTYKRQAEESEEQANTSLSK-------- 1913
Cdd:PTZ00121 1294 EAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKaeaaekkk 1373
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1072253241 1914 ---------FRKVQHELDEAEERADIAESQVNKLRAKSRDVSTKKSLNE 1953
Cdd:PTZ00121 1374 eeakkkadaAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADE 1422
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1640-1781 |
1.31e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1640 LNEMEIQLSQANRQAAEAQKQVKILQSYLKDTQIQLDDALRASEDLKENIAIVERRNTLLQAELEELRSL---------V 1710
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNkeyealqkeI 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1072253241 1711 EQTERARKLSEQELIETSERVQLLHSQNTSLINQKKKMESDLSQLQTEMEEAVQECRNAEEKAKKAITDAA 1781
Cdd:COG1579 99 ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELA 169
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
859-1016 |
1.32e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 859 KSAETEKE--MQTMKEEFQKLKEALEK-SEARRKDLEEKMVSLLQEKNDLQlqvqaeqDNLADADERCEQLIKNKIQLEA 935
Cdd:PRK12704 49 KEAEAIKKeaLLEAKEEIHKLRNEFEKeLRERRNELQKLEKRLLQKEENLD-------RKLELLEKREEELEKKEKELEQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 936 KLKEQTERLEDEEEMNAELtakKRKLEdECSELKKDiDDLELTLAKVEKE-KHATENKVKNLTEEmagldeiiVKLTKEK 1014
Cdd:PRK12704 122 KQQELEKKEEELEELIEEQ---LQELE-RISGLTAE-EAKEILLEKVEEEaRHEAAVLIKEIEEE--------AKEEADK 188
|
..
gi 1072253241 1015 KA 1016
Cdd:PRK12704 189 KA 190
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1559-1950 |
1.32e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 43.85 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1559 QSALEEAEATLEHEEGKILHAQLELHQIKADSERKLAEKdeeMEQAKRNYQRMVDTLQTSLEAETRSRnealrIKKKMEG 1638
Cdd:NF033838 54 ESQKEHAKEVESHLEKILSEIQKSLDKRKHTQNVALNKK---LSDIKTEYLYELNVLKEKSEAELTSK-----TKKELDA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1639 DLNEMEIQLSQANRQAAEAQKQVkilqsylkdtqiqlDDALRASEDLKENIAIVERRNTLLQAELEelrslVEQTERARK 1718
Cdd:NF033838 126 AFEQFKKDTLEPGKKVAEATKKV--------------EEAEKKAKDQKEEDRRNYPTNTYKTLELE-----IAESDVEVK 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1719 LSEQELIetseRVQLLHSQNTSLINQ-KKKMESD------LSQLQTEMEEAVQEC-RNAEEKAKKAITDAAMMAEELKKE 1790
Cdd:NF033838 187 KAELELV----KEEAKEPRDEEKIKQaKAKVESKkaeatrLEKIKTDREKAEEEAkRRADAKLKEAVEKNVATSEQDKPK 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1791 QdtsahleRMKKNMEQTIKDLQQRLDEAEQIALKGGKKQLQklearvrelDNELEAEQKRnAESVKGMRKYERRIKElty 1870
Cdd:NF033838 263 R-------RAKRGVLGEPATPDKKENDAKSSDSSVGEETLP---------SPSLKPEKKV-AEAEKKVEEAKKKAKD--- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1871 QTEEDRKNLArlqdlvdklqlkVKTYKRQAEESEEqantSLSKFRKVQHELDEAEERADIAESQVNKLRAKsrdVSTKKS 1950
Cdd:NF033838 323 QKEEDRRNYP------------TNTYKTLELEIAE----SDVKVKEAELELVKEEAKEPRNEEKIKQAKAK---VESKKA 383
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
999-1177 |
1.36e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 999 EMAGLDEIIVKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKirmDLERVKRKLEG--- 1075
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEA---RIKKYEEQLGNvrn 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1076 --DVKLSQESLMDLENDKQQLEEKLKKKDFEVSQLNTRIEDEQNVCIQLQKKMKELQARIEELEEELEAERTA-RAKVEK 1152
Cdd:COG1579 88 nkEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEElEAEREE 167
|
170 180
....*....|....*....|....*
gi 1072253241 1153 LRCDLSRELEEISERLEEAGGATSV 1177
Cdd:COG1579 168 LAAKIPPELLALYERIRKRKNGLAV 192
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1471-1658 |
1.40e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 42.82 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1471 LAEWKQKFE---ESQTELESSQKEARSLstELFKLKNAYEESLDHLetfKRENKNLQEEISDLTEQLGESGKSIHELE-- 1545
Cdd:pfam09787 9 LADYKQKAArilQSKEKLIASLKEGSGV--EGLDSSTALTLELEEL---RQERDLLREEIQKLRGQIQQLRTELQELEaq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1546 ------KIRKQLDQEKMEIQ---SALEEAEATLEHEEGKILHAQLELHQIKADSERKLAEKDEEMEQAKRnyQRMVDTLQ 1616
Cdd:pfam09787 84 qqeeaeSSREQLQELEEQLAterSARREAEAELERLQEELRYLEEELRRSKATLQSRIKDREAEIEKLRN--QLTSKSQS 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1617 TSLEAETRSR----NEALRIKKKMEGDL----NEMEIQLSQANRQAAEAQ 1658
Cdd:pfam09787 162 SSSQSELENRlhqlTETLIQKQTMLEALstekNSLVLQLERMEQQIKELQ 211
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1682-1941 |
1.42e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.57 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1682 SEDLKENIAIVERRNTLLQAELEELRSLVEQtERARKLSEQELIETSERVQLLHSQNT--SLINQKKKMESDLSQLQTEM 1759
Cdd:pfam17380 268 NEFLNQLLHIVQHQKAVSERQQQEKFEKMEQ-ERLRQEKEEKAREVERRRKLEEAEKArqAEMDRQAAIYAEQERMAMER 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1760 EEAVQECRNAEEKAKkaitDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQQRLDEAEQIALKGGKKQ---------- 1829
Cdd:pfam17380 347 ERELERIRQEERKRE----LERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQrkiqqqkvem 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1830 ----LQKLEARVRELdNELEAEQKRNAESVKGMRKYERRIKELTYQTEEDRKnlarlqdlvdKLQLKVKTYKRQAEESEE 1905
Cdd:pfam17380 423 eqirAEQEEARQREV-RRLEEERAREMERVRLEEQERQQQVERLRQQEEERK----------RKKLELEKEKRDRKRAEE 491
|
250 260 270
....*....|....*....|....*....|....*.
gi 1072253241 1906 QAntslskfRKVQHELDEAEERADIAESQVNKLRAK 1941
Cdd:pfam17380 492 QR-------RKILEKELEERKQAMIEEERKRKLLEK 520
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1159-1508 |
1.57e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.57 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1159 RELEEISERLEEAggatsvQMELNKKREAEFLKLRRDLEESTLHSEATAASLRKKHADSVAELSEQIDNLQRVKQKLEKE 1238
Cdd:pfam17380 287 RQQQEKFEKMEQE------RLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKR 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1239 KSEfKLELDDVTSNMEQMvkakanleklcRSLEDQANEHRTKseeNQRTVNELSSLRaKLQTENGELSRRLDEKESLVSQ 1318
Cdd:pfam17380 361 ELE-RIRQEEIAMEISRM-----------RELERLQMERQQK---NERVRQELEAAR-KVKILEEERQRKIQQQKVEMEQ 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1319 MTRGKQTYTQhlEDLKRQLEEETKAKNALAHALQSARHDSDLLREQFEEEQEAKAELQRilskansevaqwrtkyETDAI 1398
Cdd:pfam17380 425 IRAEQEEARQ--REVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEK----------------EKRDR 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1399 QRTEelEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDlmvDLERSNAAAAALDKKQRNFDKILAEWKQKF 1478
Cdd:pfam17380 487 KRAE--EQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYE---EERRREAEEERRKQQEMEERRRIQEQMRKA 561
|
330 340 350
....*....|....*....|....*....|
gi 1072253241 1479 EESQTELESSQKEaRSLSTELFKLKNAYEE 1508
Cdd:pfam17380 562 TEERSRLEAMERE-REMMRQIVESEKARAE 590
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
861-1105 |
1.57e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 861 AETEKEMQTMKE---EFQKLKEALEKSEARRKDLEEKMVSLLQEKNDLQLQVQAEQDNLADADERCEQLIKNKIQleakl 937
Cdd:COG4913 671 AELEAELERLDAssdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL----- 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 938 kEQTERLED--EEEMNAELTAKKRK-LEDECSELKKDIDDLELTLAKVEKE-KHATENKVKNLTEEMAGLDEIIVKLT-- 1011
Cdd:COG4913 746 -ELRALLEErfAAALGDAVERELREnLEERIDALRARLNRAEEELERAMRAfNREWPAETADLDADLESLPEYLALLDrl 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1012 ----------KEKKALQEAHQQALDDLQAEedkvntLTKAKAKLEQQVDDLEGSLEQ-----EKKIRMDLERVKRKlegD 1076
Cdd:COG4913 825 eedglpeyeeRFKELLNENSIEFVADLLSK------LRRAIREIKERIDPLNDSLKRipfgpGRYLRLEARPRPDP---E 895
|
250 260
....*....|....*....|....*....
gi 1072253241 1077 VKLSQESLMDLENDKQQLEEKLKKKDFEV 1105
Cdd:COG4913 896 VREFRQELRAVTSGASLFDEELSEARFAA 924
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1546-1667 |
1.61e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1546 KIRKQLDQEKMEIQSALEEAEATLE-HEEGKILHAQLELHQIKADSERKLAEKDEEMEQAKRNYQRMVDTLQTSLEAETR 1624
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEAEaIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEK 107
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1072253241 1625 SRNEALRIKKKMEGDLNEMEIQLSQANRQaaeAQKQVKILQSY 1667
Cdd:PRK12704 108 REEELEKKEKELEQKQQELEKKEEELEEL---IEEQLQELERI 147
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1515-1945 |
1.73e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 43.51 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1515 TFKRENKNLQEEIsdlteqlgesgksihelEKIRKQLDqekmEIQSALEEAEATLEheegkilhaqlelhqiKADSERKL 1594
Cdd:pfam13166 86 TLGEESIEIQEKI-----------------AKLKKEIK----DHEEKLDAAEANLQ----------------KLDKEKEK 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1595 AEKDEEMEQAKRNYQRMVDTLQTSLEAETRSRNEALRIKKKMEGDLNEMEIQLSQANRQAAEAQKQVKILQSYLKDT--Q 1672
Cdd:pfam13166 129 LEADFLDECWKKIKRKKNSALSEALNGFKYEANFKSRLLREIEKDNFNAGVLLSDEDRKAALATVFSDNKPEIAPLTfnV 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1673 IQLDDALRASEDLK----ENIAIVE-RRNTLLQAELEELRSLVEQTERARKLSEQELieTSERVQLLHSQ-NTSLINQKK 1746
Cdd:pfam13166 209 IDFDALEKAEILIQkvigKSSAIEElIKNPDLADWVEQGLELHKAHLDTCPFCGQPL--PAERKAALEAHfDDEFTEFQN 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1747 KMESDLSQLQTEMEEAVQECRNAEEKAKKAItdaammAEELKKEQdtsahLERMKKNMEQTIKDLQQRLDEAeqialkgg 1826
Cdd:pfam13166 287 RLQKLIEKVESAISSLLAQLPAVSDLASLLS------AFELDVED-----IESEAEVLNSQLDGLRRALEAK-------- 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1827 KKQLqkleARVRELD---NELEAEQKRNAESVKGMRKYERRIKELTYQTEEDRKNLARlqDLVDKLQLKVKTYKRQAEES 1903
Cdd:pfam13166 348 RKDP----FKSIELDsvdAKIESINDLVASINELIAKHNEITDNFEEEKNKAKKKLRL--HLVEEFKSEIDEYKDKYAGL 421
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1072253241 1904 EEQANtslskfrKVQHELDEAEERADIAESQVNKLRAKSRDV 1945
Cdd:pfam13166 422 EKAIN-------SLEKEIKNLEAEIKKLREEIKELEAQLRDH 456
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1369-1577 |
1.79e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1369 QEAKAELQRILSKANSEVaqwrtkyetDAIQRtEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKtkhRLQNEIEdlmv 1448
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEA---------EAIKK-EALLEAKEEIHKLRNEFEKELRERRNELQKLEK---RLLQKEE---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1449 dlersnaaaaALDKKQRNFDKIlaewKQKFEESQTELESSQKEARSLSTELFKLKNAYEESLdhletfkrenknlqEEIS 1528
Cdd:PRK12704 97 ----------NLDRKLELLEKR----EEELEKKEKELEQKQQELEKKEEELEELIEEQLQEL--------------ERIS 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1529 DLTEqlgESGKSIhELEKIRKQLDQEKME-IQSALEEAEATLEHEEGKIL 1577
Cdd:PRK12704 149 GLTA---EEAKEI-LLEKVEEEARHEAAVlIKEIEEEAKEEADKKAKEIL 194
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1511-1951 |
1.80e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 42.97 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1511 DHLETFKRENKNLQEEISDLTEQLGESGKSIHELEKIRKQLDQEKMEIQSAL--------EEAEATLEHEEGKILHAQLE 1582
Cdd:COG5278 76 SFLEPYEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIalrragglEAALALVRSGEGKALMDEIR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1583 LHQIKADSERKLAEKDEEMEQAKRNYQRMVDTLQTSLEAETRSRNEALRIKKKMEGDLNEMEIQLSQANRQAAEAQKQVK 1662
Cdd:COG5278 156 ARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1663 ILQSYLKDTQIQLDDALRASEDLKENIAIVERRNTLLQAELEELRSLVEQTERARKLSEQELIETSERVQLLHSQNTSLI 1742
Cdd:COG5278 236 AALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1743 NQKKKMESDLSQLQTEMEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQQRLDEAEQIA 1822
Cdd:COG5278 316 AAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAI 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1823 LKGGKKQLQKLEARVRELDNELEAEQKRNAESVKGMRKYERRIKELTYQTEEDRKNLARLQDLVDKLQLKVKTYKRQAEE 1902
Cdd:COG5278 396 AAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALA 475
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1072253241 1903 SEEQANTSLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDVSTKKSL 1951
Cdd:COG5278 476 ALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAA 524
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1309-1492 |
1.88e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1309 LDEKESLVSQMTRGKQTYTQHLEDLKRQLEEETKAKNALAHALQSARHDSDLLREQFEEEQEAKAELQRILSKANSevAQ 1388
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR--AL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1389 WRTKYE-------------TDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKhrlqNEIEDLMVDLERSNA 1455
Cdd:COG3883 96 YRSGGSvsyldvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKL----AELEALKAELEAAKA 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 1072253241 1456 AAAALDKKQRNFDKILAEWKQKFEESQTELESSQKEA 1492
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAA 208
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
877-1343 |
1.91e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 43.14 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 877 LKEALEKSEA---RRKDLEEKMVSLLQEKNDLQLQVQaeqdnladaderceqliknkiqleaKLKEQTERLEDEEEMNae 953
Cdd:pfam05622 2 LSEAQEEKDElaqRCHELDQQVSLLQEEKNSLQQENK-------------------------KLQERLDQLESGDDSG-- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 954 lTAKKRKLedecSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGL---DEIIVKLTKEKKALQEahqqALDDLQA 1030
Cdd:pfam05622 55 -TPGGKKY----LLLQKQLEQLQEENFRLETARDDYRIKCEELEKEVLELqhrNEELTSLAEEAQALKD----EMDILRE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1031 EEDKVntltkakAKLEQQVDDLEGSLEqekkirmDLERVKRKlegdVKLSQESLMDLENDKQQLEEKLKKKDF------- 1103
Cdd:pfam05622 126 SSDKV-------KKLEATVETYKKKLE-------DLGDLRRQ----VKLLEERNAEYMQRTLQLEEELKKANAlrgqlet 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1104 ---EVSQLNTRIEDEQNVCIQLQKKMKELQARIEELEEELEAER----TARAKVEKLRCDlsrELEEISERLEEAGGATS 1176
Cdd:pfam05622 188 ykrQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIierdTLRETNEELRCA---QLQQAELSQADALLSPS 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1177 VQMELNKKREAEFLKLRRDLEESTLHSEATAASLRKKHADSVAELSEQIDNLQRVKQKLEKEKSefklelddvtSNMEQM 1256
Cdd:pfam05622 265 SDPGDNLAAEIMPAEIREKLIRLQHENKMLRLGQEGSYRERLTELQQLLEDANRRKNELETQNR----------LANQRI 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1257 VKAKANLEKLCRSLEDQANehrtKSEENQRTVNELSSLRAKLQTENGELSRRLDEKESLVSQMTRGKQTYTQHLEDLKRQ 1336
Cdd:pfam05622 335 LELQQQVEELQKALQEQGS----KAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNLAQKIDELQEALRK 410
|
....*..
gi 1072253241 1337 LEEETKA 1343
Cdd:pfam05622 411 KDEDMKA 417
|
|
| EcCorA_ZntB-like |
cd12821 |
Escherichia coli CorA-Salmonella typhimurium ZntB_like family; A family of the MIT superfamily ... |
1313-1425 |
1.91e-03 |
|
Escherichia coli CorA-Salmonella typhimurium ZntB_like family; A family of the MIT superfamily of essential membrane proteins involved in transporting divalent cations (uptake or efflux) across membranes. Members of this family are found in all three kingdoms of life. It is a functionally diverse family, including the Mg2+ transporters Escherichia coli and Salmonella typhimurium CorAs (which can also transport Co2+, and Ni2+ ), and the Zn2+ transporter Salmonella typhimurium ZntB which mediates the efflux of Zn2+ (and Cd2+). It also includes two Saccharomyces cerevisiae members: the inner membrane Mg2+ transporters Mfm1p/Lpe10p, and Mrs2p, and a family of Arabidopsis thaliana members (AtMGTs) some of which are localized to distinct tissues, and not all of which can transport Mg2+. Structures of the intracellular domain of Vibrio parahaemolyticus and Salmonella typhimurium ZntB form funnel-shaped homopentamers, the tip of the funnel is formed from two C-terminal transmembrane (TM) helices from each monomer, and the large opening of the funnel from the N-terminal cytoplasmic domains. The GMN signature motif of the MIT superfamily occurs just after TM1, mutation within this motif is known to abolish Mg2+ transport through Salmonella typhimurium CorA, and Mrs2p. Natural variants such as GVN and GIN, such as occur in some ZntB family proteins, may be associated with the transport of different divalent cations, such as zinc and cadmium. The functional diversity of MIT transporters may also be due to minor structural differences regulating gating, substrate selection, and transport.
Pssm-ID: 213355 [Multi-domain] Cd Length: 285 Bit Score: 42.30 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1313 ESLVSQMTRGKQTYTQHLEDLKRQLEEETKAKnALAHALqSARHDSDLLREQFEEEQEAKAELQRILSKANSEvaQWRTK 1392
Cdd:cd12821 110 GAIIKALLTGIDQFEEKLEELEWDLLEGNNAI-KLDRIL-ELRRELLRLTNLIEPQQEVLMALQEAFAELLFS--EDEEE 185
|
90 100 110
....*....|....*....|....*....|...
gi 1072253241 1393 YEtDAIQRTEELEEAKKKLAQRLQEAEEAVEAV 1425
Cdd:cd12821 186 LR-RTLDRIERLLQLIEEYEQELDTLQDIEEVV 217
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1304-1470 |
2.10e-03 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 43.21 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1304 ELSRRLDEKESLVSQMTRGKQTYTQHLEDLKRQLEEETKAKNALAHALQSARHDSDLLREQFEEEQEA-KAELQRILSKA 1382
Cdd:COG1193 490 EIARRLGLPEEIIERARELLGEESIDVEKLIEELERERRELEEEREEAERLREELEKLREELEEKLEElEEEKEEILEKA 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1383 NsevaqwrtkyetdaiqrteelEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKhRLQNEIEDLMVDLERSNAAAAALDK 1462
Cdd:COG1193 570 R---------------------EEAEEILREARKEAEELIRELREAQAEEEELK-EARKKLEELKQELEEKLEKPKKKAK 627
|
....*...
gi 1072253241 1463 KQRNFDKI 1470
Cdd:COG1193 628 PAKPPEEL 635
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1797-1918 |
2.34e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 42.26 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1797 LERMKK-NMEQTIKDLQQRLDEAE------QIALKGGKKQLQKLEARVRELDNELEAEQKRNAESVkgmrkyeRRIKELT 1869
Cdd:PRK09039 71 LERQGNqDLQDSVANLRASLSAAEaersrlQALLAELAGAGAAAEGRAGELAQELDSEKQVSARAL-------AQVELLN 143
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1072253241 1870 YQTEEDRKNLARLQDLVDKLQLKVKTYKRQAEESEEQANTSLSkfRKVQ 1918
Cdd:PRK09039 144 QQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLNVALA--QRVQ 190
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1615-1944 |
2.70e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 42.97 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1615 LQTSLEAETRSRNEALR----IKKKMEGDLNEMEIQLSQANRQAAEAQKQVkilQSYLKD----TQIQLDDALRASEDLK 1686
Cdd:PLN02939 65 LQSNTDENGQLENTSLRtvmeLPQKSTSSDDDHNRASMQRDEAIAAIDNEQ---QTNSKDgeqlSDFQLEDLVGMIQNAE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1687 ENIAIVERRNTLLQAELEELRSLVEQTERARKLSEQELIETSERVQLLHSQNTSLinqkKKMESDLSQLQTEMEEAVQEC 1766
Cdd:PLN02939 142 KNILLLNQARLQALEDLEKILTEKEALQGKINILEMRLSETDARIKLAAQEKIHV----EILEEQLEKLRNELLIRGATE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1767 RNAEEKAKKAIT-----------DAAMMAEELKKEQDTS---AHLERMKKNMEQTIKDLQQRLDEAEQIALKGGKKQLQK 1832
Cdd:PLN02939 218 GLCVHSLSKELDvlkeenmllkdDIQFLKAELIEVAETEervFKLEKERSLLDASLRELESKFIVAQEDVSKLSPLQYDC 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1833 LEARVRELDNELEAEQKRNAESV---KGMRKYERRIKELTYQTEEdrKNLARLQ-DLVDKLQLKVKTYKRQAEESEEQAN 1908
Cdd:PLN02939 298 WWEKVENLQDLLDRATNQVEKAAlvlDQNQDLRDKVDKLEASLKE--ANVSKFSsYKVELLQQKLKLLEERLQASDHEIH 375
|
330 340 350
....*....|....*....|....*....|....*.
gi 1072253241 1909 TslskfrKVQHELDEAEERADIAESQVNKLRAKSRD 1944
Cdd:PLN02939 376 S------YIQLYQESIKEFQDTLSKLKEESKKRSLE 405
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
869-1133 |
2.72e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 42.87 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 869 TMKEEFQKLKEALEKSEARRKDLEEKMVSLLQEKNDLQLQVQAEQDNLADADERCEQ------LIKNKIQLEA----KLK 938
Cdd:PRK10246 430 ALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADVKTICEQearikdLEAQRAQLQAgqpcPLC 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 939 EQTERLEDEEEMNAELTAKKRKLedecselkkdiDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIVKLTKEKKALQ 1018
Cdd:PRK10246 510 GSTSHPAVEAYQALEPGVNQSRL-----------DALEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQEEQALT 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1019 EAHQQALDDL---QAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKIRMDLERVkRKLEGDVKLSQESlmdLENDKQQLE 1095
Cdd:PRK10246 579 QQWQAVCASLnitLQPQDDIQPWLDAQEEHERQLRLLSQRHELQGQIAAHNQQI-IQYQQQIEQRQQQ---LLTALAGYA 654
|
250 260 270
....*....|....*....|....*....|....*...
gi 1072253241 1096 EKLKKKDFEVSQLNTRiEDEQNVCIQLQKKMKELQARI 1133
Cdd:PRK10246 655 LTLPQEDEEASWLATR-QQEAQSWQQRQNELTALQNRI 691
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1089-1258 |
3.03e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1089 NDKQQLEEKLKKKDFEVSQLNTRIEDEQNVCIQLQKKMKELQARIEELEEELEAERTARAKVEKLRCDLSRELEEISERL 1168
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1169 EEAGGATSVQmelNKKREAEFLKLRR-DLEESTLHSEATAASLRKKHADSVAELSEQIDNLQRVKQKLEKEKSEFKLELD 1247
Cdd:COG1579 83 GNVRNNKEYE---ALQKEIESLKRRIsDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELE 159
|
170
....*....|.
gi 1072253241 1248 DVTSNMEQMVK 1258
Cdd:COG1579 160 ELEAEREELAA 170
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1450-1889 |
3.19e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 42.76 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1450 LERSNAAAAALDKKQRNFDKILAEwKQKFEESQTELESSQKEARSLSTELfkLKNAYEESLDHLETFKRENKNL------ 1523
Cdd:COG5022 798 KLQPLLSLLGSRKEYRSYLACIIK-LQKTIKREKKLRETEEVEFSLKAEV--LIQKFGRSLKAKKRFSLLKKETiylqsa 874
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1524 --QEEISDLTEQLGESGKSIHELEKIRKQLDQEKMEIQSALEEAE-ATLEHEEGKILHAQ--LELHQIKADSERKLAEKD 1598
Cdd:COG5022 875 qrVELAERQLQELKIDVKSISSLKLVNLELESEIIELKKSLSSDLiENLEFKTELIARLKklLNNIDLEEGPSIEYVKLP 954
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1599 EEMEqakrnyqrmvdtlqtsLEAETRSRNEALRIKKKMegdLNEMEIQLSQANRQAAEAQKQVKILQSYLKdtqiQLDDA 1678
Cdd:COG5022 955 ELNK----------------LHEVESKLKETSEEYEDL---LKKSTILVREGNKANSELKNFKKELAELSK----QYGAL 1011
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1679 LRASEDLKENiaivERRNTLLQAELEELRSlvEQTERARKLSEQELIETSERVQLLHSQNTSLINQKKKmesdlSQLQTE 1758
Cdd:COG5022 1012 QESTKQLKEL----PVEVAELQSASKIISS--ESTELSILKPLQKLKGLLLLENNQLQARYKALKLRRE-----NSLLDD 1080
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1759 MEEAVQECRNAEEKAKKAitdaammaeelKKEQDTSAHLERmKKNMEQTIKDLQQRLDEAEQIA---------LKGGKKQ 1829
Cdd:COG5022 1081 KQLYQLESTENLLKTINV-----------KDLEVTNRNLVK-PANVLQFIVAQMIKLNLLQEISkflsqlvntLEPVFQK 1148
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1830 LQKLEARVRELDNELEAEQKRNAESVKGMrkYERRIKELTYQTEEDRKNLARLQDLVDKL 1889
Cdd:COG5022 1149 LSVLQLELDGLFWEANLEALPSPPPFAAL--SEKRLYQSALYDEKSKLSSSEVNDLKNEL 1206
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
1683-1951 |
3.21e-03 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 42.61 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1683 EDLKENIAIVERRNTLL---QAELEELRSLVEQTERARKLSE-QELietseRVQLLHSQNTSLINQKKK---------ME 1749
Cdd:PLN03188 953 KEKYENHPEVLRTKIELkrvQDELEHYRNFYDMGEREVLLEEiQDL-----RSQLQYYIDSSLPSARKRnsllkltysCE 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1750 SDLSQLQTEMEEAVQECrnAEEKAKK-------AITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQQRLDEAEQIA 1822
Cdd:PLN03188 1028 PSQAPPLNTIPESTDES--PEKKLEQerlrwteAESKWISLAEELRTELDASRALAEKQKHELDTEKRCAEELKEAMQMA 1105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1823 LKGGKKQLQK----------LEARVRELDNELEAEQKRNAES-VKGMR--------------KYERRiKELTYQTEEDRK 1877
Cdd:PLN03188 1106 MEGHARMLEQyadleekhiqLLARHRRIQEGIDDVKKAAARAgVRGAEskfinalaaeisalKVERE-KERRYLRDENKS 1184
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1072253241 1878 NLARLQDLVDKLQLKVKTYKRqAEESEEQANTSlskfrkvQHELDEAEERADIAESQVNKLRAKSRD-VSTKKSL 1951
Cdd:PLN03188 1185 LQAQLRDTAEAVQAAGELLVR-LKEAEEALTVA-------QKRAMDAEQEAAEAYKQIDKLKRKHENeISTLNQL 1251
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
998-1106 |
3.77e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.38 E-value: 3.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 998 EEMAGLDEIIVKLTKEKKAL----QEAHQQALDDLQAEEdkvntltkakAKLEQQVDDLEGSLEQEKKIRMDLERVKRKL 1073
Cdd:COG0542 411 EELDELERRLEQLEIEKEALkkeqDEASFERLAELRDEL----------AELEEELEALKARWEAEKELIEEIQELKEEL 480
|
90 100 110
....*....|....*....|....*....|...
gi 1072253241 1074 EGDVKLSQESLMDLENDKQQLEEKLKKKDFEVS 1106
Cdd:COG0542 481 EQRYGKIPELEKELAELEEELAELAPLLREEVT 513
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1647-1851 |
3.98e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 41.17 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1647 LSQANRQAAEAQKQVKILQSYLKDTQIQLDDALRASEDLKENIAIVE----RRNTLLQ---AELEELRSLVEQTERARKL 1719
Cdd:pfam00261 3 MQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEeeleRTEERLAealEKLEEAEKAADESERGRKV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1720 SEQELIETSERVQLLHSQNTSLINQKKKMESDLSQLQTEMEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLE- 1798
Cdd:pfam00261 83 LENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSLEa 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1072253241 1799 ------RMKKNMEQTIKDLQQRLDEAEQIALKGgKKQLQKLEARVRELDNELEAEQKRN 1851
Cdd:pfam00261 163 seekasEREDKYEEQIRFLTEKLKEAETRAEFA-ERSVQKLEKEVDRLEDELEAEKEKY 220
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1399-1564 |
3.99e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 41.67 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1399 QRTEELEEAKKKLAQRLQEA--EEAVEAVNAKCSSLEKTKHR---LQNEIEDLMVDLE-----------RSNAAAAALDK 1462
Cdd:pfam09787 14 QKAARILQSKEKLIASLKEGsgVEGLDSSTALTLELEELRQErdlLREEIQKLRGQIQqlrtelqeleaQQQEEAESSRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1463 KQRNFDKILAEWKQKFEESQTELESSQKEARSLSTELFKLKNAYEESLdhletfkrenKNLQEEISDLTEQL---GESGK 1539
Cdd:pfam09787 94 QLQELEEQLATERSARREAEAELERLQEELRYLEEELRRSKATLQSRI----------KDREAEIEKLRNQLtskSQSSS 163
|
170 180
....*....|....*....|....*
gi 1072253241 1540 SIHELEKIRKQLDQEKMEIQSALEE 1564
Cdd:pfam09787 164 SQSELENRLHQLTETLIQKQTMLEA 188
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
971-1101 |
4.28e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.99 E-value: 4.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 971 DIDDLELTLAKVEKEKHATENkvknltEEMAGLDEIIVKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKAKLEQQVD 1050
Cdd:COG0542 412 ELDELERRLEQLEIEKEALKK------EQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYG 485
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1051 DLEGSLEQEKKIRMDLERVKRKLEGDV------------------KLSQEslmdlENDK-QQLEEKLKKK 1101
Cdd:COG0542 486 KIPELEKELAELEEELAELAPLLREEVteediaevvsrwtgipvgKLLEG-----EREKlLNLEEELHER 550
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
859-1061 |
4.36e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 40.78 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 859 KSAETEKEMQTMKEEFQKLKEALEKSEARRKDLEEKMVSLLQEKNDLQLQVQAEQDNLADADERCEQLIKNKIQLEAKLK 938
Cdd:pfam00261 2 KMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 939 EQTER-LEDEEEMN---AELTAKKRKLED---ECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIVKL- 1010
Cdd:pfam00261 82 VLENRaLKDEEKMEileAQLKEAKEIAEEadrKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSLe 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1072253241 1011 TKEKKALQ------EAHQQALDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKK 1061
Cdd:pfam00261 162 ASEEKASEredkyeEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKE 218
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
992-1253 |
4.89e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 4.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 992 KVKNLTEEMAGLDEIIvKLTKEKKALQEAHQQALDDLQAE-----EDKVNTLTKAKAKLEQQVDDLEgslEQEKKIRMDL 1066
Cdd:PHA02562 175 KIRELNQQIQTLDMKI-DHIQQQIKTYNKNIEEQRKKNGEniarkQNKYDELVEEAKTIKAEIEELT---DELLNLVMDI 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1067 ERVKRKLEgdvKLSQEsLMDLENDKQQL--EEKLKKKDFEVSQLNTRIEDEQNVCIQLQKKMKELQARIEeleeeleaer 1144
Cdd:PHA02562 251 EDPSAALN---KLNTA-AAKIKSKIEQFqkVIKMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLE---------- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1145 tarakveklrcDLSRELEEISERLEEAGGATSVQMELNKKREaeflKLRRDLeeSTLHSEATAA-SLRKKHADSVAELSE 1223
Cdd:PHA02562 317 -----------KLDTAIDELEEIMDEFNEQSKKLLELKNKIS----TNKQSL--ITLVDKAKKVkAAIEELQAEFVDNAE 379
|
250 260 270
....*....|....*....|....*....|..
gi 1072253241 1224 QIDNLQRVKQKLEKEKSEFKLELD--DVTSNM 1253
Cdd:PHA02562 380 ELAKLQDELDKIVKTKSELVKEKYhrGIVTDL 411
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1178-1370 |
5.08e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.06 E-value: 5.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1178 QMELNKKR--EAEFLKLRRDLEESTLHS---EATAASL-------RKKHADSVAELSEQIDNLQRVkqkLEKEKSEfKLE 1245
Cdd:pfam00038 92 EDELNLRTsaENDLVGLRKDLDEATLARvdlEAKIESLkeelaflKKNHEEEVRELQAQVSDTQVN---VEMDAAR-KLD 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1246 LDDVTSNM-----EQMVKAKANLEKLCRS----LEDQANEHrtkSEENQRTVNELSSLRAKLQTENGELSRRLDEKESLV 1316
Cdd:pfam00038 168 LTSALAEIraqyeEIAAKNREEAEEWYQSkleeLQQAAARN---GDALRSAKEEITELRRTIQSLEIELQSLKKQKASLE 244
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1072253241 1317 SQMTRGKQTYTQHLEDLKRQLEEetkaknaLAHALQSARHDsdlLREQFEEEQE 1370
Cdd:pfam00038 245 RQLAETEERYELQLADYQELISE-------LEAELQETRQE---MARQLREYQE 288
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
933-1357 |
5.13e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 41.59 E-value: 5.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 933 LEAKLKEQTERLEDEEEMNAELTAKKRKLEDECSEL---KKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIVK 1009
Cdd:pfam19220 8 LRVRLGEMADRLEDLRSLKADFSQLIEPIEAILRELpqaKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1010 LTKEKKALQEAHQQAldDLQAEEDKVNTLTKakaklEQQVDDLEGSLEQEKKIRMDLERVKRKLEGDVKLSQESLMDLEN 1089
Cdd:pfam19220 88 LVARLAKLEAALREA--EAAKEELRIELRDK-----TAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1090 DKQQLEEKLKKKDFEVSQLNTRIEDEQNVCIQLQKKMKELQARieeleeeleaERTARAKVEKLRCDLSrelEEISERlE 1169
Cdd:pfam19220 161 ELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETQ----------LDATRARLRALEGQLA---AEQAER-E 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1170 EAGGATSVQMELNKkreAEFLKLRRDLEESTLHSEAT-------AASLRKKhADSVAELSEQIDNLQRVKQKLEKEKSEF 1242
Cdd:pfam19220 227 RAEAQLEEAVEAHR---AERASLRMKLEALTARAAATeqllaeaRNQLRDR-DEAIRAAERRLKEASIERDTLERRLAGL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1243 KLELDDVTSNMEQMVKAKANLEKLCRSLEDQANEHRTKSEENQRTVnelsslrAKLQTENGELSRRLDEKeslvsqmtrg 1322
Cdd:pfam19220 303 EADLERRTQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERI-------ASLSDRIAELTKRFEVE---------- 365
|
410 420 430
....*....|....*....|....*....|....*.
gi 1072253241 1323 KQTYTQHLEDLKRQLEEEtKAKNALAH-ALQSARHD 1357
Cdd:pfam19220 366 RAALEQANRRLKEELQRE-RAERALAQgALEIARES 400
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
878-1059 |
5.27e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 40.51 E-value: 5.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 878 KEALEKSEARRKDLEEkMVSLLQEKNDLQLQVQAEQDNLADADERCEQLIKNKIQLEAKLKEQTERLEDE-EEMNAELTA 956
Cdd:cd00176 19 KEELLSSTDYGDDLES-VEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEELNQRwEELRELAEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 957 KKRKLED---------ECSELKKDIDDLELTLAKVEKEKHATE-----NKVKNLTEEMAGLDEIIVKLTKEKKALQEAHQ 1022
Cdd:cd00176 98 RRQRLEEaldlqqffrDADDLEQWLEEKEAALASEDLGKDLESveellKKHKELEEELEAHEPRLKSLNELAEELLEEGH 177
|
170 180 190
....*....|....*....|....*....|....*..
gi 1072253241 1023 QalDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQE 1059
Cdd:cd00176 178 P--DADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1699-1951 |
5.32e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 5.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1699 LQAELEELRSLVEQTERARKLSEQELIETSERVQLLHSQNTSLINQKKKMESDLSQLQTEMEEAVQECRNAEEKAKKAIT 1778
Cdd:COG4372 43 LQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1779 DAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQQRLDEAEQIALKGGKKQLQKLEARVRELDNELEAEQKRNAESVKGM 1858
Cdd:COG4372 123 ERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEEL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1859 RKYERRIKELtyQTEEDRKNLARLQDLVDKLQLKVKTYKRQAEESEEQANTSLSKFRKVQHELDEAEERADIAESQVNKL 1938
Cdd:COG4372 203 AEAEKLIESL--PRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEI 280
|
250
....*....|...
gi 1072253241 1939 RAKSRDVSTKKSL 1951
Cdd:COG4372 281 AALELEALEEAAL 293
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
919-1074 |
5.45e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 41.16 E-value: 5.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 919 ADERCEQLIKNKIQ-------LEAK----------LKEQTERLEDE-EEMNAELTAKKRKLEdECSELKKDIDDLELTL- 979
Cdd:smart00787 107 ASPDVKLLMDKQFQlvktfarLEAKkmwyewrmklLEGLKEGLDENlEGLKEDYKLLMKELE-LLNSIKPKLRDRKDALe 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 980 AKVEKEKHATENKVKNLTEEMAGLDEIIVKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQE 1059
Cdd:smart00787 186 EELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQC 265
|
170
....*....|....*.
gi 1072253241 1060 KKI-RMDLERVKRKLE 1074
Cdd:smart00787 266 RGFtFKEIEKLKEQLK 281
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1751-1916 |
5.80e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 5.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1751 DLSQLQTEMEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQQRLDEAEQiALKGGK--K 1828
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE-QLGNVRnnK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1829 QLQKLEArvreldnELEAEQKRNAESvkgmrkyERRIKELTYQTEEDRKNLARLQDLVDKLQLKVKTYKRQAEESEEQAN 1908
Cdd:COG1579 90 EYEALQK-------EIESLKRRISDL-------EDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE 155
|
....*...
gi 1072253241 1909 TSLSKFRK 1916
Cdd:COG1579 156 AELEELEA 163
|
|
| Yuri_gagarin |
pfam15934 |
Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis. |
886-1040 |
5.97e-03 |
|
Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis.
Pssm-ID: 318204 [Multi-domain] Cd Length: 234 Bit Score: 40.33 E-value: 5.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 886 ARRKDLEEKMVSLLQEKNDLQLQVQAEQDNLADADERCEQL---------------IKNKI--------QLEAKLKEQTE 942
Cdd:pfam15934 41 ENKNEQEQQLKEFTVQNQRLACQIDNLHETLKDRDHQIKQLqsmitgysdisennrLKEEIhdlkqkncVQARVVRKMGL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 943 RLEDEEEMNAELTAKKRKL----EDECSELK---KDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLdeiivkltKEKK 1015
Cdd:pfam15934 121 ELKGQEEQRVELCDKYESLlgsfEEQCQELKranRRVQSLQTRLSQVEKLQEELRTERKILREEVIAL--------KEKD 192
|
170 180
....*....|....*....|....*....
gi 1072253241 1016 ALQEAHQQALDD----LQAEEDKVNTLTK 1040
Cdd:pfam15934 193 AKSNGRERALQDqlkcCQTEIEKSRTLIR 221
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1428-1564 |
6.11e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 40.77 E-value: 6.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1428 KCSSLEKTKHRLQNEIEDLMVDLERsnaaaaaLDKKQRNFDKILAEWKQKFEESQTELESSQKEARSL----STELFKLK 1503
Cdd:smart00787 138 RMKLLEGLKEGLDENLEGLKEDYKL-------LMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELedcdPTELDRAK 210
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1072253241 1504 NAYEESLDHLETFKRENKNLQEEISDLTEQLGESGKSIHELEkirkqldQEKMEIQSALEE 1564
Cdd:smart00787 211 EKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELN-------TEIAEAEKKLEQ 264
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1483-1573 |
6.21e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.61 E-value: 6.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1483 TELESSQKEARSLSTELFKLKNAYEE-SLDHLETFKRENKNLQEEISDLTEQLGESGKSIHELEKIRKQLDQEKMEI--- 1558
Cdd:COG0542 411 EELDELERRLEQLEIEKEALKKEQDEaSFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIpel 490
|
90
....*....|....*
gi 1072253241 1559 QSALEEAEATLEHEE 1573
Cdd:COG0542 491 EKELAELEEELAELA 505
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1806-1941 |
6.35e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 6.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1806 QTIKDLQQRLDEAEQIA--LKGGKKQLQKLEARVRELDNELEAEQKRNAESVKGMRKYERRIKELTYQTEEDRKNLARLQ 1883
Cdd:COG1579 7 RALLDLQELDSELDRLEhrLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1884 DL--VDKLQLKVKTYKRQAEESEEQANTSLSKFRKVQHELDEAEERADIAESQVNKLRAK 1941
Cdd:COG1579 87 NNkeYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE 146
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
861-1208 |
6.38e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 6.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 861 AETEKEMQTMKEEFQKLKEALEKSEARRKDLEEKMVSLLQEKNDLQLQVQAEQDNLADADERCEQLIKNKIQLEAKLKEQ 940
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 941 TERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIVKLTKEKKalqea 1020
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEA----- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1021 hQQALDDLQAEEDKVNTLTKAKAKLEQQVDDLEGSLEQEKKIRMDLERVKRKLEGDVKLSQESLMDLENDKQQLEEKLKK 1100
Cdd:COG4372 182 -EQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEI 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1101 KDFEVSQLNTRIEDEQNVCIQLQKKMKELQARIEELEEELEAERTARAKVEKLRCDLSRELEEISERLEEAGGATSVQME 1180
Cdd:COG4372 261 EELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELA 340
|
330 340
....*....|....*....|....*...
gi 1072253241 1181 LNKKREAEFLKLRRDLEESTLHSEATAA 1208
Cdd:COG4372 341 DLLQLLLVGLLDNDVLELLSKGAEAGVA 368
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
909-1053 |
6.56e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.35 E-value: 6.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 909 VQAEQDNLADADERCEQLIKNKIQLEAKLKEQTERLEDEEEmnaELTAKKRKLEDECSELKKDIDDLeltLAKVEKEkha 988
Cdd:PRK00409 504 IEEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLK---EAEKLKEELEEKKEKLQEEEDKL---LEEAEKE--- 574
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1072253241 989 TENKVKNLTEEMAGLDEIIVKLTKEKKALQEAHqQALDDLQAEEDKVNTLTKAKAKLEQQVDDLE 1053
Cdd:PRK00409 575 AQQAIKEAKKEADEIIKELRQLQKGGYASVKAH-ELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1216-1493 |
7.52e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.66 E-value: 7.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1216 DSVAELSEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQMVKAKANLEKLCRSLEDQANEHRTKSEENQRTVNELSSLR 1295
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1296 AKLQTENGELSRRLDEKESLVSQMTRGKQTytqhLEDLKRQLEEETKaknalahALQSARHDSDLLREQFEEEQEAKAEL 1375
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNKAGGS----IDKLRKEIERLEW-------RQQTEVLSPEEEKELVEKIKELEKEL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1376 QRILS--KANSEVAQWRTKYETDAIQRtEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERS 1453
Cdd:COG1340 150 EKAKKalEKNEKLKELRAELKELRKEA-EEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADEL 228
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1072253241 1454 NAAAAALDKKQRNFDKILAEWKQKFEESQTELESSQKEAR 1493
Cdd:COG1340 229 HEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEK 268
|
|
| COG6 |
smart01087 |
Conserved oligomeric complex COG6; COG6 is a component of the conserved oligomeric golgi ... |
1390-1523 |
8.19e-03 |
|
Conserved oligomeric complex COG6; COG6 is a component of the conserved oligomeric golgi complex, which is composed of eight different subunits and is required for normal golgi morphology and localisation.
Pssm-ID: 215018 Cd Length: 598 Bit Score: 41.15 E-value: 8.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1390 RTKYETDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDLERSNAAAAALDKKQrnfdK 1469
Cdd:smart01087 9 RSDLEKRLLKINGEFLSEFKPVAEQLQRLSEDVQKLNNSCDSMKDQLNTAKNQTQDLISEASELQEELALLELKK----K 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1072253241 1470 ILAEWKQKFEESQTELESSQKEARSLSTELFKLknayeesLDHLETFKRENKNL 1523
Cdd:smart01087 85 LLDAFLSKFTLSQDELDVLTSREGPIDDEFFQV-------LDKVQEIHEDCSVL 131
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
1208-1554 |
8.62e-03 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 40.32 E-value: 8.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1208 ASLRKKHADSVAELSEqidnLQRVKQKLEKEKSEFKLELDDVTSNMEQMVKAKANLEKLCRSLEDQAN----EHRTKSEE 1283
Cdd:pfam09728 21 AALCKKYAELLEEMKR----LQKDLKKLKKKQDQLQKEKDQLQSELSKAILAKSKLEKLCRELQKQNKklkeESKKLAKE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1284 NQRTVNELSslrAKLQTENGELSRRLDEKESLVSQMTRGKQTYTQHLEDLKRQLEeetkaknalahalqsarhdsdlLRE 1363
Cdd:pfam09728 97 EEEKRKELS---EKFQSTLKDIQDKMEEKSEKNNKLREENEELREKLKSLIEQYE----------------------LRE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1364 QFEEEQEAKAELQRILSKAnsevaqwrtkyetdaiqRTEELEEAKKKLAQRLQEAEeaVEAVNAKCSSLEKTKHRLQNEI 1443
Cdd:pfam09728 152 LHFEKLLKTKELEVQLAEA-----------------KLQQATEEEEKKAQEKEVAK--ARELKAQVQTLSETEKELREQL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1444 EDLMvdlersnaaaaaldKKQRNFDKILAEWKQKFEESQTELESSQKEARSLSTELFKLKNAYEESLDHLETFKRENKNL 1523
Cdd:pfam09728 213 NLYV--------------EKFEEFQDTLNKSNEVFTTFKKEMEKMSKKIKKLEKENLTWKRKWEKSNKALLEMAEERQKL 278
|
330 340 350
....*....|....*....|....*....|.
gi 1072253241 1524 QEEISDLTEQlgesgksIHELEKIRKQLDQE 1554
Cdd:pfam09728 279 KEELEKLQKK-------LEKLENLCRALQAE 302
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1739-1935 |
8.65e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 40.09 E-value: 8.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1739 TSLINQKKKMESDLSQLQTEMEEAVQECRNAEEK---AKKAITDAAMMAEEL-KKEQDTSAHLERMKKNMEQTIKDLQQR 1814
Cdd:pfam06008 8 TGALPAPYKINYNLENLTKQLQEYLSPENAHKIQieiLEKELSSLAQETEELqKKATQTLAKAQQVNAESERTLGHAKEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1815 LDEAEQIAlkggkKQLQKLEARVRELDNELEA-------EQKRNAESVKGmrkyERRIKELTYQTEEDRKNLARLQDLVD 1887
Cdd:pfam06008 88 AEAIKNLI-----DNIKEINEKVATLGENDFAlpssdlsRMLAEAQRMLG----EIRSRDFGTQLQNAEAELKAAQDLLS 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1072253241 1888 KLQLKVKTYKRQAEESEEQANTSLSKFrkvQHELDEAEERADIAESQV 1935
Cdd:pfam06008 159 RIQTWFQSPQEENKALANALRDSLAEY---EAKLSDLRELLREAAAKT 203
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1367-1656 |
8.70e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.10 E-value: 8.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1367 EEQEAKAELQRILSKANSEVAQWRTKYETDAI----QRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKT------- 1435
Cdd:COG5185 239 QDPESELEDLAQTSDKLEKLVEQNTDLRLEKLgenaESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATesleeql 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1436 -KHRLQNEIEDLMVDLERSNAAA-AALDKKQRNFDKILAEWK---------QKFEESQTELESSQKEARSLSTELF-KLK 1503
Cdd:COG5185 319 aAAEAEQELEESKRETETGIQNLtAEIEQGQESLTENLEAIKeeienivgeVELSKSSEELDSFKDTIESTKESLDeIPQ 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1504 NAYEESLDHLETFK-------RENKNLQEEISDLTEQLGESGKSIHELEKIRKQLDQEKMEIQSALEEAEATLEHEEG-- 1574
Cdd:COG5185 399 NQRGYAQEILATLEdtlkaadRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRSVrs 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1575 KILHAQLELHQIkadsERKLAEKDEEMEQAKRNYQRMVDTLQTSLEAETRSRNEALRIKKKMEGDLNEMEIQLSQANRQA 1654
Cdd:COG5185 479 KKEDLNEELTQI----ESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASELIQAS 554
|
..
gi 1072253241 1655 AE 1656
Cdd:COG5185 555 NA 556
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1183-1347 |
9.09e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 41.20 E-value: 9.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1183 KKREAEFLKLRRDLEESTLhsEATAASLRKKHADS-VAELSEQIDNLqrvkqkleKEKSEFKLElDDVTSNMEQMVKAKA 1261
Cdd:pfam05911 20 EKAEAEALALKQQLESVTL--QKLTAEERAAHLDGaLKECMQQLRNV--------KEEQEQKIH-DVVLKKTKEWEKIKA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1262 NLE-KLCrsledqanehrtkseenqrtvnELSSLRAKLQTENGELSRRLDEKESLVSQMTRGKQTYTQHLEDLKRQLEEE 1340
Cdd:pfam05911 89 ELEaKLV----------------------ETEQELLRAAAENDALSRSLQERENLLMKLSEEKSQAEAEIEALKSRLESC 146
|
....*..
gi 1072253241 1341 TKAKNAL 1347
Cdd:pfam05911 147 EKEINSL 153
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1614-1881 |
9.19e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 40.83 E-value: 9.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1614 TLQTSLEAETRSRNEALRIKKKMEGDLNEMEIQLSQANRQaaeaqkqvkilqsyLKDTQIQLDDALRASEDLKENIAIVE 1693
Cdd:PRK11637 51 SIQQDIAAKEKSVRQQQQQRASLLAQLKKQEEAISQASRK--------------LRETQNTLNQLNKQIDELNASIAKLE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1694 RRntllQAELEelRSLVEQTERARKLSEQ---ELI------ETSERVQ----LLHSQNTSLINQKKKMESDLSQLQTEME 1760
Cdd:PRK11637 117 QQ----QAAQE--RLLAAQLDAAFRQGEHtglQLIlsgeesQRGERILayfgYLNQARQETIAELKQTREELAAQKAELE 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1761 EAVQECRN--AEEKAKKAitdaammaeelKKEQdtsAHLERMK--KNMEQTIKDLQQRLDEaeqialkggkkqLQKLEAR 1836
Cdd:PRK11637 191 EKQSQQKTllYEQQAQQQ-----------KLEQ---ARNERKKtlTGLESSLQKDQQQLSE------------LRANESR 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1072253241 1837 VRELDNELEAEQK-------RNAESVKGMRKYERRiKELTYQ-TEEDRKNLAR 1881
Cdd:PRK11637 245 LRDSIARAEREAKaraereaREAARVRDKQKQAKR-KGSTYKpTESERSLMSR 296
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
893-1364 |
9.50e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 41.04 E-value: 9.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 893 EKMVSLLQEKND-LQLQVQAEQDNLADADERCEQLiknkiqleaklkeqTERLEDEEEMNAELTAKKrkledeCSELKKD 971
Cdd:pfam15964 223 EKLKLLYEAKTEvLESQVKSLRKDLAESQKTCEDL--------------KERLKHKESLVAASTSSR------VGGLCLK 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 972 IDDLELTLAKVEKEKHAteNKVKNLTEEMAGLDEIIVKLTKEKKALQE----AHQQALDDLQAEEDKVNTLTKA------ 1041
Cdd:pfam15964 283 CAQHEAVLAQTHTNVHM--QTIERLTKERDDLMSALVSVRSSLAEAQQressAYEQVKQAVQMTEEANFEKTKAliqceq 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1042 -KAKLEQQVDDLEGSLE-QEKKIRMDLERVKRKLEGDVKLSQESLMDLENDKQQLEEKLKKKDFEVSQLNTRIEDEQN-- 1117
Cdd:pfam15964 361 lKSELERQKERLEKELAsQQEKRAQEKEALRKEMKKEREELGATMLALSQNVAQLEAQVEKVTREKNSLVSQLEEAQKql 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1118 ---------VCIQL-----QKKMKELQARIEELEEELEAERT---ARAKVEKLRCDLSRELEEISERLEEAGGATSVQME 1180
Cdd:pfam15964 441 asqemdvtkVCGEMryqlnQTKMKKDEAEKEHREYRTKTGRQleiKDQEIEKLGLELSESKQRLEQAQQDAARAREECLK 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1181 LNK-----KREAEFLKLRRDLEESTLHSEATAASLRKKHADSvaELSEQIDNLQRVKQKLEKEKSEFklelddVTSNMEQ 1255
Cdd:pfam15964 521 LTEllgesEHQLHLTRLEKESIQQSFSNEAKAQALQAQQREQ--ELTQKMQQMEAQHDKTVNEQYSL------LTSQNTF 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1256 MVKAKANLEKLCRSLEDQANEHRTKseenqrtVNELSSLRAKLQTENGELSRRLDEKESLVSQMTRGKQTYTQHLEDLKR 1335
Cdd:pfam15964 593 IAKLKEECCTLAKKLEEITQKSRSE-------VEQLSQEKEYLQDRLEKLQKRNEELEEQCVQHGRMHERMKQRLRQLDK 665
|
490 500 510
....*....|....*....|....*....|....*.
gi 1072253241 1336 -------QLEEETKAKNALAHALQSARHDSDLLREQ 1364
Cdd:pfam15964 666 hcqataqQLVQLLSKQNQLFKERQNLTEEVQSLRSQ 701
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1655-1847 |
9.87e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.91 E-value: 9.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1655 AEAQKQVKILQSYLKdtqiQLDDALRASEDLKENIAIVERRNTLLQAELEELRSLVEQTERARKLSEQELIETSERVQLL 1734
Cdd:COG1579 3 PEDLRALLDLQELDS----ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1735 HSQNTSLINQKkkmesDLSQLQTEMEEAVQECRNAEEKAKKAItdaammaEELKKEQDTSAHLERMKKNMEQTIKDLQQR 1814
Cdd:COG1579 79 EEQLGNVRNNK-----EYEALQKEIESLKRRISDLEDEILELM-------ERIEELEEELAELEAELAELEAELEEKKAE 146
|
170 180 190
....*....|....*....|....*....|...
gi 1072253241 1815 LDEAEQIAlkggKKQLQKLEARVRELDNELEAE 1847
Cdd:COG1579 147 LDEELAEL----EAELEELEAEREELAAKIPPE 175
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1699-1793 |
9.88e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.09 E-value: 9.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072253241 1699 LQAELEELRSLVEQTERARKLSEQELIETSERVQLLHSQNTSLINQKKKMESDLSQLQTEMEEAVQEcrnaEEKAKKAIT 1778
Cdd:PRK11448 147 LQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQE----RKQKRKEIT 222
|
90
....*....|....*
gi 1072253241 1779 DAAMMAEELkKEQDT 1793
Cdd:PRK11448 223 DQAAKRLEL-SEEET 236
|
|
| |
