|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
99-766 |
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: 1348.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 99 PAVLYNLKERYASWMIYTYSGLFCVTINPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14917 1 PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 179 ESGAGKTVNTKRVIQYFAVIAAIGDRSKKEQATGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 258
Cdd:cd14917 81 ESGAGKTVNTKRVIQYFAVIAAIGDRSKKDQTPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 259 ASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDV 338
Cdd:cd14917 161 ASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 339 LGFTTEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQ 418
Cdd:cd14917 241 LGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 419 QVVYAKGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQ 498
Cdd:cd14917 321 QVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 499 EEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSSNFQKPRNIKGKPEAHFS 578
Cdd:cd14917 401 EEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSNNFQKPRNIKGKPEAHFS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 579 LIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKKSSLKMLSSLFANYAGFDTPIEKGKGKAKKGSSFQTVSALHRENLNKL 658
Cdd:cd14917 481 LIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANYAGADAPIEKGKGKAKKGSSFQTVSALHRENLNKL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 659 MTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFIDS 738
Cdd:cd14917 561 MTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFIDS 640
|
650 660
....*....|....*....|....*...
gi 1387193866 739 RKGAEKLLGSLDIDHNQYKFGHTKVFFK 766
Cdd:cd14917 641 RKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
99-766 |
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: 1346.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 99 PAVLYNLKERYASWMIYTYSGLFCVTINPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 179 ESGAGKTVNTKRVIQYFAVIAAIGDrSKKEQATGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 258
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSK-KKKESGKKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 259 ASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDV 338
Cdd:cd01377 160 AGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEAFDI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 339 LGFTTEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQ 418
Cdd:cd01377 240 LGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 419 QVVYAKGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQ 498
Cdd:cd01377 320 QVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 499 EEYKKEGIEWEFIDFGMDLQACIDLIEKP-MGIMSILEEECMFPKATDMTFKAKLFDNHLGKSSNFQKPRniKGKPEAHF 577
Cdd:cd01377 400 EEYKKEGIEWTFIDFGLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKPK--PKKSEAHF 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 578 SLIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKKSSLKMLSSLFANYAGFDTpieKGKGKAKKGSSFQTVSALHRENLNK 657
Cdd:cd01377 478 ILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEESGG---GGGKKKKKGGSFRTVSQLHKEQLNK 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 658 LMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFiD 737
Cdd:cd01377 555 LMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIPKGFD-D 633
|
650 660
....*....|....*....|....*....
gi 1387193866 738 SRKGAEKLLGSLDIDHNQYKFGHTKVFFK 766
Cdd:cd01377 634 GKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
99-766 |
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: 1292.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 99 PAVLYNLKERYASWMIYTYSGLFCVTINPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14913 1 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 179 ESGAGKTVNTKRVIQYFAVIAAIGDRSKKEQATGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 258
Cdd:cd14913 81 ESGAGKTVNTKRVIQYFATIAATGDLAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 259 ASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDV 338
Cdd:cd14913 161 ASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLATDSAIDI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 339 LGFTTEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQ 418
Cdd:cd14913 241 LGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 419 QVVYAKGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQ 498
Cdd:cd14913 321 QVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVLEQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 499 EEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSSNFQKPRNIKGKPEAHFS 578
Cdd:cd14913 401 EEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKVVKGRAEAHFS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 579 LIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKKSSLKMLSSLFANYAGFDTPIEKGKGKAKKGSSFQTVSALHRENLNKL 658
Cdd:cd14913 481 LIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATADADSGKKKVAKKKGSSFQTVSALFRENLNKL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 659 MTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFIDS 738
Cdd:cd14913 561 MSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGQFIDS 640
|
650 660
....*....|....*....|....*...
gi 1387193866 739 RKGAEKLLGSLDIDHNQYKFGHTKVFFK 766
Cdd:cd14913 641 KKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
99-766 |
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: 1243.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 99 PAVLYNLKERYASWMIYTYSGLFCVTINPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14916 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 179 ESGAGKTVNTKRVIQYFAVIAAIGDRSKKEQA-TGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 257
Cdd:cd14916 81 ESGAGKTVNTKRVIQYFASIAAIGDRSKKENPnANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 258 LASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFD 337
Cdd:cd14916 161 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSAFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 338 VLGFTTEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNV 417
Cdd:cd14916 241 VLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 418 QQVVYAKGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 497
Cdd:cd14916 321 QQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 498 QEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSSNFQKPRNIKGKPEAHF 577
Cdd:cd14916 401 QEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRNVKGKQEAHF 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 578 SLIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKKSSLKMLSSLFANYAGFDTPIE-KGKGKAKKGSSFQTVSALHRENLN 656
Cdd:cd14916 481 SLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTGDSgKGKGGKKKGSSFQTVSALHRENLN 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 657 KLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFI 736
Cdd:cd14916 561 KLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFI 640
|
650 660 670
....*....|....*....|....*....|
gi 1387193866 737 DSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 766
Cdd:cd14916 641 DSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
100-766 |
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: 1216.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 100 AVLYNLKERYASWMIYTYSGLFCVTINPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14927 2 SVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 180 SGAGKTVNTKRVIQYFAVIAAIGDRSKKEQATGK----GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGAT 255
Cdd:cd14927 82 SGAGKTVNTKRVIQYFAIVAALGDGPGKKAQFLAtktgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 256 GKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNA 335
Cdd:cd14927 162 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSMNPYDYHFCSQGVTTVDNMDDGEELMATDHA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 336 FDVLGFTTEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 415
Cdd:cd14927 242 MDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTKGQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 416 NVQQVVYAKGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 495
Cdd:cd14927 322 SVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFI 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 496 LEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSSNFQKPR-NIKGKPE 574
Cdd:cd14927 402 LEQEEYKREGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRpDKKRKYE 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 575 AHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKKSSLKMLSSLFANYAGFDT---PIEKGKGKAKKGSSFQTVSALH 651
Cdd:cd14927 482 AHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENYVGSDStedPKSGVKEKRKKAASFQTVSQLH 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 652 RENLNKLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIP 731
Cdd:cd14927 562 KENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNPSAIP 641
|
650 660 670
....*....|....*....|....*....|....*
gi 1387193866 732 EGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 766
Cdd:cd14927 642 DDKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
99-766 |
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: 1144.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 99 PAVLYNLKERYASWMIYTYSGLFCVTINPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14923 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 179 ESGAGKTVNTKRVIQYFAVIAAIGDRsKKEQATGK--GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 256
Cdd:cd14923 81 ESGAGKTVNTKRVIQYFATIAVTGDK-KKEQQPGKmqGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 257 KLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAF 336
Cdd:cd14923 160 KLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLATDNAI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 337 DVLGFTTEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQN 416
Cdd:cd14923 240 DILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 417 VQQVVYAKGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 496
Cdd:cd14923 320 VQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 497 EQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSSNFQKPRNIKGKPEAH 576
Cdd:cd14923 400 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPAKGKAEAH 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 577 FSLIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKKSSLKMLSSLFANYAGFDTPIE--KGKGKAKKGSSFQTVSALHREN 654
Cdd:cd14923 480 FSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAGDSggSKKGGKKKGSSFQTVSAVFREN 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 655 LNKLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQ 734
Cdd:cd14923 560 LNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPEGQ 639
|
650 660 670
....*....|....*....|....*....|..
gi 1387193866 735 FIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 766
Cdd:cd14923 640 FIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
99-766 |
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: 1139.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 99 PAVLYNLKERYASWMIYTYSGLFCVTINPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14918 1 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 179 ESGAGKTVNTKRVIQYFAVIAAIGDRSKKEQATGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 258
Cdd:cd14918 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 259 ASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDV 338
Cdd:cd14918 161 ASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 339 LGFTTEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQ 418
Cdd:cd14918 241 LGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 419 QVVYAKGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQ 498
Cdd:cd14918 321 QVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 499 EEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSSNFQKPRNIKGKPEAHFS 578
Cdd:cd14918 401 EEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVVKGKAEAHFS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 579 LIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKKSSLKMLSSLFANYAGFDTPIEKGKGKAKKGSSFQTVSALHRENLNKL 658
Cdd:cd14918 481 LIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYASAEADSGAKKGAKKKGSSFQTVSALFRENLNKL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 659 MTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFIDS 738
Cdd:cd14918 561 MTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGQFIDS 640
|
650 660
....*....|....*....|....*...
gi 1387193866 739 RKGAEKLLGSLDIDHNQYKFGHTKVFFK 766
Cdd:cd14918 641 KKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
99-766 |
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: 1130.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 99 PAVLYNLKERYASWMIYTYSGLFCVTINPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14910 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 179 ESGAGKTVNTKRVIQYFAVIAAIGDRSKKEQATGK--GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 256
Cdd:cd14910 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEATSGKmqGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 257 KLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAF 336
Cdd:cd14910 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 337 DVLGFTTEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQN 416
Cdd:cd14910 241 EILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 417 VQQVVYAKGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 496
Cdd:cd14910 321 VQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 497 EQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSSNFQKPRNIKGKPEAH 576
Cdd:cd14910 401 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKVEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 577 FSLIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKKSSLKMLSSLFANYAGFDTPI-EKGKGKAKKGSSFQTVSALHRENL 655
Cdd:cd14910 481 FSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAAAEAEEgGGKKGGKKKGSSFQTVSALFRENL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 656 NKLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQF 735
Cdd:cd14910 561 NKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQF 640
|
650 660 670
....*....|....*....|....*....|.
gi 1387193866 736 IDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 766
Cdd:cd14910 641 IDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
99-766 |
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: 1125.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 99 PAVLYNLKERYASWMIYTYSGLFCVTINPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14915 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 179 ESGAGKTVNTKRVIQYFAVIAAIGDRSKKEQATGK--GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 256
Cdd:cd14915 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEAASGKmqGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 257 KLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAF 336
Cdd:cd14915 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDFAFVSQGEITVPSIDDQEELMATDSAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 337 DVLGFTTEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQN 416
Cdd:cd14915 241 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 417 VQQVVYAKGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 496
Cdd:cd14915 321 VQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 497 EQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSSNFQKPRNIKGKPEAH 576
Cdd:cd14915 401 EQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKAEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 577 FSLIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKKSSLKMLSSLFAnyAGFDTPIE---KGKGKAKKGSSFQTVSALHRE 653
Cdd:cd14915 481 FSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFS--GGQTAEAEgggGKKGGKKKGSSFQTVSALFRE 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 654 NLNKLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEG 733
Cdd:cd14915 559 NLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEG 638
|
650 660 670
....*....|....*....|....*....|...
gi 1387193866 734 QFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 766
Cdd:cd14915 639 QFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
99-766 |
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: 1115.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 99 PAVLYNLKERYASWMIYTYSGLFCVTINPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14912 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 179 ESGAGKTVNTKRVIQYFAVIAAIGDRSKKEQATGK--GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 256
Cdd:cd14912 81 ESGAGKTVNTKRVIQYFATIAVTGEKKKEEITSGKmqGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 257 KLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAF 336
Cdd:cd14912 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 337 DVLGFTTEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQN 416
Cdd:cd14912 241 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 417 VQQVVYAKGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 496
Cdd:cd14912 321 VEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 497 EQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSSNFQKPRNIKGKPEAH 576
Cdd:cd14912 401 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKVVKGKAEAH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 577 FSLIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKKSSLKMLSSLFA---NYAGFDTPIEKGKGKAKKGSSFQTVSALHRE 653
Cdd:cd14912 481 FSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSgaqTAEGASAGGGAKKGGKKKGSSFQTVSALFRE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 654 NLNKLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEG 733
Cdd:cd14912 561 NLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEG 640
|
650 660 670
....*....|....*....|....*....|...
gi 1387193866 734 QFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 766
Cdd:cd14912 641 QFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
87-766 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1076.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 87 IEDMAMLTFLHEPAVLYNLKERYASWMIYTYSGLFCVTINPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYML 166
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 167 TDRENQSILITGESGAGKTVNTKRVIQYFAVIAAIGDRSKkeqatgKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGK 246
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGN------VGRLEEQILQSNPILEAFGNAKTVRNNNSSRFGK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 247 FIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITnNPYDYAFISQ-GETTVASIDD 325
Cdd:pfam00063 155 YIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLT-NPKDYHYLSQsGCYTIDGIDD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 326 AEELMATDNAFDVLGFTTEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVK 405
Cdd:pfam00063 234 SEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 406 VGNEYVTKGQNVQQVVYAKGALAKAVYERMFNWMVTRINATLETKQ-PRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEK 484
Cdd:pfam00063 314 TGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTiEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 485 LQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLQACIDLIE-KPMGIMSILEEECMFPKATDMTFKAKLFDNHlGKSSNF 563
Cdd:pfam00063 394 LQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEkKPLGILSLLDEECLFPKATDQTFLDKLYSTF-SKHPHF 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 564 QKPRNIKgkpEAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKKSSLKMLSSLFANYAGFDTPIEKGKGKAK---- 639
Cdd:pfam00063 472 QKPRLQG---ETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGKSTpkrt 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 640 KGSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFR 719
Cdd:pfam00063 549 KKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFV 628
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1387193866 720 QRYRILNPAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 766
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 ... |
99-766 |
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: 1068.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 99 PAVLYNLKERYASWMIYTYSGLFCVTINPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 179 ESGAGKTVNTKRVIQYFAVIAAIGDRSKKEqatgkGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 258
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKKL-----GALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGML 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 259 ASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKpELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDV 338
Cdd:cd14929 156 SSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKK-ELRDLLLVSANPSDFHFCSCGAVAVESLDDAEELLATEQAMDI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 339 LGFTTEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQ 418
Cdd:cd14929 235 LGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 419 QVVYAKGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQ 498
Cdd:cd14929 315 QVTYAVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLEQ 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 499 EEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSSNFQKPRNIKGKPEAHFS 578
Cdd:cd14929 395 EEYRKEGIDWVSIDFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKPDKKKFEAHFE 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 579 LIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKKSSLKMLSSLFANYAGFDTPIEKGKGKAKKGSSFQTVSALHRENLNKL 658
Cdd:cd14929 475 LVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYISTDSAIQFGEKKRKKGASFQTVASLHKENLNKL 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 659 MTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFIDS 738
Cdd:cd14929 555 MTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTFPKSKFVSS 634
|
650 660
....*....|....*....|....*...
gi 1387193866 739 RKGAEKLLGSLDIDHNQYKFGHTKVFFK 766
Cdd:cd14929 635 RKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
80-778 |
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: 1028.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 80 NPPKFDKIEDMAMLTFLHEPAVLYNLKERYASWMIYTYSGLFCVTINPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISD 159
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 160 NAYQYMLTDRENQSILITGESGAGKTVNTKRVIQYFAVIAAigdrskkeQATGKGTLEDQIIQANPALEAFGNAKTVRND 239
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSG--------SNTEVGSVEDQILESNPILEAFGNAKTLRNN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 240 NSSRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNnPYDYAFISQGET- 318
Cdd:smart00242 153 NSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKS-PEDYRYLNQGGCl 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 319 TVASIDDAEELMATDNAFDVLGFTTEEKNSMYKLTGAIMHFGNMKFKLKQREEQA-EPDGTEEADKSAYLMGLNSADLLK 397
Cdd:smart00242 232 TVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAAsTVKDKEELSNAAELLGVDPEELEK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 398 GLCHPRVKVGNEYVTKGQNVQQVVYAKGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLC 477
Cdd:smart00242 312 ALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSFEQLC 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 478 INFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLQACIDLIE-KPMGIMSILEEECMFPKATDMTFKAKLfDNH 556
Cdd:smart00242 392 INYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEkKPPGILSLLDEECRFPKGTDQTFLEKL-NQH 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 557 LGKSSNFQKPRNikgKPEAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKKSSLKMLSSLFANYAGFDTpiekgkg 636
Cdd:smart00242 470 HKKHPHFSKPKK---KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVSNAG------- 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 637 kakKGSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYG 716
Cdd:smart00242 540 ---SKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFD 616
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387193866 717 DFRQRYRILNPAAIPEGQFiDSRKGAEKLLGSLDIDHNQYKFGHTKVFFKAGLLGLLEEMRD 778
Cdd:smart00242 617 EFLQRYRVLLPDTWPPWGG-DAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
99-766 |
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: 1019.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 99 PAVLYNLKERYASWMIYTYSGLFCVTINPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 179 ESGAGKTVNTKRVIQYFAVIAAigDRSKKEQATGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 258
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGA--SKKTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 259 ASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDV 338
Cdd:cd14909 159 AGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLSDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQAFDI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 339 LGFTTEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQ 418
Cdd:cd14909 239 LGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 419 QVVYAKGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQ 498
Cdd:cd14909 319 QVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 499 EEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSSNFQKPRNIK-GKPEAHF 577
Cdd:cd14909 399 EEYKREGIDWAFIDFGMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKpGQQAAHF 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 578 SLIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKKSSLKMLSSLFANYAGFD-TPIEKGKGKAKKGSSFQTVSALHRENLN 656
Cdd:cd14909 479 AIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSgGGEQAKGGRGKKGGGFATVSSAYKEQLN 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 657 KLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQfi 736
Cdd:cd14909 559 SLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGIQGEE-- 636
|
650 660 670
....*....|....*....|....*....|
gi 1387193866 737 DSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 766
Cdd:cd14909 637 DPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
100-766 |
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 1387193866 100 AVLYNLKERYASWMIYTYSGLFCVTINPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14934 2 SVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 180 SGAGKTVNTKRVIQYFAVIAAIGdrskKEQATGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 259
Cdd:cd14934 82 SGAGKTENTKKVIQYFANIGGTG----KQSSDGKGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 260 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDVL 339
Cdd:cd14934 158 GADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQITDVAFDVL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 340 GFTTEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQ 419
Cdd:cd14934 238 GFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNMEQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 420 VVYAKGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQE 499
Cdd:cd14934 318 CNNSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 500 EYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSSNFQKPRNIKGK-PEAHFS 578
Cdd:cd14934 398 EYKREGIEWVFIDFGLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHLGKSSNFLKPKGGKGKgPEAHFE 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 579 LIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKKSSLKMLSSLFANYAGfdtpiEKGKGKAKKGSSFQTVSALHRENLNKL 658
Cdd:cd14934 478 LVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKEEEA-----PAGSKKQKRGSSFMTVSNFYREQLNKL 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 659 MTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGqFIDS 738
Cdd:cd14934 553 MTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVIPQG-FVDN 631
|
650 660
....*....|....*....|....*...
gi 1387193866 739 RKGAEKLLGSLDIDHNQYKFGHTKVFFK 766
Cdd:cd14934 632 KKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
99-766 |
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: 844.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 99 PAVLYNLKERYASWMIYTYSGLFCVTINPYKWLPVYNAEVVAAYRGKKR-SEAPPHIFSISDNAYQYMLTDRENQSILIT 177
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRsADLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 178 GESGAGKTVNTKRVIQYFAVIAAIGDRSKKEQATGkgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 257
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSKSSSSASS---IEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 258 LASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLIT---NNPYDYAFISQGE-TTVASIDDAEELMATD 333
Cdd:cd00124 158 LVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLElllSYYYLNDYLNSSGcDRIDGVDDAEEFQELL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 334 NAFDVLGFTTEEKNSMYKLTGAIMHFGNMKFKLKQREE--QAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYV 411
Cdd:cd00124 238 DALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEdsSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 412 TKGQNVQQVVYAKGALAKAVYERMFNWMVTRINATL--ETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFF 489
Cdd:cd00124 318 TKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALspTDAAESTSFIGILDIFGFENFEVNSFEQLCINYANEKLQQFF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 490 NHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSSNFQKPRn 568
Cdd:cd00124 398 NQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEgKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKR- 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 569 ikgKPEAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKKSSlkmlsslfanyagfdtpiekgkgkakkgssfqtvs 648
Cdd:cd00124 476 ---KAKLEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGS----------------------------------- 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 649 aLHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPA 728
Cdd:cd00124 518 -QFRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAPG 596
|
650 660 670
....*....|....*....|....*....|....*...
gi 1387193866 729 AiPEGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 766
Cdd:cd00124 597 A-TEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
37-1432 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 840.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 37 VFVPDDKEEFVKATILSRE--GGKVTAE--TEHGKTVTVKEDQVLQ--QNPPKFDKIEDMAMLTFLHEPAVLYNLKERYA 110
Cdd:COG5022 12 CWIPDEEKGWIWAEIIKEAfnKGKVTEEgkKEDGESVSVKKKVLGNdrIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 111 SWMIYTYSGLFCVTINPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESGAGKTVNTKR 190
Cdd:COG5022 92 NGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 191 VIQYFAVIAAigdrskkEQATGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEK 270
Cdd:COG5022 172 IMQYLASVTS-------SSTVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 271 SRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNnPYDYAFISQGE-TTVASIDDAEELMATDNAFDVLGFTTEEKNSM 349
Cdd:COG5022 245 SRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQN-PKDYIYLSQGGcDKIDGIDDAKEFKITLDALKTIGIDEEEQDQI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 350 YKLTGAIMHFGNMKFKlKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQVVYAKGALAK 429
Cdd:COG5022 324 FKILAAILHIGNIEFK-EDRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAK 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 430 AVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWE 509
Cdd:COG5022 403 ALYSNLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWS 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 510 FIDFgMDLQACIDLIEK--PMGIMSILEEECMFPKATDMTFKAKLFDN-HLGKSSNFQKPRNIKGKpeahFSLIHYAGTV 586
Cdd:COG5022 483 FIDY-FDNQPCIDLIEKknPLGILSLLDEECVMPHATDESFTSKLAQRlNKNSNPKFKKSRFRDNK----FVVKHYAGDV 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 587 DYNIIGWLQKNKDPLNETVVDLYKKSSLKMLSSLFANYAGFDTpiekgkgkakkGSSFQTVSALHRENLNKLMTNLRSTH 666
Cdd:COG5022 558 EYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENIES-----------KGRFPTLGSRFKESLNSLMSTLNSTQ 626
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 667 PHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFI---DSRKGAE 743
Cdd:COG5022 627 PHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKSWTGEYTwkeDTKNAVK 706
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 744 KLLGSLDIDHNQYKFGHTKVFFKAGLLGLLEEMRDERLSRIITRIQAQSRGVLSRMEFKKLLERRDSLLIIQWNIRAFMG 823
Cdd:COG5022 707 SILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLRRL 786
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 824 VKNWPWMKLYFKIKPLLKSAETEKEI---------------------ALMKEEFGR----LKEALEKSEARRK--ELEEK 876
Cdd:COG5022 787 VDYELKWRLFIKLQPLLSLLGSRKEYrsylaciiklqktikrekklrETEEVEFSLkaevLIQKFGRSLKAKKrfSLLKK 866
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 877 MVSLLQEKNDLQL---QVQAEQD------NLADAEERCDQLI-------------KNKIQLE--AKVKEMTE--RLEDEE 930
Cdd:COG5022 867 ETIYLQSAQRVELaerQLQELKIdvksisSLKLVNLELESEIielkkslssdlieNLEFKTEliARLKKLLNniDLEEGP 946
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 931 EMNAELTAKKRKLEDECSELKRDIDDLELTLakveKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQ----- 1005
Cdd:COG5022 947 SIEYVKLPELNKLHEVESKLKETSEEYEDLL----KKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQlkelp 1022
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1006 -ALDDLQAEEDKVNTLTKAKvKLEQHVDDLEGSLEQEKK------VRMDLERAKRKLEGDLKLTQESIMDLEN-----DK 1073
Cdd:COG5022 1023 vEVAELQSASKIISSESTEL-SILKPLQKLKGLLLLENNqlqaryKALKLRRENSLLDDKQLYQLESTENLLKtinvkDL 1101
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1074 QQLDERLKKKDFELNAL------NARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEIS 1147
Cdd:COG5022 1102 EVTNRNLVKPANVLQFIvaqmikLNLLQEISKFLSQLVNTLEPVFQKLSVLQLELDGLFWEANLEALPSPPPFAALSEKR 1181
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1148 ER----LEEAGGATSVQIEMNK-KREAEFQKMRRDLEEatlqheataaalrkkhADSVAELSEQIDNLQRVKQKLEKEKS 1222
Cdd:COG5022 1182 LYqsalYDEKSKLSSSEVNDLKnELIALFSKIFSGWPR----------------GDKLKKLISEGWVPTEYSTSLKGFNN 1245
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1223 EFKLELDDVTSNMEQIIKAKANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQ--RAKLQTENGELSRQLDEKEALISQ 1300
Cdd:COG5022 1246 LNKKFDTPASMSNEKLLSLLNSIDNLLSSYKLEEEVLPATINSLLQYINVGLFNalRTKASSLRWKSATEVNYNSEELDD 1325
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1301 LTRgkltyTQQLEDLKRQLE---EEVKAKNALAHALQSARHDCDLLREQYEEETEA-KAELQRVLSKANSEvAQWRTKYE 1376
Cdd:COG5022 1326 WCR-----EFEISDVDEELEeliQAVKVLQLLKDDLNKLDELLDACYSLNPAEIQNlKSRYDPADKENNLP-KEILKKIE 1399
|
1450 1460 1470 1480 1490
....*....|....*....|....*....|....*....|....*....|....*...
gi 1387193866 1377 TDAIQRTEELE-EAKKKLAQRLQD-AEEAVEAVNAKCSSLEKTKhRLQNEIEDLMVDV 1432
Cdd:COG5022 1400 ALLIKQELQLSlEGKDETEVHLSEiFSEEKSLISLDRNSIYKEE-VLSSLSALLTKEK 1456
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
100-766 |
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: 800.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 100 AVLYNLKERYASWMIYTYSGLFCVTINPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14911 2 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 180 SGAGKTVNTKRVIQYFAVIAAigDRSKKEQATGK---------GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRI 250
Cdd:cd14911 82 SGAGKTENTKKVIQFLAYVAA--SKPKGSGAVPHpavnpavliGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 251 HFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLItNNPYDYAFISQGETTVASIDDAEELM 330
Cdd:cd14911 160 NFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFIL-DDVKSYAFLSNGSLPVPGVDDYAEFQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 331 ATDNAFDVLGFTTEEKNSMYKLTGAIMHFGNMKFKLKQREEQAE-PDGTEeADKSAYLMGLNSADLLKGLCHPRVKVGNE 409
Cdd:cd14911 239 ATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATlPDNTV-AQKIAHLLGLSVTDMTRAFLTPRIKVGRD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 410 YVTKGQNVQQVVYAKGALAKAVYERMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQF 488
Cdd:cd14911 318 FVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 489 FNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLgkssnfQKPRN 568
Cdd:cd14911 398 FNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAHS------MHPKF 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 569 IKG--KPEAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKKSSLKMLSSLF--ANYAGF--DTPIEKGKGKAKKGS 642
Cdd:cd14911 472 MKTdfRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWkdAEIVGMaqQALTDTQFGARTRKG 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 643 SFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRY 722
Cdd:cd14911 552 MFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRY 631
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1387193866 723 RILNPAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 766
Cdd:cd14911 632 ELLTPNVIPKG-FMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
100-766 |
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: 769.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 100 AVLYNLKERYASWMIYTYSGLFCVTINPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14920 2 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 180 SGAGKTVNTKRVIQYFAVIAAiGDRSKKEQATgKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 259
Cdd:cd14920 82 SGAGKTENTKKVIQYLAHVAS-SHKGRKDHNI-PGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 260 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPEL-LDMLLITNNpyDYAFISQGETTVASIDDAEELMATDNAFDV 338
Cdd:cd14920 160 GANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLkSDLLLEGFN--NYRFLSNGYIPIPGQQDKDNFQETMEAMHI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 339 LGFTTEEKNSMYKLTGAIMHFGNMKFKLKQREEQAE-PDGTeEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNV 417
Cdd:cd14920 238 MGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASmPENT-VAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 418 QQVVYAKGALAKAVYERMFNWMVTRINATLETKQpRQ--YFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 495
Cdd:cd14920 317 EQADFAVEALAKATYERLFRWLVHRINKALDRTK-RQgaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 496 LEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLFdNHLGKSSNFQKPRNIKGk 572
Cdd:cd14920 396 LEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLV-QEQGSHSKFQKPRQLKD- 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 573 pEAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKKSSLKMLSSLFAN---YAGFD-----TPIEKGKGKAKKGSSF 644
Cdd:cd14920 474 -KADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDvdrIVGLDqvtgmTETAFGSAYKTKKGMF 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 645 QTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRI 724
Cdd:cd14920 553 RTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 632
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1387193866 725 LNPAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 766
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 ... |
100-766 |
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: 721.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 100 AVLYNLKERYASWMIYTYSGLFCVTINPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14932 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 180 SGAGKTVNTKRVIQYFAVIAAiGDRSKKEQAT---GKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 256
Cdd:cd14932 82 SGAGKTENTKKVIQYLAYVAS-SFKTKKDQSSialSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 257 KLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPyDYAFISQGETTVASIDDAEELMATDNAF 336
Cdd:cd14932 161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYS-KYRFLSNGNVTIPGQQDKELFAETMEAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 337 DVLGFTTEEKNSMYKLTGAIMHFGNMKFKLKQREEQAE-PDGTeEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 415
Cdd:cd14932 240 RIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASmPDDT-AAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 416 NVQQVVYAKGALAKAVYERMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMF 494
Cdd:cd14932 319 TQEQAEFAVEALAKASYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 495 VLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLFdNHLGKSSNFQKPRNIKG 571
Cdd:cd14932 399 ILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVV-QEQGNNPKFQKPKKLKD 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 572 kpEAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKKSSLKMLSSLFANY---AGFD----TPIEKGKGKAKKGSSF 644
Cdd:cd14932 478 --DADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVdriVGLDkvagMGESLHGAFKTRKGMF 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 645 QTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRI 724
Cdd:cd14932 556 RTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 635
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1387193866 725 LNPAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 766
Cdd:cd14932 636 LTPNAIPKG-FMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
99-766 |
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: 704.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 99 PAVLYNLKERYA-SWMIYTYSGLFCVTINPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 177
Cdd:cd01380 1 PAVLHNLKVRFCqRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 178 GESGAGKTVNTKRVIQYFAVIAAigdrskkeQATGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 257
Cdd:cd01380 81 GESGAGKTVSAKYAMRYFATVGG--------SSSGETQVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 258 LASADIETYLLEKSRVIFQLKAERDYHIFYQILSNK-KPELLDMLLITNNpyDYAFISQGE-TTVASIDDAEELMATDNA 335
Cdd:cd01380 153 IIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAAsLPELKELHLGSAE--DFFYTNQGGsPVIDGVDDAAEFEETRKA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 336 FDVLGFTTEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 415
Cdd:cd01380 231 LTLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 416 NVQQVVYAKGALAKAVYERMFNWMVTRINATLETKQP--RQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHM 493
Cdd:cd01380 311 TLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKekQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 494 FVLEQEEYKKEGIEWEFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSSN-FQKPRNIKGK 572
Cdd:cd01380 391 FKLEQEEYVKEEIEWSFIDF-YDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNKhFKKPRFSNTA 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 573 peahFSLIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKKSSLKmlsslfanyagfdtpiekgkgkakkgssFQTVSALHR 652
Cdd:cd01380 470 ----FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKNR----------------------------KKTVGSQFR 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 653 ENLNKLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAipE 732
Cdd:cd01380 518 DSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSK--E 595
|
650 660 670
....*....|....*....|....*....|....
gi 1387193866 733 GQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 766
Cdd:cd01380 596 WLRDDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
100-766 |
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: 695.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 100 AVLYNLKERYASWMIYTYSGLFCVTINPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14921 2 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 180 SGAGKTVNTKRVIQYFAVIAAigDRSKKEQATGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 259
Cdd:cd14921 82 SGAGKTENTKKVIQYLAVVAS--SHKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 260 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPyDYAFISQGETTVASIDDAEELMATDNAFDVL 339
Cdd:cd14921 160 GANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFN-NYTFLSNGFVPIPAAQDDEMFQETLEAMSIM 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 340 GFTTEEKNSMYKLTGAIMHFGNMKFKLKQREEQAE-PDGTeEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQ 418
Cdd:cd14921 239 GFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASmPDNT-AAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 419 QVVYAKGALAKAVYERMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLE 497
Cdd:cd14921 318 QADFAIEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 498 QEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLFDNHlGKSSNFQKPRNIKGKPE 574
Cdd:cd14921 398 QEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GNHPKFQKPKQLKDKTE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 575 ahFSLIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKKSSLKMLSSLFANY---AGFDTPIEKGKGKAKKGSS-----FQT 646
Cdd:cd14921 477 --FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVdriVGLDQMAKMTESSLPSASKtkkgmFRT 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 647 VSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILN 726
Cdd:cd14921 555 VGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILA 634
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1387193866 727 PAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 766
Cdd:cd14921 635 ANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
100-766 |
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: 685.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 100 AVLYNLKERYASWMIYTYSGLFCVTINPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14919 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 180 SGAGKTVNTKRVIQYFAVIAAiGDRSKKEQatgkGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 259
Cdd:cd14919 82 SGAGKTENTKKVIQYLAHVAS-SHKSKKDQ----GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 260 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLItnNPYD-YAFISQGETTVASIDDAEELMATDNAFDV 338
Cdd:cd14919 157 GANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLL--EPYNkYRFLSNGHVTIPGQQDKDMFQETMEAMRI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 339 LGFTTEEKNSMYKLTGAIMHFGNMKFKLKQREEQAE-PDGTeEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNV 417
Cdd:cd14919 235 MGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASmPDNT-AAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 418 QQVVYAKGALAKAVYERMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 496
Cdd:cd14919 314 EQADFAIEALAKATYERMFRWLVLRINKALDkTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFIL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 497 EQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLFDNHlGKSSNFQKPRNIKGKp 573
Cdd:cd14919 394 EQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQEQ-GTHPKFQKPKQLKDK- 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 574 eAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKKSSLKMLSSLFANY---AGFD-----TPIEKGKGKAKKGSSFQ 645
Cdd:cd14919 472 -ADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVdriIGLDqvagmSETALPGAFKTRKGMFR 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 646 TVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRIL 725
Cdd:cd14919 551 TVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEIL 630
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1387193866 726 NPAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 766
Cdd:cd14919 631 TPNSIPKG-FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
100-766 |
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: 679.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 100 AVLYNLKERYASWMIYTYSGLFCVTINPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd15896 2 SVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 180 SGAGKTVNTKRVIQYFAVIAAiGDRSKKEQ---ATGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 256
Cdd:cd15896 82 SGAGKTENTKKVIQYLAHVAS-SHKTKKDQnslALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 257 KLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPyDYAFISQGETTVASIDDAEELMATDNAF 336
Cdd:cd15896 161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYN-NYRFLSNGNVTIPGQQDKDLFTETMEAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 337 DVLGFTTEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQN 416
Cdd:cd15896 240 RIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 417 VQQVVYAKGALAKAVYERMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 495
Cdd:cd15896 320 QEQAEFAVEALAKATYERMFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 496 LEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLFDNHlGKSSNFQKPRNIKGk 572
Cdd:cd15896 400 LEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPAsppGILALLDEECWFPKATDKSFVEKVLQEQ-GTHPKFFKPKKLKD- 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 573 pEAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKKSSLKMLSSLFANY---AGFDTPI---EKGKGKAKKGSSFQT 646
Cdd:cd15896 478 -EADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVdriVGLDKVSgmsEMPGAFKTRKGMFRT 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 647 VSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILN 726
Cdd:cd15896 557 VGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 636
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1387193866 727 PAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 766
Cdd:cd15896 637 PNAIPKG-FMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
100-766 |
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: 667.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 100 AVLYNLKERYASWMIYTYSGLFCVTINPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14930 2 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 180 SGAGKTVNTKRVIQYFAVIAAiGDRSKKEQATgKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 259
Cdd:cd14930 82 SGAGKTENTKKVIQYLAHVAS-SPKGRKEPGV-PGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 260 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYdYAFISQGETTVASiDDAEELMATDNAFDVL 339
Cdd:cd14930 160 GANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQETLESLRVL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 340 GFTTEEKNSMYKLTGAIMHFGNMKFKLKQREEQAE-PDGTeEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQ 418
Cdd:cd14930 238 GFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 419 QVVYAKGALAKAVYERMFNWMVTRINATLEtKQPRQ--YFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 496
Cdd:cd14930 317 QADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 497 EQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLFDNHlGKSSNFQKPRNIKGkp 573
Cdd:cd14930 396 EQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRPRHLRD-- 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 574 EAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKKSSLKMLSSLFANYAGFdTPIEKGKGK-------AKKGSSFQT 646
Cdd:cd14930 473 QADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGI-VGLEQVSSLgdgppggRPRRGMFRT 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 647 VSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILN 726
Cdd:cd14930 552 VGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILT 631
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1387193866 727 PAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 766
Cdd:cd14930 632 PNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
100-766 |
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: 656.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 100 AVLYNLKERYASWMIYTYSGLFCVTINPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 180 SGAGKTVNTKRVIQYfavIAAIGDRSKKEQATGKgtleDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 259
Cdd:cd01378 82 SGAGKTEASKRIMQY---IAAVSGGSESEVERVK----DMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 260 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAFDVL 339
Cdd:cd01378 155 GGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 340 GFTTEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDgTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEY---VTKGQN 416
Cdd:cd01378 235 GFTEEEQDSIFRILAAILHLGNIQFAEDEEGNAAISD-TSVLDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvYEVPLN 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 417 VQQVVYAKGALAKAVYERMFNWMVTRINATLETKQPRQ-YFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHhmFV 495
Cdd:cd01378 314 VEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKkKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIE--LT 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 496 L--EQEEYKKEGIEWEFIDFgMDLQACIDLIE-KPMGIMSILEEECMFP-KATDMTFKAKLfDNHLGKSSNFQKPRNIKG 571
Cdd:cd01378 392 LkaEQEEYVREGIEWTPIKY-FNNKIICDLIEeKPPGIFAILDDACLTAgDATDQTFLQKL-NQLFSNHPHFECPSGHFE 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 572 KPEAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKKSSLKMLSSLFanyagFDTPIEKGKGKAKkgssfqTVSALH 651
Cdd:cd01378 470 LRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLF-----PEGVDLDSKKRPP------TAGTKF 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 652 RENLNKLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIP 731
Cdd:cd01378 539 KNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPKTWP 618
|
650 660 670
....*....|....*....|....*....|....*
gi 1387193866 732 EGQFIDsRKGAEKLLGSLDIDHNQYKFGHTKVFFK 766
Cdd:cd01378 619 AWDGTW-QGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
99-766 |
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: 640.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 99 PAVLYNLKERYASWMIYTYSGLFCVTINPYKWLPVYNAEVVAAYRgkKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd01383 1 PSVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 179 ESGAGKTVNTKRVIQYfavIAAIGdrskkeqaTGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 258
Cdd:cd01383 79 ESGAGKTETAKIAMQY---LAALG--------GGSSGIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 259 ASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNnPYDYAFISQGET-TVASIDDAEELMATDNAFD 337
Cdd:cd01383 148 CGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKS-ASEYKYLNQSNClTIDGVDDAKKFHELKEALD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 338 VLGFTTEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNV 417
Cdd:cd01383 227 TVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 418 QQVVYAKGALAKAVYERMFNWMVTRINATLET-KQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 496
Cdd:cd01383 307 QQAIDARDALAKAIYASLFDWLVEQINKSLEVgKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 497 EQEEYKKEGIEWEFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKATDMTFKAKLfDNHLGKSSNFqkprniKGKPEA 575
Cdd:cd01383 387 EQEEYELDGIDWTKVDF-EDNQECLDLIEkKPLGLISLLDEESNFPKATDLTFANKL-KQHLKSNSCF------KGERGG 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 576 HFSLIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKKSSLKMLSSLFANYAGFDTPIEKGKGKAKKGSSFQTVSALHRENL 655
Cdd:cd01383 459 AFTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQLPQLFASKMLDASRKALPLTKASGSDSQKQSVATKFKGQL 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 656 NKLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQF 735
Cdd:cd01383 539 FKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDVSASQD 618
|
650 660 670
....*....|....*....|....*....|.
gi 1387193866 736 IDSRKGAekLLGSLDIDHNQYKFGHTKVFFK 766
Cdd:cd01383 619 PLSTSVA--ILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
100-766 |
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: 638.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 100 AVLYNLKERYASWMIYTYSGLFCVTINPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd01381 2 GILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 180 SGAGKTVNTKRVIQYFAVIAaiGDRSKKEQatgkgtledQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 259
Cdd:cd01381 82 SGAGKTESTKLILQYLAAIS--GQHSWIEQ---------QILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 260 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITnNPYDYAFISQGETTVAS-IDDAEELMATDNAFDV 338
Cdd:cd01381 151 GAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELG-DASDYYYLTQGNCLTCEgRDDAAEFADIRSAMKV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 339 LGFTTEEKNSMYKLTGAIMHFGNMKFKLKQRE--EQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQN 416
Cdd:cd01381 230 LMFTDEEIWDIFKLLAAILHLGNIKFEATVVDnlDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 417 VQQVVYAKGALAKAVYERMFNWMVTRINATLETKQPRQYF---IGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHM 493
Cdd:cd01381 310 AEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtsIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 494 FVLEQEEYKKEGIEWEFIDFgMDLQACIDLI-EKPMGIMSILEEECMFPKATDMTFKAKLFDNHlGKSSNFQKPRNikgK 572
Cdd:cd01381 390 FKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMNIMSLIDEESKFPKGTDQTMLEKLHSTH-GNNKNYLKPKS---D 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 573 PEAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKKSSLKMLSSLFANYAGFDTpiekgkgkaKKGSSFQTVSALHR 652
Cdd:cd01381 465 LNTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDISMGS---------ETRKKSPTLSSQFR 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 653 ENLNKLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPaAIPE 732
Cdd:cd01381 536 KSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVP-GIPP 614
|
650 660 670
....*....|....*....|....*....|....
gi 1387193866 733 GQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 766
Cdd:cd01381 615 AHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
100-766 |
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: 616.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 100 AVLYNLKERYASWMIYTYSGLFCVTINPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 180 SGAGKTVNTKRVIQYFAviaaigdrskkeQATGKGT-LEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 258
Cdd:cd14883 82 SGAGKTETTKLILQYLC------------AVTNNHSwVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 259 ASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKK--PELLDmLLITNNPYDYAFISQ-GETTVASIDDAEELMATDNA 335
Cdd:cd14883 150 KGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKhsKELKE-KLKLGEPEDYHYLNQsGCIRIDNINDKKDFDHLRLA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 336 FDVLGFTTEEKNSMYKLTGAIMHFGNMKFKLKQREEQAE-PDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKG 414
Cdd:cd14883 229 MNVLGIPEEMQEGIFSVLSAILHLGNLTFEDIDGETGALtVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 415 QNVQQVVYAKGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMF 494
Cdd:cd14883 309 LKVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 495 VLEQEEYKKEGIEWEFIDFgMDLQACIDLIEK-PMGIMSILEEECMFPKATDMTFKAKLFDNHlGKSSNFQKPRNIKGKP 573
Cdd:cd14883 389 KLEQEEYEKEGINWSHIVF-TDNQECLDLIEKpPLGILKLLDEECRFPKGTDLTYLEKLHAAH-EKHPYYEKPDRRRWKT 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 574 EahFSLIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKKSSLKMLSSLF-----ANYAGFDTPIEKGKGKAKKGSSFQTVS 648
Cdd:cd14883 467 E--FGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFtypdlLALTGLSISLGGDTTSRGTSKGKPTVG 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 649 ALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPA 728
Cdd:cd14883 545 DTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPR 624
|
650 660 670
....*....|....*....|....*....|....*....
gi 1387193866 729 AIPEGQfiDSRKGAEK-LLGSLDIDHNQYKFGHTKVFFK 766
Cdd:cd14883 625 ARSADH--KETCGAVRaLMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
99-766 |
0e+00 |
|
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle transport. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle.
Pssm-ID: 276835 Cd Length: 647 Bit Score: 586.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 99 PAVLYNLKERYASWMIYTYSGLFCVTINPYKWLP-VYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 177
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 178 GESGAGKTVNTKRVIQYfavIAAIGDRSKKEQATgkgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 257
Cdd:cd01384 81 GESGAGKTETTKMLMQY---LAYMGGRAVTEGRS----VEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 258 LASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLItNNPYDYAFISQGET-TVASIDDAEELMATDNAF 336
Cdd:cd01384 154 ISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKL-KDPKQFHYLNQSKCfELDGVDDAEEYRATRRAM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 337 DVLGFTTEEKNSMYKLTGAIMHFGNMKFKlKQREEQAEPDGTEEADKS----AYLMGLNSADLLKGLCHPRVKVGNEYVT 412
Cdd:cd01384 233 DVVGISEEEQDAIFRVVAAILHLGNIEFS-KGEEDDSSVPKDEKSEFHlkaaAELLMCDEKALEDALCKRVIVTPDGIIT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 413 KGQNVQQVVYAKGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHH 492
Cdd:cd01384 312 KPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQH 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 493 MFVLEQEEYKKEGIEWEFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKATDMTFKAKLFDNhLGKSSNFQKPRnikg 571
Cdd:cd01384 392 VFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPRSTHETFAQKLYQT-LKDHKRFSKPK---- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 572 KPEAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKKSSLKMLSSLFAnyagfdtpiEKGKGKAKKGSSFQTVSALH 651
Cdd:cd01384 466 LSRTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFP---------PLPREGTSSSSKFSSIGSRF 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 652 RENLNKLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIp 731
Cdd:cd01384 537 KQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPEVL- 615
|
650 660 670
....*....|....*....|....*....|....*
gi 1387193866 732 eGQFIDSRKGAEKLLGSLDIdhNQYKFGHTKVFFK 766
Cdd:cd01384 616 -KGSDDEKAACKKILEKAGL--KGYQIGKTKVFLR 647
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
99-766 |
1.38e-174 |
|
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: 545.53 E-value: 1.38e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 99 PAVLYNLKERYASWMIYTYSGLFCVTINPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 179 ESGAGKTVNTKRVIQYFAviaaigdrskkEQATGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 258
Cdd:cd14872 81 ESGAGKTEATKQCLSFFA-----------EVAGSTNGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 259 ASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLlitNNPYDYAFISQGET-TVASIDDAEELMATDNAFD 337
Cdd:cd14872 150 CGASTENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGW---GSSAAYGYLSLSGCiEVEGVDDVADFEEVVLAME 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 338 VLGFTTEEKNSMYKLTGAIMHFGNMKF------KLKQREEQAEPDGTEEAdksAYLMGLNSADLLKGLCHPRVKVgneyv 411
Cdd:cd14872 227 QLGFDDADINNVMSLIAAILKLGNIEFasgggkSLVSGSTVANRDVLKEV---ATLLGVDAATLEEALTSRLMEI----- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 412 tKGQNV-------QQVVYAKGALAKAVYERMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNE 483
Cdd:cd14872 299 -KGCDPtripltpAQATDACDALAKAAYSRLFDWLVKKINESMRpQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 484 KLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLIEK-PMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSsn 562
Cdd:cd14872 378 KLQQHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEKkQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKS-- 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 563 FQKPRNIKGKPEaHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKKSSLKMLSSLFAnyagfdtPIEkgkgkAKKGS 642
Cdd:cd14872 455 TFVYAEVRTSRT-EFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFP-------PSE-----GDQKT 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 643 SFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRY 722
Cdd:cd14872 522 SKVTLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRY 601
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1387193866 723 RILnPAAIPEGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 766
Cdd:cd14872 602 RFL-VKTIAKRVGPDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
99-766 |
8.69e-173 |
|
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: 541.29 E-value: 8.69e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 99 PAVLYNLKERYASWMIYTYSGLFCVTINPYKWLP-VYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 177
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 178 GESGAGKTVNTKRVIQYFAVIAaigdrskkeqatgkGTLED----QIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFG 253
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIA--------------GGLNDstikKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 254 ATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDmLLITNNPYDYafisQGETTVASID---DAEELM 330
Cdd:cd14903 147 KNGTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEERL-FLDSANECAY----TGANKTIKIEgmsDRKHFA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 331 ATDNAFDVLGFTTEEKNSMYKLTGAIMHFGNMKFKLKQREEQAE--PDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGN 408
Cdd:cd14903 222 RTKEALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSaiAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 409 EYVTKGQNVQQVVYAKGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQF 488
Cdd:cd14903 302 DVYTVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQK 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 489 FNHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSSNFQKPRN 568
Cdd:cd14903 382 FTQDVFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFPRT 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 569 IKgkpeAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKKSSLKMLSSLFANYAGFDTPIEKGKGKAKKGS-----S 643
Cdd:cd14903 461 SR----TQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAASTSLARGARRRrggalT 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 644 FQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYR 723
Cdd:cd14903 537 TTTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFW 616
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1387193866 724 ILNPAAipEGQFIDSRKGAEKLLGSLDIDH-NQYKFGHTKVFFK 766
Cdd:cd14903 617 LFLPEG--RNTDVPVAERCEALMKKLKLESpEQYQMGLTRIYFQ 658
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
846-1923 |
4.19e-172 |
|
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: 554.01 E-value: 4.19e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 846 EKEIALMKEEFGRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMTER 925
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 926 LEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQ 1005
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1006 ALDDLQAEEDKVNTLTKAKVKLEQHVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDF 1085
Cdd:pfam01576 164 FTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1086 ELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNK 1165
Cdd:pfam01576 244 ELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1166 KREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELSEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANL 1245
Cdd:pfam01576 324 KREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1246 EKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVKA 1325
Cdd:pfam01576 404 EHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1326 KNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAiQRTEELEEAKKKLAQRLQDAEEAVE 1405
Cdd:pfam01576 484 KLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDA-GTLEALEEGKKRLQRELEALTQQLE 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1406 AVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLK 1485
Cdd:pfam01576 563 EKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLA 642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1486 NAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKLELQSALEEAEASLEHEEGKILRAQLEF 1565
Cdd:pfam01576 643 RALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNM 722
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1566 NQIKAEMERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRLAAEAQKQVKS 1645
Cdd:pfam01576 723 QALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKK 802
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1646 LQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLIN 1725
Cdd:pfam01576 803 LQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQD 882
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1726 QKKKMEADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIAL 1805
Cdd:pfam01576 883 EKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVK 962
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1806 KGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEA 1885
Cdd:pfam01576 963 SKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEA 1042
|
1050 1060 1070
....*....|....*....|....*....|....*...
gi 1387193866 1886 EEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAK 1923
Cdd:pfam01576 1043 EEEASRANAARRKLQRELDDATESNESMNREVSTLKSK 1080
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
102-766 |
6.06e-168 |
|
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: 527.59 E-value: 6.06e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 102 LYNLKERYASWMIYTYSGLFCVTINPYKWLP-VYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGES 180
Cdd:cd01382 4 LNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVSGES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 181 GAGKTVNTKRVIQYFAVIaaigdrskkeQATGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLAS 260
Cdd:cd01382 84 GAGKTESTKYILRYLTES----------WGSGAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 261 ADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLitnnpydyafisqgetTVASIDDAEELMATDNAFDVLG 340
Cdd:cd01382 154 GFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLL----------------KDPLLDDVGDFIRMDKAMKKIG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 341 FTTEEKNSMYKLTGAIMHFGNMKFklkqrEEQAEPDG-----TEEADKS----AYLMGLNSADLLKGLCHpRVKVGNEYV 411
Cdd:cd01382 218 LSDEEKLDIFRVVAAVLHLGNIEF-----EENGSDSGggcnvKPKSEQSleyaAELLGLDQDELRVSLTT-RVMQTTRGG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 412 TKGQ------NVQQVVYAKGALAKAVYERMFNWMVTRINATLETKQpRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKL 485
Cdd:cd01382 292 AKGTvikvplKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFET-SSYFIGVLDIAGFEYFEVNSFEQFCINYCNEKL 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 486 QQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKATDMTFKAKLFDNHLgKSSNFQ 564
Cdd:cd01382 371 QQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEaKLVGILDLLDEESKLPKPSDQHFTSAVHQKHK-NHFRLS 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 565 KPRniKGKPEAH--------FSLIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKKSSLKMLSSLFANyagfDTPIEKGKG 636
Cdd:cd01382 449 IPR--KSKLKIHrnlrddegFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFES----STNNNKDSK 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 637 KAKKGSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYG 716
Cdd:cd01382 523 QKAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSFH 602
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1387193866 717 DFRQRYRILNPAAIPEgqfIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 766
Cdd:cd01382 603 DLYNMYKKYLPPKLAR---LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
100-766 |
9.72e-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: 527.42 E-value: 9.72e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 100 AVLYNLKERYASWMIYTYSGLFCVTINPYKWLP-VYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYML----TDRENQSI 174
Cdd:cd14890 2 SLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIqsgvLDPSNQSI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 175 LITGESGAGKTVNTKRVIQYFAVIAAIGDRSKKEQATGK--------GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGK 246
Cdd:cd14890 82 IISGESGAGKTEATKIIMQYLARITSGFAQGASGEGEAAseaieqtlGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 247 FIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNnPYDYAFISQGETTVASIDDA 326
Cdd:cd14890 162 FIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQT-PVEYFYLRGECSSIPSCDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 327 EELMATDNAFDVLGFTTEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEA-DKSAYLMGLNSADLLKGLCHPRVK 405
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLEDATTLQSlKLAAELLGVNEDALEKALLTRQLF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 406 VGNEYVTKGQNVQQVVYAKGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKL 485
Cdd:cd14890 321 VGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYANEKL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 486 QQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLIE-KPMGIMSILE--EEC--MFPKATDMTFKAKLFDNHLGKS 560
Cdd:cd14890 401 QRHFNQHMFEVEQVEYSNEGIDWQYITF-NDNQACLELIEgKVNGKPGIFItlDDCwrFKGEEANKKFVSQLHASFGRKS 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 561 SNFQKPRNIKGKP---------EAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKKS--SLKMLSslfanyagfdt 629
Cdd:cd14890 480 GSGGTRRGSSQHPhfvhpkfdaDKQFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSrrSIREVS----------- 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 630 piekgkgkakkgssfqtVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGF 709
Cdd:cd14890 549 -----------------VGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQIRQQGF 611
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 1387193866 710 PNRILYGDFRQRYRILNPAAIPEGQFIdsrkgaEKLLGSLDIDHNQYKFGHTKVFFK 766
Cdd:cd14890 612 ALREEHDSFFYDFQVLLPTAENIEQLV------AVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
99-766 |
7.76e-167 |
|
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: 525.41 E-value: 7.76e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 99 PAVLYNLKERYASWMIYTYSGLFCVTINPYKWLP-VYNAEVVAAYRgKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 177
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 178 GESGAGKTVNTKRVIQYFAViAAIGDRSKKEqatgkgTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHF----- 252
Cdd:cd14888 80 GESGAGKTESTKYVMKFLAC-AGSEDIKKRS------LVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFsklks 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 253 ----GATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILS-----------------------NKKPELLDMLLI-T 304
Cdd:cd14888 153 krmsGDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAaareakntglsyeendeklakgaDAKPISIDMSSFeP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 305 NNPYDYAFISqGETTVASIDDAEELMATDNAFDVLGFTTEEKNSMYKLTGAIMHFGNMKFKLKQREEQA---EPDGTEEA 381
Cdd:cd14888 233 HLKFRYLTKS-SCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGavvSASCTDDL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 382 DKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQVVYAKGALAKAVYERMFNWMVTRINATLE-TKQPRQYFIGVL 460
Cdd:cd14888 312 EKVASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGySKDNSLLFCGVL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 461 DIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLQACIDLI-EKPMGIMSILEEECM 539
Cdd:cd14888 392 DIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLqEKPLGIFCMLDEECF 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 540 FPKATDMTFKAKLFDNHLGkSSNFQKprnIKGKPEAhFSLIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKKSSLKMLSS 619
Cdd:cd14888 471 VPGGKDQGLCNKLCQKHKG-HKRFDV---VKTDPNS-FVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISN 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 620 LFANYagfdtpIEKGKGKAKKGSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVL 699
Cdd:cd14888 546 LFSAY------LRRGTDGNTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGVL 619
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387193866 700 EGIRICRKGFPNRILYGDFRQRYRILNPaaipegqfidsrkgaekllGSLDIDHNQYKFGHTKVFFK 766
Cdd:cd14888 620 QAVQVSRAGYPVRLSHAEFYNDYRILLN-------------------GEGKKQLSIWAVGKTLCFFK 667
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
99-766 |
1.96e-166 |
|
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: 522.99 E-value: 1.96e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 99 PAVLYNLKERYASWMIYTYSGLFCVTINPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd01379 1 DTIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 179 ESGAGKTVNTKRVIQYFAVIAAIGDRskkeqatgkgTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 258
Cdd:cd01379 81 ESGAGKTESANLLVQQLTVLGKANNR----------TLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 259 ASADIETYLLEKSRVIFQLKAERDYHIFYQIL----SNKKpeLLDMLLITNNPYDY-AFISQGETTVASID-DAEELMAT 332
Cdd:cd01379 151 TGARISEYLLEKSRVVHQAIGERNFHIFYYIYaglaEDKK--LAKYKLPENKPPRYlQNDGLTVQDIVNNSgNREKFEEI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 333 DNAFDVLGFTTEEKNSMYKLTGAIMHFGNMKFKLKQREEQ----AEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGN 408
Cdd:cd01379 229 EQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTEVESNHQtdksSRISNPEALNNVAKLLGIEADELQEALTSHSVVTRG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 409 EYVTKGQNVQQVVYAKGALAKAVYERMFNWMVTRINATL---ETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKL 485
Cdd:cd01379 309 ETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpdRSASDEPLSIGILDIFGFENFQKNSFEQLCINIANEQI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 486 QQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLQACID-LIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHlgKSSNFQ 564
Cdd:cd01379 389 QYYFNQHIFAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFLQKPMGLLALLDEESRFPKATDQTLVEKFHNNI--KSKYYW 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 565 KPRnikgKPEAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKKSSLKMLSslfanyagfdtpiekgkgkakkgssf 644
Cdd:cd01379 466 RPK----SNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVR-------------------------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 645 QTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRI 724
Cdd:cd01379 516 QTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYYF 595
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1387193866 725 L--NPAAIPEGqfidSRKGAEKLLGSLDIDHnqYKFGHTKVFFK 766
Cdd:cd01379 596 LafKWNEEVVA----NRENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
100-766 |
8.57e-166 |
|
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: 522.01 E-value: 8.57e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 100 AVLYNLKERYASWMIYTYSGLFCVTINPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd01387 2 TVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 180 SGAGKTVNTKRVIQYFAVIAAigdrskkeqaTGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFgATGKLA 259
Cdd:cd01387 82 SGSGKTEATKLIMQYLAAVNQ----------RRNNLVTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-EGGVIV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 260 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDM--LLitnNPYDYAFISQGETT-VASIDDAEELMATDNAF 336
Cdd:cd01387 151 GAITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKygLQ---EAEKYFYLNQGGNCeIAGKSDADDFRRLLAAM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 337 DVLGFTTEEKNSMYKLTGAIMHFGNMKFKLKQRE---EQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTK 413
Cdd:cd01387 228 QVLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRhgqEGVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRERIFT 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 414 GQNVQQVVYAKGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHM 493
Cdd:cd01387 308 PLTIDQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 494 FVLEQEEYKKEGIEWEFIDFgMDLQACIDLI-EKPMGIMSILEEECMFPKATDMTFKAKLFDNHlGKSSNFQKPRniKGK 572
Cdd:cd01387 388 FKLEQEEYIREQIDWTEIAF-ADNQPVINLIsKKPVGILHILDDECNFPQATDHSFLEKCHYHH-ALNELYSKPR--MPL 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 573 PEahFSLIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKKSSLKMLSSLFANYAgfdtPIEKGKGKAKKGSSF-------Q 645
Cdd:cd01387 464 PE--FTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHR----AQTDKAPPRLGKGRFvtmkprtP 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 646 TVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRIL 725
Cdd:cd01387 538 TVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCL 617
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1387193866 726 NPAAIPEGQFIDSRkgaEKLLGSLD--IDHNQYKFGHTKVFFK 766
Cdd:cd01387 618 VALKLPRPAPGDMC---VSLLSRLCtvTPKDMYRLGATKVFLR 657
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
99-764 |
1.83e-160 |
|
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: 507.40 E-value: 1.83e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 99 PAVLYNLKERYASWMIYTYSGLFCVTINPYKWLPVYNAEVVAAY------RGKKRSEAPPHIFSISDNAYQYMLTDRE-- 170
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 171 --NQSILITGESGAGKTVNTKRVIQYFAVIAAIgdRSKKEQATGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFI 248
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSSA--TTHGQNATERENVRDRVLESNPILEAFGNARTNRNNNSSRFGKFI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 249 RIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPyDYAFISQGETTVA--SIDDA 326
Cdd:cd14901 159 RLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVE-EYKYLNSSQCYDRrdGVDDS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 327 EELMATDNAFDVLGFTTEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAY-LMGLNSADLLKGLCHPRVK 405
Cdd:cd14901 238 VQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGGTFSMSSLANVRAACdLLGLDMDVLEKTLCTREIR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 406 VGNEYVTKGQNVQQVVYAKGALAKAVYERMFNWMVTRINATLETKQP--RQYFIGVLDIAGFEIFDFNSFEQLCINFTNE 483
Cdd:cd14901 318 AGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSEStgASRFIGIVDIFGFEIFATNSLEQLCINFANE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 484 KLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDlQACIDLIE-KPMGIMSILEEECMFPKATDMTFKAKLFDNhLGKSSN 562
Cdd:cd14901 398 KLQQLFGKFVFEMEQDEYVAEAIPWTFVEYPNN-DACVAMFEaRPTGLFSLLDEQCLLPRGNDEKLANKYYDL-LAKHAS 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 563 FQKPRNIKGKpeAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKKSSLKMLSSlfanyagfdtpiekgkgkakkgs 642
Cdd:cd14901 476 FSVSKLQQGK--RQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS----------------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 643 sfqTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRY 722
Cdd:cd14901 531 ---TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHTY 607
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1387193866 723 RILNPAAIPEGQFIDSRKGAEKLLGSLDI----DHNQYKFGHTKVF 764
Cdd:cd14901 608 SCLAPDGASDTWKVNELAERLMSQLQHSElnieHLPPFQVGKTKVF 653
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
102-766 |
7.30e-158 |
|
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: 501.91 E-value: 7.30e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 102 LYNLKERYASWMIYTYSGLFCVTINPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESG 181
Cdd:cd01385 4 LENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISGESG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 182 AGKTVNTKRVIQYFAVIaaigdrSKKEQATGkgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASA 261
Cdd:cd01385 84 SGKTESTNFLLHHLTAL------SQKGYGSG---VEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 262 DIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITnNPYDYAFISQGET-TVASIDDAEELMATDNAFDVLG 340
Cdd:cd01385 155 VVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLK-QPEDYHYLNQSDCyTLEGEDEKYEFERLKQAMEMVG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 341 FTTEEKNSMYKLTGAIMHFGNMKFKLK--QREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQ 418
Cdd:cd01385 234 FLPETQRQIFSVLSAVLHLGNIEYKKKayHRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLILPYKLP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 419 QVVYAKGALAKAVYERMFNWMVTRINATLETKQ----PRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMF 494
Cdd:cd01385 314 EAIATRDAMAKCLYSALFDWIVLRINHALLNKKdleeAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 495 VLEQEEYKKEGIEWEFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKATDMTFKAKlFDNHLGKSSNFQKPRnikgKP 573
Cdd:cd01385 394 KLEQEEYKKEGISWHNIEY-TDNTGCLQLISkKPTGLLCLLDEESNFPGATNQTLLAK-FKQQHKDNKYYEKPQ----VM 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 574 EAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKKSSL-----------------KMLSSLFANYAGF--------- 627
Cdd:cd01385 468 EPAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSafvreligidpvavfrwAVLRAFFRAMAAFreagrrraq 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 628 ---------DTPIEKGKGKAKKGSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGV 698
Cdd:cd01385 548 rtaghsltlHDRTTKSLLHLHKKKKPPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTGM 627
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387193866 699 LEGIRICRKGFPNRILYGDFRQRYRILnpaaIPEGQfIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 766
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 ... |
105-766 |
6.52e-155 |
|
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: 492.35 E-value: 6.52e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 105 LKERYASWMIYTYSGLFCVTINPYKWLP-VYNAEVVAAYRG--KKRSEAPPHIFSISDNAYQYMLTDR----ENQSILIT 177
Cdd:cd14892 7 LRRRYERDAIYTFTADILISINPYKSIPlLYDVPGFDSQRKeeATASSPPPHVFSIAERAYRAMKGVGkgqgTPQSIVVS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 178 GESGAGKTVNTKRVIQYFAVIAAIGDRSKKEQ--ATGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGAT 255
Cdd:cd14892 87 GESGAGKTEASKYIMKYLATASKLAKGASTSKgaANAHESIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQIHYNSD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 256 GKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKpELLDMLLITNNPYDYAFISQGE-TTVASIDDAEELMATDN 334
Cdd:cd14892 167 GRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLD-ANENAALELTPAESFLFLNQGNcVEVDGVDDATEFKQLRD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 335 AFDVLGFTTEEKNSMYKLTGAIMHFGNMKFKL--KQREEQAEPDGTEEADKSAYLMGLNSADLLKGLChPRVKVGneyvT 412
Cdd:cd14892 246 AMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEEnaDDEDVFAQSADGVNVAKAAGLLGVDAAELMFKLV-TQTTST----A 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 413 KGQNVQ------QVVYAKGALAKAVYERMFNWMVTRINAtlETKQ------------PRQYFIGVLDIAGFEIFDFNSFE 474
Cdd:cd14892 321 RGSVLEikltarEAKNALDALCKYLYGELFDWLISRINA--CHKQqtsgvtggaaspTFSPFIGILDIFGFEIMPTNSFE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 475 QLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLIEK-PMGIMSILEEECMFP-KATDMTFKAKL 552
Cdd:cd14892 399 QLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEF-QDNQDCLDLIQKkPLGLLPLLEEQMLLKrKTTDKQLLTIY 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 553 FDNHLGKSSNFQKPRNikgkPEAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVDLykksslkMLSSlfanyagfdtpie 632
Cdd:cd14892 478 HQTHLDKHPHYAKPRF----ECDEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDL-------LRSS------------- 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 633 kgkgkakkgSSFqtvsalhRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNR 712
Cdd:cd14892 534 ---------SKF-------RTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREGFPIR 597
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1387193866 713 ILYGDFRQRYRIL-----NPAAIPEGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 766
Cdd:cd14892 598 RQFEEFYEKFWPLarnkaGVAASPDACDATTARKKCEEIVARALERENFQLGRTKVFLR 656
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
100-766 |
5.44e-152 |
|
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: 484.30 E-value: 5.44e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 100 AVLYNLKERYASWMIYTYSGLFCVTINPYKWLP-VYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14873 2 SIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 179 ESGAGKTVNTKRVIQYFAVIA-AIGDRSKKEQATgkgTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 257
Cdd:cd14873 82 ESGAGKTESTKLILKFLSVISqQSLELSLKEKTS---CVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 258 LASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITnNPYDYAFISQ-GETTVASIDDAEELMATDNAF 336
Cdd:cd14873 159 IQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLS-TPENYHYLNQsGCVEDKTISDQESFREVITAM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 337 DVLGFTTEEKNSMYKLTGAIMHFGNMKFklkqreeqAEPDGTEEADK-----SAYLMGLNSADLLKGLCHPRVKVGNEYV 411
Cdd:cd14873 238 EVMQFSKEEVREVSRLLAGILHLGNIEF--------ITAGGAQVSFKtalgrSAELLGLDPTQLTDALTQRSMFLRGEEI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 412 TKGQNVQQVVYAKGALAKAVYERMFNWMVTRINATLETKQPRQyFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNH 491
Cdd:cd14873 310 LTPLNVQQAVDSRDSLAMALYARCFEWVIKKINSRIKGKEDFK-SIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 492 HMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHlGKSSNFQKPRnikg 571
Cdd:cd14873 389 HIFSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQH-ANNHFYVKPR---- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 572 KPEAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKKSSLKMLSSLF---ANYAGFDTPIEKGKGKAkkgssfQTVS 648
Cdd:cd14873 463 VAVNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFehvSSRNNQDTLKCGSKHRR------PTVS 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 649 ALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNP- 727
Cdd:cd14873 537 SQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRn 616
|
650 660 670
....*....|....*....|....*....|....*....
gi 1387193866 728 AAIPEgqfiDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 766
Cdd:cd14873 617 LALPE----DVRGKCTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
101-766 |
6.28e-150 |
|
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: 478.03 E-value: 6.28e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 101 VLYNLKERYASWMIYTYSGLFCVTINPYKWLPVYNAEVVAAYRGKK-RSEAPPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14897 3 IVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVSGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 180 SGAGKTVNTKRVIQYFAVIAAIGDRSkkeqatgkgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 259
Cdd:cd14897 83 SGAGKTESTKYMIKHLMKLSPSDDSD----------LLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 260 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLItNNPYDYAFISQGETTVASIDDAEELMATDNAFDVL 339
Cdd:cd14897 153 GAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFL-EDPDCHRILRDDNRNRPVFNDSEELEYYRQMFHDL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 340 -------GFTTEEKNSMYKLTGAIMHFGNMKFklkqrEEQAEPDGTEEADK-----SAYLMGLNSADLLKGLCHPRVKVG 407
Cdd:cd14897 232 tnimkliGFSEEDISVIFTILAAILHLTNIVF-----IPDEDTDGVTVADEyplhaVAKLLGIDEVELTEALISNVNTIR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 408 NEYVTKGQNVQQVVYAKGALAKAVYERMFNWMVTRINATLETKQPRQYF-----IGVLDIAGFEIFDFNSFEQLCINFTN 482
Cdd:cd14897 307 GERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDFQIMtrgpsIGILDMSGFENFKINSFDQLCINLSN 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 483 EKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLI-EKPMGIMSILEEECMFPKATDMTFKAKLfDNHLGKSS 561
Cdd:cd14897 387 ERLQQYFNDYVFPRERSEYEIEGIEWRDIEY-HDNDDVLELFfKKPLGILPLLDEESTFPQSTDSSLVQKL-NKYCGESP 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 562 NFQKPrnIKGKPEahFSLIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKKSSLKMLSSLFANYagfdtpiekgkgkakkg 641
Cdd:cd14897 465 RYVAS--PGNRVA--FGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFTSY----------------- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 642 ssfqtvsalHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQR 721
Cdd:cd14897 524 ---------FKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKR 594
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1387193866 722 YRILNPAAIPegqfidSRKGAE-KLLGSLDIDHNQ-YKFGHTKVFFK 766
Cdd:cd14897 595 YKEICDFSNK------VRSDDLgKCQKILKTAGIKgYQFGKTKVFLK 635
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
99-766 |
1.31e-144 |
|
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: 464.03 E-value: 1.31e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 99 PAVLYNLKERYASWMIYTYSGLFCVTINPYKWLP-VYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 177
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 178 GESGAGKTVNTKRVIQYFAVIAaiGDRSKKEQAtgkgtledQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 257
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVA--GGRKDKTIA--------KVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 258 LASADIETYLLEKSRVIFQLKAERDYHIFYQILSN-KKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMATDNAF 336
Cdd:cd14904 151 LIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGlSSEERKEFGLDPNCQYQYLGDSLAQMQIPGLDDAKLFASTQKSL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 337 DVLGFTTEEKNSMYKLTGAIMHFGNMKFkLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQN 416
Cdd:cd14904 231 SLIGLDNDAQRTLFKILSGVLHLGEVMF-DKSDENGSRISNGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 417 VQQVVYAKGALAKAVYERMFNWMVTRINATLETKQPRQY-FIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 495
Cdd:cd14904 310 PVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKgQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 496 LEQEEYKKEGIEWEFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNH--LGKSSNFQKPRNIKgkp 573
Cdd:cd14904 390 TVEEEYIREGLQWDHIEY-QDNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHqtKKDNESIDFPKVKR--- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 574 eAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKKSSLKMLSSLFANYAGfdTPIEKGKGKAKKGSSFQTVSALHRE 653
Cdd:cd14904 466 -TQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSEA--PSETKEGKSGKGTKAPKSLGSQFKT 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 654 NLNKLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEG 733
Cdd:cd14904 543 SLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFPPSMHSK 622
|
650 660 670
....*....|....*....|....*....|....
gi 1387193866 734 qfiDSRKGAEKLLGSLDIDHN-QYKFGHTKVFFK 766
Cdd:cd14904 623 ---DVRRTCSVFMTAIGRKSPlEYQIGKSLIYFK 653
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
101-766 |
2.80e-143 |
|
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: 460.53 E-value: 2.80e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 101 VLYNLKERYASWMIYTYSGLFCVTINPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYML----TDRENQSILI 176
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 177 TGESGAGKTVNTKRVIqyfaviaaigdRSKKEQATGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFgATG 256
Cdd:cd14889 83 SGESGAGKTESTKLLL-----------RQIMELCRGNSQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RNG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 257 KLASADIETYLLEKSRVIFQLKAERDYHIFYQI---LSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMatd 333
Cdd:cd14889 151 HVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMfagISAEDRENYGLLDPGKYRYLNNGAGCKREVQYWKKKYDEVC--- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 334 NAFDVLGFTTEEKNSMYKLTGAIMHFGNMKFKLKQREE-QAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVT 412
Cdd:cd14889 228 NAMDMVGFTEQEEVDMFTILAGILSLGNITFEMDDDEAlKVENDSNGWLKAAAGQFGVSEEDLLKTLTCTVTFTRGEQIQ 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 413 KGQNVQQVVYAKGALAKAVYERMFNWMVTRINATLETKQPRQY---FIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFF 489
Cdd:cd14889 308 RHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSVelrEIGILDIFGFENFAVNRFEQACINLANEQLQYFF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 490 NHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDL-IEKPMGIMSILEEECMFPKATDMTFKAKLfDNHLGKSSNFQKPRN 568
Cdd:cd14889 388 NHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLfLNKPIGILSLLDEQSHFPQATDESFVDKL-NIHFKGNSYYGKSRS 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 569 IKGKpeahFSLIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKKSSLKMLSSLF-ANYAGFDTPIEKGKGKAKKGSSF--- 644
Cdd:cd14889 466 KSPK----FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFtATRSRTGTLMPRAKLPQAGSDNFnst 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 645 --QTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRY 722
Cdd:cd14889 542 rkQSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAERY 621
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1387193866 723 RIL-NPAAIPegqfiDSRKGAEKLLGSLDIdhNQYKFGHTKVFFK 766
Cdd:cd14889 622 KILlCEPALP-----GTKQSCLRILKATKL--VGWKCGKTRLFFK 659
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
101-731 |
8.83e-143 |
|
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: 457.85 E-value: 8.83e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 101 VLYNLKERYASWMIYTYSGLFCVTINPYKWLP-VYNAEVVAAY-----------RGKKRSEAPPHIFSISDNAYQYM--- 165
Cdd:cd14900 3 ILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMmlg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 166 -LTDRENQSILITGESGAGKTVNTKRVIQYFAVIAAIGDRSKKEQATGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRF 244
Cdd:cd14900 83 lNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAGDNNLAASVSMGKSTSGIAAKVLQTNILLESFGNARTLRNDNSSRF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 245 GKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLdmllitnnpydyafisqgettvaSID 324
Cdd:cd14900 163 GKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAAR-----------------------KRD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 325 DAEELMAtdnAFDVLGFTTEEKNSMYKLTGAIMHFGNMKFK-------LKQREEQAEPDGTEEADKSAYLMGLNSADLLK 397
Cdd:cd14900 220 MYRRVMD---AMDIIGFTPHERAGIFDLLAALLHIGNLTFEhdensdrLGQLKSDLAPSSIWSRDAAATLLSVDATKLEK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 398 GLCHPRVKVGNEYVTKGQNVQQVVYAKGALAKAVYERMFNWMVTRINATL-----ETKQPRQYFIGVLDIAGFEIFDFNS 472
Cdd:cd14900 297 ALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmddsSKSHGGLHFIGILDIFGFEVFPKNS 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 473 FEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLI-EKPMGIMSILEEECMFPKATDMTFKAK 551
Cdd:cd14900 377 FEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEF-CDNQDCVNLIsQRPTGILSLIDEECVMPKGSDTTLASK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 552 LFdNHLGKSSNFQKPRNIKGKpeAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVDlykksslkmlssLFANYAGFdtpi 631
Cdd:cd14900 456 LY-RACGSHPRFSASRIQRAR--GLFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVD------------LFVYGLQF---- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 632 ekgkgkakkgssfqtvsalhRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPN 711
Cdd:cd14900 517 --------------------KEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVARAGFPI 576
|
650 660
....*....|....*....|
gi 1387193866 712 RILYGDFRQRYRILNPAAIP 731
Cdd:cd14900 577 RLLHDEFVARYFSLARAKNR 596
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
101-766 |
1.08e-139 |
|
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: 450.64 E-value: 1.08e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 101 VLYNLKERYASWMIYTYSGLFCVTINPYKWLP-VYNAEVVAAYRGK--------KRSEAPPHIFSISDNAYQYMLTDREN 171
Cdd:cd14907 3 LLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQiiqngeyfDIKKEPPHIYAIAALAFKQLFENNKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 172 QSILITGESGAGKTVNTKRVIQYFAVIAA-------IGDRSKKEQATGKGT--LEDQIIQANPALEAFGNAKTVRNDNSS 242
Cdd:cd14907 83 QAIVISGESGAGKTENAKYAMKFLTQLSQqeqnseeVLTLTSSIRATSKSTksIEQKILSCNPILEAFGNAKTVRNDNSS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 243 RFGKFIRIHFG-ATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNP--YDYAFISQGET- 318
Cdd:cd14907 163 RFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNQLsgDRYDYLKKSNCy 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 319 TVASIDDAEELMATDNAFDVLGFTTEEKNSMYKLTGAIMHFGNMKFKLKQ--REEQAEPDGTEEADKSAYLMGLNSADLL 396
Cdd:cd14907 243 EVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTldDNSPCCVKNKETLQIIAKLLGIDEEELK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 397 KGLCHPRVKVGNEYVTKGQNVQQVVYAKGALAKAVYERMFNWMVTRINATL--------ETKQPRQYFIGVLDIAGFEIF 468
Cdd:cd14907 323 EALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdqQLFQNKYLSIGLLDIFGFEVF 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 469 DFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEF--IDFgMDLQACIDLIEK-PMGIMSILEEECMFPKATD 545
Cdd:cd14907 403 QNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSY-TDNQDVIDLLDKpPIGIFNLLDDSCKLATGTD 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 546 MTFKAKLFDNHlGKSSNFQKPRNIKGKpeaHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKKSSLKMLSSLFanYA 625
Cdd:cd14907 482 EKLLNKIKKQH-KNNSKLIFPNKINKD---TFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIF--SG 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 626 GFDTPIEKGKGKAKKGSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRIC 705
Cdd:cd14907 556 EDGSQQQNQSKQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLESIRVR 635
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387193866 706 RKGFPNRILYGDFRQRYRILNpaaipegqfidsrkgaekllgsldidhNQYKFGHTKVFFK 766
Cdd:cd14907 636 KQGYPYRKSYEDFYKQYSLLK---------------------------KNVLFGKTKIFMK 669
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
99-727 |
1.33e-135 |
|
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: 441.25 E-value: 1.33e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 99 PAVLYNLKERYASWMIYTYSGLFCVTINPYKWLP-VYNAEVVAAYR--------GKKRSEAPPHIFSISDNAYQYML-TD 168
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLkPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 169 RENQSILITGESGAGKTVNTKRVIQYFAVIAAigDRSKKEQATGKGT-LEDQIIQANPALEAFGNAKTVRNDNSSRFGKF 247
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGR--DQSSTEQEGSDAVeIGKRILQTNPILESFGNAQTIRNDNSSRFGKF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 248 IRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNpYDYAFISQGETTVA-----S 322
Cdd:cd14902 159 IKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKG-GKYELLNSYGPSFArkravA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 323 IDDAEELMATDNAFDVLGFTTEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEA---DKSAYLMGLNSADLLKGL 399
Cdd:cd14902 238 DKYAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAVTAASRfhlAKCAELMGVDVDKLETLL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 400 CHPRVKVGNEYVTKGQNVQQVVYAKGALAKAVYERMFNWMVTRIN-------ATLETKQPRQYF--IGVLDIAGFEIFDF 470
Cdd:cd14902 318 SSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSdeinyfdSAVSISDEDEELatIGILDIFGFESLNR 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 471 NSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLqACIDLIE-KPMGIMSILEEECMFPKATDMTFK 549
Cdd:cd14902 398 NGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYPSNA-ACLALFDdKSNGLFSLLDQECLMPKGSNQALS 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 550 AKLFDNHLgkssnfqkprnikgkPEAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKKSSLKMLSSLFANYAGFDT 629
Cdd:cd14902 477 TKFYRYHG---------------GLGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGADENRDSP 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 630 PIEKGKGKAKKGSSFQT--VSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRK 707
Cdd:cd14902 542 GADNGAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRIARH 621
|
650 660
....*....|....*....|
gi 1387193866 708 GFPNRILYGDFRQRYRILNP 727
Cdd:cd14902 622 GYSVRLAHASFIELFSGFKC 641
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
99-766 |
6.80e-135 |
|
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal SH3-like domain, two IQ motifs, a coiled-coil region and a PX domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276856 Cd Length: 645 Bit Score: 436.40 E-value: 6.80e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 99 PAVLYNLKERYAS--WMIYTYSGLFCVTINPYKWLPvyNAEVvAAYRGKKRSEAPPHIFSISDNAYQYMLTDRE---NQS 173
Cdd:cd14891 1 AGILHNLEERSKLdnQRPYTFMANVLIAVNPLRRLP--EPDK-SDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqNQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 174 ILITGESGAGKTVNTKRVIQY--------FAVIAAIGDRSKKEQATGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFG 245
Cdd:cd14891 78 IVISGESGAGKTETSKIILRFlttravggKKASGQDIEQSSKKRKLSVTSLDERLMDTNPILESFGNAKTLRNHNSSRFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 246 KFIRIHFGATG-KLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITnNPYDYAFISQ-GETTVASI 323
Cdd:cd14891 158 KFMKLQFTKDKfKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLL-SPEDFIYLNQsGCVSDDNI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 324 DDAEELMATDNAFDVLGFTTEEKNSMYKLTGAIMHFGNMKFKlKQREEQAEPDGTEEADK-----SAYLMGLNSADLLKG 398
Cdd:cd14891 237 DDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFD-EEDTSEGEAEIASESDKealatAAELLGVDEEALEKV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 399 LCHPRVKVGNEYVTKGQNVQQVVYAKGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFD-FNSFEQLC 477
Cdd:cd14891 316 ITQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFEtKNDFEQLL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 478 INFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLQACIDLI-EKPMGIMSILEEECMFPKATDMTFKAKLFDNH 556
Cdd:cd14891 396 INYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIaSKPNGILPLLDNEARNPNPSDAKLNETLHKTH 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 557 lGKSSNFQKPRNiKGKPEAhFSLIHYAGTVDYNIIGWLQKNKDPLNETvvdlykksslkmLSSLFANYAGFDTPIEKgkg 636
Cdd:cd14891 475 -KRHPCFPRPHP-KDMREM-FIVKHYAGTVSYTIGSFIDKNNDIIPED------------FEDLLASSAKFSDQMQE--- 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 637 kakkgssfqtvsalhrenlnkLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYG 716
Cdd:cd14891 537 ---------------------LVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRVTYA 595
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1387193866 717 DFRQRYRILNPAAI------PEGQFIdsrkgaEKLLGSLDIDHNQYKFGHTKVFFK 766
Cdd:cd14891 596 ELVDVYKPVLPPSVtrlfaeNDRTLT------QAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
99-727 |
2.05e-131 |
|
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: 428.17 E-value: 2.05e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 99 PAVLYNLKERYASWMIYTYSGLFCVTINPYKWLPVYNAEVVAAYR--GKKRS---EAP----PHIFSISDNAYQYMLTD- 168
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSqgiESPqalgPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 169 RENQSILITGESGAGKTVNTKRVIQYFAVIAAIGDRSKKEQAT-GKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKF 247
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEGEElGKLSIMDRVLQSNPILEAFGNARTLRNDNSSRFGKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 248 IRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQIL------SNKKPELLDMLLITNN-PYDYAFISQGET-T 319
Cdd:cd14908 161 IELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLrggdeeEHEKYEFHDGITGGLQlPNEFHYTGQGGApD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 320 VASIDDAEELMATDNAFDVLGFTTEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAY---LMGLNSADLL 396
Cdd:cd14908 241 LREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEEGNEKCLARvakLLGVDVDKLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 397 KGLCHPRVKVGNEYVTKGQNVQQVVYAKGALAKAVYERMFNWMVTRINATL--ETKQPRQYFIGVLDIAGFEIFDFNSFE 474
Cdd:cd14908 321 RALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSInwENDKDIRSSVGVLDIFGFECFAHNSFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 475 QLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLQACIDLIE-KPMGIMSILEEECMFP-KATDMTFKAKL 552
Cdd:cd14908 401 QLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQaKKKGILTMLDDECRLGiRGSDANYASRL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 553 FDNHL-------GKSSNFQKPRNIKGKpeAHFSLIHYAGTVDYNI-IGWLQKNKDPLNETVvdlykksslkmlSSLFANY 624
Cdd:cd14908 480 YETYLpeknqthSENTRFEATSIQKTK--LIFAVRHFAGQVQYTVeTTFCEKNKDEIPLTA------------DSLFESG 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 625 AGFdtpiekgkgkakkgssfqtvsalhRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRI 704
Cdd:cd14908 546 QQF------------------------KAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAVRV 601
|
650 660
....*....|....*....|...
gi 1387193866 705 CRKGFPNRILYGDFRQRYRILNP 727
Cdd:cd14908 602 ARSGYPVRLPHKDFFKRYRMLLP 624
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
62-819 |
3.18e-130 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 429.45 E-value: 3.18e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 62 ETEHGKTVTVKEDQVLQQNPP-KFDKIEDMAMLTFLHEPAVLYNLKERYASWMIYTYSGLFCVTINPYKWLPVYNAEVVA 140
Cdd:PTZ00014 72 DPPTNSTFEVKPEHAFNANSQiDPMTYGDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIR 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 141 AYR-GKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESGAGKTVNTKRVIQYFAViAAIGDRSKKEQATgkgtledq 219
Cdd:PTZ00014 152 RYRdAKDSDKLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFAS-SKSGNMDLKIQNA-------- 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 220 IIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLD 299
Cdd:PTZ00014 223 IMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKE 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 300 MLLITNNPyDYAFISQGETTVASIDDAEELMATDNAFDVLGFTTEEKNSMYKLTGAIMHFGNMKFklKQREEQAEPDGTE 379
Cdd:PTZ00014 303 KYKLKSLE-EYKYINPKCLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEI--EGKEEGGLTDAAA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 380 EADKS-------AYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQVVYAKGALAKAVYERMFNWMVTRINATLETKQP 452
Cdd:PTZ00014 380 ISDESlevfneaCELLFLDYESLKKELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGG 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 453 RQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMS 532
Cdd:PTZ00014 460 FKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGKSVLS 539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 533 ILEEECMFPKATDMTFKAKLFdNHLGKSSNFQKPRNIKGKpeaHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKKS 612
Cdd:PTZ00014 540 ILEDQCLAPGGTDEKFVSSCN-TNLKNNPKYKPAKVDSNK---NFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKAS 615
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 613 SLKMLSSLFAnyagfDTPIEKGKGKAKKGSSFQTVsalhrENLNKLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQ 692
Cdd:PTZ00014 616 PNPLVRDLFE-----GVEVEKGKLAKGQLIGSQFL-----NQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQ 685
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 693 LRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNpAAIPEGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFKAGLLGL 772
Cdd:PTZ00014 686 LHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLD-LAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLKKDAAKE 764
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 1387193866 773 LEEMRDERLSR---IITRIQAQSRGVLSRmefKKLLERRDSLLIIQWNIR 819
Cdd:PTZ00014 765 LTQIQREKLAAwepLVSVLEALILKIKKK---RKVRKNIKSLVRIQAHLR 811
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
99-766 |
5.40e-130 |
|
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: 422.65 E-value: 5.40e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 99 PAVLYNLKERYASWMIYTYSGLFCVTINPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 179 ESGAGKTVNTKRVIQYFAVIAAIGDRSKKEQatgkgtLEDQIiqanPALEAFGNAKTVRNDNSSRFGKFIRIHFgATGKL 258
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSLYQDQTEDRLRQ------PEDVL----PILESFGHAKTILNANASRFGQVLRLHL-QHGVI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 259 ASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLItNNPYDYAFISQGET-TVASIDDAEELMATDNAFD 337
Cdd:cd14896 150 VGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSL-QGPETYYYLNQGGAcRLQGKEDAQDFEGLLKALQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 338 VLGFTTEEKNSMYKLTGAIMHFGNMKFKLKQRE--EQAEPDGTEEADKSAYLMGLnSADLLKGLCHPRVKVGN-EYVTKG 414
Cdd:cd14896 229 GLGLCAEELTAIWAVLAAILQLGNICFSSSEREsqEVAAVSSWAEIHTAARLLQV-PPERLEGAVTHRVTETPyGRVSRP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 415 QNVQQVVYAKGALAKAVYERMFNWMVTRINATLETKQPRQYF--IGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHH 492
Cdd:cd14896 308 LPVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESDatIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQT 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 493 MFVLEQEEYKKEGIEWEFIDfGMDLQACIDLI-EKPMGIMSILEEECMFPKATDMTFKAKLFDNHlGKSSNFQKPRNikg 571
Cdd:cd14896 388 LLAQEEEECQRELLPWVPIP-QPPRESCLDLLvDQPHSLLSILDDQTWLSQATDHTFLQKCHYHH-GDHPSYAKPQL--- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 572 kPEAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKKSSLKMLSSLFanyagfdtpiEKGKGKAKKGSSFQTVSALH 651
Cdd:cd14896 463 -PLPVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLF----------QEAEPQYGLGQGKPTLASRF 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 652 RENLNKLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILnpAAIP 731
Cdd:cd14896 532 QQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGAL--GSER 609
|
650 660 670
....*....|....*....|....*....|....*
gi 1387193866 732 EGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 766
Cdd:cd14896 610 QEALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
99-766 |
4.98e-121 |
|
class XIV myosin, motor domain; These myosins localize to plasma membranes of the intracellular parasites and may be involved in the cell invasion process. Their known functions include: transporting phagosomes to the nucleus and perturbing the developmentally regulated elimination of the macronucleus during conjugation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to their motor domain these myosins have a MyTH4-FERM protein domain combination. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276843 Cd Length: 649 Bit Score: 397.44 E-value: 4.98e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 99 PAVLYNLKERYASWMIYTYSGLFCVTINPYKWLPVYNAEVVAAYRG-KKRSEAPPHIFSIS----DNAYQYmltdRENQS 173
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDaPDLTKLPPHVFYTArralENLHGV----NKSQT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 174 ILITGESGAGKTVNTKRVIQYFAViaaigdrSKKEQATGKgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFG 253
Cdd:cd14876 77 IIVSGESGAGKTEATKQIMRYFAS-------AKSGNMDLR--IQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 254 ATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLD--MLLITNnpyDYAFISQGETTVASIDDAEELMA 331
Cdd:cd14876 148 SEGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSkyHLLGLK---EYKFLNPKCLDVPGIDDVADFEE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 332 TDNAFDVLGFTTEEKNSMYKLTGAIMHFGNMKFKLKQREEQ-----AEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKV 406
Cdd:cd14876 225 VLESLKSMGLTEEQIDTVFSIVSGVLLLGNVKITGKTEQGVddaaaISNESLEVFKEACSLLFLDPEALKRELTVKVTKA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 407 GNEYVTKGQNVQQVVYAKGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQ 486
Cdd:cd14876 305 GGQEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 487 QFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHlgKSSNFQKP 566
Cdd:cd14876 385 KNFIDIVFERESKLYKDEGIPTAELEYTSNAEVIDVLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSKL--KSNGKFKP 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 567 rnIKGKPEAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKKSSLKMLSSLFANyagfdTPIEKGKGKAKKGSSFQT 646
Cdd:cd14876 463 --AKVDSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEG-----VVVEKGKIAKGSLIGSQF 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 647 VSalhreNLNKLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILN 726
Cdd:cd14876 536 LK-----QLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFLD 610
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1387193866 727 PaAIPEGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 766
Cdd:cd14876 611 L-GIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVFLK 649
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
99-766 |
1.08e-120 |
|
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: 398.56 E-value: 1.08e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 99 PAVLYNLKERYASWMIYTYSGLFCVTINPYKWLP-VYNaevVAAYRGK--KRSEAPPHIFSISDNAYQYMLT-------D 168
Cdd:cd14895 1 PAFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIPgLYD---LHKYREEmpGWTALPPHVFSIAEGAYRSLRRrlhepgaS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 169 RENQSILITGESGAGKTVNTKRVIQYFAVIA---AIGDRSKKEQATGKgtleDQIIQANPALEAFGNAKTVRNDNSSRFG 245
Cdd:cd14895 78 KKNQTILVSGESGAGKTETTKFIMNYLAESSkhtTATSSSKRRRAISG----SELLSANPILESFGNARTLRNDNSSRFG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 246 KFIRIHFG-----ATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDML-LITNNPYDYAFISQGETT 319
Cdd:cd14895 154 KFVRMFFEgheldTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELqLELLSAQEFQYISGGQCY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 320 VAS--IDDAEELMATDNAFDVLGFTTEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGT------------------E 379
Cdd:cd14895 234 QRNdgVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEGEEDNGAasapcrlasaspssltvqQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 380 EADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQVVYAKGALAKAVYERMFNWMVTRINATLETKQPRQY---- 455
Cdd:cd14895 314 HLDIVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQFALNpnka 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 456 -------FIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLQACIDLIE-KP 527
Cdd:cd14895 394 ankdttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYE-DNSVCLEMLEqRP 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 528 MGIMSILEEECMFPKATDMTFKAKLFdNHLGKSSNFQKPRniKGKPEAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVD 607
Cdd:cd14895 473 SGIFSLLDEECVVPKGSDAGFARKLY-QRLQEHSNFSASR--TDQADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAELFS 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 608 LYKKSSLKMLSSLFANYAGFDTPIEKGKGKAKKGSSFQTVS----ALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGV 683
Cdd:cd14895 550 VLGKTSDAHLRELFEFFKASESAELSLGQPKLRRRSSVLSSvgigSQFKQQLASLLDVVQQTQTHYIRCIKPNDESASDQ 629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 684 IDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPegqfidSRKGAEKLLGSLDIDHNQykFGHTKV 763
Cdd:cd14895 630 FDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKNA------SDATASALIETLKVDHAE--LGKTRV 701
|
...
gi 1387193866 764 FFK 766
Cdd:cd14895 702 FLR 704
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
101-727 |
2.96e-111 |
|
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: 369.95 E-value: 2.96e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 101 VLYNLKERYASWMIYTYSGLFCVTINPYKWLP-VYNAEVVAAYRGKKRSEA-PPHIFSISDNAYQYMLTDRE--NQSILI 176
Cdd:cd14880 3 VLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQPQKlKPHIFTVGEQTYRNVKSLIEpvNQSIVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 177 TGESGAGKTVNTKRVIQYFAVIAAigDRSKKEQATGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 256
Cdd:cd14880 83 SGESGAGKTWTSRCLMKFYAVVAA--SPTSWESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 257 KLASADIETYLLEKSRVIFQLKAERDYHIFYQILsnkKPELLDMLLITNNP--YDYAFISQGETTVASiDDAEelmATDN 334
Cdd:cd14880 161 QMTGAAVQTYLLEKTRVACQAPSERNFHIFYQIC---KGASADERLQWHLPegAAFSWLPNPERNLEE-DCFE---VTRE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 335 AFDVLGFTTEEKNSMYKLTGAIMHFGNMKFKLKQREEQA---EPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNeyv 411
Cdd:cd14880 234 AMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPcqpMDDTKESVRTSALLLKLPEDHLLETLQIRTIRAGK--- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 412 tkgqnvQQVVYAK-----------GALAKAVYERMFNWMVTRINATLETKQPR-QYFIGVLDIAGFEIFDFNSFEQLCIN 479
Cdd:cd14880 311 ------QQQVFKKpcsraecdtrrDCLAKLIYARLFDWLVSVINSSICADTDSwTTFIGLLDVYGFESFPENSLEQLCIN 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 480 FTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKATDmtfkAKLFDNHLG 558
Cdd:cd14880 385 YANEKLQQHFVAHYLRAQQEEYAVEGLEWSFINY-QDNQTCLDLIEgSPISICSLINEECRLNRPSS----AAQLQTRIE 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 559 K--SSNFQKPRNiKGKPEAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKKSSLKMLSSLFANYAGFDTPIEkgkG 636
Cdd:cd14880 460 SalAGNPCLGHN-KLSREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEKTQEE---P 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 637 KAKKGSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYG 716
Cdd:cd14880 536 SGQSRAPVLTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQ 615
|
650
....*....|.
gi 1387193866 717 DFRQRYRILNP 727
Cdd:cd14880 616 NFVERYKLLRR 626
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
101-726 |
8.32e-108 |
|
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: 361.99 E-value: 8.32e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 101 VLYNLKERYASWMIYTYSGLFCVTINPYKWLP-VYNAEVVAAYRGKKR-SEAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14906 3 ILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIIISG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 179 ESGAGKTVNTKRVIQYFAVIAAIGDRSKKEQATGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGAT-GK 257
Cdd:cd14906 83 ESGSGKTEASKTILQYLINTSSSNQQQNNNNNNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSdGK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 258 LASADIETYLLEKSRVIFQL-KAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASI------------- 323
Cdd:cd14906 163 IDGASIETYLLEKSRISHRPdNINLSYHIFYYLVYGASKDERSKWGLNNDPSKYRYLDARDDVISSFksqssnknsnhnn 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 324 --DDAEELMATDNAFDVLGFTTEEKNSMYKLTGAIMHFGNMKFKLKQ---REEQAEPDGTEEADKSAYLMGLNSADLLKG 398
Cdd:cd14906 243 ktESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSdfsKYAYQKDKVTASLESVSKLLGYIESVFKQA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 399 LCHPRVKVGNE--YVTKGQNVQQVVYAKGALAKAVYERMFNWMVTRINAT-LETKQPRQ----------YFIGVLDIAGF 465
Cdd:cd14906 323 LLNRNLKAGGRgsVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKfNQNTQSNDlaggsnkknnLFIGVLDIFGF 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 466 EIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKAT 544
Cdd:cd14906 403 ENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEkKSDGILSLLDDECIMPKGS 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 545 DMTFKAKLFDNHLGKSSNFQKPRNiKGKpeahFSLIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKKSSLKMLSSLfany 624
Cdd:cd14906 482 EQSLLEKYNKQYHNTNQYYQRTLA-KGT----LGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSL---- 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 625 agFDTPIEKGKGKAKKGSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRI 704
Cdd:cd14906 553 --FQQQITSTTNTTKKQTQSNTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLNTIKV 630
|
650 660
....*....|....*....|..
gi 1387193866 705 CRKGFPNRILYGDFRQRYRILN 726
Cdd:cd14906 631 RKMGYSYRRDFNQFFSRYKCIV 652
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
100-723 |
2.00e-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: 358.25 E-value: 2.00e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 100 AVLYNLKERYASWMIYTYSGLFCVTINPYKWLP-VYNAEVVAAYR-------GKKRSEA---PPHIFSISDNAYQYMLTD 168
Cdd:cd14899 2 SILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYAydhnsqfGDRVTSTdprEPHLFAVARAAYIDIVQN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 169 RENQSILITGESGAGKTVNTKRVIQYFAV-------IAAIGDRSKKEQATGKGTLEDQIIQANPALEAFGNAKTVRNDNS 241
Cdd:cd14899 82 GRSQSILISGESGAGKTEATKIIMTYFAVhcgtgnnNLTNSESISPPASPSRTTIEEQVLQSNPILEAFGNARTVRNDNS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 242 SRFGKFIRIHF-GATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNK----KPELLDMLLITNNPYDYAFISQG 316
Cdd:cd14899 162 SRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSADnncvSKEQKQVLALSGGPQSFRLLNQS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 317 ETTVA--SIDDAEELMATDNAFDVLGFTTEEKNSMYKLTGAIMHFGNMKFKL--KQREEQAEPDGTEEA----------D 382
Cdd:cd14899 242 LCSKRrdGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQipHKGDDTVFADEARVMssttgafdhfT 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 383 KSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQVVYAKGALAKAVYERMFNWMVTRINATLETKQPRQY------- 455
Cdd:cd14899 322 KAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQASAPWgadesdv 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 456 --------FIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDlQACIDLIE-K 526
Cdd:cd14899 402 ddeedatdFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNN-RACLELFEhR 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 527 PMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSSNFQKPRNIKGKPEAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVV 606
Cdd:cd14899 481 PIGIFSLTDQECVFPQGTDRALVAKYYLEFEKKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFCESAA 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 607 DLYKKSSLKMLSSLFANYAGFDTPIEKGKGKAKKGSSFQTVSAL--------HRENLNKLMTNLRSTHPHFVRCIIPNET 678
Cdd:cd14899 561 QLLAGSSNPLIQALAAGSNDEDANGDSELDGFGGRTRRRAKSAIaavsvgtqFKIQLNELLSTVRATTPRYVRCIKPNDS 640
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1387193866 679 KSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYR 723
Cdd:cd14899 641 HVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRYR 685
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
101-766 |
4.35e-106 |
|
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain binding domain, and a C-terminal GPA/Q-rich domain. There is little known about the function of this myosin class. Two of the earliest members identified in this class are green alga Acetabularia cliftonii, Aclmyo1 and Aclmyo2. They are striking with their short tail of Aclmyo1 of 18 residues and the maximum of 7 IQ motifs in Aclmyo2. It is thought that these myosins are involved in organelle transport and tip growth. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276842 [Multi-domain] Cd Length: 664 Bit Score: 355.27 E-value: 4.35e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 101 VLYNLKERYASWMI-YTYSGLFCVTINPYKWLPvYNAEVvaaYRGKKRSEA-----PPHIFSISDNAY-QYMLTDRENQS 173
Cdd:cd14875 3 LLHCIKERFEKLHQqYSLMGEMVLSVNPFRLMP-FNSEE---ERKKYLALPdprllPPHIWQVAHKAFnAIFVQGLGNQS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 174 ILITGESGAGKTVNTKRVIQYFAVIAAIGDRSKKEQatgkgTLEDQIIQ----ANPALEAFGNAKTVRNDNSSRFGKFIR 249
Cdd:cd14875 79 VVISGESGSGKTENAKMLIAYLGQLSYMHSSNTSQR-----SIADKIDEnlkwSNPVMESFGNARTVRNDNSSRFGKYIK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 250 IHF-GATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTV------AS 322
Cdd:cd14875 154 LYFdPTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELGGLKTAQDYKCLNGGNTFVrrgvdgKT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 323 IDDAEELMATDNAFDVLGFTTEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEAdKSAYLMGLNSADLLKGLChp 402
Cdd:cd14875 234 LDDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQNDKAQIADETPFL-TACRLLQLDPAKLRECFL-- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 403 rVKVGNEYVTKGQNVQQVVYAKGALAKAVYERMFNWMVTRINATLetkQPRQ-----YFIGVLDIAGFEIFDFNSFEQLC 477
Cdd:cd14875 311 -VKSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASI---TPQGdcsgcKYIGLLDIFGFENFTRNSFEQLC 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 478 INFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGmDLQACIDLIE-KPMGIMSILEEECMFPKATDMTFKAKLFDNH 556
Cdd:cd14875 387 INYANESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFDqKRTGIFSMLDEECNFKGGTTERFTTNLWDQW 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 557 LGKSSNFQKPrniKGKPEAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKKSSLKMLSSLFANYAGFDtpiekgkg 636
Cdd:cd14875 466 ANKSPYFVLP---KSTIPNQFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTEKGLA-------- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 637 kakkgSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYG 716
Cdd:cd14875 535 -----RRKQTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIE 609
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 1387193866 717 DF-RQRYRILNPAAIPEGQFIDSRKGAEKLLGSLDIDHN----QYKFGHTKVFFK 766
Cdd:cd14875 610 QFcRYFYLIMPRSTASLFKQEKYSEAAKDFLAYYQRLYGwakpNYAVGKTKVFLR 664
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
101-766 |
7.18e-104 |
|
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: 349.69 E-value: 7.18e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 101 VLYNLKERYASWMIYTYSGLFCVTINPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGES 180
Cdd:cd01386 3 VLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLGRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 181 GAGKTVNTKRVIQYFAVIA-AIGDRSKKEQatgkgtledqiIQA-NPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 258
Cdd:cd01386 83 GSGKTTNCRHILEYLVTAAgSVGGVLSVEK-----------LNAaLTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 259 ASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFisqGETTVASIDD----AEELMATDN 334
Cdd:cd01386 152 ASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAESNSF---GIVPLQKPEDkqkaAAAFSKLQA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 335 AFDVLGFTTEEKNSMYKLTGAIMHFGN---MKFKLKQREEQAEPdgtEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYV 411
Cdd:cd01386 229 AMKTLGISEEEQRAIWSILAAIYHLGAagaTKAASAGRKQFARP---EWAQRAAYLLGCTLEELSSAIFKHHLSGGPQQS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 412 TK------------GQNVQQVVYAKGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFN------SF 473
Cdd:cd01386 306 TTssgqesparsssGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPAHSgsqrgaTF 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 474 EQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEK---------------PMGIMSILEEEC 538
Cdd:cd01386 386 EDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQapqqalvrsdlrdedRRGLLWLLDEEA 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 539 MFPKATDMTFKAKLFdNHLGKS--SNFQKPRNIKGKPEaHFSLIHYAGT--VDYNIIGWLQKNK-DPLNETVVDLYKKSS 613
Cdd:cd01386 466 LYPGSSDDTFLERLF-SHYGDKegGKGHSLLRRSEGPL-QFVLGHLLGTnpVEYDVSGWLKAAKeNPSAQNATQLLQESQ 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 614 LKM----LSSLFANYagfdtpiekgkgkakkgsSFQtvsalhrenLNKLMTNLRSTHPHFVRCIIPN------------E 677
Cdd:cd01386 544 KETaavkRKSPCLQI------------------KFQ---------VDALIDTLRRTGLHFVHCLLPQhnagkderstssP 596
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 678 TKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPA----AIPEGQFIDSRKGAEKLLGSLDIDH 753
Cdd:cd01386 597 AAGDELLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPltkkLGLNSEVADERKAVEELLEELDLEK 676
|
730
....*....|...
gi 1387193866 754 NQYKFGHTKVFFK 766
Cdd:cd01386 677 SSYRIGLSQVFFR 689
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
105-766 |
4.50e-103 |
|
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: 346.10 E-value: 4.50e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 105 LKERYASWMIYTYSGLFCVTINPYKWLP-VYNAEVVAAYRGKKRS-----EAPPHIFSISDNAYQYMLTDRENQSILITG 178
Cdd:cd14886 7 LRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQSCIVSG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 179 ESGAGKTVNTKRVIQYFAViaaigdrskkEQATGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 258
Cdd:cd14886 87 ESGAGKTETAKQLMNFFAY----------GHSTSSTDVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 259 ASADIETYLLEKSRVIFQLKAERDYHIFYQI---LSNKKPELLDMLLITNnpydYAFISQGET-TVASIDDAEELMATDN 334
Cdd:cd14886 157 KGGKITSYMLELSRIEFQSTNERNYHIFYQCikgLSPEEKKSLGFKSLES----YNFLNASKCyDAPGIDDQKEFAPVRS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 335 AFDVLgFTTEEKNSMYKLTGAIMHFGNMKFKLKQR---EEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYV 411
Cdd:cd14886 233 QLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgvINAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNETI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 412 TKGQNVQQVVYAKGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNH 491
Cdd:cd14886 312 ISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFIN 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 492 HMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLIEKP-MGIMSILEEECMFPKATDMTFKAKLfDNHLgKSSNFqkprnIK 570
Cdd:cd14886 392 QVFKSEIQEYEIEGIDHSMITF-TDNSNVLAVFDKPnLSIFSFLEEQCLIQTGSSEKFTSSC-KSKI-KNNSF-----IP 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 571 GKPEA-HFSLIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKKSSLKMLSSLFAnyagfDTPIEKGKGKAkkgssfQTVSA 649
Cdd:cd14886 464 GKGSQcNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFS-----DIPNEDGNMKG------KFLGS 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 650 LHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRIL---N 726
Cdd:cd14886 533 TFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILishN 612
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1387193866 727 PAAIPEGQfiDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 766
Cdd:cd14886 613 SSSQNAGE--DLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
100-741 |
4.60e-98 |
|
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: 329.17 E-value: 4.60e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 100 AVLYNLKERYASWMIYTYSGLFCVTINPYKwlPVYNAEVVAAYRgKKRSEAPPHIFSISDNAYQYMLTdRENQSILITGE 179
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYE--TIYGAGAMKAYL-KNYSHVEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 180 SGAGKTVNTKRVIQYFAviaaigdrskkEQATGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFgaTGKLA 259
Cdd:cd14898 78 SGSGKTENAKLVIKYLV-----------ERTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKF--DGKIT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 260 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKpelldmLLITNNPYDYAFISQGETTVasIDDAEELMATDNAFDVL 339
Cdd:cd14898 145 GAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKR------LNIKNDFIDTSSTAGNKESI--VQLSEKYKMTCSAMKSL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 340 GFTTEEknSMYKLTGAIMHFGNMKFklkQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQ 419
Cdd:cd14898 217 GIANFK--SIEDCLLGILYLGSIQF---VNDGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQ 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 420 VVYAKGALAKAVYERMFNWMVTRINATLETKQPRQyfIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQE 499
Cdd:cd14898 292 ARTIRNSMARLLYSNVFNYITASINNCLEGSGERS--ISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 500 EYKKEGIEWEFIDFgMDLQACIDLIEKPMGIMSILEEECMFPKAT--DMTFKAKLFDNHlgkssnfqkprNIKGKPEAHF 577
Cdd:cd14898 370 MYKEEGIEWPDVEF-FDNNQCIRDFEKPCGLMDLISEESFNAWGNvkNLLVKIKKYLNG-----------FINTKARDKI 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 578 SLIHYAGTVDYNIIGWLQKNKDplnetvvdlykKSSLKMLSSLFANYAGfdtpiekgkgkakkgsSFQTVSALHRENLNK 657
Cdd:cd14898 438 KVSHYAGDVEYDLRDFLDKNRE-----------KGQLLIFKNLLINDEG----------------SKEDLVKYFKDSMNK 490
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 658 LMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIpegQFID 737
Cdd:cd14898 491 LLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGITLF---EVVD 567
|
....
gi 1387193866 738 SRKG 741
Cdd:cd14898 568 YRKG 571
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
100-725 |
4.87e-97 |
|
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: 328.70 E-value: 4.87e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 100 AVLYNLKERYASWMIYTYSGLFCVTINPYKWLPVYNAEVVAAYR---GKKRSEAPPHIFSISDNAYQYMLTDRENQSILI 176
Cdd:cd14878 2 SLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 177 TGESGAGKTVNTKRVIQYFAViaaigdRSkkeqATGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 256
Cdd:cd14878 82 SGERGSGKTEASKQIMKHLTC------RA----SSSRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFCERK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 257 K-LASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLItNNPYDYAFISQGE----TTVASIDDAEELMA 331
Cdd:cd14878 152 KhLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHL-NNLCAHRYLNQTMredvSTAERSLNREKLAV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 332 TDNAFDVLGFTTEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYV 411
Cdd:cd14878 231 LKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 412 TKGQNVQQVVYAKGALAKAVYERMFNWMVTRINATL----ETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQ 487
Cdd:cd14878 311 IRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqdEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHH 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 488 FFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACID-LIEKPMGIMSILEEECMFPKATDMTFKAKLfdNHLGKSSNFQ-- 564
Cdd:cd14878 391 YINEVLFLQEQTECVQEGVTMETAYSPGNQTGVLDfFFQKPSGFLSLLDEESQMIWSVEPNLPKKL--QSLLESSNTNav 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 565 ----KPRNIKGKPEAH---FSLIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKKSSLKMLSSLFanyagfdtpiekgkgk 637
Cdd:cd14878 469 yspmKDGNGNVALKDQgtaFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLF---------------- 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 638 akkGSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGD 717
Cdd:cd14878 533 ---QSKLVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSD 609
|
....*...
gi 1387193866 718 FRQRYRIL 725
Cdd:cd14878 610 FLSRYKPL 617
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
99-766 |
4.02e-91 |
|
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: 313.51 E-value: 4.02e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 99 PAVLYNLKERYAS--------WMIYTYSGLFCVTINPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRE 170
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 171 NQSILITGESGAGKTVNTKRVIQYfavIAAIGDRSKKEQATGkgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRI 250
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTY---LAAVSDRRHGADSQG---LEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 251 HFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKK-PELLDMLLITNNPYDYafisqgettvasiddaeEL 329
Cdd:cd14887 155 HFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVaAATQKSSAGEGDPEST-----------------DL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 330 MATDNAFDVLGFTTEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPD-------GTEE--ADKS--AYLMGLNS------ 392
Cdd:cd14887 218 RRITAAMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRkltsvsvGCEEtaADRShsSEVKCLSSglkvte 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 393 ------ADLLKGLCHPRVKVGNEYV------------TKGQNVQQVVYAKGALAKAVYERMFNWMVTRINATLETKQPRQ 454
Cdd:cd14887 298 asrkhlKTVARLLGLPPGVEGEEMLrlalvsrsvretRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKPS 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 455 Y--------------FIGVLDIAGFEIF---DFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFI--DFGM 515
Cdd:cd14887 378 EsdsdedtpsttgtqTIGILDLFGFEDLrnhSKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDcsAFPF 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 516 DLQACIDLIEKP------------------------MGIMSILEEE-CMFPKATDMTFKAKLFDNHLGKS-SNFQKPRNI 569
Cdd:cd14887 458 SFPLASTLTSSPsstspfsptpsfrsssafatspslPSSLSSLSSSlSSSPPVWEGRDNSDLFYEKLNKNiINSAKYKNI 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 570 K---GKPEAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVDLYkksslkMLSSLFANYAGFDtpieKGKGKAKKGSSFQT 646
Cdd:cd14887 538 TpalSRENLEFTVSHFACDVTYDARDFCRANREATSDELERLF------LACSTYTRLVGSK----KNSGVRAISSRRST 607
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 647 VSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILN 726
Cdd:cd14887 608 LSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYETKL 687
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 1387193866 727 PAAIPEgqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 766
Cdd:cd14887 688 PMALRE--ALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
101-766 |
3.09e-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: 296.54 E-value: 3.09e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 101 VLYNLKERYASWMIYTYSGLFCVTINPYKWLPVYNAEvvaaYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGES 180
Cdd:cd14937 3 VLNMLALRYKKNYIYTIAEPMLISINPYQVIDVDINE----YKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 181 GAGKTVNTKRVIQYFavIAAIgdrskKEQATGKGTLEDqiiqANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLAS 260
Cdd:cd14937 79 GSGKTEASKLVIKYY--LSGV-----KEDNEISNTLWD----SNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 261 ADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPyDYAFISQGETTVASIDDAEELMATDNAFDVLG 340
Cdd:cd14937 148 SSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSEN-EYKYIVNKNVVIPEIDDAKDFGNLMISFDKMN 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 341 FTTEEKNSMYKLTGAIMhFGNMKFKL-----KQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 415
Cdd:cd14937 227 MHDMKDDLFLTLSGLLL-LGNVEYQEiekggKTNCSELDKNNLELVNEISNLLGINYENLKDCLVFTEKTIANQKIEIPL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 416 NVQQVVYAKGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 495
Cdd:cd14937 306 SVEESVSICKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 496 LEQEEYKKEGIEWEFIDFGMDlQACIDLIEKPMGIMSILEEECMFPKATDMTfkakLFDNHLGKSSNFQKPRNIKGKPEA 575
Cdd:cd14937 386 KETELYKAEDILIESVKYTTN-ESIIDLLRGKTSIISILEDSCLGPVKNDES----IVSVYTNKFSKHEKYASTKKDINK 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 576 HFSLIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKKSSLKMLSSLFANYAGFDTpiekgkgkakkGSSFQTVSALHRENL 655
Cdd:cd14937 461 NFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVSES-----------LGRKNLITFKYLKNL 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 656 NKLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRIcRKGFPNRILYGDFRQRYRILNPAAIPEGQF 735
Cdd:cd14937 530 NNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEYLDYSTSKDSSL 608
|
650 660 670
....*....|....*....|....*....|.
gi 1387193866 736 IDSRKGAEKLLGSLDIDhnQYKFGHTKVFFK 766
Cdd:cd14937 609 TDKEKVSMILQNTVDPD--LYKVGKTMVFLK 637
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
105-765 |
8.65e-85 |
|
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: 292.53 E-value: 8.65e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 105 LKERYASWMIYTY---SGLfcVTINPYKWLPVYNAEVVAAYR-------GKKRSEAPPHIFSISDNAYQYMLTDRENQSI 174
Cdd:cd14879 10 LASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRMRRRSEDQAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 175 LITGESGAGKTVNTKRVIQyfaviaAIGDRSKkeqATGKGT-LEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFG 253
Cdd:cd14879 88 VFLGETGSGKSESRRLLLR------QLLRLSS---HSKKGTkLSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQFN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 254 ATGKLASADIETYLLEKSRVIfQLKA-ERDYHIFYQILSNKKPELLDMLLItNNPYDYAFI--SQGETTVAS--IDDAEE 328
Cdd:cd14879 159 ERGRLIGAKVLDYRLERSRVA-SVPTgERNFHVFYYLLAGASPEERQHLGL-DDPSDYALLasYGCHPLPLGpgSDDAEG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 329 LMATDNAFDVLGFTTEEKNSMYKLTGAIMHFGNMKFklkqreeQAEPDGTEEA---------DKSAYLMGLNSADLLKGL 399
Cdd:cd14879 237 FQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEF-------TYDHEGGEESavvkntdvlDIVAAFLGVSPEDLETSL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 400 CHPRVKVGNEYVTkgqnvqqvVY--AKGA------LAKAVYERMFNWMVTRINATL-ETKQPRQYFIGVLDIAGFEIFD- 469
Cdd:cd14879 310 TYKTKLVRKELCT--------VFldPEGAaaqrdeLARTLYSLLFAWVVETINQKLcAPEDDFATFISLLDFPGFQNRSs 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 470 --FNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLI-EKPMGIMSILEEEC-MFPKATD 545
Cdd:cd14879 382 tgGNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLrGKPGGLLGILDDQTrRMPKKTD 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 546 MTFKAKLfDNHLGKSSNFQKPRNIKGKPEAH-FSLIHYAGTVDYNIIGWLQKNKDPLNETVVdlykksslkmlsSLFANY 624
Cdd:cd14879 461 EQMLEAL-RKRFGNHSSFIAVGNFATRSGSAsFTVNHYAGEVTYSVEGFLERNGDVLSPDFV------------NLLRGA 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 625 AGFdtpiekgkgkakkgssfqtvsalhRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRI 704
Cdd:cd14879 528 TQL------------------------NAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELAAR 583
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387193866 705 CRKGFPNRILYGDFRQRYrilnpaaIPEGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFF 765
Cdd:cd14879 584 LRVEYVVSLEHAEFCERY-------KSTLRGSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
99-714 |
2.54e-76 |
|
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: 269.08 E-value: 2.54e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 99 PAVLYNLKERYASWMIYTYSGLFCVTINPYKWLP-VYNAEVVAAYRGKKRSEA-------PPHIFSISDNAYQYMLTDRE 170
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSAasaapfpKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 171 NQSILITGESGAGKTVNTKRVIQYFAVIAaiGDRSKKEqatgkgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRI 250
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYIQ--TDSQMTE-------RIDKLIYINNILESMSNATTIKNNNSSRCGRINLL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 251 HF---------GATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGE---- 317
Cdd:cd14884 152 IFeeventqknMFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLARRNLVRNCGVYGLLNPDEshqk 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 318 --------TTVASIDDAEELMATD--------NAFDVLGFTTEEKNSMYKLTGAIMHFGNMKFKLkqreeqaepdgteea 381
Cdd:cd14884 232 rsvkgtlrLGSDSLDPSEEEKAKDeknfvallHGLHYIKYDERQINEFFDIIAGILHLGNRAYKA--------------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 382 dkSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQVVYAKGALAKAVYERMFNWMVTRINAT----------LETKQ 451
Cdd:cd14884 297 --AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNvlkckekdesDNEDI 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 452 PR--QYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEW--EFIDFGMDLQACIDLIEKP 527
Cdd:cd14884 375 YSinEAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICcsDVAPSYSDTLIFIAKIFRR 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 528 MGIMSILEEECMfpKATDMTFKAKLFD-----------------NHLGKSSNfqKPRNIKgkpEAHFSLIHYAGTVDYNI 590
Cdd:cd14884 455 LDDITKLKNQGQ--KKTDDHFFRYLLNnerqqqlegkvsygfvlNHDADGTA--KKQNIK---KNIFFIRHYAGLVTYRI 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 591 IGWLQKNKDPLNETVVDLYKKSSLKMLSSLFANyagfdtpiekgkgkaKKGSSFQTVSALHRENLNKLMTNLRSTHPHFV 670
Cdd:cd14884 528 NNWIDKNSDKIETSIETLISCSSNRFLREANNG---------------GNKGNFLSVSKKYIKELDNLFTQLQSTDMYYI 592
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1387193866 671 RCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRIL 714
Cdd:cd14884 593 RCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIP 636
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
100-734 |
3.74e-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: 257.88 E-value: 3.74e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 100 AVLYNLKERYASWMIYTYSGLFCVTINPYKWLPVYNAEVVAAYrgkkrseappHIFSISDNAYQYMLTDREN-QSILITG 178
Cdd:cd14874 2 GIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFGG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 179 ESGAGKTVNTKRVIQYFAviaaigdRSKKEQATGKGTLEDQIIqanpaLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 258
Cdd:cd14874 72 ESGSGKSYNAFQVFKYLT-------SQPKSKVTTKHSSAIESV-----FKSFGCAKTLKNDEATRFGCSIDLLYKRNVLT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 259 ASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNpYDYAFISQGETTVASIDDAEELMATDNAFDV 338
Cdd:cd14874 140 GLNLKYTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGL-QKFFYINQGNSTENIQSDVNHFKHLEDALHV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 339 LGFTTEEKNSMYKLTGAIMHFGNMKFKLKQ----REEQAEPDGTEEADKSAYLMGLNSADLLKGLChPRVKVGNEYvtkg 414
Cdd:cd14874 219 LGFSDDHCISIYKIISTILHIGNIYFRTKRnpnvEQDVVEIGNMSEVKWVAFLLEVDFDQLVNFLL-PKSEDGTTI---- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 415 qNVQQVVYAKGALAKAVYERMFNWMVTRINatLETKQPRQY-FIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHM 493
Cdd:cd14874 294 -DLNAALDNRDSFAMLIYEELFKWVLNRIG--LHLKCPLHTgVISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHS 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 494 FVLEQEEYKKEGIEwefIDFGMdlQACID-------LIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSSnFQKP 566
Cdd:cd14874 371 FHDQLVDYAKDGIS---VDYKV--PNSIEngktvelLFKKPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSS-YGKA 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 567 RNikgKPEAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKKSSLKMLSSLFANYaGFDTPIEKGKGKAKKGSSFQT 646
Cdd:cd14874 445 RN---KERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESY-SSNTSDMIVSQAQFILRGAQE 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 647 VSalhrENLNKlmtnlrsTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILN 726
Cdd:cd14874 521 IA----DKING-------SHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCLL 589
|
....*...
gi 1387193866 727 PAAIPEGQ 734
Cdd:cd14874 590 PGDIAMCQ 597
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
100-746 |
1.57e-72 |
|
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: 256.19 E-value: 1.57e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 100 AVLYNLKERYASWMIYTYSGLFCVTINPYKWLPvyNAEVVAAYRGKKRSeapPHIFSISDNAYQYMLTDRENQSILITGE 179
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPYRDVG--NPLTLTSTRSSPLA---PQLLKVVQEAVRQQSETGYPQAIILSGT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 180 SGAGKTVNTKRVI-QYFAViaaigdrskkeqaTGKGTLED---QIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFgAT 255
Cdd:cd14881 77 SGSGKTYASMLLLrQLFDV-------------AGGGPETDafkHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQV-TD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 256 GKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITN-NPYDYAFISQGETTVASIDDAEELMATDN 334
Cdd:cd14881 143 GALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGySPANLRYLSHGDTRQNEAEDAARFQAWKA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 335 AFDVLG--FTteeknSMYKLTGAIMHFGNMKFkLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGL---CHprvkvgne 409
Cdd:cd14881 223 CLGILGipFL-----DVVRVLAAVLLLGNVQF-IDGGGLEVDVKGETELKSVAALLGVSGAALFRGLttrTH-------- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 410 yVTKGQNVQQVVYA------KGALAKAVYERMFNWMVTRIN------ATLETKQpRQYFIGVLDIAGFEIFDFNSFEQLC 477
Cdd:cd14881 289 -NARGQLVKSVCDAnmsnmtRDALAKALYCRTVATIVRRANslkrlgSTLGTHA-TDGFIGILDMFGFEDPKPSQLEHLC 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 478 INFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEF-IDFgMDLQACIDLIEK-PMGIMSILEEECMfPKATDMTFKAKLFDN 555
Cdd:cd14881 367 INLCAETMQHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCIDLISSlRTGLLSMLDVECS-PRGTAESYVAKIKVQ 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 556 HLGkSSNFQKPRNIKGKpeaHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKKSSLKMlsslfanyaGFDTpiekgk 635
Cdd:cd14881 445 HRQ-NPRLFEAKPQDDR---MFGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQNCNF---------GFAT------ 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 636 gkakKGSSFQTvsalhreNLNKLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILY 715
Cdd:cd14881 506 ----HTQDFHT-------RLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRF 574
|
650 660 670
....*....|....*....|....*....|.
gi 1387193866 716 GDFRQRYRILNPAAiPEGQFIDSRKGAEKLL 746
Cdd:cd14881 575 KAFNARYRLLAPFR-LLRRVEEKALEDCALI 604
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
105-718 |
3.97e-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: 235.76 E-value: 3.97e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 105 LKERYASWMIYTYSGLFCVTINPYKWLP-VYNAEVVAAYrgKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESGAG 183
Cdd:cd14905 7 IQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNY--NQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGGESGSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 184 KTVNTKRVIQYfaVIAAIGDRSKkeqatgkgTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADI 263
Cdd:cd14905 85 KSENTKIIIQY--LLTTDLSRSK--------YLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 264 ETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITN-NPYDYafISQGET-TVASIDDAEELMATDNAFDVLGF 341
Cdd:cd14905 155 YSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDiNSYHY--LNQGGSiSVESIDDNRVFDRLKMSFVFFDF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 342 TTEEKNSMYKLTGAIMHFGNMKFKLKQREeqaepdgTEEADKSaylmglnsadLLKGLCH----PRVKVGNEYVT-KGQN 416
Cdd:cd14905 233 PSEKIDLIFKTLSFIIILGNVTFFQKNGK-------TEVKDRT----------LIESLSHnitfDSTKLENILISdRSMP 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 417 VQQVVYAKGALAKAVYERMFNWMVTRINATLetkQPRQY--FIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMF 494
Cdd:cd14905 296 VNEAVENRDSLARSLYSALFHWIIDFLNSKL---KPTQYshTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 495 VLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKpmgIMSILEEECMFPKATDMTFKAKLfdnhlgksSNFQKPRNIKGKPE 574
Cdd:cd14905 373 KQEQREYQTERIPWMTPISFKDNEESVEMMEK---IINLLDQESKNINSSDQIFLEKL--------QNFLSRHHLFGKKP 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 575 AHFSLIHYAGTVDYNIIGWLQKNKDP-------------------------LNETVVDL---------YKKSSLKMLSSL 620
Cdd:cd14905 442 NKFGIEHYFGQFYYDVRGFIIKNRDEilqrtnvlhknsitkylfsrdgvfnINATVAELnqmfdakntAKKSPLSIVKVL 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 621 FA--------------NYAGFDTPIEKGKGKAKKGSSFQTVSAlhrenLNKLMTNlRSTHPHFVRCIIPNETKSPGVIDN 686
Cdd:cd14905 522 LScgsnnpnnvnnpnnNSGGGGGGGNSGGGSGSGGSTYTTYSS-----TNKAINN-SNCDFHFIRCIKPNSKKTHLTFDV 595
|
650 660 670
....*....|....*....|....*....|....*.
gi 1387193866 687 PLVMHQLRCNGVLEGIRICRKGFP----NRILYGDF 718
Cdd:cd14905 596 KSVNEQIKSLCLLETTRIQRFGYTihynNKIFFDRF 631
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
101-725 |
6.26e-64 |
|
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: 231.17 E-value: 6.26e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 101 VLYNLKERYASWMIYTYSGLFCVTINPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGES 180
Cdd:cd14882 3 ILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 181 GAGKTVNTKRVIQYFAViaaIGDrskkeqatGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLAS 260
Cdd:cd14882 83 YSGKTTNARLLIKHLCY---LGD--------GNRGATGRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 261 ADIETYLLEKSRVIFQLKAERDYHIFYQILS--NKKPELLDMLLITNNPYDYAFISQG-------------ETTVASIDD 325
Cdd:cd14882 152 AIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDfiEAQNRLKEYNLKAGRNYRYLRIPPEvppsklkyrrddpEGNVERYKE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 326 AEELmatdnaFDVLGFTTEEKNSMYKLTGAIMHFGNMKFklKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVK 405
Cdd:cd14882 232 FEEI------LKDLDFNEEQLETVRKVLAAILNLGEIRF--RQNGGYAELENTEIASRVAELLRLDEKKFMWALTNYCLI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 406 VGNEYVTKGQNVQQVVYAKGALAKAVYERMFNWMVTRINATLETkqPR-----QYFIGVLDIAGFEIFDFNSFEQLCINF 480
Cdd:cd14882 304 KGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSF--PRavfgdKYSISIHDMFGFECFHRNRLEQLMVNT 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 481 TNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEecmfpKATDMTFKAKLFDNHLGKS 560
Cdd:cd14882 382 LNEQMQYHYNQRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPDGLFYIIDD-----ASRSCQDQNYIMDRIKEKH 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 561 SNFQKPRNikgkpeAH-FSLIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKKSSLKMLSSLFANyagfdtpiekgkgkaK 639
Cdd:cd14882 457 SQFVKKHS------AHeFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN---------------S 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 640 KGSSFQTVSALHR----ENLNKLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILY 715
Cdd:cd14882 516 QVRNMRTLAATFRatslELLKMLSIGANSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPF 595
|
650
....*....|
gi 1387193866 716 GDFRQRYRIL 725
Cdd:cd14882 596 QEFLRRYQFL 605
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
102-765 |
3.35e-62 |
|
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but possess tandem MyTH4 and FERM domains. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276858 Cd Length: 741 Bit Score: 228.32 E-value: 3.35e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 102 LYNLKERYASWMIYTYSGLFCVTINPYKWLPVYNAEVVAAYRGKKR----------SEAPPHIFSISDNAYQYMLTDREN 171
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 172 QSILITGESGAGKTVNTKRVIQYfavIAAIGD----RSKKEQATGKG-TLEDQIIQANPALEAFGNAKTVRNDNSSRFGK 246
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQY---LCEIGDetepRPDSEGASGVLhPIGQQILHAFTILEAFGNAATRQNRNSSRFAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 247 FIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKK--PELLDMLLITNNPYDYAFISQG--ETTVAS 322
Cdd:cd14893 161 MISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQhdPTLRDSLEMNKCVNEFVMLKQAdpLATNFA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 323 ID--DAEELMATdnaFDVLGFTTEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLN-------SA 393
Cdd:cd14893 241 LDarDYRDLMSS---FSALRIRKNQRVEIVRIVAALLHLGNVDFVPDPEGGKSVGGANSTTVSDAQSCALKdpaqillAA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 394 DLLKglCHPRV------------KVGNEYVT--KGQNVQQVVYAKGALAKAVYERMFNWMVTRINATLETKQPR------ 453
Cdd:cd14893 318 KLLE--VEPVVldnyfrtrqffsKDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILGGIFDRyeksni 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 454 ---QYFIGVLDIAGFEIFD--FNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWE-------FIDFGMDLQACI 521
Cdd:cd14893 396 vinSQGVHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYVQNTLAINFSFLEDESQQVEnrltvnsNVDITSEQEKCL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 522 DLIE-KPMGIMSILEEECMFPKATDMTFKAKLFDNH-----LGKSSNFQKPRNIKGKPEAHFSLI----HYAGTVDYNII 591
Cdd:cd14893 476 QLFEdKPFGIFDLLTENCKVRLPNDEDFVNKLFSGNeavggLSRPNMGADTTNEYLAPSKDWRLLfivqHHCGKVTYNGK 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 592 GWLQKNKDPLNETVVDLYKKSSLKMLSSLFANY---AGFDTPIEKGKGKAKKGSSFQTVSALHRENLN------------ 656
Cdd:cd14893 556 GLSSKNMLSISSTCAAIMQSSKNAVLHAVGAAQmaaASSEKAAKQTEERGSTSSKFRKSASSARESKNitdsaatdvynq 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 657 --KLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRilnpaaipegQ 734
Cdd:cd14893 636 adALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYK----------N 705
|
730 740 750
....*....|....*....|....*....|....*
gi 1387193866 735 FIDSRKGAEKLLGSLD----IDHNQYKFGHTKVFF 765
Cdd:cd14893 706 VCGHRGTLESLLRSLSaigvLEEEKFVVGKTKVYL 740
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
121-250 |
4.79e-61 |
|
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: 206.81 E-value: 4.79e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 121 FCVTINPYKWLPVYNAEVV-AAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESGAGKTVNTKRVIQYFAVIA 199
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIiVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1387193866 200 AIGDRSKKEQAT-----GKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRI 250
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 ... |
99-764 |
5.76e-48 |
|
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: 184.65 E-value: 5.76e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 99 PAVLYNLKERYASWMIYTYSGLFCVTINPYKWLPVYNAEVVAAYRGKKRSE-APPHIFSISDNAYQYMLTDRENQSILIT 177
Cdd:cd14938 1 PSVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKCIDCIEdLSLNEYHVVHNALKNLNELKRNQSIIIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 178 GESGAGKTVNTKRVIQYFAViAAIGDRSK--------------KEQATGKGTLEDQIIQANPALEAFGNAKTVRNDNSSR 243
Cdd:cd14938 81 GESGSGKSEIAKNIINFIAY-QVKGSRRLptnlndqeednihnEENTDYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 244 FGKFIRIHFgATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYdYAFISQGETTVASI 323
Cdd:cd14938 160 FSKFCTIHI-ENEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIEN-YSMLNNEKGFEKFS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 324 DDAEELMATDNAFDVLGFTTEEKNSMYKLTGAIMHFGN-------------MKFKLKQRE----------EQAEPDGTEE 380
Cdd:cd14938 238 DYSGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNteivkafrkksllMGKNQCGQNinyetilselENSEDIGLDE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 381 ADKSAYL----MGLNSADLLKGLCHPRVkVGNEYVTKGQNVQQVVYAKGALAKAVYERMFNWMVTRINATLETKQPRQYF 456
Cdd:cd14938 318 NVKNLLLacklLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNININ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 457 ---IGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM--GIM 531
Cdd:cd14938 397 tnyINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTegSLF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 532 SILEEECMfPKATDMTFKAKLFDNHLGKSSNFQKPRNIKGKPEAhFSLIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKK 611
Cdd:cd14938 477 SLLENVST-KTIFDKSNLHSSIIRKFSRNSKYIKKDDITGNKKT-FVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQ 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 612 SSLKMLSSL--FANYAGFDTPIEKGKG----------KAKKGSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETK 679
Cdd:cd14938 555 SENEYMRQFcmFYNYDNSGNIVEEKRRysiqsalklfKRRYDTKNQMAVSLLRNNLTELEKLQETTFCHFIVCMKPNESK 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 680 SP-GVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPaaipegqfiDSRKGAEKLLGSLDIDHNQYKF 758
Cdd:cd14938 635 RElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE---------DLKEKVEALIKSYQISNYEWMI 705
|
....*.
gi 1387193866 759 GHTKVF 764
Cdd:cd14938 706 GNNMIF 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1173-1930 |
2.76e-32 |
|
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: 137.88 E-value: 2.76e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1173 KMRRdlEEATLQHEATAAALrKKHADSVAELSEQIDNLQRVKQK----LEKEKSEFKLELDDVTSNMEQIIKAKANLEKM 1248
Cdd:TIGR02168 171 KERR--KETERKLERTRENL-DRLEDILNELERQLKSLERQAEKaeryKELKAELRELELALLVLRLEELREELEELQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1249 CRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEevkAKNA 1328
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE---LEAQ 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1329 LAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRtkyetDAIQRTEELEEAKKKLAQRLQDAEEAVEAVN 1408
Cdd:TIGR02168 325 LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE-----ELESRLEELEEQLETLRSKVAQLELQIASLN 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1409 AKCSSLEKTKHRLQNEIEDLMVDVE--RSNAAAAALDKKQRNF---DKILAEWKQKYEESQSELESSQKEARSLSTELFK 1483
Cdd:TIGR02168 400 NEIERLEARLERLEDRRERLQQEIEelLKKLEEAELKELQAELeelEEELEELQEELERLEEALEELREELEEAEQALDA 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1484 LKN----------AYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEA---EKLE------LQSAL 1544
Cdd:TIGR02168 480 AERelaqlqarldSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAalgGRLQavvvenLNAAK 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1545 EEAEASLEHEEGK---ILRAQLEFNQIKAEMERKLAEKDEEMEQAKR----------------NHLRVVDSLQTSLDAET 1605
Cdd:TIGR02168 560 KAIAFLKQNELGRvtfLPLDSIKGTEIQGNDREILKNIEGFLGVAKDlvkfdpklrkalsyllGGVLVVDDLDNALELAK 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1606 RSRNEALRVKKkmEGDL-----------NEMEIQLSHANRLAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIV 1674
Cdd:TIGR02168 640 KLRPGYRIVTL--DGDLvrpggvitggsAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQL 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1675 -------ERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMEADLSQLQTEVEEAVQE 1747
Cdd:TIGR02168 718 rkeleelSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE 797
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1748 CRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKGgKKQLQKLEARVRELENELE 1827
Cdd:TIGR02168 798 LKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL-AAEIEELEELIEELESELE 876
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1828 AEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFR-KVQHELDEA 1906
Cdd:TIGR02168 877 ALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSeEYSLTLEEA 956
|
810 820
....*....|....*....|....
gi 1387193866 1907 EERADIAESQVNKLRAKSRDIGTK 1930
Cdd:TIGR02168 957 EALENKIEDDEEEARRRLKRLENK 980
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
840-1672 |
2.15e-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: 128.25 E-value: 2.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 840 LKSAETEKEIALMKEEFGRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKV 919
Cdd:TIGR02168 218 LKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 920 KEMTERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKAL 999
Cdd:TIGR02168 298 SRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1000 QEAHQQALDDLQAEEDKVNTLTKAKVKLEQHVDDLEGSLEQEKKVRMDLEraKRKLEGDLKLTQESIMDLENDKQQLDER 1079
Cdd:TIGR02168 378 EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL--KKLEEAELKELQAELEELEEELEELQEE 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1080 LKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERT---ARAKVEKLRSDLSRELEEISER------- 1149
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGfseGVKALLKNQSGLSGILGVLSELisvdegy 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1150 ---LEEAGGATSVQIEMNKKREA----EFQKMRRDLEEATLqhEATAAALRKKHADSvAELSEQIDNLQRVKQKLEKEKS 1222
Cdd:TIGR02168 536 eaaIEAALGGRLQAVVVENLNAAkkaiAFLKQNELGRVTFL--PLDSIKGTEIQGND-REILKNIEGFLGVAKDLVKFDP 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1223 EFKLEL----------DDVTSNMEQIIKAKANLekMCRTLEDQM-----------NEHRSKAEETQRSVNDLTSQRAKLQ 1281
Cdd:TIGR02168 613 KLRKALsyllggvlvvDDLDNALELAKKLRPGY--RIVTLDGDLvrpggvitggsAKTNSSILERRREIEELEEKIEELE 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1282 TENGELSRQLDEKEALISQLtrgkltyTQQLEDLKRQLEEEVKAKNALAHALQSArhdcdllreqyEEETEAKAELQRVL 1361
Cdd:TIGR02168 691 EKIAELEKALAELRKELEEL-------EEELEQLRKELEELSRQISALRKDLARL-----------EAEVEQLEERIAQL 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1362 SKANSEVAQWRTKYEtdaiQRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLmvdversNAAAAA 1441
Cdd:TIGR02168 753 SKELTELEAEIEELE----ERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL-------NEEAAN 821
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1442 LDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGK 1521
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSE 901
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1522 TIHELEKVRKQLEAEKLELQSALEEAEASLEheegkilRAQLEFNQIKAemerKLAEKDE-EMEQAKRNHLRVVDSLQts 1600
Cdd:TIGR02168 902 ELRELESKRSELRRELEELREKLAQLELRLE-------GLEVRIDNLQE----RLSEEYSlTLEEAEALENKIEDDEE-- 968
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387193866 1601 ldaETRSRNEALRVKKKMEGDLNEMEIQlshanrlaaEAQKQVKSLQSLLKdtqiQLDDAVRANDDLKENIA 1672
Cdd:TIGR02168 969 ---EARRRLKRLENKIKELGPVNLAAIE---------EYEELKERYDFLTA----QKEDLTEAKETLEEAIE 1024
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
963-1871 |
2.99e-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: 127.87 E-value: 2.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 963 KVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALD--DLQAEEDKVNtLTKAKVKLEQHVDDLEGSLEQ 1040
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERykELKAELRELE-LALLVLRLEELREELEELQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1041 EKKvrmdLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNALNARIEDeqalgsqLQKKLKELQARIEELEE 1120
Cdd:TIGR02168 248 LKE----AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISR-------LEQQKQILRERLANLER 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1121 ELEAERTARAKVEKLRSDLSRELEEISERLEEAggatSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKhadsV 1200
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEEL----KEELESLEAELEELEAELEELESRLEELEEQLETLRSK----V 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1201 AELSEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKmcRTLEDQMNEHRSKAEETQRSVNDLTSQRAKL 1280
Cdd:TIGR02168 389 AQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAEL--KELQAELEELEEELEELQEELERLEEALEEL 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1281 QTENGELSRQLDEKEALISQLtRGKLTYTQQLEDLKRQLEEEVkaKNALAHALQSARHDcDLLREQYEEETEAKAELQRV 1360
Cdd:TIGR02168 467 REELEEAEQALDAAERELAQL-QARLDSLERLQENLEGFSEGV--KALLKNQSGLSGIL-GVLSELISVDEGYEAAIEAA 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1361 LSKANSEVAqwrTKYETDAIQRTEELEEAKK--------------KLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIE 1426
Cdd:TIGR02168 543 LGGRLQAVV---VENLNAAKKAIAFLKQNELgrvtflpldsikgtEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALS 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1427 DL-----MVD-VERSNAAAAALDKKQRNF----DKILAEWkqkyeesqseleSSQKEARSLSTELFKLKNAYEESLEHLE 1496
Cdd:TIGR02168 620 YLlggvlVVDdLDNALELAKKLRPGYRIVtldgDLVRPGG------------VITGGSAKTNSSILERRREIEELEEKIE 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1497 TFKRENKNLQEEISDLTEQLgssgktiHELEKVRKQLEAEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEMERKL 1576
Cdd:TIGR02168 688 ELEEKIAELEKALAELRKEL-------EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1577 AEKDEEMEQakrnhlrvvdslqtsLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRlaaeaqkQVKSLQSLLKDTQIQ 1656
Cdd:TIGR02168 761 AEIEELEER---------------LEEAEEELAEAEAEIEELEAQIEQLKEELKALRE-------ALDELRAELTLLNEE 818
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1657 LDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIEtservqlLHSQNTSLINQKKKMEADLSQ 1736
Cdd:TIGR02168 819 AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE-------LESELEALLNERASLEEALAL 891
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1737 LQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQdtsAHLERMKKNMEQTIKDL--QHRLDEAEQIALK-GGKKQLQ 1813
Cdd:TIGR02168 892 LRSELEELSEELRELESKRSELRRELEELREKLAQLE---LRLEGLEVRIDNLQERLseEYSLTLEEAEALEnKIEDDEE 968
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*...
gi 1387193866 1814 KLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKL 1871
Cdd:TIGR02168 969 EARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
839-1452 |
2.03e-26 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 118.50 E-value: 2.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 839 LLKSAETEKEIALMKEEFGRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAK 918
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 919 VKEMTERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKA 998
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 999 LQEAHQQALDDLQAEEDKVNTLTKAKVKLEQHVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDE 1078
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1079 RLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTAR--AKVEKLRSDLSRELEEISERLEEAGGA 1156
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGlaGAVAVLIGVEAAYEAALEAALAAALQN 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1157 TSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELSEQIDNLQRVKQKLEKEKSEFKLELDDVTSNME 1236
Cdd:COG1196 551 IVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAA 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1237 QIIKAKAnlekmcrtledQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLK 1316
Cdd:COG1196 631 RLEAALR-----------RAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEAL 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1317 RQLEEEVKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAqwrtKYETDAIQRTEELEEAKKKLAQR 1396
Cdd:COG1196 700 LAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEA----LEELPEPPDLEELERELERLERE 775
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387193866 1397 LQD-------AEEAVEAVNAKCSSLEKTKHRLQNEIEDLM-----VDVERSNAAAAALDKKQRNFDKI 1452
Cdd:COG1196 776 IEAlgpvnllAIEEYEELEERYDFLSEQREDLEEARETLEeaieeIDRETRERFLETFDAVNENFQEL 843
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1310-1928 |
7.56e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 110.03 E-value: 7.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1310 QQLEDLKRQ-----------LEEEVKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVaqwrtkyetd 1378
Cdd:COG1196 200 RQLEPLERQaekaeryrelkEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAEL---------- 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1379 aiqrtEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQ 1458
Cdd:COG1196 270 -----EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1459 KYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKL 1538
Cdd:COG1196 345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1539 ELQSALEEAEASLEHEEGKILRAQLEFNQIKAEMERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRsrneaLRVKKKM 1618
Cdd:COG1196 425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR-----LLLLLEA 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1619 EGDlnemeiqlshanrlAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQaeleelRAVVEQTERS 1698
Cdd:COG1196 500 EAD--------------YEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQ------NIVVEDDEVA 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1699 RKLAEQELIETSERVQLLHSqntSLINQKKKMEADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAH 1778
Cdd:COG1196 560 AAAIEYLKAAKAGRATFLPL---DKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAAL 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1779 LERMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEARVRELENELEAEQKRNAESVkgmRKSERRIKELTYQTEEDR 1858
Cdd:COG1196 637 RRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELEL---EEALLAEEEEERELAEAE 713
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1859 KNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSkfrKVQHELDEAEERADIAESQVNKLRAKSRDIG 1928
Cdd:COG1196 714 EERLEEELEEEALEEQLEAEREELLEELLEEEELLE---EEALEELPEPPDLEELERELERLEREIEALG 780
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1106-1909 |
9.05e-24 |
|
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: 110.16 E-value: 9.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1106 KKLKELQARIEELEeeleaertarAKVEKLRsdlsRELEEISERLEEaggatsVQIEMNKKREaEFQKMRRDLEEAtlqh 1185
Cdd:TIGR02169 156 RKIIDEIAGVAEFD----------RKKEKAL----EELEEVEENIER------LDLIIDEKRQ-QLERLRREREKA---- 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1186 EATAAALRKKHADSVAELSEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKMCRTLEDQMNEHRS-KAE 1264
Cdd:TIGR02169 211 ERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEeEQL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1265 ETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVKAKNALAHALQSARHDCDLLR 1344
Cdd:TIGR02169 291 RVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLR 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1345 EQYEEETEAKAELQRvlskansEVAQWRTKYEtDAIQRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNE 1424
Cdd:TIGR02169 371 AELEEVDKEFAETRD-------ELKDYREKLE-KLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEE 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1425 IEDLMVDVErsnaaaaALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLknayEESLEHLETFKRENKN 1504
Cdd:TIGR02169 443 KEDKALEIK-------KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEA----EAQARASEERVRGGRA 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1505 LQEEISDLTEqlGSSGkTIHELEKVRkqlEAEKLELQSAL------------EEAEASLEH-EEGKILRAQ-LEFNQIKA 1570
Cdd:TIGR02169 512 VEEVLKASIQ--GVHG-TVAQLGSVG---ERYATAIEVAAgnrlnnvvveddAVAKEAIELlKRRKAGRATfLPLNKMRD 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1571 EMERK--------------LAEKDEEMEQAKRNHLR---VVDSLQT-----------SLDAE-----------TRSRNEA 1611
Cdd:TIGR02169 586 ERRDLsilsedgvigfavdLVEFDPKYEPAFKYVFGdtlVVEDIEAarrlmgkyrmvTLEGElfeksgamtggSRAPRGG 665
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1612 LRVKKKMEGDLNEMEIQLSHANRLAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAV 1691
Cdd:TIGR02169 666 ILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEED 745
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1692 VEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMEADLSqlQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKK 1771
Cdd:TIGR02169 746 LSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLS--HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNR 823
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1772 EQDTSAHLERMKKNMEQTIKDLQHRLDE-AEQIALKGGKK-----QLQKLEARVRELENELEAEQKRNAESVKGMRKSER 1845
Cdd:TIGR02169 824 LTLEKEYLEKEIQELQEQRIDLKEQIKSiEKEIENLNGKKeeleeELEELEAALRDLESRLGDLKKERDELEAQLRELER 903
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387193866 1846 RIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSkFRKVQHELDEAEER 1909
Cdd:TIGR02169 904 KIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELS-LEDVQAELQRVEEE 966
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
840-1700 |
1.64e-23 |
|
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: 109.00 E-value: 1.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 840 LKSAETEKEIAlmkEEFGRLKEalEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKV 919
Cdd:TIGR02169 200 LERLRREREKA---ERYQALLK--EKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 920 KEMTERLEDE-EEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKA 998
Cdd:TIGR02169 275 EELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDK 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 999 LQEAHQQALDDLQAEEDKVNTLTKAKVKLEQHVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDkqqlde 1078
Cdd:TIGR02169 355 LTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAA------ 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1079 rLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERL----EEAG 1154
Cdd:TIGR02169 429 -IAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQAraseERVR 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1155 GATSVQIEMNKKREAEF----QKMRRDLEEATLQHEATAAALRKKHADSVAELSEQIDNLQRVKQ------KLEKEKSEf 1224
Cdd:TIGR02169 508 GGRAVEEVLKASIQGVHgtvaQLGSVGERYATAIEVAAGNRLNNVVVEDDAVAKEAIELLKRRKAgratflPLNKMRDE- 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1225 klELDDVTSNMEQIIKAKANLekmcRTLEDQMNEHRSKAEETQRSVNDLTSQRA-----KLQTENGELSrqldEKEALIS 1299
Cdd:TIGR02169 587 --RRDLSILSEDGVIGFAVDL----VEFDPKYEPAFKYVFGDTLVVEDIEAARRlmgkyRMVTLEGELF----EKSGAMT 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1300 ----QLTRGKLTYTQQLEDLKRQLEEEVKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRvLSKANSEVAQwrtkY 1375
Cdd:TIGR02169 657 ggsrAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGE-IEKEIEQLEQ----E 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1376 ETDAIQRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNaaaaaLDKKQRNFDKIlae 1455
Cdd:TIGR02169 732 EEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSR-----IPEIQAELSKL--- 803
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1456 wkqkyeesqselessQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEA 1535
Cdd:TIGR02169 804 ---------------EEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEE 868
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1536 EKLELQSALEEAEASLEHEEGKILRAQLEfnqiKAEMERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVK 1615
Cdd:TIGR02169 869 ELEELEAALRDLESRLGDLKKERDELEAQ----LRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE 944
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1616 KKMEGDLNEMEIQlshANRLAAEAqkQVKSLQSLLKDTQIQLDDAVRANDDLKEniaiverRNNLLQAELEELRAVVEQT 1695
Cdd:TIGR02169 945 EIPEEELSLEDVQ---AELQRVEE--EIRALEPVNMLAIQEYEEVLKRLDELKE-------KRAKLEEERKAILERIEEY 1012
|
....*
gi 1387193866 1696 ERSRK 1700
Cdd:TIGR02169 1013 EKKKR 1017
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1074-1747 |
2.46e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 108.49 E-value: 2.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1074 QQLDERLKKKD-----FELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISE 1148
Cdd:COG1196 216 RELKEELKELEaelllLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1149 RLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALrkkhadsvAELSEQIDNLQRVKQKLEKEKSEFKLEL 1228
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL--------EELEEELEEAEEELEEAEAELAEAEEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1229 DDVTSNMEQIIKAKANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTrgklty 1308
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE------ 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1309 tQQLEDLKRQLEEEVKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEE 1388
Cdd:COG1196 442 -EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1389 AKKKLAQRLQDAEEAVEAVnakcsslektkhrLQNEIEDLMVDVERSNAAAAAldkKQRNFDKILAEWKQKYEESQSELE 1468
Cdd:COG1196 521 GLAGAVAVLIGVEAAYEAA-------------LEAALAAALQNIVVEDDEVAA---AAIEYLKAAKAGRATFLPLDKIRA 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1469 SSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKLELQSALEEAE 1548
Cdd:COG1196 585 RAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTG 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1549 ASLEHEEGKILRAQlefnqikAEMERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQ 1628
Cdd:COG1196 665 GSRRELLAALLEAE-------AELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREEL 737
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1629 LSHANRLAAEaqkqvkslqsllkdtqiqLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEqtersrkLAEQELIE 1708
Cdd:COG1196 738 LEELLEEEEL------------------LEEEALEELPEPPDLEELERELERLEREIEALGPVNL-------LAIEEYEE 792
|
650 660 670
....*....|....*....|....*....|....*....
gi 1387193866 1709 TSERVQLLHSQNTSLINQKKKMEADLSQLQTEVEEAVQE 1747
Cdd:COG1196 793 LEERYDFLSEQREDLEEARETLEEAIEEIDRETRERFLE 831
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
843-1589 |
5.94e-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: 5.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 843 AETEKEIALMKEEFGRLKEALEKSEARRKELEEKMVSLLQEKND--------------------------------LQLQ 890
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKaeryqallkekreyegyellkekealerqkeaIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 891 VQAEQDNLADAEERCDQLIKNKIQLEAKVKEMTERLED--EEEMNA------ELTAKKRKLEDECSELKRDIDDLELTLA 962
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDlgEEEQLRvkekigELEAEIASLERSIAEKERELEDAEERLA 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 963 KVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQHVDDLEGSLEQEK 1042
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1043 KVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFE--------------LNALNARIEDEQALGSQLQKKL 1108
Cdd:TIGR02169 406 RELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEikkqewkleqlaadLSKYEQELYDLKEEYDRVEKEL 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1109 KELQARIEELEEELEAERTA----RAKVEKLRSDLS------RELEEISER----LEEAGG-----------ATSVQ-IE 1162
Cdd:TIGR02169 486 SKLQRELAEAEAQARASEERvrggRAVEEVLKASIQgvhgtvAQLGSVGERyataIEVAAGnrlnnvvveddAVAKEaIE 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1163 MNKKREA------EFQKMRRDLEEATLQHEATAAALrkkhADSVAELSEQIDNLQR-------VKQKLEKEKS---EFKL 1226
Cdd:TIGR02169 566 LLKRRKAgratflPLNKMRDERRDLSILSEDGVIGF----AVDLVEFDPKYEPAFKyvfgdtlVVEDIEAARRlmgKYRM 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1227 -----ELDDVTSNMEQIIKAKANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQL 1301
Cdd:TIGR02169 642 vtlegELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEI 721
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1302 TRGKLTYTQQLEDLKRQLEEEVKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIq 1381
Cdd:TIGR02169 722 EKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAEL- 800
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1382 rtEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYE 1461
Cdd:TIGR02169 801 --SKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALR 878
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1462 ESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVR------KQLEA 1535
Cdd:TIGR02169 879 DLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPeeelslEDVQA 958
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1536 EKLELQSALEEAE-----ASLEHEEGKILRAQLEFNQIKAEMERK-LAEKDEEMEQAKRN 1589
Cdd:TIGR02169 959 ELQRVEEEIRALEpvnmlAIQEYEEVLKRLDELKEKRAKLEEERKaILERIEEYEKKKRE 1018
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
835-1428 |
7.65e-22 |
|
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: 103.60 E-value: 7.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 835 KIKPLLKSAETEKEIALMKEEFGRLKEALEKSEARRKELEEKM--------------VSLLQEKNDLQLQVQAEQDNLAD 900
Cdd:TIGR02168 332 LDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLeeleeqletlrskvAQLELQIASLNNEIERLEARLER 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 901 AEERCDQLIKNKIQL-----EAKVKEMTERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKV 975
Cdd:TIGR02168 412 LEDRRERLQQEIEELlkkleEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARL 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 976 ---KNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEED---KVNT-----LTKAKVKLEQHVDDLEGSLEQEKKV 1044
Cdd:TIGR02168 492 dslERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGyeaAIEAalggrLQAVVVENLNAAKKAIAFLKQNELG 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1045 RMDL-------ERAKRKLEGDLKLTQESIMDLENDKQQLDERLKK------------KDFElNALNARIE---------- 1095
Cdd:TIGR02168 572 RVTFlpldsikGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKalsyllggvlvvDDLD-NALELAKKlrpgyrivtl 650
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1096 --------------DEQALGSQLQKK--LKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAggatsv 1159
Cdd:TIGR02168 651 dgdlvrpggvitggSAKTNSSILERRreIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL------ 724
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1160 qiemnkkrEAEFQKMRRDLEEATLQHEATAAALRKKHADsVAELSEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQII 1239
Cdd:TIGR02168 725 --------SRQISALRKDLARLEAEVEQLEERIAQLSKE-LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLK 795
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1240 KAKANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQL 1319
Cdd:TIGR02168 796 EELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL 875
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1320 EEEVKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQD 1399
Cdd:TIGR02168 876 EALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEE 955
|
650 660
....*....|....*....|....*....
gi 1387193866 1400 AEEAVEAVNAKCSSLEKTKHRLQNEIEDL 1428
Cdd:TIGR02168 956 AEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
978-1860 |
7.65e-21 |
|
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: 100.53 E-value: 7.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 978 LTEEMAGLDEIIAKLTKEKKALQEAHQQaLDDLQAEEDKVNT----LTKAKVKLEQHVDDLEGSLEQEKKVRM----DLE 1049
Cdd:TIGR02169 158 IIDEIAGVAEFDRKKEKALEELEEVEEN-IERLDLIIDEKRQqlerLRREREKAERYQALLKEKREYEGYELLkekeALE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1050 RAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNALNARI----EDEQAlgsQLQKKLKELQARI-------EEL 1118
Cdd:TIGR02169 237 RQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIkdlgEEEQL---RVKEKIGELEAEIaslersiAEK 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1119 EEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEAtlqhEATAAALRKKHAD 1198
Cdd:TIGR02169 314 ERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEV----DKEFAETRDELKD 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1199 SVAELS---EQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTS 1275
Cdd:TIGR02169 390 YREKLEklkREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQ 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1276 QRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQlEEEVKAKNALAHALQSarhDCDLLREQYEE--ETEA 1353
Cdd:TIGR02169 470 ELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAV-EEVLKASIQGVHGTVA---QLGSVGERYATaiEVAA 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1354 KAELQRVLSKaNSEVAQWRTKYETD------------AIQRTEELEEAKKK-----LAQRLQDAEEAVEAVNAKC----- 1411
Cdd:TIGR02169 546 GNRLNNVVVE-DDAVAKEAIELLKRrkagratflplnKMRDERRDLSILSEdgvigFAVDLVEFDPKYEPAFKYVfgdtl 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1412 --SSLEKTKhRLQNEIEDLMVD---VERSNAAAAALDKKQRnfdkilaewkqkyeeSQSELESSQKEARSLSTELFKLKN 1486
Cdd:TIGR02169 625 vvEDIEAAR-RLMGKYRMVTLEgelFEKSGAMTGGSRAPRG---------------GILFSRSEPAELQRLRERLEGLKR 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1487 AYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVR-------KQLEAEKLELQSALEEAEASLEHEEGKIL 1559
Cdd:TIGR02169 689 ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEeklkerlEELEEDLSSLEQEIENVKSELKELEARIE 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1560 RAQLEFNQIKAEMERKLAEKDEEMEQAKRNHLRVVDslqtsldaETRSRNEALrvkkkmegdLNEMEIQLSHANRLAAEA 1639
Cdd:TIGR02169 769 ELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLE--------EEVSRIEAR---------LREIEQKLNRLTLEKEYL 831
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1640 QKQVKSLQSLlkdtqiqlddavraNDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSErvqllhsq 1719
Cdd:TIGR02169 832 EKEIQELQEQ--------------RIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKK-------- 889
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1720 ntslinQKKKMEADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKkeqdtsaHLERMKKNMEQtikdlqhrlDE 1799
Cdd:TIGR02169 890 ------ERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELS-------EIEDPKGEDEE---------IP 947
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387193866 1800 AEQIALKGGKKQLQKLEARVRELE-------NELEAEQKRNAESVKGMRK--SERR-IKELTYQTEEDRKN 1860
Cdd:TIGR02169 948 EEELSLEDVQAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDELKEKRAKleEERKaILERIEEYEKKKRE 1018
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
220-706 |
7.96e-21 |
|
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: 100.20 E-value: 7.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 220 IIQANPALEAFGNAKTVRNDNSSRFGKF--IRIHFGATG---KLASADIETYLLEKSRVIFQL------KAERDYHIFYQ 288
Cdd:cd14894 249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPwefQICGCHISPFLLEKSRVTSERgresgdQNELNFHILYA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 289 ILSNKKPELLDMLLITNNPYD------YAFISQGETTVASIDDAEELMATD--------NAFDVLGFTTEEKNSMYKLTG 354
Cdd:cd14894 329 MVAGVNAFPFMRLLAKELHLDgidcsaLTYLGRSDHKLAGFVSKEDTWKKDverwqqviDGLDELNVSPDEQKTIFKVLS 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 355 AIMHFGNMKFKLKQREEQAEPDGT---EEADKSAYLMGLNSADLLKGLCHPR---VKVGNEYVTKGQNVQQVVYAKGALA 428
Cdd:cd14894 409 AVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGSVEKLERMLMTKsvsLQSTSETFEVTLEKGQVNHVRDTLA 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 429 KAVYERMFNWMV------TRINATLETKQPRQY-----------FIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNH 491
Cdd:cd14894 489 RLLYQLAFNYVVfvmneaTKMSALSTDGNKHQMdsnasapeavsLLKIVDVFGFEDLTHNSLDQLCINYLSEKLYAREEQ 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 492 HMFVLEQEEYKKEGIEWEfidfgmdlQACIDLIEKPMGIMSILEEECMFPKATDMTF-----KAKLFDNHL--GKSSNFQ 564
Cdd:cd14894 569 VIAVAYSSRPHLTARDSE--------KDVLFIYEHPLGVFASLEELTILHQSENMNAqqeekRNKLFVRNIydRNSSRLP 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 565 KPRNIKGKPEAH---------FSLIHYAGTVDYNIIGWLQKNKDPLNETVVDLYKKSSLKMLSSLFANYAGF----DTPI 631
Cdd:cd14894 641 EPPRVLSNAKRHtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRMLNESSQLgwspNTNR 720
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387193866 632 EKGKGKAKKGSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICR 706
Cdd:cd14894 721 SMLGSAESRLSGTKSFVGQFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQMEICR 795
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
841-1512 |
3.36e-20 |
|
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: 98.21 E-value: 3.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 841 KSAETEKEIALMKEEFGRLKEALEKSEARRKELEEKM-------VSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKI 913
Cdd:TIGR02168 345 KLEELKEELESLEAELEELEAELEELESRLEELEEQLetlrskvAQLELQIASLNNEIERLEARLERLEDRRERLQQEIE 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 914 QL-----EAKVKEMTERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKV---KNLTEEMAGL 985
Cdd:TIGR02168 425 ELlkkleEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLdslERLQENLEGF 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 986 DEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQH--VDDLE------GSLEQEKKVRMDL-------ER 1050
Cdd:TIGR02168 505 SEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAvvVENLNaakkaiAFLKQNELGRVTFlpldsikGT 584
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1051 AKRKLEGDLKLTQESIMDLENDKQQLDERLKK------------KDFElNALNARIE----------------------- 1095
Cdd:TIGR02168 585 EIQGNDREILKNIEGFLGVAKDLVKFDPKLRKalsyllggvlvvDDLD-NALELAKKlrpgyrivtldgdlvrpggvitg 663
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1096 -DEQALGSQLQKK--LKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAggatsvqiemnkkrEAEFQ 1172
Cdd:TIGR02168 664 gSAKTNSSILERRreIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL--------------SRQIS 729
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1173 KMRRDLEEATLQHEATAAALRKKHADsVAELSEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKMCRTL 1252
Cdd:TIGR02168 730 ALRKDLARLEAEVEQLEERIAQLSKE-LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL 808
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1253 EDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVKAKNALAHA 1332
Cdd:TIGR02168 809 RAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEA 888
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1333 LQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEAVEAVNAKCS 1412
Cdd:TIGR02168 889 LALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEE 968
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1413 SLEKTKHRLQNEIEDLmvdverSNAAAAALDKkqrnfdkiLAEWKQKYEESQselessqKEARSLSTELFKLKNAYEE-- 1490
Cdd:TIGR02168 969 EARRRLKRLENKIKEL------GPVNLAAIEE--------YEELKERYDFLT-------AQKEDLTEAKETLEEAIEEid 1027
|
730 740
....*....|....*....|....*
gi 1387193866 1491 ---SLEHLETFKRENKNLQEEISDL 1512
Cdd:TIGR02168 1028 reaRERFKDTFDQVNENFQRVFPKL 1052
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1286-1828 |
5.02e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 97.70 E-value: 5.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1286 ELSRQLDEKEALISQLTRGKLTytQQLEDLKRQLEEEVKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKAN 1365
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELE--AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1366 SEVAQwrtkyetdAIQRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKK 1445
Cdd:COG1196 295 AELAR--------LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1446 QRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHE 1525
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1526 LEKVRKQLEAEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEMERKLAEKDEEM---EQAKRNHLR---------- 1592
Cdd:COG1196 447 AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEgflEGVKAALLLaglrglagav 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1593 -VVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEI-------QLSHANRLAAEAQKQVKSLQSLLKDTQIQLDDAVRAN 1664
Cdd:COG1196 527 aVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAieylkaaKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVAS 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1665 DDLKENIAIVERRNNLLQAELEELRA--------VVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMEADLSQ 1736
Cdd:COG1196 607 DLREADARYYVLGDTLLGRTLVAARLeaalrravTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAE 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1737 LQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLE 1816
Cdd:COG1196 687 RLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE 766
|
570
....*....|....*
gi 1387193866 1817 ---ARvreLENELEA 1828
Cdd:COG1196 767 relER---LEREIEA 778
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
917-1772 |
2.04e-19 |
|
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: 95.91 E-value: 2.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 917 AKVKEMTERLEDEEEMNAELTAKKRKLEDECSELKRdIDDLELTLAKVE-----KEKHATENKVKNLTEEMAGLDEIIAK 991
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRREREKAER-YQALLKEKREYEgyellKEKEALERQKEAIERQLASLEEELEK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 992 LTKEKKALQEAHQQALDDLQAEEDKVNTLTkakvkleqhvddlEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLEN 1071
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEELNKKIKDLG-------------EEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1072 DKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLE 1151
Cdd:TIGR02169 323 RLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREIN 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1152 EAggatsvqiemnKKREAEFQKMRRDLEEATLQHEATAAALRKKHAdsvaelseqidnlqrvkqKLEKEKSEFKLELDDV 1231
Cdd:TIGR02169 403 EL-----------KRELDRLQEELQRLSEELADLNAAIAGIEAKIN------------------ELEEEKEDKALEIKKQ 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1232 TSNMEQIIKAKANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEA-------LISQLTRG 1304
Cdd:TIGR02169 454 EWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKAsiqgvhgTVAQLGSV 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1305 KLTYTQQLEDLKRQ------LEEEVKAKNA--LAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYE 1376
Cdd:TIGR02169 534 GERYATAIEVAAGNrlnnvvVEDDAVAKEAieLLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYE 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1377 TD---AIQRT---EELEEAKK--------KLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAAL 1442
Cdd:TIGR02169 614 PAfkyVFGDTlvvEDIEAARRlmgkyrmvTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSL 693
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1443 DKKQRNFDKILAEWKQKyeesqselessqkeARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKT 1522
Cdd:TIGR02169 694 QSELRRIENRLDELSQE--------------LSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSE 759
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1523 IHELEKVRKQLEAEKLELQSALEEAEASLEHEEGKILRAQLEF--------NQIKAEMERKLAEKDEEMEQA--KRNHLR 1592
Cdd:TIGR02169 760 LKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKleeevsriEARLREIEQKLNRLTLEKEYLekEIQELQ 839
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1593 VVDSLQTSLDAETRSRNEALRVK--------KKMEGDLNEMEIQLSHANRLAAEAQKQVKSLQSLLKDTQIQLDDAVRAN 1664
Cdd:TIGR02169 840 EQRIDLKEQIKSIEKEIENLNGKkeeleeelEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRL 919
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1665 DDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLaEQELIETSERVQLLHSQNTSLINQKKKMEADLSQLqteveea 1744
Cdd:TIGR02169 920 SELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDV-QAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDEL------- 991
|
890 900
....*....|....*....|....*...
gi 1387193866 1745 vQECRNAEEKAKKAITDAAMMAEELKKE 1772
Cdd:TIGR02169 992 -KEKRAKLEEERKAILERIEEYEKKKRE 1018
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
987-1801 |
5.23e-19 |
|
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: 94.41 E-value: 5.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 987 EIIAKLTKE--KKALQEAHQQaLDDLQAEEDKVNTL-TKAKVKLEQHVDDLEGSLEQ---EKKVRMDLERAKRKLEGDLK 1060
Cdd:pfam15921 66 KIIAYPGKEhiERVLEEYSHQ-VKDLQRRLNESNELhEKQKFYLRQSVIDLQTKLQEmqmERDAMADIRRRESQSQEDLR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1061 -LTQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQAR-----IEELEEELEAERTARAKVEK 1134
Cdd:pfam15921 145 nQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEAsgkkiYEHDSMSTMHFRSLGSAISK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1135 LRSDLSRELEEISERLEEAGGA-TSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELSEQIDNLQRV 1213
Cdd:pfam15921 225 ILRELDTEISYLKGRIFPVEDQlEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEII 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1214 KQKLEKEKSEFKLELDDVTSNMEQIikaKANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLde 1293
Cdd:pfam15921 305 QEQARNQNSMYMRQLSDLESTVSQL---RSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQL-- 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1294 kEALISQLTRGKLTYTQQLEDLKRQLEEEVKAKNALAHalqsarhdcdlLREQYEEETEAKAELQRVLSKANSEvAQWRT 1373
Cdd:pfam15921 380 -QKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDH-----------LRRELDDRNMEVQRLEALLKAMKSE-CQGQM 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1374 KYETDAIQRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLmvdversnaaAAALDKKQRNFDKIL 1453
Cdd:pfam15921 447 ERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDL----------TASLQEKERAIEATN 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1454 AEwkqkYEESQSELESSQKEARSLSTELFKLKNAYEESlEHLETFKRENKN----LQEEISDLTEQLGSSGKTIHELEKV 1529
Cdd:pfam15921 517 AE----ITKLRSRVDLKLQELQHLKNEGDHLRNVQTEC-EALKLQMAEKDKvieiLRQQIENMTQLVGQHGRTAGAMQVE 591
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1530 RKQLEAE----KLELQS---ALEEAEASLEHEEGKILRAQLE-FNQIKAEMERKLAEKDEEMEQAK-RNHLRVVDSLQTS 1600
Cdd:pfam15921 592 KAQLEKEindrRLELQEfkiLKDKKDAKIRELEARVSDLELEkVKLVNAGSERLRAVKDIKQERDQlLNEVKTSRNELNS 671
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1601 LDAETRSRNEALRVK-KKMEGDLNEMEIQLShanrlaaEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNN 1679
Cdd:pfam15921 672 LSEDYEVLKRNFRNKsEEMETTTNKLKMQLK-------SAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQID 744
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1680 LLQAELEELRAVVEQTERSRKLAEQELIETSERVqllhsqnTSLINQKKKMEADLSQLQTEVEEAVQECRNAEEKAKKAI 1759
Cdd:pfam15921 745 ALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQEL-------STVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKAS 817
|
810 820 830 840
....*....|....*....|....*....|....*....|..
gi 1387193866 1760 TDAAMMAEELKKEQDTSAHLErmkknmeqtikdLQHRLDEAE 1801
Cdd:pfam15921 818 LQFAECQDIIQRQEQESVRLK------------LQHTLDVKE 847
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
870-1425 |
1.02e-18 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 93.18 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 870 RKELEEKmvsllqEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMTERLEDEEEMNAELTakkrkledecsE 949
Cdd:PRK02224 193 KAQIEEK------EEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELE-----------T 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 950 LKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKE---KKALQEAHQQALDDLQAEEDKV-NTLTKAKV 1025
Cdd:PRK02224 256 LEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEaglDDADAEAVEARREELEDRDEELrDRLEECRV 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1026 KLEQHVDDLEGSLEQEKKVRmdlERAKRK------LEGDLKLTQESIMDLENDKQQLDErlkkkdfELNALNARIEDEQA 1099
Cdd:PRK02224 336 AAQAHNEEAESLREDADDLE---ERAEELreeaaeLESELEEAREAVEDRREEIEELEE-------EIEELRERFGDAPV 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1100 LGSQLQKKLKELQARIEEleeeleaertARAKVEKLRSDLSRELEEISE--RLEEAGG--------ATSVQIEMNKKREA 1169
Cdd:PRK02224 406 DLGNAEDFLEELREERDE----------LREREAELEATLRTARERVEEaeALLEAGKcpecgqpvEGSPHVETIEEDRE 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1170 EFQKMRRDLEEATLQHEATAAALRKkhADSVAELSEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKMC 1249
Cdd:PRK02224 476 RVEELEAELEDLEEEVEEVEERLER--AEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEA 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1250 RTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSR---QLDEKEALISQLT--RGKLTYTQQLEDLKR-QLEEEV 1323
Cdd:PRK02224 554 EEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERirtLLAAIADAEDEIErlREKREALAELNDERReRLAEKR 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1324 KAKNALAHALQSARhdcdllreqYEEETEAKAELQRVLSKANSEVAQWRTkyETDAIQRT--------EELEEAKKKLAQ 1395
Cdd:PRK02224 634 ERKRELEAEFDEAR---------IEEAREDKERAEEYLEQVEEKLDELRE--ERDDLQAEigavenelEELEELRERREA 702
|
570 580 590
....*....|....*....|....*....|
gi 1387193866 1396 rLQDAEEAVEAVNAKCSSLEKTKHRLQNEI 1425
Cdd:PRK02224 703 -LENRVEALEALYDEAEELESMYGDLRAEL 731
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1253-1927 |
3.28e-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: 91.78 E-value: 3.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1253 EDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLD-------EKEALISQLTRGKLTYTQQLEDLKRQLEEEVKA 1325
Cdd:pfam01576 11 EEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQaetelcaEAEEMRARLAARKQELEEILHELESRLEEEEER 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1326 KNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEeLEEAKKKLAQRLQDAEEAVE 1405
Cdd:pfam01576 91 SQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSK-LSKERKLLEERISEFTSNLA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1406 AVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLK 1485
Cdd:pfam01576 170 EEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAAL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1486 NAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKLELQSALEEAEASLEHEEGKILRAQLEF 1565
Cdd:pfam01576 250 ARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1566 NQIKAEMERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRLAAEAQKQVKS 1645
Cdd:pfam01576 330 TELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKK 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1646 LQSLLKDTQIQLDDAVRANDDLKEniaiverRNNLLQAELEELRAVVEQTE-RSRKLA------EQELIETSERVQLLHS 1718
Cdd:pfam01576 410 LEGQLQELQARLSESERQRAELAE-------KLSKLQSELESVSSLLNEAEgKNIKLSkdvsslESQLQDTQELLQEETR 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1719 QNTSLINQKKKMEADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLD 1798
Cdd:pfam01576 483 QKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLE 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1799 EAEQIALKggkkqLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTyqtEEDRKNLLRLQDLVDKlqlkvkay 1878
Cdd:pfam01576 563 EKAAAYDK-----LEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQML---AEEKAISARYAEERDR-------- 626
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1387193866 1879 krqaeeAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDI 1927
Cdd:pfam01576 627 ------AEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDL 669
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
841-1435 |
7.41e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 90.97 E-value: 7.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 841 KSAETEKEIALMKEEFGRLKEALEKSEARRKELEEKMVSllQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIqlEAKVK 920
Cdd:PTZ00121 1261 RMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAE--EKKKADEAKKKAEEAKKADEAKKKAEEAKKKA--DAAKK 1336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 921 EMTERLEDEEEMNAELTAKKRKLEDecSELKRDIDDLEltlaKVEKEKHATENKVKnlTEEMAGLDEIIAKLTKEKKALQ 1000
Cdd:PTZ00121 1337 KAEEAKKAAEAAKAEAEAAADEAEA--AEEKAEAAEKK----KEEAKKKADAAKKK--AEEKKKADEAKKKAEEDKKKAD 1408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1001 EAHQQALDDLQAEEdkvntlTKAKVKLEQHVDDLEGSLEQEKKVrmdlERAKRKLEGDLKltqesimdLENDKQQLDERL 1080
Cdd:PTZ00121 1409 ELKKAAAAKKKADE------AKKKAEEKKKADEAKKKAEEAKKA----DEAKKKAEEAKK--------AEEAKKKAEEAK 1470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1081 KKKDFELNALNARIEDEqalgsqLQKKLKELQARIEELEEELEAERTA---RAKVEKLRSDLSRELEEiSERLEEAGGAT 1157
Cdd:PTZ00121 1471 KADEAKKKAEEAKKADE------AKKKAEEAKKKADEAKKAAEAKKKAdeaKKAEEAKKADEAKKAEE-AKKADEAKKAE 1543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1158 SVQI--EMNKKREAEFQKMRRDLEEATLQHEATAAALRKkhadsvAELSEQIDNlQRVKQKLEKEKSEFKLELDDVTSNM 1235
Cdd:PTZ00121 1544 EKKKadELKKAEELKKAEEKKKAEEAKKAEEDKNMALRK------AEEAKKAEE-ARIEEVMKLYEEEKKMKAEEAKKAE 1616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1236 EQIIKAkanlekmcrtledqmnEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDL 1315
Cdd:PTZ00121 1617 EAKIKA----------------EELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEA 1680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1316 KRQLEEEVKAKNALAHALQSARhDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAiQRTEEL---EEAKKK 1392
Cdd:PTZ00121 1681 KKAEEDEKKAAEALKKEAEEAK-KAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDK-KKAEEAkkdEEEKKK 1758
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1387193866 1393 LAQRLQDAEEAVEAVNAKCSSLekTKHRLQNEIEDLMVDVERS 1435
Cdd:PTZ00121 1759 IAHLKKEEEKKAEEIRKEKEAV--IEEELDEEDEKRRMEVDKK 1799
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1128-1907 |
1.01e-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: 90.18 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1128 ARAKVEKLRSDLSRELEEISERLEEAGgatsvqiEMNKKREAEFQK----MRRDLEEATLQHEATAAaLRKKHADSVAEL 1203
Cdd:pfam15921 72 GKEHIERVLEEYSHQVKDLQRRLNESN-------ELHEKQKFYLRQsvidLQTKLQEMQMERDAMAD-IRRRESQSQEDL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1204 SEQidnLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKMCRTLED-----------QMNEHRSKAEETQRSVND 1272
Cdd:pfam15921 144 RNQ---LQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSilvdfeeasgkKIYEHDSMSTMHFRSLGS 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1273 LTSQRAK-LQTENGELSRQL----DEKEALISQLTRGKLTYTQQLEDLKRQL--EEEVKAkNALAHALQSARHDCDLLRE 1345
Cdd:pfam15921 221 AISKILReLDTEISYLKGRIfpveDQLEALKSESQNKIELLLQQHQDRIEQLisEHEVEI-TGLTEKASSARSQANSIQS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1346 QYE----EETEAKAELQRVLSKANSEVAQWRTkyetdaiqrteELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHR- 1420
Cdd:pfam15921 300 QLEiiqeQARNQNSMYMRQLSDLESTVSQLRS-----------ELREAKRMYEDKIEELEKQLVLANSELTEARTERDQf 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1421 ------LQNEIEDLMVDV-ERSNAAAAALDKKQRNFDKILAEwKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLE 1493
Cdd:pfam15921 369 sqesgnLDDQLQKLLADLhKREKELSLEKEQNKRLWDRDTGN-SITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQME 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1494 -HLETFKRENKNLqEEISDLTEQLGSsgkTIHELEKVRKQLEAEKLELQSA---LEEAEASLEHEEGKILRAQLEFNQIK 1569
Cdd:pfam15921 448 rQMAAIQGKNESL-EKVSSLTAQLES---TKEMLRKVVEELTAKKMTLESSertVSDLTASLQEKERAIEATNAEITKLR 523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1570 AEMERKLaekdEEMEQAKR--NHLRVVdslQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRLAAEAQKQVKSLQ 1647
Cdd:pfam15921 524 SRVDLKL----QELQHLKNegDHLRNV---QTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLE 596
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1648 SLLKDTQIQLDDAVRANDdlKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQElietSERVQLLHSQNTSLiNQK 1727
Cdd:pfam15921 597 KEINDRRLELQEFKILKD--KKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIK----QERDQLLNEVKTSR-NEL 669
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1728 KKMEADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEE----LKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAE-- 1801
Cdd:pfam15921 670 NSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQtrntLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQsk 749
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1802 ----QIALKGGKKQLQKLEARVRELENELEA---EQKRNAESVKGMRKSERRIKEltyqteedrkNLLRLQDLVDKLQLK 1874
Cdd:pfam15921 750 iqflEEAMTNANKEKHFLKEEKNKLSQELSTvatEKNKMAGELEVLRSQERRLKE----------KVANMEVALDKASLQ 819
|
810 820 830
....*....|....*....|....*....|...
gi 1387193866 1875 VkAYKRQAEEAEEQANTNLskfrKVQHELDEAE 1907
Cdd:pfam15921 820 F-AECQDIIQRQEQESVRL----KLQHTLDVKE 847
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1077-1837 |
1.12e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 90.20 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1077 DERLK--KKDFELNALNARIEDEQAlgSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAG 1154
Cdd:PTZ00121 1069 DEGLKpsYKDFDFDAKEDNRADEAT--EEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEAR 1146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1155 GATSVQIEMNKKREAEFQKMR--RDLEEATLQHEA-TAAALRKKHADSVAELSEQIDNLQRVKQKLEKEKSEfKLELDDV 1231
Cdd:PTZ00121 1147 KAEDAKRVEIARKAEDARKAEeaRKAEDAKKAEAArKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEAR-KAEDAKK 1225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1232 TSNMEQIIKAKANLEKMCRTLEDQMNEHRSKAEETQRSvnDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQ 1311
Cdd:PTZ00121 1226 AEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMA--HFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKK 1303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1312 LEDLKRQLEEEVKAKNALAHAlQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELE--EA 1389
Cdd:PTZ00121 1304 ADEAKKKAEEAKKADEAKKKA-EEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKkaDA 1382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1390 KKKLAQRLQDAEEA---VEAVNAKCSSLEKtKHRLQNEIEDLMVDVERSNAAAAAldKKQRNFDKILAEWKQKYEESQSE 1466
Cdd:PTZ00121 1383 AKKKAEEKKKADEAkkkAEEDKKKADELKK-AAAAKKKADEAKKKAEEKKKADEA--KKKAEEAKKADEAKKKAEEAKKA 1459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1467 LESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQlGSSGKTIHELEKVRKQLEAEKLELQSALEE 1546
Cdd:PTZ00121 1460 EEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA-KKKADEAKKAEEAKKADEAKKAEEAKKADE 1538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1547 AEASLEHEEGKILRAQLEFNqiKAEMERKLAEKDEEmEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDlnemE 1626
Cdd:PTZ00121 1539 AKKAEEKKKADELKKAEELK--KAEEKKKAEEAKKA-EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE----E 1611
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1627 IQLSHANRLAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKEniaivERRNNLLQAElEELRAVVEQTERSRKLAEQEL 1706
Cdd:PTZ00121 1612 AKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKK-----AEEENKIKAA-EEAKKAEEDKKKAEEAKKAEE 1685
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1707 IETSERVQLLHSQNtslinQKKKMEADLSQLQTEVEEAvQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNM 1786
Cdd:PTZ00121 1686 DEKKAAEALKKEAE-----EAKKAEELKKKEAEEKKKA-EELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKI 1759
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 1387193866 1787 EQTIKDLQHRLDEAEQIALKGGKKQLQKLEARVRELENELEAEQKRNAESV 1837
Cdd:PTZ00121 1760 AHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANI 1810
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
843-1455 |
2.47e-17 |
|
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: 88.97 E-value: 2.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 843 AETEKEIALMKEEFGRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEM 922
Cdd:TIGR02169 374 EEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 923 TERLE-------DEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKE 995
Cdd:TIGR02169 454 EWKLEqlaadlsKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSV 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 996 KKALQEAHQQAL----------DDLQAEED--------------------KVNTLTKAKVKLEQHVDDLEGSLEQEKKVR 1045
Cdd:TIGR02169 534 GERYATAIEVAAgnrlnnvvveDDAVAKEAiellkrrkagratflplnkmRDERRDLSILSEDGVIGFAVDLVEFDPKYE 613
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1046 -------------MDLERAKR--------KLEGDL--------------KLTQESIMDLENDKQQLDERLKKKDFELNAL 1090
Cdd:TIGR02169 614 pafkyvfgdtlvvEDIEAARRlmgkyrmvTLEGELfeksgamtggsrapRGGILFSRSEPAELQRLRERLEGLKRELSSL 693
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1091 NARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAggatsvqiemnkkrEAE 1170
Cdd:TIGR02169 694 QSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENV--------------KSE 759
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1171 FQKMRRDLEEatlqHEATAAALRKKHADSVAELS-EQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKMC 1249
Cdd:TIGR02169 760 LKELEARIEE----LEEDLHKLEEALNDLEARLShSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEI 835
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1250 RTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEevkaknal 1329
Cdd:TIGR02169 836 QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE-------- 907
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1330 ahalqsARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQwrTKYETDAIQRTEELEEAKKKLAQRLQD-------AEE 1402
Cdd:TIGR02169 908 ------LEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGE--DEEIPEEELSLEDVQAELQRVEEEIRAlepvnmlAIQ 979
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 1387193866 1403 AVEAVNAKCSSLEKTKHRLQNEIEDL-----MVDVERSNAAAAALDKKQRNFDKILAE 1455
Cdd:TIGR02169 980 EYEEVLKRLDELKEKRAKLEEERKAIlerieEYEKKKREVFMEAFEAINENFNEIFAE 1037
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
841-1618 |
1.12e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 87.12 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 841 KSAETEKEIALMKEEFGRLKEALEKSEARRKELEEKMVSLLQekndlqlqvQAEQDNLADAEERCDQlIKNKIQLEAKVK 920
Cdd:PTZ00121 1177 KAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEAR---------KAEDAKKAEAVKKAEE-AKKDAEEAKKAE 1246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 921 EMTERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLEltlaKVEKEKHATENKVknlTEEMAGLDEIIAKLTKEKKA-- 998
Cdd:PTZ00121 1247 EERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELK----KAEEKKKADEAKK---AEEKKKADEAKKKAEEAKKAde 1319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 999 ----LQEAHQQALDDLQAEEDKVNTLTKAKVKLEQHVDDLEGSLEQEKKVRMDLERAKRKLEgDLKLTQESIMDLENDKQ 1074
Cdd:PTZ00121 1320 akkkAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAD-AAKKKAEEKKKADEAKK 1398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1075 QLDERLKKKDfELNalnaRIEDEQALGSQLQKKLKELQarieeleeeleaertaRAKVEKLRSDLSRELEEISERLEEAG 1154
Cdd:PTZ00121 1399 KAEEDKKKAD-ELK----KAAAAKKKADEAKKKAEEKK----------------KADEAKKKAEEAKKADEAKKKAEEAK 1457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1155 GATSVQIEMNKKREAEfqKMRRDLEEATLQHEATAAALR-KKHADSVAELSEQIDNLQRVKQKLEKEKSEfKLELDDVTS 1233
Cdd:PTZ00121 1458 KAEEAKKKAEEAKKAD--EAKKKAEEAKKADEAKKKAEEaKKKADEAKKAAEAKKKADEAKKAEEAKKAD-EAKKAEEAK 1534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1234 NMEQIIKA--KANLEKMCRTLEDQMNEHRSKAEETQRSvndltSQRAKLQTENGELSRQLDEKEaLISQLTRGKLTYTQQ 1311
Cdd:PTZ00121 1535 KADEAKKAeeKKKADELKKAEELKKAEEKKKAEEAKKA-----EEDKNMALRKAEEAKKAEEAR-IEEVMKLYEEEKKMK 1608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1312 LEDLKRQLEEEVKAKNalAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAiQRTEEL----E 1387
Cdd:PTZ00121 1609 AEEAKKAEEAKIKAEE--LKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK-KKAEEAkkaeE 1685
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1388 EAKKKLAQRLQDAEEA--VEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSnaaaaaldKKQRNFDKILAEWKQKYEESQS 1465
Cdd:PTZ00121 1686 DEKKAAEALKKEAEEAkkAEELKKKEAEEKKKAEELKKAEEENKIKAEEA--------KKEAEEDKKKAEEAKKDEEEKK 1757
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1466 ELESSQKEARSLSTELFKLKNAY--EESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKLE---- 1539
Cdd:PTZ00121 1758 KIAHLKKEEEKKAEEIRKEKEAVieEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKevad 1837
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1540 -LQSALEEAEASLEHEEGK------------------ILRAQLEFNQIKAEMERKLAEKDEEMEQAKRNHL-RVVDSLQT 1599
Cdd:PTZ00121 1838 sKNMQLEEADAFEKHKFNKnnengedgnkeadfnkekDLKEDDEEEIEEADEIEKIDKDDIEREIPNNNMAgKNNDIIDD 1917
|
810
....*....|....*....
gi 1387193866 1600 SLDAETRSRNEALRVKKKM 1618
Cdd:PTZ00121 1918 KLDKDEYIKRDAEETREEI 1936
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
931-1785 |
1.73e-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: 1.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 931 EMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDL 1010
Cdd:pfam02463 166 RLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1011 QAEEDKVNTLTKAKVKLEQHvddlegSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNAL 1090
Cdd:pfam02463 246 LRDEQEEIESSKQEIEKEEE------KLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKES 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1091 NARIEdeqalgsQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAE 1170
Cdd:pfam02463 320 EKEKK-------KAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1171 FQKM----------RRDLEEATLQHEATAAALRKKHADSVAELSEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIK 1240
Cdd:pfam02463 393 KEEElelkseeekeAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSED 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1241 AKANLEKMCRTLEDQMNEHRSKAEEtqrsvnDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLE 1320
Cdd:pfam02463 473 LLKETQLVKLQEQLELLLSRQKLEE------RSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAIS 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1321 EEVKAKNALAHAlqsarhDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDA 1400
Cdd:pfam02463 547 TAVIVEVSATAD------EVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDK 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1401 EEAVEAVNAKCSSLEKTKHRLQNEIEDLM--VDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLS 1478
Cdd:pfam02463 621 RAKVVEGILKDTELTKLKESAKAKESGLRkgVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLE 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1479 TELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKLELQSALEEAEASLEHEEGKI 1558
Cdd:pfam02463 701 IKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEER 780
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1559 LRAQLEFNQIKAEMERKLAEKDEEMEQAKRNH----LRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQlsHANR 1634
Cdd:pfam02463 781 EKTEKLKVEEEKEEKLKAQEEELRALEEELKEeaelLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEE--ELER 858
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1635 LAAEAQKQVKSLQSLLKDTQIQLDDAVRanddlkENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQ 1714
Cdd:pfam02463 859 LEEEITKEELLQELLLKEEELEEQKLKD------ELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLK 932
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387193866 1715 LLHSQNTSLINQKKKMEADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKN 1785
Cdd:pfam02463 933 YEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEE 1003
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
839-1600 |
9.96e-16 |
|
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: 83.48 E-value: 9.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 839 LLKSAETEKEIALMKEEFGRLKEALEKSEARRKELEEKMvsllqekNDLQLQVQAEQDnlaDAEERCDQLIKNKIQLEAK 918
Cdd:TIGR00618 158 LKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKA-------ELLTLRSQLLTL---CTPCMPDTYHERKQVLEKE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 919 VKEMTERLEDEEEMNAELTAK------KRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKnlteemagldeiIAKL 992
Cdd:TIGR00618 228 LKHLREALQQTQQSHAYLTQKreaqeeQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARK------------AAPL 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 993 TKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQHVDDlEGSLEQEKKVRMDLERAKRKLEgDLKLTQESIMDLEND 1072
Cdd:TIGR00618 296 AAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQ-QSSIEEQRRLLQTLHSQEIHIR-DAHEVATSIREISCQ 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1073 KQQLDERLKKKDFELNALnariEDEQALGSQLQKKLKELQARIEELEEELEAERtarakVEKLRSDLSRELEEISERLEE 1152
Cdd:TIGR00618 374 QHTLTQHIHTLQQQKTTL----TQKLQSLCKELDILQREQATIDTRTSAFRDLQ-----GQLAHAKKQQELQQRYAELCA 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1153 AGGATSVQIEmnKKREAEFQKMRRDLEEATlQHEATAAALRKKHADSVAELSEQIDNLQRVKQKLEKEKSEFKLELDDV- 1231
Cdd:TIGR00618 445 AAITCTAQCE--KLEKIHLQESAQSLKERE-QQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDId 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1232 -----TSNMEQII-------KAKANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALIS 1299
Cdd:TIGR00618 522 npgplTRRMQRGEqtyaqleTSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTE 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1300 QLTRGKLTYTQQLEDLKRQLEEEvkaknalAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDA 1379
Cdd:TIGR00618 602 KLSEAEDMLACEQHALLRKLQPE-------QDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKEL 674
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1380 IQRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLE-------KTKHRLQNEIEDLMVDVERSNAAAAALDKK------- 1445
Cdd:TIGR00618 675 LASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELEthieeydREFNEIENASSSLGSDLAAREDALNQSLKElmhqart 754
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1446 ---------QRNFDKILAEWK--QKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKR-ENKNLQEEISDLT 1513
Cdd:TIGR00618 755 vlkarteahFNNNEEVTAALQtgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNlQCETLVQEEEQFL 834
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1514 EQLGSSGKTIHELEKVRKQLEAEKLELQSALEEaEASLEHEEGKILRAQLEFNQIKAEMERKLAEK-------DEEMEQA 1586
Cdd:TIGR00618 835 SRLEEKSATLGEITHQLLKYEECSKQLAQLTQE-QAKIIQLSDKLNGINQIKIQFDGDALIKFLHEitlyanvRLANQSE 913
|
810
....*....|....
gi 1387193866 1587 KRNHLRVVDSLQTS 1600
Cdd:TIGR00618 914 GRFHGRYADSHVNA 927
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
858-1553 |
1.48e-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: 82.76 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 858 RLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLiKNKIQ-LEAKVKEMTERLEDEEEMNAEL 936
Cdd:TIGR04523 23 GYKNIANKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNS-NNKIKiLEQQIKDLNDKLKKNKDKINKL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 937 TAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATE-------NKVKNLTEEMAGLDEIIAKLTKEKKALqeahqqaldd 1009
Cdd:TIGR04523 102 NSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKknidkflTEIKKKEKELEKLNNKYNDLKKQKEEL---------- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1010 lqaeEDKVNTLTKAKVKLEQHVDDLEGSLEQEKKVRMDLErakrKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNA 1089
Cdd:TIGR04523 172 ----ENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLK----KKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1090 LNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEaggatsvqiEMNKKREA 1169
Cdd:TIGR04523 244 KTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQ---------DWNKELKS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1170 EFQKMRRDLEEATLQheataaalRKKHADSVAELSEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKMC 1249
Cdd:TIGR04523 315 ELKNQEKKLEEIQNQ--------ISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEI 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1250 RTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLtrgkltyTQQLEDLKRQLEEEVKAKNAL 1329
Cdd:TIGR04523 387 KNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKN-------NSEIKDLTNQDSVKELIIKNL 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1330 AHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVaqwrtkyetdaiqrtEELEEAKKKLAQRLQDAEEAVEAVNA 1409
Cdd:TIGR04523 460 DNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKEL---------------KKLNEEKKELEEKVKDLTKKISSLKE 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1410 KCSSLEKTKHRLQNEIEDLMVDVER--SNAAAAALDKKQRNFDKILAEWKQKYEesqselessqkearslstelfKLKNA 1487
Cdd:TIGR04523 525 KIEKLESEKKEKESKISDLEDELNKddFELKKENLEKEIDEKNKEIEELKQTQK---------------------SLKKK 583
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387193866 1488 YEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKLELQSALEEAEASLEH 1553
Cdd:TIGR04523 584 QEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQ 649
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1270-1927 |
1.62e-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: 82.81 E-value: 1.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1270 VNDLTSQRAKLQTENGELSRQLDEKEALISQLTrgkltytQQLEDLKRQLEEEVKAKN-----------ALAHALQSARH 1338
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKR-------QQLERLRREREKAERYQAllkekreyegyELLKEKEALER 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1339 DCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTK 1418
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKEREL 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1419 HRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETF 1498
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1499 KRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEMERKLAE 1578
Cdd:TIGR02169 398 KREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEE 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1579 KD---EEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEG------DLNEME------IQLSHANRL-------- 1635
Cdd:TIGR02169 478 YDrveKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGvhgtvaQLGSVGeryataIEVAAGNRLnnvvvedd 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1636 --AAEAQKQVKS-------------LQSLLKDTQIQLDDAVRAN-------DDLKENIAIVERRNNLLQAELEELRAVVE 1693
Cdd:TIGR02169 558 avAKEAIELLKRrkagratflplnkMRDERRDLSILSEDGVIGFavdlvefDPKYEPAFKYVFGDTLVVEDIEAARRLMG 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1694 Q----------------------TERSRKL----AEQELIETSERVQLLHSQNTSLINQKKKMEADLSQLQTEVEEAVQE 1747
Cdd:TIGR02169 638 KyrmvtlegelfeksgamtggsrAPRGGILfsrsEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRK 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1748 CRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQiALKGGKKQLQKLEAR-----VREL 1822
Cdd:TIGR02169 718 IGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEE-DLHKLEEALNDLEARlshsrIPEI 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1823 ENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHE 1902
Cdd:TIGR02169 797 QAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAA 876
|
730 740
....*....|....*....|....*
gi 1387193866 1903 LDEAEERADIAESQVNKLRAKSRDI 1927
Cdd:TIGR02169 877 LRDLESRLGDLKKERDELEAQLREL 901
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1258-1840 |
1.68e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 82.78 E-value: 1.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1258 EHRSKAEETQRSVNDLTSQRaklQTENGELSRQLDEKEA--LISQLTRgkltytqqLEDLKRQLEEEVKAKNALAHALQS 1335
Cdd:PRK02224 166 EYRERASDARLGVERVLSDQ---RGSLDQLKAQIEEKEEkdLHERLNG--------LESELAELDEEIERYEEQREQARE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1336 ARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYET------DAIQRTEELEEAKKKLAQRLQDAEEAVEAVNA 1409
Cdd:PRK02224 235 TRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREElaeevrDLRERLEELEEERDDLLAEAGLDDADAEAVEA 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1410 KCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQkyeesqselessqkEARSLSTELfklknayE 1489
Cdd:PRK02224 315 RREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELRE--------------EAAELESEL-------E 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1490 ESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKLELQSALEEAEASLEHEEGKILRAQLEFNQIK 1569
Cdd:PRK02224 374 EAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGK 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1570 -----------------AEMERKLAEKDEEMEQAKRNHLRVVDSLQTSLDA-ETRSRNEALRVKKKMEGDLNEMEIQLSH 1631
Cdd:PRK02224 454 cpecgqpvegsphvetiEEDRERVEELEAELEDLEEEVEEVEERLERAEDLvEAEDRIERLEERREDLEELIAERRETIE 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1632 ANRLAAEA-QKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERsRKLAEQELIETS 1710
Cdd:PRK02224 534 EKRERAEElRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAA-IADAEDEIERLR 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1711 ERVQLLHSQNTSLINQKKKMEADLSQLQTEVEEA-VQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQT 1789
Cdd:PRK02224 613 EKREALAELNDERRERLAEKRERKRELEAEFDEArIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEE 692
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1387193866 1790 IKDLQHRLDeaeqiALKGGKKQLQKLEARVRELEN---ELEAE-QKRNAESVKGM 1840
Cdd:PRK02224 693 LEELRERRE-----ALENRVEALEALYDEAEELESmygDLRAElRQRNVETLERM 742
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
848-1729 |
2.03e-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: 82.71 E-value: 2.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 848 EIALMKEEFGRLKEALEKsearRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERcdQLIKNKIQLEAKVKEMTERLE 927
Cdd:pfam02463 160 EEAAGSRLKRKKKEALKK----LIEETENLAELIIDLEELKLQELKLKEQAKKALEY--YQLKEKLELEEEYLLYLDYLK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 928 DEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQAL 1007
Cdd:pfam02463 234 LNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1008 DDLQAEEDKVNTLTKAKVKLEQHVDDLEGSLEQEKKVRMDLERAKRKLEgdlkltqesiMDLENDKQQLDERLKKKDFEL 1087
Cdd:pfam02463 314 EKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELE----------KLQEKLEQLEEELLAKKKLES 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1088 NALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKR 1167
Cdd:pfam02463 384 ERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKD 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1168 EAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELSEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEK 1247
Cdd:pfam02463 464 ELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKV 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1248 MCRTLEDQMNEhrskaeetqrSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVKAKN 1327
Cdd:pfam02463 544 AISTAVIVEVS----------ATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATL 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1328 ALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQrTEELEEAKKKLAQRLQDAEEAVEAV 1407
Cdd:pfam02463 614 EADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKAS-LSELTKELLEIQELQEKAESELAKE 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1408 NAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNa 1487
Cdd:pfam02463 693 EILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSL- 771
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1488 YEESLEHLETFKRENKNLQEEISDLTEQLGSsgktihELEKVRKQLEAEKLELQSALEEAEASLEHEEGKILRAQLEFNQ 1567
Cdd:pfam02463 772 KEKELAEEREKTEKLKVEEEKEEKLKAQEEE------LRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEE 845
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1568 IKAEMERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEgdLNEMEIQLSHANRLAAEAQKQVKSLQ 1647
Cdd:pfam02463 846 QKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKE--EKKELEEESQKLNLLEEKENEIEERI 923
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1648 SLLKDTQIQLDDaVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQ--ELIETSERVQLLHSQNTSLIN 1725
Cdd:pfam02463 924 KEEAEILLKYEE-EPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAieEFEEKEERYNKDELEKERLEE 1002
|
....
gi 1387193866 1726 QKKK 1729
Cdd:pfam02463 1003 EKKK 1006
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
840-1424 |
5.21e-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: 5.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 840 LKSAETEKEIALMKEEFGRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNladAEERCDQLIKNKIQLEAKV 919
Cdd:pfam15921 250 LKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQ---ARNQNSMYMRQLSDLESTV 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 920 kemterledeEEMNAELTAKKRKLEDECSELKRD--IDDLELTLAKVEKEKHATENkvKNLTEEmagLDEIIAKLTKEKK 997
Cdd:pfam15921 327 ----------SQLRSELREAKRMYEDKIEELEKQlvLANSELTEARTERDQFSQES--GNLDDQ---LQKLLADLHKREK 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 998 ALQEAHQQ--------------------ALDDLQAEEDKVNTLTKA-----KVKLEQHVDDLEG---SLEQEKKVRMDLE 1049
Cdd:pfam15921 392 ELSLEKEQnkrlwdrdtgnsitidhlrrELDDRNMEVQRLEALLKAmksecQGQMERQMAAIQGkneSLEKVSSLTAQLE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1050 RAKRKLEGDLKLTQESIMDLENDKQ---QLDERLKKKDFELNALNARIedeQALGSQLQKKLKELQ------ARIEELEE 1120
Cdd:pfam15921 472 STKEMLRKVVEELTAKKMTLESSERtvsDLTASLQEKERAIEATNAEI---TKLRSRVDLKLQELQhlknegDHLRNVQT 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1121 ELEAERTARAKVEKLRSDLSRELEEISERLEEAG-GATSVQIEmNKKREAEFQKMRRDLEEATLqheataaaLRKKHADS 1199
Cdd:pfam15921 549 ECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGrTAGAMQVE-KAQLEKEINDRRLELQEFKI--------LKDKKDAK 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1200 VAELSEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIK----AKANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTS 1275
Cdd:pfam15921 620 IRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNevktSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKM 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1276 QRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVKAKNALAHALQSARHDCDLLReqyEEETEAKA 1355
Cdd:pfam15921 700 QLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLK---EEKNKLSQ 776
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387193866 1356 ELQRVLSKANSEVAQwrtkyetdaiqrTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNE 1424
Cdd:pfam15921 777 ELSTVATEKNKMAGE------------LEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQE 833
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
840-1414 |
5.93e-15 |
|
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: 80.99 E-value: 5.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 840 LKSAETEKEIALMKEEFGRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKV 919
Cdd:pfam01576 419 ARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDER 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 920 KEMTERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKAL 999
Cdd:pfam01576 499 NSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRL 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1000 QEAHQQALDDLQAEEDKVNTLTKAKVKLEQ-------------------------------------------------- 1029
Cdd:pfam01576 579 QQELDDLLVDLDHQRQLVSNLEKKQKKFDQmlaeekaisaryaeerdraeaeareketralslaraleealeakeelert 658
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1030 ------HVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNALNARIE-DEQALGS 1102
Cdd:pfam01576 659 nkqlraEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFErDLQARDE 738
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1103 QLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEA- 1181
Cdd:pfam01576 739 QGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEAr 818
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1182 -------------------------TLQHEATAAALRKKHADSVA-ELSEQIDN-------LQRVKQKLEKEKSEFKLEL 1228
Cdd:pfam01576 819 asrdeilaqskesekklknleaellQLQEDLAASERARRQAQQERdELADEIASgasgksaLQDEKRRLEARIAQLEEEL 898
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1229 DDVTSNMEQIIKAKANLEKMCRTLEDQMNEHRSKAEETQrsvndltSQRAKLQTENGELSRQLDEKEALI-SQLTRGKLT 1307
Cdd:pfam01576 899 EEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSE-------SARQQLERQNKELKAKLQEMEGTVkSKFKSSIAA 971
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1308 YTQQLEDLKRQLEEEVKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYEtDAIQRTEELE 1387
Cdd:pfam01576 972 LEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE-EAEEEASRAN 1050
|
650 660
....*....|....*....|....*..
gi 1387193866 1388 EAKKKLAQRLQDAEEAVEAVNAKCSSL 1414
Cdd:pfam01576 1051 AARRKLQRELDDATESNESMNREVSTL 1077
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1174-1697 |
6.55e-15 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 81.11 E-value: 6.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1174 MRRDLEEATLQHEATAAAlrKKHADSVAELSEQIDNLQRVKQKLEKEKSEFKLELDDvtsnmEQIIKAKANLEKmcrtLE 1253
Cdd:COG4913 240 AHEALEDAREQIELLEPI--RELAERYAAARERLAELEYLRAALRLWFAQRRLELLE-----AELEELRAELAR----LE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1254 DQMNEHRSKAEETQRSVNDLTSQRAKLQTEN-GELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVKAKNALAHA 1332
Cdd:COG4913 309 AELERLEARLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAE 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1333 LQSARHDCDLLREQYEEeteAKAELQRVLSKANSEVAQWRTkyETDAIQRT-----EELEEAKKKLAQRLQDAEEAVEAV 1407
Cdd:COG4913 389 AAALLEALEEELEALEE---ALAEAEAALRDLRRELRELEA--EIASLERRksnipARLLALRDALAEALGLDEAELPFV 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1408 nakCSSLE-KTKHRL-QNEIE--------DLMVDVERSNAAAAALDK---KQR-NFDKIlaewkqkyEESQSELESSQKE 1473
Cdd:COG4913 464 ---GELIEvRPEEERwRGAIErvlggfalTLLVPPEHYAAALRWVNRlhlRGRlVYERV--------RTGLPDPERPRLD 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1474 ARSLSTELFKLKNAYEESLEHL-------------ETFKRENKNLQEE--ISDLTE--------------QLGSSGKT-I 1523
Cdd:COG4913 533 PDSLAGKLDFKPHPFRAWLEAElgrrfdyvcvdspEELRRHPRAITRAgqVKGNGTrhekddrrrirsryVLGFDNRAkL 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1524 HELEKVRKQLEAEKLELQSALEEAEASLEHEEGKILR----AQLEFNQIK-AEMERKLAEKDEEMEQAKRNHlRVVDSLQ 1598
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREAlqrlAEYSWDEIDvASAEREIAELEAELERLDASS-DDLAALE 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1599 TSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRLAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRn 1678
Cdd:COG4913 692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELREN- 770
|
570
....*....|....*....
gi 1387193866 1679 nlLQAELEELRAVVEQTER 1697
Cdd:COG4913 771 --LEERIDALRARLNRAEE 787
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
939-1570 |
9.83e-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: 80.06 E-value: 9.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 939 KKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLD----EIIAKLTKEKKALQEAHQqaldDLQAEE 1014
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEqqikDLNDKLKKNKDKINKLNS----DLSKIN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1015 DKVNTLTKAKVKLEQHVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNALNARI 1094
Cdd:TIGR04523 110 SEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1095 EDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISErLEEAGGATSVQIEMNKKreaEFQKM 1174
Cdd:TIGR04523 190 DKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINE-KTTEISNTQTQLNQLKD---EQNKI 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1175 RRDLEEATLQHEATAAALRkkhadsvaELSEQIDNLQRVKQKLEKEKSEfkleldDVTSNMEQIIKakaNLEKMCRTLED 1254
Cdd:TIGR04523 266 KKQLSEKQKELEQNNKKIK--------ELEKQLNQLKSEISDLNNQKEQ------DWNKELKSELK---NQEKKLEEIQN 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1255 QMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLE-------DLKRQLEEEVKAKN 1327
Cdd:TIGR04523 329 QISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKnlesqinDLESKIQNQEKLNQ 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1328 ALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYE------TDAIQRTEELEEAKKKLAQRLQDAE 1401
Cdd:TIGR04523 409 QKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKnldntrESLETQLKVLSRSINKIKQNLEQKQ 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1402 EAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQ--KEARSLST 1479
Cdd:TIGR04523 489 KELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENleKEIDEKNK 568
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1480 ELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKLELQSALEEAEASLEHEEGKIL 1559
Cdd:TIGR04523 569 EIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVK 648
|
650
....*....|.
gi 1387193866 1560 RAQLEFNQIKA 1570
Cdd:TIGR04523 649 QIKETIKEIRN 659
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
962-1428 |
4.27e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 78.16 E-value: 4.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 962 AKVEKEKHAT----ENKVKNLTEEMAGLDE--IIAKLTKEKKALQ-EAHQQALDDLQAEEDKVNTLTKAKVKLEQHVDDL 1034
Cdd:PRK02224 198 EKEEKDLHERlnglESELAELDEEIERYEEqrEQARETRDEADEVlEEHEERREELETLEAEIEDLRETIAETEREREEL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1035 EGSLEQEKKVRMDLERAKRKLEGDLKLT-------QESIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKK 1107
Cdd:PRK02224 278 AEEVRDLRERLEELEEERDDLLAEAGLDdadaeavEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEER 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1108 LKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEA----GGATSVQIEMN------KKREAEFQKMRRD 1177
Cdd:PRK02224 358 AEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDApvdlGNAEDFLEELReerdelREREAELEATLRT 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1178 LEEATLQHEATAAALR----------KKHADSVAELSEQIDnlqrvkqKLEKEKSEFKLELDDVTSNMEQIIKAKA---- 1243
Cdd:PRK02224 438 ARERVEEAEALLEAGKcpecgqpvegSPHVETIEEDRERVE-------ELEAELEDLEEEVEEVEERLERAEDLVEaedr 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1244 --NLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTEnGELSRQLDEKEALISQLTRGKL-TYTQQLEDLKRQLE 1320
Cdd:PRK02224 511 ieRLEERREDLEELIAERRETIEEKRERAEELRERAAELEAE-AEEKREAAAEAEEEAEEAREEVaELNSKLAELKERIE 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1321 EEVKAKNALAhALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIqrtEELEEAKKKLAQRLQDA 1400
Cdd:PRK02224 590 SLERIRTLLA-AIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARI---EEAREDKERAEEYLEQV 665
|
490 500
....*....|....*....|....*...
gi 1387193866 1401 EEAVEAVNAKCSSLEKTKHRLQNEIEDL 1428
Cdd:PRK02224 666 EEKLDELREERDDLQAEIGAVENELEEL 693
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
32-76 |
4.54e-14 |
|
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: 67.84 E-value: 4.54e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1387193866 32 DLKKDVFVPDDKEEFVKATILSREGGKVTAETEHGKTVTVKEDQV 76
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVETEDGKTVTVKKDDV 45
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
940-1574 |
6.38e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 77.65 E-value: 6.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 940 KRKLEDECSELKRDIDDLELTLAKVEKEKHATE--NKVKNLTEEMAGLDEIIAKLTKEKKALQ-EAHQQALDDLQAEEDK 1016
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALEDAREQIEllEPIRELAERYAAARERLAELEYLRAALRlWFAQRRLELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1017 vntLTKAKVKLEQHVDDLEGSLEQEKKVRMDLERAKRKLEGD-LKLTQESIMDLENDKQQLDERLKKKDFELNALNARIE 1095
Cdd:COG4913 300 ---LRAELARLEAELERLEARLDALREELDELEAQIRGNGGDrLEQLEREIERLERELEERERRRARLEALLAALGLPLP 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1096 DEQAlgsQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEaggatsvqIEMNKKR-EAEFQKM 1174
Cdd:COG4913 377 ASAE---EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS--------LERRKSNiPARLLAL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1175 RRDLEEATLQHEA-------------------TAA--ALR---------KKHADSVAELSEQID-----NLQRVKQKLEK 1219
Cdd:COG4913 446 RDALAEALGLDEAelpfvgelievrpeeerwrGAIerVLGgfaltllvpPEHYAAALRWVNRLHlrgrlVYERVRTGLPD 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1220 EKSEF--------KLELDD--VTSNMEQIIKAKANLEKmCRTLEDQMNEHRS-------KAEETQRSVNDLTSQRAKLQT 1282
Cdd:COG4913 526 PERPRldpdslagKLDFKPhpFRAWLEAELGRRFDYVC-VDSPEELRRHPRAitragqvKGNGTRHEKDDRRRIRSRYVL 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1283 --ENGelsRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVKAKNALAHALQSARHDCDLLREQyEEETEAKAELQRv 1360
Cdd:COG4913 605 gfDNR---AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAE-REIAELEAELER- 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1361 LSKANSEVaqwrtkyetdaiqrtEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVErsnaAAA 1440
Cdd:COG4913 680 LDASSDDL---------------AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE----AAE 740
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1441 ALDKKQRNFDkiLAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNlqeEISDLTEQLGSsg 1520
Cdd:COG4913 741 DLARLELRAL--LEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPA---ETADLDADLES-- 813
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 1387193866 1521 ktIHELEKVRKQLEAEKL-ELQSALEEAEASLEHEEGKILRAQL--EFNQIKAEMER 1574
Cdd:COG4913 814 --LPEYLALLDRLEEDGLpEYEERFKELLNENSIEFVADLLSKLrrAIREIKERIDP 868
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
851-1516 |
6.55e-14 |
|
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: 77.45 E-value: 6.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 851 LMKEEFGRLKEALEKSEARRKELEEKMVSLlqeKNDLQLQVQAEQDNLADAEercdqliKNKIQLEAKVKEMTERLED-E 929
Cdd:pfam05483 159 LLKETCARSAEKTKKYEYEREETRQVYMDL---NNNIEKMILAFEELRVQAE-------NARLEMHFKLKEDHEKIQHlE 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 930 EEMNAELTAKKRK---LEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQA 1006
Cdd:pfam05483 229 EEYKKEINDKEKQvslLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRS 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1007 LDDLQAEEDKVNTLTKAKVKL----EQHVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKK 1082
Cdd:pfam05483 309 MSTQKALEEDLQIATKTICQLteekEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1083 KDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISErLEEAGGATSVQIE 1162
Cdd:pfam05483 389 KSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHD-LEIQLTAIKTSEE 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1163 MNKKreaEFQKMRRDLEEATLQHeataaalrkkhadsvAELSEQIDNLQRVKQKLEKEKSEFKLELDDvtsNMEQIIKAK 1242
Cdd:pfam05483 468 HYLK---EVEDLKTELEKEKLKN---------------IELTAHCDKLLLENKELTQEASDMTLELKK---HQEDIINCK 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1243 ANLEKMCRTLEDqmnehrskAEETQRSV-NDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQ--- 1318
Cdd:pfam05483 527 KQEERMLKQIEN--------LEEKEMNLrDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKcnn 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1319 LEEEVKAKNALAHALQsarHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQ 1398
Cdd:pfam05483 599 LKKQIENKNKNIEELH---QENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLE 675
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1399 DAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMvdversnaaaAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLS 1478
Cdd:pfam05483 676 EVEKAKAIADEAVKLQKEIDKRCQHKIAEMV----------ALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALE 745
|
650 660 670
....*....|....*....|....*....|....*...
gi 1387193866 1479 TELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQL 1516
Cdd:pfam05483 746 IELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAIL 783
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1053-1800 |
6.92e-14 |
|
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: 77.37 E-value: 6.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1053 RKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKelqarieeleeeleaerTARAKV 1132
Cdd:TIGR04523 36 KQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLK-----------------KNKDKI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1133 EKLRSDLSRELEEISERLEEaggatsvqieMNKKrEAEFQKMRRDLEEATLQHEATAAALRKKHADsVAELSEQIDNLQR 1212
Cdd:TIGR04523 99 NKLNSDLSKINSEIKNDKEQ----------KNKL-EVELNKLEKQKKENKKNIDKFLTEIKKKEKE-LEKLNNKYNDLKK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1213 VKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKMCRTLEDQMNEHRSkaeetqrsvndLTSQRAKLQTENGELSRQLD 1292
Cdd:TIGR04523 167 QKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKS-----------LESQISELKKQNNQLKDNIE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1293 EKEALISQLTRGKLTYTQQLEDLKRQLEEEVKAknalahaLQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQ-W 1371
Cdd:TIGR04523 236 KKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQ-------LSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQdW 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1372 RTKYETDAIQRTEELEEAKKKLAQrlqdAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDK 1451
Cdd:TIGR04523 309 NKELKSELKNQEKKLEEIQNQISQ----NNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1452 ILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQlgssgktIHELEKVRK 1531
Cdd:TIGR04523 385 EIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQ-------DSVKELIIK 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1532 QLEAEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEMErKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEA 1611
Cdd:TIGR04523 458 NLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELK-KLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEK 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1612 LRVKKKMEGDLNEMEIQLSHANrLAAEAQKQVKSLqSLLKDTQIQLDdavRANDDLKENIAIVERRNNLLQAELEELRAV 1691
Cdd:TIGR04523 537 ESKISDLEDELNKDDFELKKEN-LEKEIDEKNKEI-EELKQTQKSLK---KKQEEKQELIDQKEKEKKDLIKEIEEKEKK 611
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1692 VEQTERSRKLAEQELIEtservqlLHSQNTSLINQKKKMEADLSQLQTEVEEAVQECRNAEEKAKKAIT----------- 1760
Cdd:TIGR04523 612 ISSLEKELEKAKKENEK-------LSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTkiddiielmkd 684
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1761 --------------------DAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEA 1800
Cdd:TIGR04523 685 wlkelslhykkyitrmirikDLPKLEEKYKEIEKELKKLDEFSKELENIIKNFNKKFDDA 744
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1516-1872 |
9.12e-14 |
|
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: 77.40 E-value: 9.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1516 LGSSGKTIHELEKVRKQLEAEKLELQSALEEAeasleheeGKILRaqleFNQIKAEMERKLAEKDEEMEQAKRNhLRVVD 1595
Cdd:TIGR02168 133 LGKRSYSIIEQGKISEIIEAKPEERRAIFEEA--------AGISK----YKERRKETERKLERTRENLDRLEDI-LNELE 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1596 SLQTSLDAETRSRNEALRVKKKME--------GDLNEMEIQLSHANRLAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDL 1667
Cdd:TIGR02168 200 RQLKSLERQAEKAERYKELKAELRelelallvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSEL 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1668 KENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMEADLSQLQTEVE---EA 1744
Cdd:TIGR02168 280 EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELEsleAE 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1745 VQECRNAEEKAKKAITD--------AAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLE 1816
Cdd:TIGR02168 360 LEELEAELEELESRLEEleeqletlRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQ 439
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1387193866 1817 ARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQ 1872
Cdd:TIGR02168 440 AELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLE 495
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1077-1923 |
9.73e-14 |
|
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: 77.32 E-value: 9.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1077 DERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEEleaertARAKVEKLRSDLSRELEEISERLEEAGGA 1156
Cdd:pfam02463 152 PERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELK------LQELKLKEQAKKALEYYQLKEKLELEEEY 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1157 TSVQIEMnkKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELSEQIDNLQRVKQKLEKEKSEFKLELDDVTSNME 1236
Cdd:pfam02463 226 LLYLDYL--KLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1237 Q-------IIKAKANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYT 1309
Cdd:pfam02463 304 KlerrkvdDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLES 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1310 QQLEDLKRQLEEEvkaknaLAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEA 1389
Cdd:pfam02463 384 ERLSSAAKLKEEE------LELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQE 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1390 KKKLAQRLQDAEEAVEAVNAKCsSLEKTKHRLQNEIEDLMVDVERSNAA---AAALDKKQRNFDKILAEWKQKYEESQSE 1466
Cdd:pfam02463 458 LKLLKDELELKKSEDLLKETQL-VKLQEQLELLLSRQKLEERSQKESKArsgLKVLLALIKDGVGGRIISAHGRLGDLGV 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1467 LESSQKEARSLST-ELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKLElqsalE 1545
Cdd:pfam02463 537 AVENYKVAISTAViVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDK-----A 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1546 EAEASLEHEEGKILRAQLEFNQIKAEMERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEM 1625
Cdd:pfam02463 612 TLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAK 691
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1626 EIQLSHANRLAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIV---ERRNNLLQAELEELRAVVEQTERSRKLA 1702
Cdd:pfam02463 692 EEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLlkqKIDEEEEEEEKSRLKKEEKEEEKSELSL 771
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1703 EQELIETSERVQLLHSQNTSLINQKKKMEADLSQLQTEVEEAVQECRNAEEKAKKA----ITDAAMMAEELKKEQDTSAH 1778
Cdd:pfam02463 772 KEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEekikEEELEELALELKEEQKLEKL 851
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1779 LE---RMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTE 1855
Cdd:pfam02463 852 AEeelERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILL 931
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387193866 1856 EDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAK 1923
Cdd:pfam02463 932 KYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKER 999
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
835-1385 |
1.33e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 76.64 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 835 KIKPLLKSAETEKEIALMKEEFGRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQaeqdNLADAEERCDQLIKNKIQ 914
Cdd:PRK03918 274 EIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK----ELEEKEERLEELKKKLKE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 915 LEAKVKEMTERLEDEEEMNAeLTAKKRKLEDECSELkrDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTK 994
Cdd:PRK03918 350 LEKRLEELEERHELYEEAKA-KKEELERLKKRLTGL--TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKK 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 995 EKKALQEAHQQ--ALDDLQAEEDKVNTLTKAKVKLEQHVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESimDLEND 1072
Cdd:PRK03918 427 AIEELKKAKGKcpVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLK--ELAEQ 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1073 KQQLDERLKKKDFElnalnariedeqalgsQLQKKLKELqarieeleeeleaeRTARAKVEKLRSDLSRELEEIsERLEE 1152
Cdd:PRK03918 505 LKELEEKLKKYNLE----------------ELEKKAEEY--------------EKLKEKLIKLKGEIKSLKKEL-EKLEE 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1153 AggatsvqiemnKKREAEFQKMRRDLEE--ATLQHEataaaLRKKHADSVAELSEQIDNLQRVKQK---LEKEKSEFKLE 1227
Cdd:PRK03918 554 L-----------KKKLAELEKKLDELEEelAELLKE-----LEELGFESVEELEERLKELEPFYNEyleLKDAEKELERE 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1228 LDDVTSNMEQIIKAKANLEKMCRTLEdqmnEHRSKAEETQRSVNDltSQRAKLQTENGELSRQLDEKEALISQLTRGKLT 1307
Cdd:PRK03918 618 EKELKKLEEELDKAFEELAETEKRLE----ELRKELEELEKKYSE--EEYEELREEYLELSRELAGLRAELEELEKRREE 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1308 YTQQLEDLKRQLEEEVKAKNALaHALQSARHDCDLLREQY-----EEETEAKAELQRVLSKANSEVAQwrTKYETDAIQR 1382
Cdd:PRK03918 692 IKKTLEKLKEELEEREKAKKEL-EKLEKALERVEELREKVkkykaLLKERALSKVGEIASEIFEELTE--GKYSGVRVKA 768
|
...
gi 1387193866 1383 TEE 1385
Cdd:PRK03918 769 EEN 771
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1198-1871 |
2.33e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 75.72 E-value: 2.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1198 DSVAELSEQIDNLQRVKQKLEKEKSEFKLeLDDVTSNMEQIIKAKAN---LEKMCRTLEDQMNEHRSKAEETQRSvnDLT 1274
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAREQIEL-LEPIRELAERYAAARERlaeLEYLRAALRLWFAQRRLELLEAELE--ELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1275 SQRAKLQTENGELSRQLDEKEALISQLTRGKLTY-TQQLEDLKRQLEEEVKAKNALAHALQSARHDCDLLREQYEEETEA 1353
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1354 KAELQRVLSKANSEVAQWRTKYE---TDAIQRTEELEEAKKKLAQRLQDAE--------EAVEAVNAKCSSLEKTKHRL- 1421
Cdd:COG4913 382 FAALRAEAAALLEALEEELEALEealAEAEAALRDLRRELRELEAEIASLErrksnipaRLLALRDALAEALGLDEAELp 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1422 ---------------QNEIE--------DLMVDVERSNAAAAALDK---KQR-NFDKIlaewkqkyEESQSELESSQKEA 1474
Cdd:COG4913 462 fvgelievrpeeerwRGAIErvlggfalTLLVPPEHYAAALRWVNRlhlRGRlVYERV--------RTGLPDPERPRLDP 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1475 RSLSTELFKLKNAYEESLEHL-------------ETFKRENKNlqeeisdLTEQ-LGSSGKTIHelEKVRKQLEAEKLEL 1540
Cdd:COG4913 534 DSLAGKLDFKPHPFRAWLEAElgrrfdyvcvdspEELRRHPRA-------ITRAgQVKGNGTRH--EKDDRRRIRSRYVL 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1541 QSaleEAEASLEHEEGKILRAQLEFNQIKAEMErKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRnealrvkkkmeg 1620
Cdd:COG4913 605 GF---DNRAKLAALEAELAELEEELAEAEERLE-ALEAELDALQERREALQRLAEYSWDEIDVASAER------------ 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1621 DLNEMEIQLSHANrlaaEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRK 1700
Cdd:COG4913 669 EIAELEAELERLD----ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAR 744
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1701 LAEQELIEtsERVQLLHSQNT------SLINQKKKMEADLSQLQTEVEEAVQE-CRNAEEKAKKAITDAAMMAEELK--- 1770
Cdd:COG4913 745 LELRALLE--ERFAAALGDAVerelreNLEERIDALRARLNRAEEELERAMRAfNREWPAETADLDADLESLPEYLAlld 822
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1771 --KEQDTSAHLERMK----KNMEQTIKDLQHRLDEAEQIAlkggKKQLQKLEARVRELE-NE-----LEAEQKRNAEsVK 1838
Cdd:COG4913 823 rlEEDGLPEYEERFKellnENSIEFVADLLSKLRRAIREI----KERIDPLNDSLKRIPfGPgrylrLEARPRPDPE-VR 897
|
730 740 750
....*....|....*....|....*....|....*
gi 1387193866 1839 GMRKSERRIKELTYQTEED--RKNLLRLQDLVDKL 1871
Cdd:COG4913 898 EFRQELRAVTSGASLFDEElsEARFAALKRLIERL 932
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1381-1926 |
3.22e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 75.10 E-value: 3.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1381 QRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKhrlqNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKy 1460
Cdd:PRK03918 200 KELEEVLREINEISSELPELREELEKLEKEVKELEELK----EEIEELEKELESLEGSKRKLEEKIRELEERIEELKKE- 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1461 eesqselESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVR---KQLEAEK 1537
Cdd:PRK03918 275 -------IEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEerlEELKKKL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1538 LELQSALEEAEASLE-HEEGKILRAQLEfnQIKAEME----RKLAEKDEEMEQAK---RNHLRVVDSLQTSLDAETRSRN 1609
Cdd:PRK03918 348 KELEKRLEELEERHElYEEAKAKKEELE--RLKKRLTgltpEKLEKELEELEKAKeeiEEEISKITARIGELKKEIKELK 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1610 EALRVKKKMEGD--LNEMEIQLSHANRLAAEAQKQVKSLQSLLKDTQIQLDDAvRANDDLKENIAIVERRNNLLQAELEE 1687
Cdd:PRK03918 426 KAIEELKKAKGKcpVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKL-RKELRELEKVLKKESELIKLKELAEQ 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1688 LRAVVEQTErsrKLAEQELIETSERVQLLHSQNTslinqkkKMEADLSQLQTEVEEAvqecrNAEEKAKKAITDAAMMAE 1767
Cdd:PRK03918 505 LKELEEKLK---KYNLEELEKKAEEYEKLKEKLI-------KLKGEIKSLKKELEKL-----EELKKKLAELEKKLDELE 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1768 ELKKEQdtsahLERMKKNMEQTIKDLQHRLDEAEQ-----IALKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRK 1842
Cdd:PRK03918 570 EELAEL-----LKELEELGFESVEELEERLKELEPfyneyLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEE 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1843 SERRIKELTYQ-TEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERAD---IAESQVN 1918
Cdd:PRK03918 645 LRKELEELEKKySEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEkleKALERVE 724
|
....*...
gi 1387193866 1919 KLRAKSRD 1926
Cdd:PRK03918 725 ELREKVKK 732
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
901-1548 |
3.66e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 75.10 E-value: 3.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 901 AEERCDQLIKNKIQLEAKVKEMTERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTE 980
Cdd:PRK03918 187 RTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 981 EMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLtKAKVKLEQHVDDLE---GSLEQEKKVRMDLERAKRKLEG 1057
Cdd:PRK03918 267 RIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYL-DELREIEKRLSRLEeeiNGIEERIKELEEKEERLEELKK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1058 DLKLTQESIMDLENDKQQLDERLKKKDfELNALNARIEDEQAlgSQLQKKLKELQARIEELEEELEAERTARAKVEKLRS 1137
Cdd:PRK03918 346 KLKELEKRLEELEERHELYEEAKAKKE-ELERLKKRLTGLTP--EKLEKELEELEKAKEEIEEEISKITARIGELKKEIK 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1138 DLSRELEEiserLEEAGGATSVqiemnkkreaefqkMRRDLEEatlqhEATAAALRKKHadsvAELSEQIDNLQRVKQKL 1217
Cdd:PRK03918 423 ELKKAIEE----LKKAKGKCPV--------------CGRELTE-----EHRKELLEEYT----AELKRIEKELKEIEEKE 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1218 EKEKSEFKlELDDVTSNMEQIIKAKANLEKMcRTLEDQMNEHR-SKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEA 1296
Cdd:PRK03918 476 RKLRKELR-ELEKVLKKESELIKLKELAEQL-KELEEKLKKYNlEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1297 LISQLTrgkltytqQLEDLKRQLEEEVKaknalahalqsarhdcDLLREQYEEETEAKAELQRvlskansevaqwrtkye 1376
Cdd:PRK03918 554 LKKKLA--------ELEKKLDELEEELA----------------ELLKELEELGFESVEELEE----------------- 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1377 tdaiqRTEELEEAKKKLaqrlqdaeeaVEAVNAkcsslEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEW 1456
Cdd:PRK03918 593 -----RLKELEPFYNEY----------LELKDA-----EKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEEL 652
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1457 KQKYeeSQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQ---EEISDLTEQLGSSGKTIHELEKVRKQL 1533
Cdd:PRK03918 653 EKKY--SEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKeelEEREKAKKELEKLEKALERVEELREKV 730
|
650
....*....|....*.
gi 1387193866 1534 EAEKLEL-QSALEEAE 1548
Cdd:PRK03918 731 KKYKALLkERALSKVG 746
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1037-1926 |
4.19e-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: 75.08 E-value: 4.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1037 SLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFElNALNARIEDEQALGSQLQKKLKELQARIE 1116
Cdd:TIGR00606 187 ALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESS-REIVKSYENELDPLKNRLKEIEHNLSKIM 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1117 ELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGatsvQIEMNKKREA-EFQKMRRDLEEATLQHEATAAALRKK 1195
Cdd:TIGR00606 266 KLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLN----DLYHNHQRTVrEKERELVDCQRELEKLNKERRLLNQE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1196 HAD-----SVAELSEQIDNLQRVKQKLEKEKSEFKLELD------DVTSNMEQIIK-AKANLEKMCRTLEDQMNEHRSKA 1263
Cdd:TIGR00606 342 KTEllveqGRLQLQADRHQEHIRARDSLIQSLATRLELDgfergpFSERQIKNFHTlVIERQEDEAKTAAQLCADLQSKE 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1264 EETQRSVNDLTSQRAKL----QTENGELSRQLDEKEALISQLTRgkltYTQQLEDLKRQLEEEVKAKNALAHALQSARHD 1339
Cdd:TIGR00606 422 RLKQEQADEIRDEKKGLgrtiELKKEILEKKQEELKFVIKELQQ----LEGSSDRILELDQELRKAERELSKAEKNSLTE 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1340 CDLLREQYEEetEAKAELQRVLSKANSEVAQWRTKYETdaiqRTEELEEAKKKLaqrlqDAEEAVEAVNAKCSS------ 1413
Cdd:TIGR00606 498 TLKKEVKSLQ--NEKADLDRKLRKLDQEMEQLNHHTTT----RTQMEMLTKDKM-----DKDEQIRKIKSRHSDeltsll 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1414 --------LEKTKHRLQNEI---EDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEES-------------QSELES 1469
Cdd:TIGR00606 567 gyfpnkkqLEDWLHSKSKEInqtRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKlfdvcgsqdeesdLERLKE 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1470 SQKEARSLSTELFKLKNAYEESLEHLET------------FKREnKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEK 1537
Cdd:TIGR00606 647 EIEKSSKQRAMLAGATAVYSQFITQLTDenqsccpvcqrvFQTE-AELQEFISDLQSKLRLAPDKLKSTESELKKKEKRR 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1538 LELQSALEEAEASLEHEEGKILRAQLEFNQIKAEMERKLA--EKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVK 1615
Cdd:TIGR00606 726 DEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNdiEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVE 805
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1616 KKMEGDLNEMEiqlshanrlAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRA----V 1691
Cdd:TIGR00606 806 RKIAQQAAKLQ---------GSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSeklqI 876
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1692 VEQTERSRKLAEQeLIETSERVQLLHSQNTSLINQKKKMEADLSQLQTEVEEAVQecrNAEEKAKKAITDAAMMAEELKK 1771
Cdd:TIGR00606 877 GTNLQRRQQFEEQ-LVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELIS---SKETSNKKAQDKVNDIKEKVKN 952
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1772 --------EQDTSAHLERMKKNMEQTIKDLQHRLDEAEQialkggkkQLQKLEARVRELENELEAE--QKRNAESVKGMR 1841
Cdd:TIGR00606 953 ihgymkdiENKIQDGKDDYLKQKETELNTVNAQLEECEK--------HQEKINEDMRLMRQDIDTQkiQERWLQDNLTLR 1024
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1842 KSERRIKELtyqtEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLR 1921
Cdd:TIGR00606 1025 KRENELKEV----EEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAE 1100
|
....*
gi 1387193866 1922 AKSRD 1926
Cdd:TIGR00606 1101 EKYRE 1105
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
843-1599 |
4.42e-13 |
|
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: 75.01 E-value: 4.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 843 AETEKEIALMKEEfgrlkeaLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEM 922
Cdd:pfam02463 275 KEEEKEKKLQEEE-------LKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKEL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 923 TERLEDEEEMNAELTAKKRKLEdecsELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEA 1002
Cdd:pfam02463 348 EIKREAEEEEEEELEKLQEKLE----QLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1003 HQQALDDLQAEEDKVNTLTKAKVKLEQHVDDLEGSLEQEKKVRMDLERAKRKLEgdlKLTQESIMDLENDKQQLDERLKK 1082
Cdd:pfam02463 424 EKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKET---QLVKLQEQLELLLSRQKLEERSQ 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1083 KDFELNALNARIEdeqaLGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIE 1162
Cdd:pfam02463 501 KESKARSGLKVLL----ALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLG 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1163 MNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELSEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAK 1242
Cdd:pfam02463 577 ARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEE 656
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1243 ANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRqldeKEALISQLTRGKLTYTQQLEDLKRQLEEE 1322
Cdd:pfam02463 657 GLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKK----KEQREKEELKKLKLEAEELLADRVQEAQD 732
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1323 VKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTE-----ELEEAKKKLAQRL 1397
Cdd:pfam02463 733 KINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEklkaqEEELRALEEELKE 812
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1398 QDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVErsnaAAAALDKKQRNFDKILAEWK------QKYEESQSELESSQ 1471
Cdd:pfam02463 813 EAELLEEEQLLIEQEEKIKEEELEELALELKEEQKL----EKLAEEELERLEEEITKEELlqelllKEEELEEQKLKDEL 888
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1472 KEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKLELQSALEEAEASL 1551
Cdd:pfam02463 889 ESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLA 968
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 1387193866 1552 EHEEGKILRAQLEFNQIKAEMERKLAEKDEEMEQAKRNHLRVVDSLQT 1599
Cdd:pfam02463 969 KEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETC 1016
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
854-1580 |
5.58e-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: 74.70 E-value: 5.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 854 EEFGRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQ--VQAEQDNLADAEERCDQL----------IKNKIQLEAKVKE 921
Cdd:TIGR00606 319 RELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQadRHQEHIRARDSLIQSLATrleldgfergPFSERQIKNFHTL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 922 MTERLEDEEEMNAELTA--------KKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLT 993
Cdd:TIGR00606 399 VIERQEDEAKTAAQLCAdlqskerlKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQ 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 994 KEKKALQEAhqqaldDLQAEEDKVNTLTKAKVKLEQHVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQesimdlenDK 1073
Cdd:TIGR00606 479 ELRKAEREL------SKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTK--------DK 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1074 QQLDERLKKKDF----ELNALNARIEDEQALGSQLQKKLKE---LQARIEELEEELEAERTARAKVEKLRSDLSRELEEI 1146
Cdd:TIGR00606 545 MDKDEQIRKIKSrhsdELTSLLGYFPNKKQLEDWLHSKSKEinqTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSY 624
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1147 SERLEEAGGATSVQIEMNKKREaEFQKMRRDLE-------------EATLQHEATAAALRKKHADSVAELSEQIDNLQRV 1213
Cdd:TIGR00606 625 EDKLFDVCGSQDEESDLERLKE-EIEKSSKQRAmlagatavysqfiTQLTDENQSCCPVCQRVFQTEAELQEFISDLQSK 703
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1214 KQKLEKEKSEFKLELDDVTSNMEQII----KAKANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSR 1289
Cdd:TIGR00606 704 LRLAPDKLKSTESELKKKEKRRDEMLglapGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEES 783
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1290 QLDEK------EALISQLTRGKLTYTQQLE-----DLKRQLEEEVKAKNALAHALQSARHDCDLLREQYEEETEAKAELQ 1358
Cdd:TIGR00606 784 AKVCLtdvtimERFQMELKDVERKIAQQAAklqgsDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLK 863
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1359 RVLSKANSEVAQWRTkyetdAIQRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAA 1438
Cdd:TIGR00606 864 SKTNELKSEKLQIGT-----NLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKK 938
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1439 AA-ALDKKQRNFDKILAEWK--QKYEESQSELESSQKEarslsTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQ 1515
Cdd:TIGR00606 939 AQdKVNDIKEKVKNIHGYMKdiENKIQDGKDDYLKQKE-----TELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQ 1013
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1516 ---------LGSSGKTIHELEKVRKQLEAEKLELQ--------SALEEAEASLEHEEGKILRAQLEFNQIKAEMERKLAE 1578
Cdd:TIGR00606 1014 erwlqdnltLRKRENELKEVEEELKQHLKEMGQMQvlqmkqehQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELRE 1093
|
..
gi 1387193866 1579 KD 1580
Cdd:TIGR00606 1094 PQ 1095
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
844-1327 |
6.51e-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: 74.29 E-value: 6.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 844 ETEKEIALMKEEFGRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADaeercdqlIKNKI-QLEAKVKEM 922
Cdd:TIGR04523 135 ENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDK--------IKNKLlKLELLLSNL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 923 TERLEDEEEMNAELT---AKKRKLEDECSELKRDIDDLELTLAKVE---------------------KEKHATENKVKNL 978
Cdd:TIGR04523 207 KKKIQKNKSLESQISelkKQNNQLKDNIEKKQQEINEKTTEISNTQtqlnqlkdeqnkikkqlsekqKELEQNNKKIKEL 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 979 TEEMAGLDEIIAKLTKEKKalQEAHQQALDDLQAEEDKVNTLTKAKVKLEQHVDDLEGSLEQEKKVRMDLERAKRKLEGD 1058
Cdd:TIGR04523 287 EKQLNQLKSEISDLNNQKE--QDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRE 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1059 LKLTQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSD 1138
Cdd:TIGR04523 365 LEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1139 LSRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAAL------RKKHADSVAELSEQIDNLQR 1212
Cdd:TIGR04523 445 LTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELkklneeKKELEEKVKDLTKKISSLKE 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1213 VKQKLEKEKSEFKLELDDVTSNmeqIIKAKANLEKmcRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTEngelsrqLD 1292
Cdd:TIGR04523 525 KIEKLESEKKEKESKISDLEDE---LNKDDFELKK--ENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQEL-------ID 592
|
490 500 510
....*....|....*....|....*....|....*
gi 1387193866 1293 EKEALISQLTRGKLTYTQQLEDLKRQLeEEVKAKN 1327
Cdd:TIGR04523 593 QKEKEKKDLIKEIEEKEKKISSLEKEL-EKAKKEN 626
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1253-1925 |
1.92e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 73.25 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1253 EDQMNEHRSKAEETQRSVNDltsQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKrqLEEEVKAKNALAHA 1332
Cdd:PTZ00121 1050 EDIDGNHEGKAEAKAHVGQD---EGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGK--AEEARKAEEAKKKA 1124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1333 LQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKK----KLAQRLQDAEEAVEAVN 1408
Cdd:PTZ00121 1125 EDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKaeevRKAEELRKAEDARKAEA 1204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1409 AKCSSLEKT-----KHRLQNEIEDLM-VDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELF 1482
Cdd:PTZ00121 1205 ARKAEEERKaeearKAEDAKKAEAVKkAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELK 1284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1483 KLknayEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKLELQSALEEAEASLEHEEGKILRAQ 1562
Cdd:PTZ00121 1285 KA----EEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAE 1360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1563 lefnqiKAEMERKLAEKDEEMEQAKRNHLRVvdslqtslDAETRSRNEALRvKKKMEGDLNEMEIQLSHANRLAAEAQKQ 1642
Cdd:PTZ00121 1361 ------AAEEKAEAAEKKKEEAKKKADAAKK--------KAEEKKKADEAK-KKAEEDKKKADELKKAAAAKKKADEAKK 1425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1643 VKSLQSLLKDTQIQLDDAVRAnDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTS 1722
Cdd:PTZ00121 1426 KAEEKKKADEAKKKAEEAKKA-DEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKK 1504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1723 LINQKKKMEadlSQLQTEVEEAVQECRNAEEKAKkaiTDAAMMAEELKKEQDTSAhLERMKKNMEQTIKDLQHRLDEAEQ 1802
Cdd:PTZ00121 1505 AAEAKKKAD---EAKKAEEAKKADEAKKAEEAKK---ADEAKKAEEKKKADELKK-AEELKKAEEKKKAEEAKKAEEDKN 1577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1803 IALKGGKKQLQKLEARVRELENELEAEQKRNAESVKgmRKSERRIK-ELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQ 1881
Cdd:PTZ00121 1578 MALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK--KAEEAKIKaEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKA 1655
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1387193866 1882 AEE----AEEQANTNLSKFRKVQhELDEAEERADIAESQVNKLRAKSR 1925
Cdd:PTZ00121 1656 EEEnkikAAEEAKKAEEDKKKAE-EAKKAEEDEKKAAEALKKEAEEAK 1702
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
890-1209 |
2.15e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 72.64 E-value: 2.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 890 QVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMTERLEDEE--EMNAELTAKKRKLEDECSELKRDIDDLELT---LAKV 964
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAELERLDASsddLAAL 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 965 EKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKvkLEQHVDDLEGSlEQEKKV 1044
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL--LEERFAAALGD-AVEREL 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1045 RMDLERAKRKLEGDLKLTQEsimDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQK-KLKELQARIEELEEele 1123
Cdd:COG4913 768 RENLEERIDALRARLNRAEE---ELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEdGLPEYEERFKELLN--- 841
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1124 aeRTARAKVEKLRSDLSRELEEISERLEEA---------GGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRK 1194
Cdd:COG4913 842 --ENSIEFVADLLSKLRRAIREIKERIDPLndslkripfGPGRYLRLEARPRPDPEVREFRQELRAVTSGASLFDEELSE 919
|
330
....*....|....*
gi 1387193866 1195 KHADSVAELSEQIDN 1209
Cdd:COG4913 920 ARFAALKRLIERLRS 934
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1487-1924 |
2.66e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 72.38 E-value: 2.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1487 AYEESLEHLETfkrenknLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKLELQSALEEAEASLEHEEGKILRAQLEfn 1566
Cdd:PRK02224 245 EHEERREELET-------LEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEAR-- 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1567 qiKAEMERKLAEKDEEMEQAK---RNHLRVVDSLQTSLDaETRSRNEALRVK-KKMEGDLNEMEIQLSHANRLAAEAQKQ 1642
Cdd:PRK02224 316 --REELEDRDEELRDRLEECRvaaQAHNEEAESLREDAD-DLEERAEELREEaAELESELEEAREAVEDRREEIEELEEE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1643 VKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSR---KLAE--QElIETSERVQLLH 1717
Cdd:PRK02224 393 IEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLeagKCPEcgQP-VEGSPHVETIE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1718 SQNtsliNQKKKMEADLSQLQTEVEEAvqecrnaEEKAKKAitdaammaEELKKEQDTSAHLERMKKNMEQTIKDLQHRL 1797
Cdd:PRK02224 472 EDR----ERVEELEAELEDLEEEVEEV-------EERLERA--------EDLVEAEDRIERLEERREDLEELIAERRETI 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1798 DEAEQialkggkkQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEE---DRKNLLRLQDLVDKLQLK 1874
Cdd:PRK02224 533 EEKRE--------RAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAElkeRIESLERIRTLLAAIADA 604
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1387193866 1875 VKAYKRQAEEAEEQANTN------LSKFRKVQHELDEAEERADIAESQVNKLRAKS 1924
Cdd:PRK02224 605 EDEIERLREKREALAELNderrerLAEKRERKRELEAEFDEARIEEAREDKERAEE 660
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
843-1300 |
3.23e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 71.99 E-value: 3.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 843 AETEKEialmKEEFgrlKEALEKSEARRKELEEKMVSLLQEK--NDLQLQ-VQAEQDNLADAEERC-DQLIKNKIQLEAK 918
Cdd:PRK02224 268 AETERE----REEL---AEEVRDLRERLEELEEERDDLLAEAglDDADAEaVEARREELEDRDEELrDRLEECRVAAQAH 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 919 VKE---MTERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKE 995
Cdd:PRK02224 341 NEEaesLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREE 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 996 KKALQEAHQQALDDLQAEEDKVN-------------------------TLTKAKVKLEQHVDDLEGSLEQEKKVRMDLER 1050
Cdd:PRK02224 421 RDELREREAELEATLRTARERVEeaealleagkcpecgqpvegsphveTIEEDRERVEELEAELEDLEEEVEEVEERLER 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1051 AKrklegDLKLTQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARA 1130
Cdd:PRK02224 501 AE-----DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVA 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1131 KVEKLRSDLSRE---LEEISERLEEAGGATSVQIEMNKKRE-------------AEFQKMRRDLEEATLQHEATAAALRK 1194
Cdd:PRK02224 576 ELNSKLAELKERiesLERIRTLLAAIADAEDEIERLREKREalaelnderrerlAEKRERKRELEAEFDEARIEEAREDK 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1195 KHADS-VAELSEQIDNLQRVKQKLEKEKSEFKLELDdvtsNMEQIIKAKANLEKMCRTLEDQMNEhrskAEETQRSVNDL 1273
Cdd:PRK02224 656 ERAEEyLEQVEEKLDELREERDDLQAEIGAVENELE----ELEELRERREALENRVEALEALYDE----AEELESMYGDL 727
|
490 500
....*....|....*....|....*...
gi 1387193866 1274 tsqRAKLQTEN-GELSRQLDEKEALISQ 1300
Cdd:PRK02224 728 ---RAELRQRNvETLERMLNETFDLVYQ 752
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
844-1428 |
1.35e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 69.94 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 844 ETEKEIALMKEEFGRLKEA---LEKSEARRK---ELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKI-QLE 916
Cdd:COG4913 222 DTFEAADALVEHFDDLERAheaLEDAREQIEllePIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELeELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 917 AKVKEMTERLEDEEEMNAELTAKKRKLEDECSELK-RDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKE 995
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 996 KKALQEAHQQALDDLQAEEDKV-NTLTKAKVKLEQHVDDLEgSLEQE------KKVRMD--LERAKRKLEGDLKLTQESI 1066
Cdd:COG4913 382 FAALRAEAAALLEALEEELEALeEALAEAEAALRDLRRELR-ELEAEiaslerRKSNIParLLALRDALAEALGLDEAEL 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1067 M---DLendkqqLDERLKKKDFElNALnariedEQALGSQ----L--QKKLKE---------LQARIEELEEELEAERTA 1128
Cdd:COG4913 461 PfvgEL------IEVRPEEERWR-GAI------ERVLGGFaltlLvpPEHYAAalrwvnrlhLRGRLVYERVRTGLPDPE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1129 RAK------VEKLRSDLSRELEEISERLEEAGGATSV-----------------QIEMNKKReaeFQK-MRRDLEE---- 1180
Cdd:COG4913 528 RPRldpdslAGKLDFKPHPFRAWLEAELGRRFDYVCVdspeelrrhpraitragQVKGNGTR---HEKdDRRRIRSryvl 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1181 --------ATLQHEATAAALRKKHADS-VAELSEQIDNLQRVKQKLEK--EKSEFKLELDDVTSNMEQIIKAKANLEK-- 1247
Cdd:COG4913 605 gfdnraklAALEAELAELEEELAEAEErLEALEAELDALQERREALQRlaEYSWDEIDVASAEREIAELEAELERLDAss 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1248 -MCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLT-RGKLTYTQQLEDLKRQLEEEvKA 1325
Cdd:COG4913 685 dDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEdLARLELRALLEERFAAALGD-AV 763
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1326 KNALAHALQSARHDCDLLREQYEEETEAKaeLQRVLSKANSEVAQWRTKYET----DAI---QRTEELEEAKKKLAQRLQ 1398
Cdd:COG4913 764 ERELRENLEERIDALRARLNRAEEELERA--MRAFNREWPAETADLDADLESlpeyLALldrLEEDGLPEYEERFKELLN 841
|
650 660 670
....*....|....*....|....*....|
gi 1387193866 1399 DAEEavEAVNAKCSSLEKTKHRLQNEIEDL 1428
Cdd:COG4913 842 ENSI--EFVADLLSKLRRAIREIKERIDPL 869
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1488-1828 |
2.33e-11 |
|
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: 68.56 E-value: 2.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1488 YEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKLELQsaleEAEASLEHEEGKILRAQLEFNQ 1567
Cdd:pfam05622 140 YKKKLEDLGDLRRQVKLLEERNAEYMQRTLQLEEELKKANALRGQLETYKRQVQ----ELHGKLSEESKKADKLEFEYKK 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1568 IKA-------EMERKLAEKD---EEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRLAA 1637
Cdd:pfam05622 216 LEEklealqkEKERLIIERDtlrETNEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLR 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1638 EAQKQvkSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRavveqtersRKLAEQElietservqllh 1717
Cdd:pfam05622 296 LGQEG--SYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQ---------KALQEQG------------ 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1718 SQNTSLINQKKKMEADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEEL-----KKEQDTSAHLERMKKNMEQ---T 1789
Cdd:pfam05622 353 SKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNLAQKIDELqealrKKDEDMKAMEERYKKYVEKaksV 432
|
330 340 350
....*....|....*....|....*....|....*....
gi 1387193866 1790 IKDLQHRLDEAEQIALKGGKKQLQKLEARVRELENELEA 1828
Cdd:pfam05622 433 IKTLDPKQNPASPPEIQALKNQLLEKDKKIEHLERDFEK 471
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
834-1858 |
2.60e-11 |
|
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: 69.31 E-value: 2.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 834 FKIKPLLKSAETEKEIALMK----EEFGRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLI 909
Cdd:TIGR00606 179 FSATRYIKALETLRQVRQTQgqkvQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 910 KNK---IQLEAKVKEMTERLEDEEEMNAELTAKKRKLEDECSELKRDIDdleltlakvekekHATENKVKNLTEEMAGLD 986
Cdd:TIGR00606 259 HNLskiMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLY-------------HNHQRTVREKERELVDCQ 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 987 EIIAKLTKEKKALQEAH-----QQALDDLQAEEDKVNTLTKAKVKLEQ----HVDDLEGSLEQEKKVRMDLERAKRKLEG 1057
Cdd:TIGR00606 326 RELEKLNKERRLLNQEKtellvEQGRLQLQADRHQEHIRARDSLIQSLatrlELDGFERGPFSERQIKNFHTLVIERQED 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1058 DLKLTQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQALgsqLQKKLKELQARIEELEEELEAERTARAKVEKLRS 1137
Cdd:TIGR00606 406 EAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEI---LEKKQEELKFVIKELQQLEGSSDRILELDQELRK 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1138 DLsRELEEISErleeaggatSVQIEMNKKREAEFQKMRRDLEEaTLQHEATAAALRKKHADSVAELseqidnlqrvkQKL 1217
Cdd:TIGR00606 483 AE-RELSKAEK---------NSLTETLKKEVKSLQNEKADLDR-KLRKLDQEMEQLNHHTTTRTQM-----------EML 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1218 EKEKSEFKLELDDVTSNMEQIIKAKANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEAL 1297
Cdd:TIGR00606 541 TKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQ 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1298 ISQLTR------GKLTYTQQLEDLKRQLEEEVKAKNALAHAlqSARHDcDLLREQYEEETEAKAELQRVLskansevaqw 1371
Cdd:TIGR00606 621 LSSYEDklfdvcGSQDEESDLERLKEEIEKSSKQRAMLAGA--TAVYS-QFITQLTDENQSCCPVCQRVF---------- 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1372 rtkyetdaiQRTEELEEAKKKLAQRLQDAEEAVEavnakcsSLEKTKHRLQNEIEDLMVDVErsnaaaaaldKKQRNFDK 1451
Cdd:TIGR00606 688 ---------QTEAELQEFISDLQSKLRLAPDKLK-------STESELKKKEKRRDEMLGLAP----------GRQSIIDL 741
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1452 ILAEWKQkyeesqselesSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLT--EQLgssgktIHELEKV 1529
Cdd:TIGR00606 742 KEKEIPE-----------LRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTimERF------QMELKDV 804
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1530 RKQLEAEKLELQSAleEAEASLEHEEGKILRAQLEFNQIKAEMErkLAEKDEEMEQAKRNHLRvvdSLQTSLDAETRSRN 1609
Cdd:TIGR00606 805 ERKIAQQAAKLQGS--DLDRTVQQVNQEKQEKQHELDTVVSKIE--LNRKLIQDQQEQIQHLK---SKTNELKSEKLQIG 877
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1610 EALRVKKKMEGDLNEMEIQLSHANRLAAEAQKQVKSLQSLLKDTQIQLDDAVRANddlkeniaivERRNNLLQAELEELR 1689
Cdd:TIGR00606 878 TNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSK----------ETSNKKAQDKVNDIK 947
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1690 AVVEQTERSRKLAEQELIETSERvqllhsqntslinQKKKMEADLSQLQTEVEEAVQECRNAEE--KAKKAITDAAMMAE 1767
Cdd:TIGR00606 948 EKVKNIHGYMKDIENKIQDGKDD-------------YLKQKETELNTVNAQLEECEKHQEKINEdmRLMRQDIDTQKIQE 1014
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1768 ELKKEQDTSAHLERMKKNMEQTIKdlQHrLDEAEQIALKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRI 1847
Cdd:TIGR00606 1015 RWLQDNLTLRKRENELKEVEEELK--QH-LKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKEL 1091
|
1050
....*....|.
gi 1387193866 1848 KELTYQTEEDR 1858
Cdd:TIGR00606 1092 REPQFRDAEEK 1102
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1473-1934 |
3.03e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.79 E-value: 3.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1473 EARSLSTELFKLKNAYEESLEhletfKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKLELQSALEEAEasLE 1552
Cdd:COG4913 226 AADALVEHFDDLERAHEALED-----AREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAE--LE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1553 HEEGKILRAQLEFNQIKAEmERKLAEKDEEMEQAKRNH-LRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSH 1631
Cdd:COG4913 299 ELRAELARLEAELERLEAR-LDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1632 A----NRLAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKEN-------IAIVERRNNLLQAELEELRAVVEqteRSRK 1700
Cdd:COG4913 378 SaeefAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRElreleaeIASLERRKSNIPARLLALRDALA---EALG 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1701 LAEQ------ELIETS----------ERVqlLHSQNTSL-------------INQKK----------------------- 1728
Cdd:COG4913 455 LDEAelpfvgELIEVRpeeerwrgaiERV--LGGFALTLlvppehyaaalrwVNRLHlrgrlvyervrtglpdperprld 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1729 ------KMEADLSQLQTEVEEAVQE------CRNAEE--KAKKAITDAAMMAEELKK-EQDTSAHLER---MKKNMEQTI 1790
Cdd:COG4913 533 pdslagKLDFKPHPFRAWLEAELGRrfdyvcVDSPEElrRHPRAITRAGQVKGNGTRhEKDDRRRIRSryvLGFDNRAKL 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1791 KDLQHRLDEAEQiALKGGKKQLQKLEARVRELENELEAEQK--RNAESVKGMRKSERRIKELtyqtEEDRKNLLRLQDLV 1868
Cdd:COG4913 613 AALEAELAELEE-ELAEAEERLEALEAELDALQERREALQRlaEYSWDEIDVASAEREIAEL----EAELERLDASSDDL 687
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387193866 1869 DKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGTKGLNE 1934
Cdd:COG4913 688 AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEE 753
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
860-1695 |
6.56e-11 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 68.06 E-value: 6.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 860 KEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQliKNKI-QLEAKVKEMTERLEDEE-------E 931
Cdd:PRK04863 299 RRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQ--QEKIeRYQADLEELEERLEEQNevveeadE 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 932 MNAELTAKKRKLEDECSELKRDIDDL-------------------------------ELTLAKVEKEKHATENKVKNLTE 980
Cdd:PRK04863 377 QQEENEARAEAAEEEVDELKSQLADYqqaldvqqtraiqyqqavqalerakqlcglpDLTADNAEDWLEEFQAKEQEATE 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 981 EMAGL-------DEIIAKLTKEKKALQ---------EAHQQALDDL-QAEEDKVntLTKAKVKLEQHVDDLEGSLEQEKk 1043
Cdd:PRK04863 457 ELLSLeqklsvaQAAHSQFEQAYQLVRkiagevsrsEAWDVARELLrRLREQRH--LAEQLQQLRMRLSELEQRLRQQQ- 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1044 vrmDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKkkdfelnALNARIEDEQALGSQLQKKLKELQARIEELEEELE 1123
Cdd:PRK04863 534 ---RAERLLAEFCKRLGKNLDDEDELEQLQEELEARLE-------SLSESVSEARERRMALRQQLEQLQARIQRLAARAP 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1124 AERTARAKVEKLRSDLSRELEEiSERLEEAggatsvqiemnkkreaeFQKMRRDLEEATLQHEATAAALRkkhadsvaEL 1203
Cdd:PRK04863 604 AWLAAQDALARLREQSGEEFED-SQDVTEY-----------------MQQLLERERELTVERDELAARKQ--------AL 657
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1204 SEQIDNLQ--------RVKQKLEKEKSEFKLEL-DDVTSN------------MEQII-----KAKANLEKMCRTLED--- 1254
Cdd:PRK04863 658 DEEIERLSqpggsedpRLNALAERFGGVLLSEIyDDVSLEdapyfsalygpaRHAIVvpdlsDAAEQLAGLEDCPEDlyl 737
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1255 ------QMNEHRSKAEETQRSVNDLTSQRAklqtengelSRqldekealISQLTR----GKLTYTQQLEDLKRQLEEEVk 1324
Cdd:PRK04863 738 iegdpdSFDDSVFSVEELEKAVVVKIADRQ---------WR--------YSRFPEvplfGRAAREKRIEQLRAEREELA- 799
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1325 aknalahalqsarhdcdllrEQYEEETEAKAELQRVLSKANSEVA-------QWRTKYETDAIQRT--------EELEEA 1389
Cdd:PRK04863 800 --------------------ERYATLSFDVQKLQRLHQAFSRFIGshlavafEADPEAELRQLNRRrveleralADHESQ 859
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1390 KKKLAQRLQDAEEAVEAVN--AKCSSLEKTKHrLQNEIEDLMVDVERSNAAAAALDKKQRNFDKI-------------LA 1454
Cdd:PRK04863 860 EQQQRSQLEQAKEGLSALNrlLPRLNLLADET-LADRVEEIREQLDEAEEAKRFVQQHGNALAQLepivsvlqsdpeqFE 938
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1455 EWKQKYEESQSELESSQKEARSLsTELFKLKN--AYEESLEHLetfkrenknlqEEISDLTEQLgssgktiheleKVR-K 1531
Cdd:PRK04863 939 QLKQDYQQAQQTQRDAKQQAFAL-TEVVQRRAhfSYEDAAEML-----------AKNSDLNEKL-----------RQRlE 995
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1532 QLEAEKLELQSALEEAEAslEHEEGKILRAQLE-----FNQIKAEMERKLAE----KDEEMEQAKRNHLrvvDSLQTSLD 1602
Cdd:PRK04863 996 QAEQERTRAREQLRQAQA--QLAQYNQVLASLKssydaKRQMLQELKQELQDlgvpADSGAEERARARR---DELHARLS 1070
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1603 AETRSRNEALRVKKKMEGDLNEMEIQLSHANRLAAEAQKQV----KSLQSLLKdtqiqlddAVRANDdlkeniaiVERRn 1678
Cdd:PRK04863 1071 ANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVvnakAGWCAVLR--------LVKDNG--------VERR- 1133
|
970 980
....*....|....*....|..
gi 1387193866 1679 nLLQAEL-----EELRAVVEQT 1695
Cdd:PRK04863 1134 -LHRRELaylsaDELRSMSDKA 1154
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
834-1246 |
8.25e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.40 E-value: 8.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 834 FKIKPLLKSAETEKEIALMKEEFGRLKEALEKSEARR---KELEEKMVSLLQEKNDLQLQVQAEQDNLADAEE----RCD 906
Cdd:PRK03918 301 FYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEerlEELKKKLKELEKRLEELEERHELYEEAKAKKEElerlKKR 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 907 QLIKNKIQLEAKVKEMTERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLE-----LTLAKVEKEKHATEN-------K 974
Cdd:PRK03918 381 LTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKkakgkCPVCGRELTEEHRKElleeytaE 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 975 VKNLTEEMAGLDEIIAKLTKEKKALqEAHQQALDDLQAEEDKVNTLTKAKVKLEQHvdDLEgSLEQEKKVRMDLERAKRK 1054
Cdd:PRK03918 461 LKRIEKELKEIEEKERKLRKELREL-EKVLKKESELIKLKELAEQLKELEEKLKKY--NLE-ELEKKAEEYEKLKEKLIK 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1055 LEGDLKLTQ---ESIMDLENDKQQLDERLKKKDFELNALNARI-----EDEQALGSQLQK---------KLKELQARIEE 1117
Cdd:PRK03918 537 LKGEIKSLKkelEKLEELKKKLAELEKKLDELEEELAELLKELeelgfESVEELEERLKElepfyneylELKDAEKELER 616
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1118 LEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVqiEMNKKREAEFQKMRRDLEEATLQHEaTAAALRKKHA 1197
Cdd:PRK03918 617 EEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE--EEYEELREEYLELSRELAGLRAELE-ELEKRREEIK 693
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1387193866 1198 DSVAELSEQIDNLQRVKQKLEKekseFKLELDDVTSNMEQIIKAKANLE 1246
Cdd:PRK03918 694 KTLEKLKEELEEREKAKKELEK----LEKALERVEELREKVKKYKALLK 738
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
914-1140 |
9.41e-11 |
|
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: 65.94 E-value: 9.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 914 QLEAKVKEMTERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLT 993
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 994 KEKK----ALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQHVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDL 1069
Cdd:COG4942 104 EELAellrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387193866 1070 ENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIE--ELEEELEAERTARAKVEKLRSDLS 1140
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIArlEAEAAAAAERTPAAGFAALKGKLP 256
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1027-1669 |
1.22e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.86 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1027 LEQHVDDLEGSLEQekkvrmdLERAKRKLE--GDLKLTQESIMDLENDKQQLDE-----RLKKKDFELNALNARIEDEQA 1099
Cdd:COG4913 230 LVEHFDDLERAHEA-------LEDAREQIEllEPIRELAERYAAARERLAELEYlraalRLWFAQRRLELLEAELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1100 LGSQLQKKLKELQARIEELEEELEAERTARAKVE-KLRSDLSRELEEISERLEEAggatsvqiemnKKREAEFQKMRRDL 1178
Cdd:COG4913 303 ELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEER-----------ERRRARLEALLAAL 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1179 EEATLQHEATAAALRKKHADSVAELSEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKMCRTLEDQMNE 1258
Cdd:COG4913 372 GLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1259 HRSKAEETQRSVNDLtsqrakLQTENGELS--------------------RQLDEKEALISQL-TRGKLTYtQQLEDLKR 1317
Cdd:COG4913 452 ALGLDEAELPFVGEL------IEVRPEEERwrgaiervlggfaltllvppEHYAAALRWVNRLhLRGRLVY-ERVRTGLP 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1318 QLEEEVKAKNALAHALQSARHDC-DLLREQYEEET-----EAKAELQRV--------LSKANSEVAQ------WRTKYET 1377
Cdd:COG4913 525 DPERPRLDPDSLAGKLDFKPHPFrAWLEAELGRRFdyvcvDSPEELRRHpraitragQVKGNGTRHEkddrrrIRSRYVL 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1378 --DAIQRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQN--EIEDLMVDVERSNAAAAALDKKQRNFDKIL 1453
Cdd:COG4913 605 gfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaEYSWDEIDVASAEREIAELEAELERLDASS 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1454 AEWKQkyeesqselessqkearsLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQL 1533
Cdd:COG4913 685 DDLAA------------------LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE 746
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1534 EAEKLELQSALEEAEASLEHeegkiLRAQLEfNQIKAEmERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALR 1613
Cdd:COG4913 747 LRALLEERFAAALGDAVERE-----LRENLE-ERIDAL-RARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLA 819
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387193866 1614 VKKKMEGD------------LNEMEIQ-----LSHANRLAAEAQKQVKSLQSLLK------DTQIQLDDAVRANDDLKE 1669
Cdd:COG4913 820 LLDRLEEDglpeyeerfkelLNENSIEfvadlLSKLRRAIREIKERIDPLNDSLKripfgpGRYLRLEARPRPDPEVRE 898
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1313-1904 |
1.62e-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: 66.28 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1313 EDLKRQLEEEVKAKNALAHALQSARHDCDLLRE--------------QYEEETEAKAELQRVLSKANSEVAQWRTKYETD 1378
Cdd:pfam05483 130 EKVSLKLEEEIQENKDLIKENNATRHLCNLLKEtcarsaektkkyeyEREETRQVYMDLNNNIEKMILAFEELRVQAENA 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1379 AIQRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQ 1458
Cdd:pfam05483 210 RLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIE 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1459 KyeesqselessqkeARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSgktIHELEKVRKQLEAEKL 1538
Cdd:pfam05483 290 K--------------KDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQ---MEELNKAKAAHSFVVT 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1539 ELQSALEEAEASLEHEEGKILRAQLEFNQIKAEMERKLAEKdEEMEQAKRNHLRVVDSLQTSLDAETRSRNEalrvKKKM 1618
Cdd:pfam05483 353 EFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSEL-EEMTKFKNNKEVELEELKKILAEDEKLLDE----KKQF 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1619 EGDLNEMEIQLSHANRLAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELravveqters 1698
Cdd:pfam05483 428 EKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKL---------- 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1699 rKLAEQELI-ETSERVQLLHSQNTSLINQKKKMEADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSA 1777
Cdd:pfam05483 498 -LLENKELTqEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENAR 576
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1778 HLERMKKNMEQTIKDLQHRLDEAeqialkggKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEED 1857
Cdd:pfam05483 577 SIEYEVLKKEKQMKILENKCNNL--------KKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASA 648
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1858 RKnllRLQDLVDKLQLKVKAYKRQAE---EAEEQANTNLSKFRKVQHELD 1904
Cdd:pfam05483 649 KQ---KFEEIIDNYQKEIEDKKISEEkllEEVEKAKAIADEAVKLQKEID 695
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
835-1271 |
1.80e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 66.70 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 835 KIKPLLKSAETEKEIALMKEEFGRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQ 914
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYE 1602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 915 LEAKVKEMTERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHatENKVKnlTEEMAGLDEIIAKLTK 994
Cdd:PTZ00121 1603 EEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE--ENKIK--AAEEAKKAEEDKKKAE 1678
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 995 EKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQHVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDlENDKQ 1074
Cdd:PTZ00121 1679 EAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD-EEEKK 1757
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1075 QLDERlkKKDFELNALNARIEDEQALGSQLQKKlkelqarieeleeeleaERTARAKVEKLRSDLSRELEEISERLEEAG 1154
Cdd:PTZ00121 1758 KIAHL--KKEEEKKAEEIRKEKEAVIEEELDEE-----------------DEKRRMEVDKKIKDIFDNFANIIEGGKEGN 1818
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1155 GATSVQIEM---NKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELSEQIDNLQRVKQKLEKEKSEFKLELDDV 1231
Cdd:PTZ00121 1819 LVINDSKEMedsAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDI 1898
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1387193866 1232 TSNMEQIIKAKANLEKMCRTLEDQMNEHRSKAEETQRSVN 1271
Cdd:PTZ00121 1899 EREIPNNNMAGKNNDIIDDKLDKDEYIKRDAEETREEIIK 1938
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1180-1757 |
1.93e-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: 66.28 E-value: 1.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1180 EATLQHEATAAALRKKHADSVAELSEQIDNLQRVKQKLEKEKSEFKLELDDvtsNMEQIIKAKANLEKMCRTLEDQMNEH 1259
Cdd:pfam05483 169 EKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKE---DHEKIQHLEEEYKKEINDKEKQVSLL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1260 RSKAEETQRSVNDLTSqrakLQTENGELSRQLDEKEAL----ISQLTRGKLTYTQQLEDLKRQLEEEVKAKNALAHALQS 1335
Cdd:pfam05483 246 LIQITEKENKMKDLTF----LLEESRDKANQLEEKTKLqdenLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQI 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1336 A-RHDCDLLRE---QYEEETEAKAELQRVLSKANSEVAQWRTKYETDAiQRTEELEEAKKKLAQRLQ----DAEEAVEAV 1407
Cdd:pfam05483 322 AtKTICQLTEEkeaQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQ-QRLEKNEDQLKIITMELQkkssELEEMTKFK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1408 NAKCSSLEKTKHRLqNEIEDLMVDVERSNAAAAALDKKQRNF-------DKILAEWKQKYEESQSELESSQKEARSLSTE 1480
Cdd:pfam05483 401 NNKEVELEELKKIL-AEDEKLLDEKKQFEKIAEELKGKEQELifllqarEKEIHDLEIQLTAIKTSEEHYLKEVEDLKTE 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1481 LFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTI----HELEKVRKQ---LEAEKLELQSALEEAEASL-- 1551
Cdd:pfam05483 480 LEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIinckKQEERMLKQienLEEKEMNLRDELESVREEFiq 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1552 EHEEGKILRAQLEFNQIKAEMERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEG-DLNEMEIQLs 1630
Cdd:pfam05483 560 KGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENkQLNAYEIKV- 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1631 haNRLAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENI---AIVERRNNLLQAELE-----ELRAVVEQTERSRKLA 1702
Cdd:pfam05483 639 --NKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVekaKAIADEAVKLQKEIDkrcqhKIAEMVALMEKHKHQY 716
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1387193866 1703 EQELIETSERVQLLHSQNTSLINQKKKMEADLSQLQTEVEEAVQECRNAEEKAKK 1757
Cdd:pfam05483 717 DKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEK 771
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1481-1909 |
5.61e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 64.70 E-value: 5.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1481 LFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKLELQSALEEAE------ASLEHE 1554
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEelkeeiEELEKE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1555 EGKILRAQLEFNQIKAEMERKLAEKDEEMEQAKRNhLRVVDSLQTslDAETRSRNEALRVKKKMEgdLNEMEIQLSHANR 1634
Cdd:PRK03918 247 LESLEGSKRKLEEKIRELEERIEELKKEIEELEEK-VKELKELKE--KAEEYIKLSEFYEEYLDE--LREIEKRLSRLEE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1635 LAAEAQKQVKSLQSLlkdtqiqlddaVRANDDLKENIAIVERRNNLLQA---ELEELRAVVEQTERSRK-LAEQELIETS 1710
Cdd:PRK03918 322 EINGIEERIKELEEK-----------EERLEELKKKLKELEKRLEELEErheLYEEAKAKKEELERLKKrLTGLTPEKLE 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1711 ERVQLLHSQNTSLINQKKKMEADLSQLQTEVEEAvqecRNAEEKAKKAITDAAMMAEELKKEqdtsaHLERMKKNMEQTI 1790
Cdd:PRK03918 391 KELEELEKAKEEIEEEISKITARIGELKKEIKEL----KKAIEELKKAKGKCPVCGRELTEE-----HRKELLEEYTAEL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1791 KDLQHRLDEAEqialkggkKQLQKLEARVRELENELEAEQK--RNAESVKGMRKSERRIKELTYQT-EEDRKNLLRLQDL 1867
Cdd:PRK03918 462 KRIEKELKEIE--------EKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKKYNLEElEKKAEEYEKLKEK 533
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1387193866 1868 VDKLQLKVKAYKRQAEEAEEQANtnlsKFRKVQHELDEAEER 1909
Cdd:PRK03918 534 LIKLKGEIKSLKKELEKLEELKK----KLAELEKKLDELEEE 571
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1327-1922 |
5.75e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 64.68 E-value: 5.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1327 NALAHALQSARHDC--DLLR----EQYEEET-EAKAELQRVLSKANSEV----AQWRTKYETDAIQRTEELEEAKKKLAQ 1395
Cdd:PRK02224 141 NKLINATPSDRQDMidDLLQlgklEEYRERAsDARLGVERVLSDQRGSLdqlkAQIEEKEEKDLHERLNGLESELAELDE 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1396 RLQDAEE----AVEAVNAKCSSLEKTKHRLQnEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQ 1471
Cdd:PRK02224 221 EIERYEEqreqARETRDEADEVLEEHEERRE-ELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLL 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1472 KEArslstelfKLKNAYEESLE-HLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKLELQSALEEAEAS 1550
Cdd:PRK02224 300 AEA--------GLDDADAEAVEaRREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1551 LEHEEGKIlraqlefnqikAEMERKLAEKDEEMEQAKRnhlRVVDSLQTSLDAETRsRNEALRVKKKMEGDLNEMEIQLS 1630
Cdd:PRK02224 372 LEEAREAV-----------EDRREEIEELEEEIEELRE---RFGDAPVDLGNAEDF-LEELREERDELREREAELEATLR 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1631 HANRLAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQ--ELIE 1708
Cdd:PRK02224 437 TARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRieRLEE 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1709 TSERVQLLHSQNTSLINQKkkmEADLSQLQTEVEEAVQECRNAEEKAKKAitdaammAEELKKEQDTSAHLERMKKNMEQ 1788
Cdd:PRK02224 517 RREDLEELIAERRETIEEK---RERAEELRERAAELEAEAEEKREAAAEA-------EEEAEEAREEVAELNSKLAELKE 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1789 TIKDLQHRLDEAEQIAlkggkkqlqKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRknllrlqdlV 1868
Cdd:PRK02224 587 RIESLERIRTLLAAIA---------DAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEAR---------I 648
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387193866 1869 DKLQLKvkayKRQAEEAEEQANTNLSKFRK-----------VQHELDEAE---ERADIAESQVNKLRA 1922
Cdd:PRK02224 649 EEARED----KERAEEYLEQVEEKLDELREerddlqaeigaVENELEELEelrERREALENRVEALEA 712
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
835-1319 |
5.84e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.78 E-value: 5.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 835 KIKPLLKSAETEKEialmKEEFGRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQ 914
Cdd:PTZ00121 1458 KAEEAKKKAEEAKK----ADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEA 1533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 915 LEAKVKEMTERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVknltEEMAGLDEIIAKLTK 994
Cdd:PTZ00121 1534 KKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARI----EEVMKLYEEEKKMKA 1609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 995 EKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQHVDDLEGSLEQEKKVRMDLERAKRKLEGDlKLTQESIMDLENDKQ 1074
Cdd:PTZ00121 1610 EEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED-KKKAEEAKKAEEDEK 1688
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1075 QLDERLKKKdfelnalnariEDEQALGSQLQKKLKElqaRIEELEEELEAERTARAKVEKLRsdlsRELEEISERLEEAg 1154
Cdd:PTZ00121 1689 KAAEALKKE-----------AEEAKKAEELKKKEAE---EKKKAEELKKAEEENKIKAEEAK----KEAEEDKKKAEEA- 1749
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1155 gatsvqiemnKKREAEFQKMRRDLEEatlqHEATAAALRKKHADSVAELSEQIDNLQR--VKQKLEKEKSEFKLELDDVT 1232
Cdd:PTZ00121 1750 ----------KKDEEEKKKIAHLKKE----EEKKAEEIRKEKEAVIEEELDEEDEKRRmeVDKKIKDIFDNFANIIEGGK 1815
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1233 SNMEQIIKAKANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQL 1312
Cdd:PTZ00121 1816 EGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDK 1895
|
....*..
gi 1387193866 1313 EDLKRQL 1319
Cdd:PTZ00121 1896 DDIEREI 1902
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1527-1927 |
8.39e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.39 E-value: 8.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1527 EKVRKQLEAEKLELQSALEEAEASLEHEEGKILRAQLEFNQI----KAEMERKLAEKDEEMEQAKRNHLRVVDSLQTSLD 1602
Cdd:PTZ00121 1161 EDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAeaarKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAE 1240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1603 AETRSRNEALRVKKKMEGDLNEMEIQLSHANRLAAEAQK--QVKSLQSLLKDTQIQLDDAVRANDDLKENiAIVERRNNL 1680
Cdd:PTZ00121 1241 EAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKadELKKAEEKKKADEAKKAEEKKKADEAKKK-AEEAKKADE 1319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1681 LQAELEELRavvEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMEADLSQLQTEVEEAVQECRNAEEK-----A 1755
Cdd:PTZ00121 1320 AKKKAEEAK---KKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKkkadeA 1396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1756 KKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKdlqhrLDEAEQialkggkkqlqKLEARVRELENELEAEQKRNAE 1835
Cdd:PTZ00121 1397 KKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKK-----ADEAKK-----------KAEEAKKADEAKKKAEEAKKAE 1460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1836 SVKGMRKSERRIKELTYQTEEDRKnllrlqdlVDKLQLKVKAYKRQAEEAE--EQANTNLSKFRKVQH-----ELDEAEE 1908
Cdd:PTZ00121 1461 EAKKKAEEAKKADEAKKKAEEAKK--------ADEAKKKAEEAKKKADEAKkaAEAKKKADEAKKAEEakkadEAKKAEE 1532
|
410
....*....|....*....
gi 1387193866 1909 RADIAESQVNKLRAKSRDI 1927
Cdd:PTZ00121 1533 AKKADEAKKAEEKKKADEL 1551
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
914-1343 |
9.01e-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: 63.38 E-value: 9.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 914 QLEAKVKEMTERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLT 993
Cdd:pfam07888 35 RLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 994 KEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQHVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDK 1073
Cdd:pfam07888 115 EEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1074 QQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSreleeiserleEA 1153
Cdd:pfam07888 195 QELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELS-----------SM 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1154 GGATSvqiemnkKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELSEQIDNLQRVKQKLEKEKSEFKLELDDVTS 1233
Cdd:pfam07888 264 AAQRD-------RTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQE 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1234 NMEQIIKAKANL--EKMCrtledqmneHRSKAEETQRsvnDLTSQRAKLQTENGELSRQLDEKEALisqltrgkLTYTQQ 1311
Cdd:pfam07888 337 ERMEREKLEVELgrEKDC---------NRVQLSESRR---ELQELKASLRVAQKEKEQLQAEKQEL--------LEYIRQ 396
|
410 420 430
....*....|....*....|....*....|..
gi 1387193866 1312 LEdlkRQLEEEVKAKNALAHALQSARHDCDLL 1343
Cdd:pfam07888 397 LE---QRLETVADAKWSEAALTSTERPDSPLS 425
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1615-1848 |
9.48e-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: 9.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1615 KKKMEGDLNEMEIQLSHANRLAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQ 1694
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1695 TER--SRKLAEQELIETSERVQLLHSQNTS--LINQKKKMEADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELK 1770
Cdd:COG4942 102 QKEelAELLRALYRLGRQPPLALLLSPEDFldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387193866 1771 KEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIAlkggkKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIK 1848
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAELAAEL-----AELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
842-1567 |
1.01e-09 |
|
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: 63.69 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 842 SAETEKEIALMKEEfgrlkealeksEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKE 921
Cdd:pfam10174 38 SPELKKERALRKEE-----------AARISVLKEQYRVTQEENQHLQLTIQALQDELRAQRDLNQLLQQDFTTSPVDGED 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 922 MTERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELtlaKVEKEKHATENKvknlteemaglDEIIAKLtkekkaLQE 1001
Cdd:pfam10174 107 KFSTPELTEENFRRLQSEHERQAKELFLLRKTLEEMEL---RIETQKQTLGAR-----------DESIKKL------LEM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1002 AHQQALDDLQAEEDkvNTLTKAKVKLEQHVDDLEGSLEQEKKVRMDL-ERAKRKLEGDLKLTQESIMdlendkQQLDERL 1080
Cdd:pfam10174 167 LQSKGLPKKSGEED--WERTRRIAEAEMQLGHLEVLLDQKEKENIHLrEELHRRNQLQPDPAKTKAL------QTVIEMK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1081 KKKDFELNALNARIEDE-QALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSR---ELEEISERLEEAGGA 1156
Cdd:pfam10174 239 DTKISSLERNIRDLEDEvQMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQELSKkesELLALQTKLETLTNQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1157 TS---VQIEMNKKREAEfqkmrRDLEEATLQHEATAAALRKKHADSVaeLSEQIDNLQRvkqkLEKEKSEFKLELDDVtS 1233
Cdd:pfam10174 319 NSdckQHIEVLKESLTA-----KEQRAAILQTEVDALRLRLEEKESF--LNKKTKQLQD----LTEEKSTLAGEIRDL-K 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1234 NMEQIIKAKAN-LEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLtrgkltyTQQL 1312
Cdd:pfam10174 387 DMLDVKERKINvLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERL-------KEQR 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1313 EDLKRQLEEEVKaknALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKK- 1391
Cdd:pfam10174 460 EREDRERLEELE---SLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKl 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1392 ----KLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSEL 1467
Cdd:pfam10174 537 enqlKKAHNAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQ 616
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1468 ESSQKEARSLSTELfKLKNAYEESLEHLETFKRENKNLQEEISDLTEqlgssgktihELEKVRKQLEAEKLEL---QSAL 1544
Cdd:pfam10174 617 NKKVANIKHGQQEM-KKKGAQLLEEARRREDNLADNSQQLQLEELMG----------ALEKTRQELDATKARLsstQQSL 685
|
730 740
....*....|....*....|....*.
gi 1387193866 1545 EEAEA---SLEHEEGKILRAQLEFNQ 1567
Cdd:pfam10174 686 AEKDGhltNLRAERRKQLEEILEMKQ 711
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1477-1923 |
1.20e-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: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1477 LSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKLELQSALEEA---EASLEH 1553
Cdd:TIGR04523 122 LEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIknkLLKLEL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1554 ---------EEGKILRAQL-----EFNQIKAEMERKLAEKDEEMEQAKRNHLRVVDSLQ------TSLDAETRSRNEALR 1613
Cdd:TIGR04523 202 llsnlkkkiQKNKSLESQIselkkQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDeqnkikKQLSEKQKELEQNNK 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1614 VKKKMEGDLNEMEIQLSHANR-----LAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEEL 1688
Cdd:TIGR04523 282 KIKELEKQLNQLKSEISDLNNqkeqdWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEK 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1689 RAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMEADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEE 1768
Cdd:TIGR04523 362 QRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSE 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1769 LKKEQDTSAHLERMKKNMEQTIKDLQHRLD-------------EAEQIALKGGKKQLQKLEARVRELENELEAEQKRNAE 1835
Cdd:TIGR04523 442 IKDLTNQDSVKELIIKNLDNTRESLETQLKvlsrsinkikqnlEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1836 SVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQL-KVKAYKRQAEEAEEQANTNLSKfrkvqhELDEAEERADIAE 1914
Cdd:TIGR04523 522 LKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLeKEIDEKNKEIEELKQTQKSLKK------KQEEKQELIDQKE 595
|
....*....
gi 1387193866 1915 SQVNKLRAK 1923
Cdd:TIGR04523 596 KEKKDLIKE 604
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1045-1283 |
1.79e-09 |
|
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: 62.09 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1045 RMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIeeleeelea 1124
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI--------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1125 ertarakvEKLRSDLSRELEEISERLEEA---GGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRkkhadsva 1201
Cdd:COG4942 93 --------AELRAELEAQKEELAELLRALyrlGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR-------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1202 elsEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQ 1281
Cdd:COG4942 157 ---ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
..
gi 1387193866 1282 TE 1283
Cdd:COG4942 234 AE 235
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1472-1935 |
3.03e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.39 E-value: 3.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1472 KEARSLSTELFKLknayEESLEHLETFKRENKNLQEEISDLTEQLGSsgktiheLEKVRKQLEAEKLELQSALEEAEASL 1551
Cdd:PRK03918 207 REINEISSELPEL----REELEKLEKEVKELEELKEEIEELEKELES-------LEGSKRKLEEKIRELEERIEELKKEI 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1552 EHEEGKILRaqLEFNQIKAEMERKLAEKDEEMEQAKRNhlrvVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSH 1631
Cdd:PRK03918 276 EELEEKVKE--LKELKEKAEEYIKLSEFYEEYLDELRE----IEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKE 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1632 ANRLAAEAQKQVKSLQSLL-KDTQIQLDDAVRAN---DDLKENIAIVERRNNLLQAELEEL---RAVVEQTERSRKLAEQ 1704
Cdd:PRK03918 350 LEKRLEELEERHELYEEAKaKKEELERLKKRLTGltpEKLEKELEELEKAKEEIEEEISKItarIGELKKEIKELKKAIE 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1705 ELIETSERVQLLHSQNTSliNQKKKMEADLSQLQTEVEEAVQECRNAEEKAKKAitdaammAEELKKEQDTSAHLERMKK 1784
Cdd:PRK03918 430 ELKKAKGKCPVCGRELTE--EHRKELLEEYTAELKRIEKELKEIEEKERKLRKE-------LRELEKVLKKESELIKLKE 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1785 NMEQtIKDLQHRLDEAEQIALKGGKKQLQKLEARVRELENELEAeQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLR- 1863
Cdd:PRK03918 501 LAEQ-LKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKS-LKKELEKLEELKKKLAELEKKLDELEEELAELLKe 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1864 --------LQDLVDKLQLKVKAYKR--QAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGTKGLN 1933
Cdd:PRK03918 579 leelgfesVEELEERLKELEPFYNEylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE 658
|
..
gi 1387193866 1934 EE 1935
Cdd:PRK03918 659 EE 660
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1262-1705 |
3.56e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.71 E-value: 3.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1262 KAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLtRGKLTYTQQLEDLKRQLEEEVKAKNALAHALQSARHdcd 1341
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEEL-REELEKLEKLLQLLPLYQELEALEAELAELPERLEE--- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1342 lLREQYEEETEAKAELQRvlskANSEVAQWRTkyetdaiQRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRL 1421
Cdd:COG4717 151 -LEERLEELRELEEELEE----LEAELAELQE-------ELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1422 QNEIEDLMVDVERSNAAAAALDKKQRNFDK------------ILAEWKQKYEESQSELESSQKEARSLS---TELFKLKN 1486
Cdd:COG4717 219 QEELEELEEELEQLENELEAAALEERLKEArlllliaaallaLLGLGGSLLSLILTIAGVLFLVLGLLAllfLLLAREKA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1487 AYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKLELQSALEEAEASLEHEEGKILRAQLeFN 1566
Cdd:COG4717 299 SLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAL-LA 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1567 QIKAEMERKLAEKDEEMEQAkRNHLRVVDSLQTSLDAETRSRNEALRvkkkmEGDLNEMEIQLSHANRLAAEAQKQVKSL 1646
Cdd:COG4717 378 EAGVEDEEELRAALEQAEEY-QELKEELEELEEQLEELLGELEELLE-----ALDEEELEEELEELEEELEELEEELEEL 451
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387193866 1647 QSLLKDTQIQLDDAVRAN--DDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQE 1705
Cdd:COG4717 452 REELAELEAELEQLEEDGelAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1615-1925 |
4.12e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.88 E-value: 4.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1615 KKKMEGDLNEMEIQLSHANRLAAEAQKQVKSLQsllkdtqIQLDDAVRANDdLKEniAIVERRNNLLQAELEELRAVVEQ 1694
Cdd:COG1196 174 KEEAERKLEATEENLERLEDILGELERQLEPLE-------RQAEKAERYRE-LKE--ELKELEAELLLLKLRELEAELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1695 TERSRKLAEQELIETSERVQLLHSQNTSLinqkkkmEADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQD 1774
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEEL-------RLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1775 TSAHLERMKKNMEQTIKDLQHRLDEAEQialkggkkQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQT 1854
Cdd:COG1196 317 RLEELEEELAELEEELEELEEELEELEE--------ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387193866 1855 EEDRKNLLRLQDlvdklqlkvkayKRQAEEAEEQANTN-LSKFRKVQHELDEAEERADIAESQVNKLRAKSR 1925
Cdd:COG1196 389 LEALRAAAELAA------------QLEELEEAEEALLErLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
844-1238 |
4.23e-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: 61.57 E-value: 4.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 844 ETEKEIALMKEEFGRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQV-----QAEQDNLADAEERCDQLIKNKIQLEAK 918
Cdd:TIGR04523 250 NTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEIsdlnnQKEQDWNKELKSELKNQEKKLEEIQNQ 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 919 VKEMTERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKA 998
Cdd:TIGR04523 330 ISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 999 LQEAHQQALDDLQAEEDKVNTLTKAKVKLEQHVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDE 1078
Cdd:TIGR04523 410 KDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQK 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1079 RLKKKDFELNALNARIedeqalgSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATS 1158
Cdd:TIGR04523 490 ELKSKEKELKKLNEEK-------KELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKE 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1159 VQ-----IEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHAD---SVAELSEQIDNLQRVKQKLEKEKSEFKLELDD 1230
Cdd:TIGR04523 563 IDeknkeIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEkekKISSLEKELEKAKKENEKLSSIIKNIKSKKNK 642
|
....*...
gi 1387193866 1231 VTSNMEQI 1238
Cdd:TIGR04523 643 LKQEVKQI 650
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1197-1413 |
5.39e-09 |
|
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: 60.55 E-value: 5.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1197 ADSVAELSEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQ 1276
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1277 RAKLQTENGELSRQL------DEKEALIS-----QLTRGKLTYTQQLEDLKRQLEEEVKAKNALAHALQSARHDCDLLRE 1345
Cdd:COG4942 99 LEAQKEELAELLRALyrlgrqPPLALLLSpedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387193866 1346 QYEEETEAKAELQRVLSKANSEVAQWRTKYETDAiQRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSS 1413
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELA-AELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
835-1255 |
5.65e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.32 E-value: 5.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 835 KIKPLLKSAETEKEIALMKEEFGRLKEALEKSEARRKELEE---KMVSLLQEKNDLQLQVQAEQD--NLADAEERCDQLI 909
Cdd:COG4717 66 PELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEEleaELEELREELEKLEKLLQLLPLyqELEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 910 KNKIQLEAKVKEMTERLEDEEEMNAELTAKKRKLEDEC-----------SELKRDIDDLELTLAKVEKEKHATENKVKNL 978
Cdd:COG4717 146 ERLEELEERLEELRELEEELEELEAELAELQEELEELLeqlslateeelQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 979 TEEMAGLDEIIAKLTKEKKALQE-----------AHQQALDDLQAEEDKV---------------NTLTKAKVKLEQHVD 1032
Cdd:COG4717 226 EEELEQLENELEAAALEERLKEArlllliaaallALLGLGGSLLSLILTIagvlflvlgllallfLLLAREKASLGKEAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1033 DLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKkdfelnalnARIEDEQALGSQLQKKLKELQ 1112
Cdd:COG4717 306 ELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLRE---------AEELEEELQLEELEQEIAALL 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1113 ARIEELEEELEAertARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKR--EAEFQKMRRDLEEATLQHEataa 1190
Cdd:COG4717 377 AEAGVEDEEELR---AALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEelEEELEELEEELEELEEELE---- 449
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387193866 1191 ALRKKHADSVAELS--EQIDNLQRVKQKLEKEKSEFKLELDDVTSNMeqiiKAKANLEKMCRTLEDQ 1255
Cdd:COG4717 450 ELREELAELEAELEqlEEDGELAELLQELEELKAELRELAEEWAALK----LALELLEEAREEYREE 512
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1432-1880 |
1.05e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.17 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1432 VERSNAAAAALDKKQ-RNFDKILAEWKQKyeesqselESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEIS 1510
Cdd:COG4717 48 LERLEKEADELFKPQgRKPELNLKELKEL--------EEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1511 DLtEQLGSSGKTIHELEKVRKQLEAEKLELQsALEEAEASLEHEEGKILRAQLEFNQIKAEMERKLAEKDEEMEQAKRNH 1590
Cdd:COG4717 120 KL-EKLLQLLPLYQELEALEAELAELPERLE-ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1591 LRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLshanrLAAEAQKQVKSLQSLLK--DTQIQLDDAVRANDDLK 1668
Cdd:COG4717 198 AEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL-----EAAALEERLKEARLLLLiaAALLALLGLGGSLLSLI 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1669 ENIA-----------IVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMEADLSQL 1737
Cdd:COG4717 273 LTIAgvlflvlgllaLLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQEL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1738 QTEVEEAVQECRNAEEKAKKA----------ITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALkg 1807
Cdd:COG4717 353 LREAEELEEELQLEELEQEIAallaeagvedEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEEL-- 430
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387193866 1808 gKKQLQKLEARVRELENELEAEQKRnaesvkgMRKSERRIKELTyQTEEDRKNLLRLQDLVDKLQLKVKAYKR 1880
Cdd:COG4717 431 -EEELEELEEELEELEEELEELREE-------LAELEAELEQLE-EDGELAELLQELEELKAELRELAEEWAA 494
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1647-1897 |
1.19e-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: 59.39 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1647 QSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQllhsqntSLINQ 1726
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA-------ELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1727 KKKMEADLSQLQTEVEEAVqecRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQI--A 1804
Cdd:COG4942 92 IAELRAELEAQKEELAELL---RALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALraE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1805 LKGGKKQLQKLEARVRELENELEAEQKRNAESVKgmrKSERRIKELTYQTEEDRKNLLRLQDLVDKLQlkvkayKRQAEE 1884
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLA---RLEKELAELAAELAELQQEAEELEALIARLE------AEAAAA 239
|
250
....*....|...
gi 1387193866 1885 AEEQANTNLSKFR 1897
Cdd:COG4942 240 AERTPAAGFAALK 252
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1592-1894 |
1.22e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 60.03 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1592 RVVDSLQ--TSLDAETRSRNEAL-----RVKKKMEGDLNEMEIQLSHANrlAAEAQKQVKSLQSLLKDTQIQLddavran 1664
Cdd:COG3206 98 RVVDKLNldEDPLGEEASREAAIerlrkNLTVEPVKGSNVIEISYTSPD--PELAAAVANALAEAYLEQNLEL------- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1665 ddlkeNIAIVERRNNLLQAELEELRAVVEQTERSRK--LAEQELIETSERVQLLHSQNTSLINQKKKMEADLSQLQTEVE 1742
Cdd:COG3206 169 -----RREEARKALEFLEEQLPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1743 eAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMK----------KNMEQTIKDLQHRLDEAEQIALKGGKKQL 1812
Cdd:COG3206 244 -ALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSarytpnhpdvIALRAQIAALRAQLQQEAQRILASLEAEL 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1813 QKLEARVRELENELEAEQKRnaesVKGMRKSERRIKELTYQTEEDRKNllrLQDLVDKLQlkvkaykrQAEEAEEQANTN 1892
Cdd:COG3206 323 EALQAREASLQAQLAQLEAR----LAELPELEAELRRLEREVEVAREL---YESLLQRLE--------EARLAEALTVGN 387
|
..
gi 1387193866 1893 LS 1894
Cdd:COG3206 388 VR 389
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1472-1713 |
1.46e-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: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1472 KEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKLELQSALEEAEASL 1551
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1552 EHEEGKIlraqlefnqikAEMERKLaekdeeMEQAKRNHLRVVDSLQTSLDAETRSRNEAlRVKKKMEGDLNEMEIQLSH 1631
Cdd:COG4942 100 EAQKEEL-----------AELLRAL------YRLGRQPPLALLLSPEDFLDAVRRLQYLK-YLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1632 ANRLAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSE 1711
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
..
gi 1387193866 1712 RV 1713
Cdd:COG4942 242 RT 243
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1554-1934 |
1.50e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.15 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1554 EEGKILRAQLEFNQIKAEMERKLAEKDEEMEQAKR-NHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHA 1632
Cdd:PTZ00121 1095 EAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKaEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAED 1174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1633 NRLAAEAQK--QVKSLQSLLKDTQIQLDDAVRANDDLKEnIAIVERRNNLLQAE----LEELRAVVEQTERSRKLAEQEL 1706
Cdd:PTZ00121 1175 AKKAEAARKaeEVRKAEELRKAEDARKAEAARKAEEERK-AEEARKAEDAKKAEavkkAEEAKKDAEEAKKAEEERNNEE 1253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1707 IETSERVQLLH-SQNTSLINQKKKMEADLSQLQTEVEEA-----VQECRNAEEKAKKA-----ITDAAMMAEELKKEQDT 1775
Cdd:PTZ00121 1254 IRKFEEARMAHfARRQAAIKAEEARKADELKKAEEKKKAdeakkAEEKKKADEAKKKAeeakkADEAKKKAEEAKKKADA 1333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1776 SAH-LERMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQT 1854
Cdd:PTZ00121 1334 AKKkAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKA 1413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1855 EEDRKNLLRLQDLVDKLQlKVKAYKRQAEEAE--EQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGTKGL 1932
Cdd:PTZ00121 1414 AAAKKKADEAKKKAEEKK-KADEAKKKAEEAKkaDEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKA 1492
|
..
gi 1387193866 1933 NE 1934
Cdd:PTZ00121 1493 EE 1494
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1038-1447 |
1.67e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.78 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1038 LEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQalgsqLQKKLKELQARIEE 1117
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEA-----LEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1118 LEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHA 1197
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1198 DSVAELseqidNLQRVKQKLEKEKSEFKLE------LDDVTSNMEQIIKAKANLEKMCRTLEDQMNEHRSKAEETQRSVN 1271
Cdd:COG4717 231 QLENEL-----EAAALEERLKEARLLLLIAaallalLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1272 DLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVKAKNALAhaLQSARHDCDLLREQY---- 1347
Cdd:COG4717 306 ELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ--LEELEQEIAALLAEAgved 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1348 EEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKK-LAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIE 1426
Cdd:COG4717 384 EEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEeLEEELEELEEELEELEEELEELREELAELEAELE 463
|
410 420
....*....|....*....|.
gi 1387193866 1427 DLMVDVERSNAAAAALDKKQR 1447
Cdd:COG4717 464 QLEEDGELAELLQELEELKAE 484
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
915-1602 |
3.09e-08 |
|
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: 59.08 E-value: 3.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 915 LEAKVKEMTERLEDEEEMNAELTAKKRkledecSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTK 994
Cdd:pfam12128 263 LHFGYKSDETLIASRQEERQETSAELN------QLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLD 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 995 EKKALQEAHQQALDDLQAE-----------EDKVNTLTKAKVKL-----EQHVDDLEGSLEQEKKVRMDLERAKRKLEGD 1058
Cdd:pfam12128 337 ADIETAAADQEQLPSWQSElenleerlkalTGKHQDVTAKYNRRrskikEQNNRDIAGIKDKLAKIREARDRQLAVAEDD 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1059 LKlTQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSqlQKKLKELQARIEELEEELEAERTARAKVEKLRSD 1138
Cdd:pfam12128 417 LQ-ALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATAT--PELLLQLENFDERIERAREEQEAANAEVERLQSE 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1139 LsRELEEISERLEEAGGATSVQIEMNKKREAEFQKMrRDLEEATLQHeataaALRKKHADSVAELSEQIDNLQRVKQKLE 1218
Cdd:pfam12128 494 L-RQARKRRDQASEALRQASRRLEERQSALDELELQ-LFPQAGTLLH-----FLRKEAPDWEQSIGKVISPELLHRTDLD 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1219 KEKSEF----KLELDDVTSNMEQIIKAKANlekmcrTLEDQMNEHRSKAEEtqrsvnDLTSQRAKLQTENGELSRQLDEK 1294
Cdd:pfam12128 567 PEVWDGsvggELNLYGVKLDLKRIDVPEWA------ASEEELRERLDKAEE------ALQSAREKQAAAEEQLVQANGEL 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1295 EALISQLTRGKLTYTQQLEDLKRQLEEEVKAKNALAHALQSARhdcdllREQYEEETEAKAELQRVLSKANSEVAQWRTK 1374
Cdd:pfam12128 635 EKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERK------DSANERLNSLEAQLKQLDKKHQAWLEEQKEQ 708
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1375 YETDAIQRTE---ELEEAKK-KLAQRLQDAEEAVEAVNAKCSSLEKTKHRlqnEIEDLMVDVERsnaaAAALDKKQRNFD 1450
Cdd:pfam12128 709 KREARTEKQAywqVVEGALDaQLALLKAAIAARRSGAKAELKALETWYKR---DLASLGVDPDV----IAKLKREIRTLE 781
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1451 KILAEWKQKyeesqselessqkeaRSLSTELFKLKNayEESLEHLETFKRENKNLQEEISDLTEQLgssGKTIHELEKVR 1530
Cdd:pfam12128 782 RKIERIAVR---------------RQEVLRYFDWYQ--ETWLQRRPRLATQLSNIERAISELQQQL---ARLIADTKLRR 841
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387193866 1531 KQLEAEKLELQSALEEAEASLEHEEGKILR-AQLEFNQIKAEMERKLAEKDEEMEQAKRNHLRVVDSLQTSLD 1602
Cdd:pfam12128 842 AKLEMERKASEKQQVRLSENLRGLRCEMSKlATLKEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVE 914
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1681-1928 |
3.16e-08 |
|
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: 59.03 E-value: 3.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1681 LQAELEELRAVVEQteRSRKLaEQELIETSERVQLLHSQNTSLINQKKKMEADLSQLQTEVEEavQECRNAEEKAKKAIT 1760
Cdd:pfam01576 55 LCAEAEEMRARLAA--RKQEL-EEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDE--EEAARQKLQLEKVTT 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1761 DAAM--MAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIAlKGGKKQLQKLEARVRELENELEAEQKRNAESVK 1838
Cdd:pfam01576 130 EAKIkkLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKA-KSLSKLKNKHEAMISDLEERLKKEEKGRQELEK 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1839 GMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVN 1918
Cdd:pfam01576 209 AKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARN 288
|
250
....*....|
gi 1387193866 1919 KLRAKSRDIG 1928
Cdd:pfam01576 289 KAEKQRRDLG 298
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
945-1152 |
3.93e-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: 57.85 E-value: 3.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 945 DECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQeahqqalDDLQAEEDKVNTLTKAK 1024
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALE-------QELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1025 VKLEQHVDDLEGSLEQEKKVrmdLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQL 1104
Cdd:COG4942 93 AELRAELEAQKEELAELLRA---LYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1387193866 1105 QKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEE 1152
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1185-1916 |
4.47e-08 |
|
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: 58.70 E-value: 4.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1185 HEATAAALRKKHADSVAELSEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKMCRTLEDQMNEHRSKAE 1264
Cdd:pfam12128 228 RDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELN 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1265 etqrsvNDLTSQRAKLQTENGELSRqLDEkealisqltrgkltytqqleDLKRQLEEEVKAKNALAHALQSARHDCDLLR 1344
Cdd:pfam12128 308 ------GELSAADAAVAKDRSELEA-LED--------------------QHGAFLDADIETAAADQEQLPSWQSELENLE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1345 EQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEAVEA-----VNAKCSSLEKTKH 1419
Cdd:pfam12128 361 ERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESelreqLEAGKLEFNEEEY 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1420 RLQNEIEDLMVdveRSNAAAAALDKK--QRNFDKILAEWKQKyeesqseLESSQKEARSLSTELFKLKNAYEESLEHLET 1497
Cdd:pfam12128 441 RLKSRLGELKL---RLNQATATPELLlqLENFDERIERAREE-------QEAANAEVERLQSELRQARKRRDQASEALRQ 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1498 FKRENKNLQEEISDLTEQLGSSGKTIHELekvrkqleaeklelqsaLEEAEASLEHEEGKIL-RAQLEFNQIKAEMERKl 1576
Cdd:pfam12128 511 ASRRLEERQSALDELELQLFPQAGTLLHF-----------------LRKEAPDWEQSIGKVIsPELLHRTDLDPEVWDG- 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1577 AEKDEEMEQAKRNHLRVVDSlqtsldAETRSRNEALRVKkkmegdLNEMEIQLSHANRLAAEAQKQVKSLQSLLKDTQIQ 1656
Cdd:pfam12128 573 SVGGELNLYGVKLDLKRIDV------PEWAASEEELRER------LDKAEEALQSAREKQAAAEEQLVQANGELEKASRE 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1657 LDDAVRAnddLKENIAIVERRNNLLQAeleELRAVVEQTERSRKLAEqelietsERVQLLHSQNTSLINQKKKMEADLSQ 1736
Cdd:pfam12128 641 ETFARTA---LKNARLDLRRLFDEKQS---EKDKKNKALAERKDSAN-------ERLNSLEAQLKQLDKKHQAWLEEQKE 707
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1737 LQTEVEEAVQECRNAEEKAKKAiTDAAMMAEELKKEQDTSAHLERMKKNMEqtiKDLQHRLDEAEQIAlkggkkqlqKLE 1816
Cdd:pfam12128 708 QKREARTEKQAYWQVVEGALDA-QLALLKAAIAARRSGAKAELKALETWYK---RDLASLGVDPDVIA---------KLK 774
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1817 ARVRELENELEAEQKRNAESVKGMRKSERRI----KELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQ-------AEEA 1885
Cdd:pfam12128 775 REIRTLERKIERIAVRRQEVLRYFDWYQETWlqrrPRLATQLSNIERAISELQQQLARLIADTKLRRAKlemerkaSEKQ 854
|
730 740 750
....*....|....*....|....*....|.
gi 1387193866 1886 EEQANTNLSKFRKVQHELDEAEERADIAESQ 1916
Cdd:pfam12128 855 QVRLSENLRGLRCEMSKLATLKEDANSEQAQ 885
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1484-1923 |
5.62e-08 |
|
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: 58.21 E-value: 5.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1484 LKNAYEESLEHLETfkreNKNLQEEIsdlteqLGSSGKTIHELEKVRKQLEAEKLELQSAL---EEAEASLEHEEGKIlr 1560
Cdd:pfam15921 143 LRNQLQNTVHELEA----AKCLKEDM------LEDSNTQIEQLRKMMLSHEGVLQEIRSILvdfEEASGKKIYEHDSM-- 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1561 AQLEFNQIKAEMERKLAEKDEEMEQAKRNHLRVVDSLQTsLDAETRSRNEAL--RVKKKMEGDLNEMEIQLSHANRLAAE 1638
Cdd:pfam15921 211 STMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEA-LKSESQNKIELLlqQHQDRIEQLISEHEVEITGLTEKASS 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1639 AQKQVKSLQSLLkdtqiqlddavranddlkeniaiverrnnllqaeleelravveqtersrklaeqELIETSERvqllhS 1718
Cdd:pfam15921 290 ARSQANSIQSQL------------------------------------------------------EIIQEQAR-----N 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1719 QNTSLINQKKKMEADLSQLQTEVEEA--------------------------------VQECRNAEEKAKKAITDAAMMA 1766
Cdd:pfam15921 311 QNSMYMRQLSDLESTVSQLRSELREAkrmyedkieelekqlvlanseltearterdqfSQESGNLDDQLQKLLADLHKRE 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1767 EELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQialkggkkQLQKLEARVRELENELEAEQKRNAESVKGMRKSERR 1846
Cdd:pfam15921 391 KELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNM--------EVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEK 462
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387193866 1847 IKELTYQTEEDRKnllRLQDLVDKLqlkvkAYKRQAEEAEEQANTNLSKfrkvqhELDEAEERADIAESQVNKLRAK 1923
Cdd:pfam15921 463 VSSLTAQLESTKE---MLRKVVEEL-----TAKKMTLESSERTVSDLTA------SLQEKERAIEATNAEITKLRSR 525
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1481-1927 |
5.64e-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: 57.56 E-value: 5.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1481 LFKLKNAYEEsLEHLETFKRE--NKNLQEEISDLtEQLGSSGKTIHELEKVRKQ----LEAEKLELQSALEEAEASLEhe 1554
Cdd:pfam06160 2 LLLRKKIYKE-IDELEERKNElmNLPVQEELSKV-KKLNLTGETQEKFEEWRKKwddiVTKSLPDIEELLFEAEELND-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1555 EGKILRAQLEFNQIkaemERKLAEKDEEMEQakrnhlrVVDSLQTSLDAETRSRNEALRVKKK----------------- 1617
Cdd:pfam06160 78 KYRFKKAKKALDEI----EELLDDIEEDIKQ-------ILEELDELLESEEKNREEVEELKDKyrelrktllanrfsygp 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1618 ----MEGDLNEMEIQLSHANRLAA-----EAQKQVKSLQSLLKDTQIQLDDavranddlkenI-AIVERRNNLLQAELEE 1687
Cdd:pfam06160 147 aideLEKQLAEIEEEFSQFEELTEsgdylEAREVLEKLEEETDALEELMED-----------IpPLYEELKTELPDQLEE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1688 LRAVVEQTERSR-KLAEQELIETSERVQLLHSQNTSLINQK--KKMEADLSQLQTEVEEaVQECRNAEEKAKKaitdaam 1764
Cdd:pfam06160 216 LKEGYREMEEEGyALEHLNVDKEIQQLEEQLEENLALLENLelDEAEEALEEIEERIDQ-LYDLLEKEVDAKK------- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1765 maeELKKEQDT-SAHLERMKKNMEQTIKDLQH-----RLDEAEQIALKGGKKQLQKLEARVRELENELEAEQKRNAESVK 1838
Cdd:pfam06160 288 ---YVEKNLPEiEDYLEHAEEQNKELKEELERvqqsyTLNENELERVRGLEKQLEELEKRYDEIVERLEEKEVAYSELQE 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1839 GMRKSERRIKELTYQTEEDRKNL-------LRLQDLVDKLQLKVKAYKRQAE----------------EAEEQANTNLSK 1895
Cdd:pfam06160 365 ELEEILEQLEEIEEEQEEFKESLqslrkdeLEAREKLDEFKLELREIKRLVEksnlpglpesyldyffDVSDEIEDLADE 444
|
490 500 510
....*....|....*....|....*....|..
gi 1387193866 1896 FRKVQHELDEAEERADIAESQVNKLRAKSRDI 1927
Cdd:pfam06160 445 LNEVPLNMDEVNRLLDEAQDDVDTLYEKTEEL 476
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
831-1145 |
7.90e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.77 E-value: 7.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 831 KLYFKIKPLLKSAETEKEIALMKEEFGRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIK 910
Cdd:PRK03918 477 KLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKK 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 911 NKIQLEAKVKEMTERLedeeemnAELTAKKRKLEDEC-SELKRDIDDLE------LTLAKVEKEKHATENKVKNLTEEma 983
Cdd:PRK03918 557 KLAELEKKLDELEEEL-------AELLKELEELGFESvEELEERLKELEpfyneyLELKDAEKELEREEKELKKLEEE-- 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 984 gLDEIIAKLTKEKKALQEAHQQaLDDLQAEEDKvntltkakvkleqhvDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQ 1063
Cdd:PRK03918 628 -LDKAFEELAETEKRLEELRKE-LEELEKKYSE---------------EEYEELREEYLELSRELAGLRAELEELEKRRE 690
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1064 ESIMDLENDKQQLDERLKKKDfELNALNARIEDEQAlgsqLQKKLKELQARIeeleeeleaERTARAKVEKLRSDLSREL 1143
Cdd:PRK03918 691 EIKKTLEKLKEELEEREKAKK-ELEKLEKALERVEE----LREKVKKYKALL---------KERALSKVGEIASEIFEEL 756
|
..
gi 1387193866 1144 EE 1145
Cdd:PRK03918 757 TE 758
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1232-1791 |
8.72e-08 |
|
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: 57.52 E-value: 8.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1232 TSNMEQIIKAK----ANLEKMCRTLEDQMNEHRSKA-------EETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQ 1300
Cdd:pfam10174 228 TKALQTVIEMKdtkiSSLERNIRDLEDEVQMLKTNGllhtedrEEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLA 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1301 LTRGKLTYTQQLEDLKRQLE---EEVKAKNALAHALQSarhDCDLLREQYEEEteakaelQRVLSKansevaqwrtkyET 1377
Cdd:pfam10174 308 LQTKLETLTNQNSDCKQHIEvlkESLTAKEQRAAILQT---EVDALRLRLEEK-------ESFLNK------------KT 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1378 DAIQRteeLEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWK 1457
Cdd:pfam10174 366 KQLQD---LTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLE 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1458 QKyEESQSELESSQKEARSLSTElfklknayeESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEK 1537
Cdd:pfam10174 443 EA-LSEKERIIERLKEQREREDR---------ERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSG 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1538 LELQSALEEAEASLEH--EEGKILRAQLEFNQIKAEMERK---LAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEAL 1612
Cdd:pfam10174 513 LKKDSKLKSLEIAVEQkkEECSKLENQLKKAHNAEEAVRTnpeINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVE 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1613 RVKKKMEGDLNEMEIQLSHANRLAAEAQKQVKSLQSLLKDTQIQ-LDDAVRANDDLKENIAiverrnnllQAELEELRAV 1691
Cdd:pfam10174 593 NEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQlLEEARRREDNLADNSQ---------QLQLEELMGA 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1692 VEQTersrklaEQELIETSERV----QLLHSQNTSLINQKKKMEADLSqlqtEVEEAVQECRNAEEKAKKA-ITDAAMMA 1766
Cdd:pfam10174 664 LEKT-------RQELDATKARLsstqQSLAEKDGHLTNLRAERRKQLE----EILEMKQEALLAAISEKDAnIALLELSS 732
|
570 580
....*....|....*....|....*
gi 1387193866 1767 EELKKEQDTSAHLERMKKNMEQTIK 1791
Cdd:pfam10174 733 SKKKKTQEEVMALKREKDRLVHQLK 757
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
835-1013 |
8.97e-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: 54.93 E-value: 8.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 835 KIKPLLKSAETEKEIALMKEEFGRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLiKNKIQ 914
Cdd:COG1579 5 DLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY-EEQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 915 LEAKVKEMtERLEDEEEMnaeLTAKKRKLEDECSELKRDIDDLELTLAKVEKEKhatENKVKNLTEEMAGLDEIIAKLTK 994
Cdd:COG1579 84 NVRNNKEY-EALQKEIES---LKRRISDLEDEILELMERIEELEEELAELEAEL---AELEAELEEKKAELDEELAELEA 156
|
170
....*....|....*....
gi 1387193866 995 EKKALQEAHQQALDDLQAE 1013
Cdd:COG1579 157 ELEELEAEREELAAKIPPE 175
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
853-1428 |
1.02e-07 |
|
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: 57.27 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 853 KEEFGRLKEALEK--SEARRKELEEKMVSLLQEKNDLQLQVQAEQD---NLADAEERCDQL-----------------IK 910
Cdd:COG3096 471 RRQFEKAYELVCKiaGEVERSQAWQTARELLRRYRSQQALAQRLQQlraQLAELEQRLRQQqnaerlleefcqrigqqLD 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 911 NKIQLEAKVKEMTERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELT----------LAKVEKEKHATENKVKNLTE 980
Cdd:COG3096 551 AAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARapawlaaqdaLERLREQSGEALADSQEVTA 630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 981 EMAGLDEIIAKLTKEKKALQEAHQQALDDLQ-------AEEDKVNTLTKA--KVKLEQHVDD-----------LEGSLEQ 1040
Cdd:COG3096 631 AMQQLLEREREATVERDELAARKQALESQIErlsqpggAEDPRLLALAERlgGVLLSEIYDDvtledapyfsaLYGPARH 710
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1041 EKKVRmDLERAKRKLEGdLKLTQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKklkelqarieelee 1120
Cdd:COG3096 711 AIVVP-DLSAVKEQLAG-LEDCPEDLYLIEGDPDSFDDSVFDAEELEDAVVVKLSDRQWRYSRFPE-------------- 774
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1121 eleAERTARAKVEKLRSDLSRELEEISERLEEAggATSVQiemnkkreaEFQKMRRDLEEATLQH---------EATAAA 1191
Cdd:COG3096 775 ---VPLFGRAAREKRLEELRAERDELAEQYAKA--SFDVQ---------KLQRLHQAFSQFVGGHlavafapdpEAELAA 840
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1192 LRKKHADSVAELSEQIDNLQRVKQKLEKEKSEFKL--------ELDDVTSNMEQIIKAKANLEKmCRTLEDQMNEHRSKA 1263
Cdd:COG3096 841 LRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLlnkllpqaNLLADETLADRLEELREELDA-AQEAQAFIQQHGKAL 919
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1264 EETQRSVNDLTS---QRAKLQTENGELSRQLDEKEALISQLT-----RGKLTYtqqlEDLKRQLEEEVKAKNALAHALQS 1335
Cdd:COG3096 920 AQLEPLVAVLQSdpeQFEQLQADYLQAKEQQRRLKQQIFALSevvqrRPHFSY----EDAVGLLGENSDLNEKLRARLEQ 995
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1336 ARHDCDLLREQYEEETEAKAELQRVLSKANSevaQWRTKYET--DAIQRTEELE-----EAKKKLAQRLQDAEEAVEAVN 1408
Cdd:COG3096 996 AEEARREAREQLRQAQAQYSQYNQVLASLKS---SRDAKQQTlqELEQELEELGvqadaEAEERARIRRDELHEELSQNR 1072
|
650 660
....*....|....*....|
gi 1387193866 1409 AKCSSLEKTKHRLQNEIEDL 1428
Cdd:COG3096 1073 SRRSQLEKQLTRCEAEMDSL 1092
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
847-1366 |
1.13e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.08 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 847 KEIALMKEEFGRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAeQDNLADAEERCDQLIKNKIQLEAKVKEMTERL 926
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL-LPLYQELEALEAELAELPERLEELEERLEELR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 927 EDEEEMnaeltakkRKLEDECSELKRDIDDLEltlakvEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQA 1006
Cdd:COG4717 160 ELEEEL--------EELEAELAELQEELEELL------EQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1007 LDDLQAEEDKVNTLtkakvKLEQHVDDLEGSLEqekkvrmdLERAKRKLEGDLKLTQESIMDLendkqqlderlkkkdfe 1086
Cdd:COG4717 226 EEELEQLENELEAA-----ALEERLKEARLLLL--------IAAALLALLGLGGSLLSLILTI----------------- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1087 LNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGatsvQIEMNKK 1166
Cdd:COG4717 276 AGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLD----RIEELQE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1167 REAEFQKMRRDLEEATLQHEAtAAALRKKHADSVAELSEQIDNLQRvKQKLEKEKSEFKLELDDVTSNMEQIIKA--KAN 1244
Cdd:COG4717 352 LLREAEELEEELQLEELEQEI-AALLAEAGVEDEEELRAALEQAEE-YQELKEELEELEEQLEELLGELEELLEAldEEE 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1245 LEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTEnGELSRQLDEKEALISQLtrgkltytqqledlkRQLEEEVK 1324
Cdd:COG4717 430 LEEELEELEEELEELEEELEELREELAELEAELEQLEED-GELAELLQELEELKAEL---------------RELAEEWA 493
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1387193866 1325 AKNALAHALQSArhdcdllREQYEEETeakaeLQRVLSKANS 1366
Cdd:COG4717 494 ALKLALELLEEA-------REEYREER-----LPPVLERASE 523
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
843-1055 |
1.41e-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: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 843 AETEKEIALMKEEFGRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEM 922
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 923 ---TERLEDEEEMNAELTAKK--------RKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAK 991
Cdd:COG4942 110 lraLYRLGRQPPLALLLSPEDfldavrrlQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAA 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387193866 992 LTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQHVDDLEGSLEQ--EKKVRMDLERAKRKL 1055
Cdd:COG4942 190 LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAaaERTPAAGFAALKGKL 255
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1356-1775 |
1.50e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.70 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1356 ELQRVLSKANSEVAQWRTKYET--DAIQRTEELEEAKKKLAQRLQDAEEAVEAVnakcsSLEKTKHRLQNEIEDLMVDVE 1433
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEEleELEEELEELEAELEELREELEKLEKLLQLL-----PLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1434 RSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSlstELFKLKNAYEESLEHLETFKRENKNLQEEISDLT 1513
Cdd:COG4717 150 ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE---ELQDLAEELEELQQRLAELEEELEEAQEELEELE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1514 EQLGSSgKTIHELEKVRKQLEAEK---------LELQSALEEAEASLEHEEGK------ILRAQLEFNQIKAEMERKLAE 1578
Cdd:COG4717 227 EELEQL-ENELEAAALEERLKEARlllliaaalLALLGLGGSLLSLILTIAGVlflvlgLLALLFLLLAREKASLGKEAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1579 KDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRlAAEAQKQVKSLQSLLKDTQIQLD 1658
Cdd:COG4717 306 ELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE-ELQLEELEQEIAALLAEAGVEDE 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1659 DAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLA---------EQELIETSERVQLLHSQNTSLINQKKK 1729
Cdd:COG4717 385 EELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEeleeeleelEEELEELEEELEELREELAELEAELEQ 464
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1387193866 1730 MEAD--LSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDT 1775
Cdd:COG4717 465 LEEDgeLAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1240-1455 |
1.64e-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: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1240 KAKANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQL 1319
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1320 EEEVKA-KNALAHALQSARHDCDLLREQYEEETEAKAELQRVlskanSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQ 1398
Cdd:COG4942 100 EAQKEElAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYL-----KYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1387193866 1399 DAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAE 1455
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1175-1928 |
1.85e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 56.50 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1175 RRDLEEATLQHEATAAALRKKHA--DSVAELSEQIDNLQRVKQKLEKEKSEFKLELDDVTSNM---EQIIKAKANLEKMC 1249
Cdd:PRK04863 282 RVHLEEALELRRELYTSRRQLAAeqYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALrqqEKIERYQADLEELE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1250 RTLEDQM----------NEHRSKAEETQRSVNDLTSQRAklqtengelsrqlDEKEALISQLTRGkLTYTQQLedlkrQL 1319
Cdd:PRK04863 362 ERLEEQNevveeadeqqEENEARAEAAEEEVDELKSQLA-------------DYQQALDVQQTRA-IQYQQAV-----QA 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1320 EEEVKAKNALAH-ALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYE-----TDAIQRTEELEEAKKKL 1393
Cdd:PRK04863 423 LERAKQLCGLPDlTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQlvrkiAGEVSRSEAWDVARELL 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1394 A----QRLQDAEeaVEAVNAKCSSLEKtkhRLQNeiedlmvdversnaaaaaldkkQRNFDKILAEWKQKYEESQSELEs 1469
Cdd:PRK04863 503 RrlreQRHLAEQ--LQQLRMRLSELEQ---RLRQ----------------------QQRAERLLAEFCKRLGKNLDDED- 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1470 sqkearslstELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSgktIHELEkvrkQLEAEKLELQSALEE-AE 1548
Cdd:PRK04863 555 ----------ELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQAR---IQRLA----ARAPAWLAAQDALARlRE 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1549 ASLEHEEGkilRAQL-EFNQIKAEMERKLAEKDEEMEQAKRNHLRVVDSLQTsldAETRSRNEALRVKKKMEGDL----- 1622
Cdd:PRK04863 618 QSGEEFED---SQDVtEYMQQLLERERELTVERDELAARKQALDEEIERLSQ---PGGSEDPRLNALAERFGGVLlseiy 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1623 NEMEIQ-----------LSHA---NRLAAeAQKQVKSLQSLLKDTQI------QLDDAVRANDDLKENIAIV-------- 1674
Cdd:PRK04863 692 DDVSLEdapyfsalygpARHAivvPDLSD-AAEQLAGLEDCPEDLYLiegdpdSFDDSVFSVEELEKAVVVKiadrqwry 770
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1675 --------------ERRNNLLQAELEELravveqTERSRKLAEQelietSERVQLLHSQNTSLINQKKKM------EADL 1734
Cdd:PRK04863 771 srfpevplfgraarEKRIEQLRAEREEL------AERYATLSFD-----VQKLQRLHQAFSRFIGSHLAVafeadpEAEL 839
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1735 SQLQT---EVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERmkKNMEQTIKDLQHRLDEAEQ----IALKG 1807
Cdd:PRK04863 840 RQLNRrrvELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLAD--ETLADRVEEIREQLDEAEEakrfVQQHG 917
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1808 GK-KQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTE-------EDRKNLL-RLQDLVDKLQLKVKAY 1878
Cdd:PRK04863 918 NAlAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQrrahfsyEDAAEMLaKNSDLNEKLRQRLEQA 997
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1879 KRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIG 1928
Cdd:PRK04863 998 EQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLG 1047
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
651-675 |
2.03e-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: 52.73 E-value: 2.03e-07
10 20
....*....|....*....|....*
gi 1387193866 651 HRENLNKLMTNLRSTHPHFVRCIIP 675
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1010-1223 |
2.12e-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: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1010 LQAEEDKVNTLTKAKVKLEQHVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNA 1089
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1090 LNARIEDEQALGSQLQKKL--KELQARIEELEEELEAERTARA-----KVEKLRSDLSRELEEISERLEEAGGATSVQIE 1162
Cdd:COG4942 95 LRAELEAQKEELAELLRALyrLGRQPPLALLLSPEDFLDAVRRlqylkYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387193866 1163 MNKKREAEFQKMRRDLEEATLQHEATAAALRKK---HADSVAELSEQIDNLQRVKQKLEKEKSE 1223
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKElaeLAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1619-1836 |
2.12e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.22 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1619 EGDLNEMEIQLSHANRLAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEqtERS 1698
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG--ERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1699 RKLAEQ-----------------ELIETSERVQLLHSQNTSLINQKKKMEADLSQLQTEVEEAVQEcrnaeekakkaitd 1761
Cdd:COG3883 93 RALYRSggsvsyldvllgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE-------------- 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387193866 1762 aammAEELKKEqdtsahLERMKKNMEQTIKDLQHRLDEAEQialkggkkQLQKLEARVRELENELEAEQKRNAES 1836
Cdd:COG3883 159 ----LEALKAE------LEAAKAELEAQQAEQEALLAQLSA--------EEAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1668-1933 |
2.77e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.84 E-value: 2.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1668 KENIAIVERRNNLLQAELEELRAVVE--QTERSRKLAEQELIETSERVQLlhsqnTSLINQKKKMEADLSQLQTEVEEAV 1745
Cdd:TIGR02169 176 LEELEEVEENIERLDLIIDEKRQQLErlRREREKAERYQALLKEKREYEG-----YELLKEKEALERQKEAIERQLASLE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1746 QEcrnaEEKAKKAITDAAMMAEELKKEQDTSAhlERMKKNMEQTIKDLQHRLDEAEqialkggkKQLQKLEARVRELENE 1825
Cdd:TIGR02169 251 EE----LEKLTEEISELEKRLEEIEQLLEELN--KKIKDLGEEEQLRVKEKIGELE--------AEIASLERSIAEKERE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1826 LEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDE 1905
Cdd:TIGR02169 317 LEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEK 396
|
250 260
....*....|....*....|....*...
gi 1387193866 1906 AEERADIAESQVNKLRAKSRDIGTKGLN 1933
Cdd:TIGR02169 397 LKREINELKRELDRLQEELQRLSEELAD 424
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
861-1082 |
3.28e-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: 54.77 E-value: 3.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 861 EALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMTERLEDEEEMNAELTAKK 940
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 941 RKLEDECSELKRDIddleltlakvekEKHATENKVKNLT-----EEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEED 1015
Cdd:COG4942 100 EAQKEELAELLRAL------------YRLGRQPPLALLLspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387193866 1016 KVNTLTKAKVKLEQHVDDLEGSLEQEKKVRmdlERAKRKLEGDLKLTQESIMDLENDKQQLDERLKK 1082
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAER---QKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
859-1835 |
3.31e-07 |
|
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: 55.83 E-value: 3.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 859 LKEALEKSEARRKELEEKMVSLLQEKNdlQLQVQAEQDNLADAEERCDQLIKNKIQLEAKvkemtERLEDEEEMNAELTA 938
Cdd:TIGR01612 753 LNKILEDFKNKEKELSNKINDYAKEKD--ELNKYKSKISEIKNHYNDQINIDNIKDEDAK-----QNYDKSKEYIKTISI 825
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 939 KKRKLEDECSELKRDIDDLeltLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQ-EAHQQALDD-------- 1009
Cdd:TIGR01612 826 KEDEIFKIINEMKFMKDDF---LNKVDKFINFENNCKEKIDSEHEQFAELTNKIKAEISDDKlNDYEKKFNDskslinei 902
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1010 ---LQAEEDKVNTLTKakvkLEQHVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFE 1086
Cdd:TIGR01612 903 nksIEEEYQNINTLKK----VDEYIKICENTKESIEKFHNKQNILKEILNKNIDTIKESNLIEKSYKDKFDNTLIDKINE 978
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1087 LNAL--NARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAkvEKLRSDLSRELEE------------------I 1146
Cdd:TIGR01612 979 LDKAfkDASLNDYEAKNNELIKYFNDLKANLGKNKENMLYHQFDEK--EKATNDIEQKIEDanknipnieiaihtsiynI 1056
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1147 SERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELSEQIDNLQRVKQKLEKEKSEFKl 1226
Cdd:TIGR01612 1057 IDEIEKEIGKNIELLNKEILEEAEINITNFNEIKEKLKHYNFDDFGKEENIKYADEINKIKDDIKNLDQKIDHHIKALE- 1135
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1227 ELDDVTSNMEQIIKAKAN-LEKMCRTLedQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGK 1305
Cdd:TIGR01612 1136 EIKKKSENYIDEIKAQINdLEDVADKA--ISNDDPEEIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEIEKDKTSLEEVK 1213
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1306 ---LTYTQQLEDL-KRQLEEEVKAKNALAHALQSARHDCDLLREQYEE-------ETEAKAELQrVLSKANSEvaqwRTK 1374
Cdd:TIGR01612 1214 ginLSYGKNLGKLfLEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEienemgiEMDIKAEME-TFNISHDD----DKD 1288
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1375 YETDAIQRTEELEEAKKKLAQRLQDaeeaveavNAKCSSLEKTKHRLQNEIedlmVDVERSNAAAAALDKKQRNFDKILa 1454
Cdd:TIGR01612 1289 HHIISKKHDENISDIREKSLKIIED--------FSEESDINDIKKELQKNL----LDAQKHNSDINLYLNEIANIYNIL- 1355
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1455 ewkqkyeesqselessqkearslstELFKLKNAYEESLEHLETFKRENKNLQEEISDlTEQLGssgKTIHElekvRKQLE 1534
Cdd:TIGR01612 1356 -------------------------KLNKIKKIIDEVKEYTKEIEENNKNIKDELDK-SEKLI---KKIKD----DINLE 1402
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1535 AEKLELQSALEEAEAsleheEGKILRAQLEFNQIKAEMerklAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNeALRV 1614
Cdd:TIGR01612 1403 ECKSKIESTLDDKDI-----DECIKKIKELKNHILSEE----SNIDTYFKNADENNENVLLLFKNIEMADNKSQH-ILKI 1472
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1615 KKK-----MEGDLNEMEIQLSHANRLAAEAQKQVKSLQS---LLKdtQIQLDDAVRAND----DLKENIAIVERRNNLLQ 1682
Cdd:TIGR01612 1473 KKDnatndHDFNINELKEHIDKSKGCKDEADKNAKAIEKnkeLFE--QYKKDVTELLNKysalAIKNKFAKTKKDSEIII 1550
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1683 AELEELRAVV----EQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMEADLSQLQ--TEVEEAVQECRNAEEKAK 1756
Cdd:TIGR01612 1551 KEIKDAHKKFileaEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLENFENKFLkiSDIKKKINDCLKETESIE 1630
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1757 KAITDAAMMAEE--LKKEQDTSAHLERMKKNMEQTIKDLQHRldeaeqialkggKKQLQKLEARVRELENELEaEQKRNA 1834
Cdd:TIGR01612 1631 KKISSFSIDSQDteLKENGDNLNSLQEFLESLKDQKKNIEDK------------KKELDELDSEIEKIEIDVD-QHKKNY 1697
|
.
gi 1387193866 1835 E 1835
Cdd:TIGR01612 1698 E 1698
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
841-1111 |
3.71e-07 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 55.29 E-value: 3.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 841 KSAETEKEIALMKEEFGRLKEALEKS-----EARRKELEEkMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKI-- 913
Cdd:PLN02939 118 NSKDGEQLSDFQLEDLVGMIQNAEKNilllnQARLQALED-LEKILTEKEALQGKINILEMRLSETDARIKLAAQEKIhv 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 914 -----QLEAKVKEMTERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKekhaTENKVKNLTEEMAGLDEI 988
Cdd:PLN02939 197 eileeQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAE----TEERVFKLEKERSLLDAS 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 989 IAKLTKEKKALQEAHQQaLDDLQAEE--DKVNTLTKAKVKLEQHVDDLEGSLEQEKkvrmDLERAKRKLEGDL------K 1060
Cdd:PLN02939 273 LRELESKFIVAQEDVSK-LSPLQYDCwwEKVENLQDLLDRATNQVEKAALVLDQNQ----DLRDKVDKLEASLkeanvsK 347
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1387193866 1061 LTQESIMDLENDKQQLDERLKKKDFElnaLNARIEDEQALGSQLQKKLKEL 1111
Cdd:PLN02939 348 FSSYKVELLQQKLKLLEERLQASDHE---IHSYIQLYQESIKEFQDTLSKL 395
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
921-1339 |
3.79e-07 |
|
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: 54.69 E-value: 3.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 921 EMTERLEDEEEMNAELTAKKRKLEDECSEL---KRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKK 997
Cdd:pfam19220 14 EMADRLEDLRSLKADFSQLIEPIEAILRELpqaKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 998 ALQEAHQQAldDLQAEEDKVNTLTKakvklEQHVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLD 1077
Cdd:pfam19220 94 KLEAALREA--EAAKEELRIELRDK-----TAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATAR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1078 ERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARieeleeeleaERTARAKVEKLRSDLSRELEEiSERLEEAggat 1157
Cdd:pfam19220 167 ERLALLEQENRRLQALSEEQAAELAELTRRLAELETQ----------LDATRARLRALEGQLAAEQAE-RERAEAQ---- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1158 svqiemnkkreaefqkmrRDLEEATLQHEATAAALRKKHADSVAELSEQIDNLQRvKQKLEKEKSEFKLElddvtSNMEQ 1237
Cdd:pfam19220 232 ------------------LEEAVEAHRAERASLRMKLEALTARAAATEQLLAEAR-NQLRDRDEAIRAAE-----RRLKE 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1238 IIKAKANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKL----QTENGELSRQLDEKEAL---ISQLTR----GKL 1306
Cdd:pfam19220 288 ASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEMLtkalAAKDAALERAEERIASLsdrIAELTKrfevERA 367
|
410 420 430
....*....|....*....|....*....|....
gi 1387193866 1307 TYTQQLEDLKRQLEEEvKAKNALAH-ALQSARHD 1339
Cdd:pfam19220 368 ALEQANRRLKEELQRE-RAERALAQgALEIARES 400
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
840-1097 |
3.90e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.41 E-value: 3.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 840 LKSAETEKEIALMKEEFGRLKEALEKSEARRKELEEKMVSLlqeknDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKV 919
Cdd:COG3206 168 LRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLV-----DLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 920 KEMTERLEDEEEMNAELTAkkrklEDECSELKRDIDDLELTLAkvEKEKHATEN--KVKNLTEEMAGLdeiiakltkeKK 997
Cdd:COG3206 243 AALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAELEAELA--ELSARYTPNhpDVIALRAQIAAL----------RA 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 998 ALQEAHQQALDDLQAEedkVNTLTKAKVKLEQHVDDLEGSLEQEKKVRMDLERAKRklegDLKLTQESIMDLENDKQQLD 1077
Cdd:COG3206 306 QLQQEAQRILASLEAE---LEALQAREASLQAQLAQLEARLAELPELEAELRRLER----EVEVARELYESLLQRLEEAR 378
|
250 260
....*....|....*....|
gi 1387193866 1078 ERLkkkdfELNALNARIEDE 1097
Cdd:COG3206 379 LAE-----ALTVGNVRVIDP 393
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1211-1896 |
4.12e-07 |
|
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: 55.03 E-value: 4.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1211 QRVKQKLEKEKSEFKlelddvtsNMEQIIKakaNLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQ 1290
Cdd:TIGR04523 36 KQLEKKLKTIKNELK--------NKEKELK---NLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1291 LDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQ 1370
Cdd:TIGR04523 105 LSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1371 WRTKYETDAIQRT--EELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRN 1448
Cdd:TIGR04523 185 IQKNIDKIKNKLLklELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNK 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1449 FDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLehLETFKRENKNLQEEISDLTEQLGSSGKTIHELEK 1528
Cdd:TIGR04523 265 IKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDW--NKELKSELKNQEKKLEEIQNQISQNNKIISQLNE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1529 VRKQLEAEKLELQSALEEAEASLEHEEGKILRAQLEfNQIKAEMERKLAEKDEEMEQAKRNHLRVVDSLQTSLDaetrsr 1608
Cdd:TIGR04523 343 QISQLKKELTNSESENSEKQRELEEKQNEIEKLKKE-NQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIK------ 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1609 nealrvKKKMEGDLNEMEIQLSHANRLaaEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEEL 1688
Cdd:TIGR04523 416 ------KLQQEKELLEKEIERLKETII--KNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQK 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1689 RAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMEADLSQLQTEVeeavqecRNAEEKAKKaitdaamMAEE 1768
Cdd:TIGR04523 488 QKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKI-------SDLEDELNK-------DDFE 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1769 LKKEQdtsahLERMKKNMEQTIKDLQHRLDEaeqialkggkkqlqkLEARVRELENELEAEQKRNAESVKGMRKSERRIK 1848
Cdd:TIGR04523 554 LKKEN-----LEKEIDEKNKEIEELKQTQKS---------------LKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKIS 613
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1387193866 1849 ELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKF 1896
Cdd:TIGR04523 614 SLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKW 661
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
929-1424 |
4.47e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 4.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 929 EEEMNAELTAKKRKLEDECSELKRDIDDLElTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALqEAHQQALD 1008
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELK-EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-EKLLQLLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1009 DLQAEEDKVNTLTKAKVKLEQhvddlegsLEQEKKVRMDLERAKRKLEGDLKLTQESI-MDLENDKQQLDERLKKKDFEL 1087
Cdd:COG4717 130 LYQELEALEAELAELPERLEE--------LEERLEELRELEEELEELEAELAELQEELeELLEQLSLATEEELQDLAEEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1088 NALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRS--------DLSRELEEISERLEEAGGATSV 1159
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLlliaaallALLGLGGSLLSLILTIAGVLFL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1160 QIEMNKKREAEFQKMRRDLEEATLQHEATAAAlrkkhadsvAELSEQidNLQRVKQKLEKEKSEFKLELDDVTSNMEQII 1239
Cdd:COG4717 282 VLGLLALLFLLLAREKASLGKEAEELQALPAL---------EELEEE--ELEELLAALGLPPDLSPEELLELLDRIEELQ 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1240 KAKANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQtengelsrQLDEKEALisqltrgkltyTQQLEDLKRQL 1319
Cdd:COG4717 351 ELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALE--------QAEEYQEL-----------KEELEELEEQL 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1320 EEEVKAKNALAhalqsARHDCDLLREQYEEETEAKAELQRVLSKANSEVAqwRTKYETDAIQRTEELEEAKKKLAQRLQD 1399
Cdd:COG4717 412 EELLGELEELL-----EALDEEELEEELEELEEELEELEEELEELREELA--ELEAELEQLEEDGELAELLQELEELKAE 484
|
490 500
....*....|....*....|....*...
gi 1387193866 1400 AEEAVEAVNAKC---SSLEKTKHRLQNE 1424
Cdd:COG4717 485 LRELAEEWAALKlalELLEEAREEYREE 512
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
854-1231 |
4.57e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 55.29 E-value: 4.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 854 EEFGRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIK----NKIQLEAKVKEMTERLEDE 929
Cdd:PRK01156 342 IKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKiqeiDPDAIKKELNEINVKLQDI 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 930 EEMNAELTAKKRKLEDECSELKRD-------------------------IDDLELTLAKVEKEKHATENKVKNLTEEMAG 984
Cdd:PRK01156 422 SSKVSSLNQRIRALRENLDELSRNmemlngqsvcpvcgttlgeeksnhiINHYNEKKSRLEEKIREIEIEVKDIDEKIVD 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 985 LDEIIAKLTKEKKALQEAHQQALDDLQAE----EDKVNTLTKAKVKLEQ--------HVDDLEGSLEQEKK--------- 1043
Cdd:PRK01156 502 LKKRKEYLESEEINKSINEYNKIESARADlediKIKINELKDKHDKYEEiknrykslKLEDLDSKRTSWLNalavislid 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1044 ---VRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNALNAR---IEDEQALGSQLQKKLKELQARIEE 1117
Cdd:PRK01156 582 ietNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKyneIQENKILIEKLRGKIDNYKKQIAE 661
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1118 LEEELEAERTARAKVEKLRSDL---SRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRK 1194
Cdd:PRK01156 662 IDSIIPDLKEITSRINDIEDNLkksRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKAIGDLKRL 741
|
410 420 430
....*....|....*....|....*....|....*....
gi 1387193866 1195 KHADSVAELSEQI--DNLQRVKQKLEKEKSEFKLELDDV 1231
Cdd:PRK01156 742 REAFDKSGVPAMIrkSASQAMTSLTRKYLFEFNLDFDDI 780
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
847-1277 |
4.80e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 55.11 E-value: 4.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 847 KEIALmkEEFGRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMTERL 926
Cdd:pfam05483 403 KEVEL--EELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTEL 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 927 EDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQA 1006
Cdd:pfam05483 481 EKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQK 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1007 LDDLQAEEDKVntltkakvklEQHVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFE 1086
Cdd:pfam05483 561 GDEVKCKLDKS----------EENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQ 630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1087 LNALNARIEDEQALGSQLQKKLKELqarieeleeeleaERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKK 1166
Cdd:pfam05483 631 LNAYEIKVNKLELELASAKQKFEEI-------------IDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKR 697
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1167 REAEFQKMrrdleeatlqheataAALRKKHADSVAELSEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMeqiikaKANLE 1246
Cdd:pfam05483 698 CQHKIAEM---------------VALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNI------KAELL 756
|
410 420 430
....*....|....*....|....*....|.
gi 1387193866 1247 KMCRTLEDQMNEHRSKAEETQRSVNDLTSQR 1277
Cdd:pfam05483 757 SLKKQLEIEKEEKEKLKMEAKENTAILKDKK 787
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
843-1447 |
5.69e-07 |
|
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: 54.96 E-value: 5.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 843 AETEKEIALMKEEFGRLKEALEKSEARRKELEEKmvslLQEKND-LQLQVQAEQdnLADAEERCdqliknkiqlEAKVKE 921
Cdd:COG3096 295 FGARRQLAEEQYRLVEMARELEELSARESDLEQD----YQAASDhLNLVQTALR--QQEKIERY----------QEDLEE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 922 MTERLEDEEEMNAELT-------AKKRKLEDECSELKRDIDDL-------------------------------ELTLAK 963
Cdd:COG3096 359 LTERLEEQEEVVEEAAeqlaeaeARLEAAEEEVDSLKSQLADYqqaldvqqtraiqyqqavqalekaralcglpDLTPEN 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 964 VEKEKHATENKVKNLTEEMAGLDE--IIAKLTKEK--KALQ------------EAHQQALDDLQAEEDKVNTLTKAkVKL 1027
Cdd:COG3096 439 AEDYLAAFRAKEQQATEEVLELEQklSVADAARRQfeKAYElvckiageversQAWQTARELLRRYRSQQALAQRL-QQL 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1028 EQHVDDLEGSLEQEKKVRMDLERAKRKLEGDLkltqESIMDLENDKQQLDERLKKkdfelnaLNARIEDEQALGSQLQKK 1107
Cdd:COG3096 518 RAQLAELEQRLRQQQNAERLLEEFCQRIGQQL----DAAEELEELLAELEAQLEE-------LEEQAAEAVEQRSELRQQ 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1108 LKELQARIEELEEELEAERTARAKVEKLRsdlsrelEEISERLEEAGGATS-VQIEMNKKREAEFQKmrrdlEEATLQHE 1186
Cdd:COG3096 587 LEQLRARIKELAARAPAWLAAQDALERLR-------EQSGEALADSQEVTAaMQQLLEREREATVER-----DELAARKQ 654
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1187 ATAAALRKKHADSVAE------LSEQ---------------------------------IDNLQRVKQKL---------- 1217
Cdd:COG3096 655 ALESQIERLSQPGGAEdprllaLAERlggvllseiyddvtledapyfsalygparhaivVPDLSAVKEQLagledcpedl 734
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1218 -------------------------------------------------EKEKSEFKLELDDVTsnmEQIIKAKANLEKM 1248
Cdd:COG3096 735 yliegdpdsfddsvfdaeeledavvvklsdrqwrysrfpevplfgraarEKRLEELRAERDELA---EQYAKASFDVQKL 811
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1249 CRTLED-------------------QMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTrgkL--- 1306
Cdd:COG3096 812 QRLHQAfsqfvgghlavafapdpeaELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQAN---Llad 888
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1307 -TYTQQLEDLKRQLEEEVKAKNALAH-------------ALQSARHDCDLLREQYEeetEAKAELQRVLSK--ANSEVAQ 1370
Cdd:COG3096 889 eTLADRLEELREELDAAQEAQAFIQQhgkalaqleplvaVLQSDPEQFEQLQADYL---QAKEQQRRLKQQifALSEVVQ 965
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1371 WRT--KYEtDAIQRTEELEEAKKKLAQRLQDAE-------EAVEAVNAKCS-------SLeKTKHR--------LQNEIE 1426
Cdd:COG3096 966 RRPhfSYE-DAVGLLGENSDLNEKLRARLEQAEearrearEQLRQAQAQYSqynqvlaSL-KSSRDakqqtlqeLEQELE 1043
|
810 820
....*....|....*....|.
gi 1387193866 1427 DLMVDVErSNAAAAALDKKQR 1447
Cdd:COG3096 1044 ELGVQAD-AEAEERARIRRDE 1063
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1356-1930 |
5.93e-07 |
|
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: 54.64 E-value: 5.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1356 ELQRVLSKANSEVA---QWRTKYETDAIQRTEELEEAKKKLAQ---RLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLM 1429
Cdd:TIGR04523 100 KLNSDLSKINSEIKndkEQKNKLEVELNKLEKQKKENKKNIDKfltEIKKKEKELEKLNNKYNDLKKQKEELENELNLLE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1430 VDversnaaaaaLDKKQRNFDKILAEWKQKYEESQSELESSQKEaRSLSTELFKLKNAYEESLEHLETFKRENKNLQEEI 1509
Cdd:TIGR04523 180 KE----------KLNIQKNIDKIKNKLLKLELLLSNLKKKIQKN-KSLESQISELKKQNNQLKDNIEKKQQEINEKTTEI 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1510 SDLTEQLGSsgkTIHELEKVRKQLEAEKLELQSA---LEEAEASLEHEEGKI--LRAQLEFNQIKaEMERKLAEKDEEME 1584
Cdd:TIGR04523 249 SNTQTQLNQ---LKDEQNKIKKQLSEKQKELEQNnkkIKELEKQLNQLKSEIsdLNNQKEQDWNK-ELKSELKNQEKKLE 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1585 QAK---RNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRLAAEAQKQVKSLQSLLKDTQIQLDDAV 1661
Cdd:TIGR04523 325 EIQnqiSQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQE 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1662 RANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMEADLSQLQTEV 1741
Cdd:TIGR04523 405 KLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNL 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1742 EEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLD--EAEQIALKGGKKQlQKLEARV 1819
Cdd:TIGR04523 485 EQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISdlEDELNKDDFELKK-ENLEKEI 563
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1820 RELENELEaEQKRNAESVKgmrKSERRIKELTYQTEEDRKNLLRLQDLVDKLQLKVkayKRQAEEAEEQANTNLSKFRKV 1899
Cdd:TIGR04523 564 DEKNKEIE-ELKQTQKSLK---KKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSL---EKELEKAKKENEKLSSIIKNI 636
|
570 580 590
....*....|....*....|....*....|.
gi 1387193866 1900 QHELDEAEERADIAESQVNKLRAKSRDIGTK 1930
Cdd:TIGR04523 637 KSKKNKLKQEVKQIKETIKEIRNKWPEIIKK 667
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
852-1017 |
7.29e-07 |
|
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: 52.23 E-value: 7.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 852 MKEEFGRLKEaLEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMTERLE-DEE 930
Cdd:COG1579 2 MPEDLRALLD-LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKkYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 931 EMNAELTAKKRK-LEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDD 1009
Cdd:COG1579 81 QLGNVRNNKEYEaLQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEE 160
|
....*...
gi 1387193866 1010 LQAEEDKV 1017
Cdd:COG1579 161 LEAEREEL 168
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1042-1868 |
9.19e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.19 E-value: 9.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1042 KKVRMDLERAKRKLegdlKLTQESIMDLENDKQQLDERLKK------KDFELNALNARIEDEQALGSQlqkklKELQAri 1115
Cdd:PRK04863 229 RKAFQDMEAALREN----RMTLEAIRVTQSDRDLFKHLITEstnyvaADYMRHANERRVHLEEALELR-----RELYT-- 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1116 eeleeeleaERTARAKVEKLRSDLSRELEEISER---LEEAGGATS--VQIEMNKKREAE-FQKMRRDLEEATLQHEATA 1189
Cdd:PRK04863 298 ---------SRRQLAAEQYRLVEMARELAELNEAesdLEQDYQAASdhLNLVQTALRQQEkIERYQADLEELEERLEEQN 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1190 AAlrkkhadsVAELSEQIDNLQRVKQKLEKEKSEFKLELDDVTSNME-------QIIKAKANLEK---MCRT-------L 1252
Cdd:PRK04863 369 EV--------VEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDvqqtraiQYQQAVQALERakqLCGLpdltadnA 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1253 EDQMNEHRSKAEETQRSVNDL-----TSQRAKLQTENG---------------------ELSRQLDEKEALISQLTRGKl 1306
Cdd:PRK04863 441 EDWLEEFQAKEQEATEELLSLeqklsVAQAAHSQFEQAyqlvrkiagevsrseawdvarELLRRLREQRHLAEQLQQLR- 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1307 tytQQLEDLKRQLEEEVKAKNALAHALQSARHDCDLlREQYEEETEAKAELQRVLSKANSEVAQWRTKYEtdaiQRTEEL 1386
Cdd:PRK04863 520 ---MRLSELEQRLRQQQRAERLLAEFCKRLGKNLDD-EDELEQLQEELEARLESLSESVSEARERRMALR----QQLEQL 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1387 EEAKKKLAQR---LQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLmvdVERSNAAAAALDKKQRNFDKILAEWKQKYEES 1463
Cdd:PRK04863 592 QARIQRLAARapaWLAAQDALARLREQSGEEFEDSQDVTEYMQQL---LERERELTVERDELAARKQALDEEIERLSQPG 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1464 QSELESSQKEARSLSTELfkLKNAYEE-SLEH-------------------LETFKRENKNLQEEISDL------TEQLG 1517
Cdd:PRK04863 669 GSEDPRLNALAERFGGVL--LSEIYDDvSLEDapyfsalygparhaivvpdLSDAAEQLAGLEDCPEDLyliegdPDSFD 746
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1518 SSGKTIHELEK----------VR----------------KQLEAEKLELQSaLEEAEASLEHEEGKILRAQLEFNQIKAE 1571
Cdd:PRK04863 747 DSVFSVEELEKavvvkiadrqWRysrfpevplfgraareKRIEQLRAEREE-LAERYATLSFDVQKLQRLHQAFSRFIGS 825
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1572 MERKLAEKDEEME----QAKRNHLrvvDSLQTSLDAETRSRNEALRVKKKMEGDLNEMeiqLSHANRLAAEaqkqvkSLQ 1647
Cdd:PRK04863 826 HLAVAFEADPEAElrqlNRRRVEL---ERALADHESQEQQQRSQLEQAKEGLSALNRL---LPRLNLLADE------TLA 893
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1648 SLLKDTQIQLDDAVRANDDLKEN---IAIVERRNNLLQA---ELEELRAVVEQTERSRKLAEQELIETSERVQLLH---- 1717
Cdd:PRK04863 894 DRVEEIREQLDEAEEAKRFVQQHgnaLAQLEPIVSVLQSdpeQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAhfsy 973
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1718 SQNTSLINQkkkmEADLS-QLQTEVEEAVQECRNAEEKAKKA---ITDAAMMAEELKKEQDTsahLERMKKNMEQTIKDL 1793
Cdd:PRK04863 974 EDAAEMLAK----NSDLNeKLRQRLEQAEQERTRAREQLRQAqaqLAQYNQVLASLKSSYDA---KRQMLQELKQELQDL 1046
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387193866 1794 QHRLDEAEQIALKGGKKQLQKLEARVRELENELEAE---QKRNAES-VKGMRKSERRIKELTYQTEEDRKNLLRLQDLV 1868
Cdd:PRK04863 1047 GVPADSGAEERARARRDELHARLSANRSRRNQLEKQltfCEAEMDNlTKKLRKLERDYHEMREQVVNAKAGWCAVLRLV 1125
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
833-1247 |
1.28e-06 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 53.30 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 833 YFKIKPLLKSAE-----TEKEIALMKEEFGRLKEALEKSEARRKELEEKMvsllqekNDLQLQVQAEQDNLADAEErcdq 907
Cdd:PRK04778 100 FRKAKHEINEIEslldlIEEDIEQILEELQELLESEEKNREEVEQLKDLY-------RELRKSLLANRFSFGPALD---- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 908 liknkiQLEAKVKEMTERLEDEEEMNAE---LTAKK--RKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKN----L 978
Cdd:PRK04778 169 ------ELEKQLENLEEEFSQFVELTESgdyVEAREilDQLEEELAALEQIMEEIPELLKELQTELPDQLQELKAgyreL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 979 TEEMAGLDEIiaKLTKEKKALQEAHQQALDDLQAEEdkvntLTKAKVKLEQ---HVDDLEGSLEQEKKVRMDLERAKRKL 1055
Cdd:PRK04778 243 VEEGYHLDHL--DIEKEIQDLKEQIDENLALLEELD-----LDEAEEKNEEiqeRIDQLYDILEREVKARKYVEKNSDTL 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1056 EGDLKLTQESIMDLENDKQQLDERlkkkdFELNalnariEDEQALGSQLQKKLKELQARIEELEEELeaertarAKVEKL 1135
Cdd:PRK04778 316 PDFLEHAKEQNKELKEEIDRVKQS-----YTLN------ESELESVRQLEKQLESLEKQYDEITERI-------AEQEIA 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1136 RSDLSRELEEISERLEEAggatsvqiemnKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAEL---------SEQ 1206
Cdd:PRK04778 378 YSELQEELEEILKQLEEI-----------EKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIKRYLeksnlpglpEDY 446
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1387193866 1207 IDNLQRVK---QKLEKEKSEFKLELDDVTSNMEQIIKAKANLEK 1247
Cdd:PRK04778 447 LEMFFEVSdeiEALAEELEEKPINMEAVNRLLEEATEDVETLEE 490
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
839-1056 |
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 1387193866 839 LLKSAETEKEIALMKEEFGRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAK 918
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 919 VKEMTERLEDEEEMNAELTAKKRKLEDEcSELK-----RDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLT 993
Cdd:COG4942 92 IAELRAELEAQKEELAELLRALYRLGRQ-PPLAlllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387193866 994 KEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQHVDDLEGSLEQEKKVRMDLERAKRKLE 1056
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1437-1677 |
1.51e-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: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1437 AAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQl 1516
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1517 gssgktiheLEKVRKQLEAEKLELQSALEEAEASLEHEEGKILRAQLEFNQI--KAEMERKLAEKDEEMEQAKRNHLRVV 1594
Cdd:COG4942 92 ---------IAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAvrRLQYLKYLAPARREQAEELRADLAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1595 DSLQTSLDAEtrsrnealrvKKKMEGDLNEMEIQLSHANRLAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIV 1674
Cdd:COG4942 163 AALRAELEAE----------RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
...
gi 1387193866 1675 ERR 1677
Cdd:COG4942 233 EAE 235
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1351-1587 |
1.54e-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: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1351 TEAKAELQRVLSKANSEVAQwrtkyetdAIQRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMv 1430
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAE--------LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1431 dvERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEIS 1510
Cdd:COG4942 90 --KEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387193866 1511 DLTEQLGSSGKTIHELEKVRKQLEAEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEMERKLAEKDEEMEQAK 1587
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1056-1286 |
1.59e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.52 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1056 EGDLKLTQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEeleeeleaerTARAKVEKL 1135
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA----------EAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1136 RSDLSRELEEISERLEEAG------GATSV-----QIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKhadsVAELS 1204
Cdd:COG3883 85 REELGERARALYRSGGSVSyldvllGSESFsdfldRLSALSKIADADADLLEELKADKAELEAKKAELEAK----LAELE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1205 EQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTEN 1284
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
..
gi 1387193866 1285 GE 1286
Cdd:COG3883 241 AA 242
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1001-1162 |
1.83e-06 |
|
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: 51.08 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1001 EAHQQALDDLQAEEDKVNTLTKAKVKLEQHVDDLEGSLEQEKKVRM-------DLERAKRKLEGDLKLTQESImdlENDK 1073
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEaakteleDLEKEIKRLELEIEEVEARI---KKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1074 QQLDERLKKKdfELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEA 1153
Cdd:COG1579 80 EQLGNVRNNK--EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
|
....*....
gi 1387193866 1154 GGATSVQIE 1162
Cdd:COG1579 158 LEELEAERE 166
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1273-1697 |
3.05e-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: 3.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1273 LTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVKAknaLAHALQSARHDCDLLREQYEEETE 1352
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAE---LKEELRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1353 AKAELqrvlskanSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDV 1432
Cdd:pfam07888 109 SSEEL--------SEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1433 ERSnaaaaaldkkqrnfdkilaewkqkyeesqselessQKEARSLSTELFKLKNAYEESLEHLETfkrenknLQEEISDL 1512
Cdd:pfam07888 181 QQT-----------------------------------EEELRSLSKEFQELRNSLAQRDTQVLQ-------LQDTITTL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1513 TEQLGSSGKTIHELEKVRKqleaeklELQSALEEAEASLEHEEGkilraqlefnqIKAEMERKLAEKDEEMEQAKRNHLR 1592
Cdd:pfam07888 219 TQKLTTAHRKEAENEALLE-------ELRSLQERLNASERKVEG-----------LGEELSSMAAQRDRTQAELHQARLQ 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1593 VVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRLAAEAQKQVKSLQSLLKDTQ--------------IQLD 1658
Cdd:pfam07888 281 AAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREklevelgrekdcnrVQLS 360
|
410 420 430
....*....|....*....|....*....|....*....
gi 1387193866 1659 DAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTER 1697
Cdd:pfam07888 361 ESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQ 399
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1310-1578 |
3.18e-06 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 51.07 E-value: 3.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1310 QQLEDLKRQLEEEVKAKNALAHALQSARHDC-----DLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTE 1384
Cdd:pfam00038 21 RFLEQQNKLLETKISELRQKKGAEPSRLYSLyekeiEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1385 eLEEAKKKLAQRLQDAEEAVEAVNAKCSSLE------KTKHR-----LQNEIEDLMVDVERSNAaaaaldkKQRNFDKIL 1453
Cdd:pfam00038 101 -AENDLVGLRKDLDEATLARVDLEAKIESLKeelaflKKNHEeevreLQAQVSDTQVNVEMDAA-------RKLDLTSAL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1454 AEWKQKYEEsqselessqkearslstelfkLKNAYEESLEhlETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQL 1533
Cdd:pfam00038 173 AEIRAQYEE---------------------IAAKNREEAE--EWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSL 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1387193866 1534 EAE-------KLELQSALEEAEASLEHE----EGKILRAQLEFNQIKAEMERKLAE 1578
Cdd:pfam00038 230 EIElqslkkqKASLERQLAETEERYELQladyQELISELEAELQETRQEMARQLRE 285
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1473-1829 |
3.45e-06 |
|
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: 51.61 E-value: 3.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1473 EARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKLELQSALEEAEASLE 1552
Cdd:pfam19220 21 DLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1553 HEEGKILRAQLEFNQ---IKAEMERKLAEKDEEME------QAKRNHLRVVDSLQTSLDAETRSRNEALRV----KKKME 1619
Cdd:pfam19220 101 EAEAAKEELRIELRDktaQAEALERQLAAETEQNRaleeenKALREEAQAAEKALQRAEGELATARERLALleqeNRRLQ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1620 GDLNEMEIQLSHANRLAAEAQKQVKSLQSLLKDTQIQLDDAV----RANDDLKENIAIVERRNNLLQAELEELRAVVEQT 1695
Cdd:pfam19220 181 ALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAEQaereRAEAQLEEAVEAHRAERASLRMKLEALTARAAAT 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1696 ERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMEADLSQLQTEVEEAVQEcRNAEEKAKKAITD-AAMMAEELKkeqD 1774
Cdd:pfam19220 261 EQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQ-FQEMQRARAELEErAEMLTKALA---A 336
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1387193866 1775 TSAHLERMkknmEQTIKDLQHRLDEAEQIALKggkkQLQKLEARVRELENELEAE 1829
Cdd:pfam19220 337 KDAALERA----EERIASLSDRIAELTKRFEV----ERAALEQANRRLKEELQRE 383
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1168-1906 |
3.63e-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: 52.26 E-value: 3.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1168 EAEFQKMRRDLEEATLQHEATAAALRKKHA---DSVAELSEQIDNLQRVKQKL-EKEKSE-FKLELDDVTSNMEQIIKAK 1242
Cdd:COG3096 291 RRELFGARRQLAEEQYRLVEMARELEELSAresDLEQDYQAASDHLNLVQTALrQQEKIErYQEDLEELTERLEEQEEVV 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1243 ANLEkmcrtleDQMNEHRSKAEETQRSVNDLTSQRAKLQtengelsrqldekEALISQLTRGkLTYTQQLedlkrqleee 1322
Cdd:COG3096 371 EEAA-------EQLAEAEARLEAAEEEVDSLKSQLADYQ-------------QALDVQQTRA-IQYQQAV---------- 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1323 vkaknalaHALQSARHDCDLLReqyeeeteakaelqrvLSKANseVAQWRTKYETDAIQRTEELEEakkkLAQRLQDAEE 1402
Cdd:COG3096 420 --------QALEKARALCGLPD----------------LTPEN--AEDYLAAFRAKEQQATEEVLE----LEQKLSVADA 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1403 AveavnakcssleKTKHRLQNEIEDLMVD-VERSNAAAAAldkKQrnfdkILAEWKqkyeesqselessqkEARSLSTEL 1481
Cdd:COG3096 470 A------------RRQFEKAYELVCKIAGeVERSQAWQTA---RE-----LLRRYR---------------SQQALAQRL 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1482 FKLKNAYEEslehLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKLELQSALEEAEA---SLEHEEGKi 1558
Cdd:COG3096 515 QQLRAQLAE----LEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEqrsELRQQLEQ- 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1559 LRAQLEFNQIKAEMERKLAEK----DEEMEQAKRNHLRVVDSLQTSLDAE---TRSRNEALRVKKKMEGDLNEmeiqLSH 1631
Cdd:COG3096 590 LRARIKELAARAPAWLAAQDAlerlREQSGEALADSQEVTAAMQQLLEREreaTVERDELAARKQALESQIER----LSQ 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1632 AN-----RLAAEAQKQVKSLQSLLKDtQIQLDDA-------------------------VRANDDLKENIAIVERR---- 1677
Cdd:COG3096 666 PGgaedpRLLALAERLGGVLLSEIYD-DVTLEDApyfsalygparhaivvpdlsavkeqLAGLEDCPEDLYLIEGDpdsf 744
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1678 -NNLLQAELEELRAVVEQTERS-------------RKLAEQELIETSE-----------------RVQLLHSQNTSLINQ 1726
Cdd:COG3096 745 dDSVFDAEELEDAVVVKLSDRQwrysrfpevplfgRAAREKRLEELRAerdelaeqyakasfdvqKLQRLHQAFSQFVGG 824
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1727 KKKM------EADLSQLQ---TEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLErmKKNMEQTIKDLQHRL 1797
Cdd:COG3096 825 HLAVafapdpEAELAALRqrrSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLA--DETLADRLEELREEL 902
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1798 DEAEQ----IALKGgkKQLQKLEARVRELEN-------------ELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRkn 1860
Cdd:COG3096 903 DAAQEaqafIQQHG--KALAQLEPLVAVLQSdpeqfeqlqadylQAKEQQRRLKQQIFALSEVVQRRPHFSYEDAVGL-- 978
|
810 820 830 840
....*....|....*....|....*....|....*....|....*.
gi 1387193866 1861 LLRLQDLVDKLQLKVkaykRQAEEAEEQANTNLskfRKVQHELDEA 1906
Cdd:COG3096 979 LGENSDLNEKLRARL----EQAEEARREAREQL---RQAQAQYSQY 1017
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
1245-1446 |
3.81e-06 |
|
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: 52.16 E-value: 3.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1245 LEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVK 1324
Cdd:pfam09726 400 LEQDIKKLKAELQASRQTEQELRSQISSLTSLERSLKSELGQLRQENDLLQTKLHNAVSAKQKDKQTVQQLEKRLKAEQE 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1325 AKNALAHALQSARHdcdllREQYEEETEAKAELQRVLSKANSevaqwrtkyeTDAI-QRTEELEEAKKKLAQRLQDAEEA 1403
Cdd:pfam09726 480 ARASAEKQLAEEKK-----RKKEEEATAARAVALAAASRGEC----------TESLkQRKRELESEIKKLTHDIKLKEEQ 544
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1387193866 1404 VEAVNAKCSSLEKTKHRlQNEIEDLMvdversNAAAAALDKKQ 1446
Cdd:pfam09726 545 IRELEIKVQELRKYKES-EKDTEVLM------SALSAMQDKNQ 580
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1102-1337 |
4.42e-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: 51.30 E-value: 4.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1102 SQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAggatsvqiemnkkrEAEFQKMRRDLEEA 1181
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL--------------EQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1182 TLQheatAAALRKKHADSVAELSEQIDNLQRVKQKLEKE---KSEFKLELDDVTSNMEQIIKA-KANLEKMCRT---LED 1254
Cdd:COG4942 89 EKE----IAELRAELEAQKEELAELLRALYRLGRQPPLAlllSPEDFLDAVRRLQYLKYLAPArREQAEELRADlaeLAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1255 QMNEHRSKAEETQRSVNDLTSQRAKLQtengelsRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVKAKNALAHALQ 1334
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALE-------ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
...
gi 1387193866 1335 SAR 1337
Cdd:COG4942 238 AAA 240
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
883-1531 |
5.46e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.44 E-value: 5.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 883 EKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMTERLEDEEEMNAELtakkRKLEDECSELKRDIDDLELTLA 962
Cdd:PRK01156 139 EMDSLISGDPAQRKKILDEILEINSLERNYDKLKDVIDMLRAEISNIDYLEEKL----KSSNLELENIKKQIADDEKSHS 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 963 KVEKEKHATENKVKNLTEEMAGLDEIIAKLT---KEKKALQEAHQQALDDLQAEEDKVNtltkakvkleqhvdDLEGSLE 1039
Cdd:PRK01156 215 ITLKEIERLSIEYNNAMDDYNNLKSALNELSsleDMKNRYESEIKTAESDLSMELEKNN--------------YYKELEE 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1040 QEKKVRMDLERAKRklegdlkltqESIMDLENDKQQLD---ERLKKKDFELNALNARIedeqalgsqlqKKLKELQArie 1116
Cdd:PRK01156 281 RHMKIINDPVYKNR----------NYINDYFKYKNDIEnkkQILSNIDAEINKYHAII-----------KKLSVLQK--- 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1117 eleeeleaERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRR---DLEEATLQHEATAAALR 1193
Cdd:PRK01156 337 --------DYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERmsaFISEILKIQEIDPDAIK 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1194 KKHAD---SVAELSEQIDNLQRVKQKLEKEKsefklelDDVTSNMEqiIKAKANLEKMCRT------LEDQMNEHRSKAE 1264
Cdd:PRK01156 409 KELNEinvKLQDISSKVSSLNQRIRALRENL-------DELSRNME--MLNGQSVCPVCGTtlgeekSNHIINHYNEKKS 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1265 ETQRSVNDLTSQRAKLqteNGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVKAKNALAHALQSARHDCDLLR 1344
Cdd:PRK01156 480 RLEEKIREIEIEVKDI---DEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYK 556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1345 EQYEEETEAKAElqrVLSKANSEvaqwRTKYETDAIQ-RTEELEEAKKKLAQRLQDAEEAVEAVNakcSSLEKTKHRLQN 1423
Cdd:PRK01156 557 SLKLEDLDSKRT---SWLNALAV----ISLIDIETNRsRSNEIKKQLNDLESRLQEIEIGFPDDK---SYIDKSIREIEN 626
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1424 EIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKeARSLSTELFKLKNAYEESLEHLETFKRENK 1503
Cdd:PRK01156 627 EANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSR-INDIEDNLKKSRKALDDAKANRARLESTIE 705
|
650 660
....*....|....*....|....*...
gi 1387193866 1504 NLQEEISDLTEQLGSSGKTIHELEKVRK 1531
Cdd:PRK01156 706 ILRTRINELSDRINDINETLESMKKIKK 733
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
896-1754 |
5.73e-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: 51.88 E-value: 5.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 896 DNLADAEERcDQLIKNKIQLEAKVKEMTERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATEnKV 975
Cdd:COG3096 272 DYMRHANER-RELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALRQQE-KI 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 976 KNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQHVDDLEGSLEQEKKVRMDLERAKRKL 1055
Cdd:COG3096 350 ERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQALEKARALC 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1056 EGDlKLTQESIMDLEndkQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLkELQARIEELEEELEAERTARAKVEKL 1135
Cdd:COG3096 430 GLP-DLTPENAEDYL---AAFRAKEQQATEEVLELEQKLSVADAARRQFEKAY-ELVCKIAGEVERSQAWQTARELLRRY 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1136 RSD---------LSRELEEISERLEEAGGATSVQIEMNKKREAEFQKmRRDLEEatlqHEATAAALRKKHADSVAELSEQ 1206
Cdd:COG3096 505 RSQqalaqrlqqLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDA-AEELEE----LLAELEAQLEELEEQAAEAVEQ 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1207 IDNLQRVKQKLEKEKSEFklelddvTSNMEQIIKAKANLEKmcrtLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGE 1286
Cdd:COG3096 580 RSELRQQLEQLRARIKEL-------AARAPAWLAAQDALER----LREQSGEALADSQEVTAAMQQLLEREREATVERDE 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1287 LSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLE--------EEVKAKNA---------LAHAL-----------QSARH 1338
Cdd:COG3096 649 LAARKQALESQIERLSQPGGAEDPRLLALAERLGgvllseiyDDVTLEDApyfsalygpARHAIvvpdlsavkeqLAGLE 728
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1339 DC--DLLREQYEEET------EAKAELQRVLSKanSEVAQWR-TKYETDAI-------QRTEELEEAKKKLAQRLQDAEE 1402
Cdd:COG3096 729 DCpeDLYLIEGDPDSfddsvfDAEELEDAVVVK--LSDRQWRySRFPEVPLfgraareKRLEELRAERDELAEQYAKASF 806
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1403 AVEavnaKCSSLEKTKHRLQNE------IEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESqselessqKEARS 1476
Cdd:COG3096 807 DVQ----KLQRLHQAFSQFVGGhlavafAPDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQL--------KEQLQ 874
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1477 LSTELFKLKNAYEEslEHLETFKREnknLQEEISDLTEQ---LGSSGKTIHELEKVRKQLEAEKL---ELQSALEEAEAS 1550
Cdd:COG3096 875 LLNKLLPQANLLAD--ETLADRLEE---LREELDAAQEAqafIQQHGKALAQLEPLVAVLQSDPEqfeQLQADYLQAKEQ 949
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1551 LeheegKILRAQLEfnqikaemerklaekdeEMEQ--AKRNHLRVVDSLQtsLDAETRSRNEALRVKkkmegdLNEMEIQ 1628
Cdd:COG3096 950 Q-----RRLKQQIF-----------------ALSEvvQRRPHFSYEDAVG--LLGENSDLNEKLRAR------LEQAEEA 999
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1629 LSHANRLAAEAQKQVKSLQSLLKDtqiqLDDAVRA-NDDLKEniaiverrnnlLQAELEEL--RAVVEQTERSRklaeqe 1705
Cdd:COG3096 1000 RREAREQLRQAQAQYSQYNQVLAS----LKSSRDAkQQTLQE-----------LEQELEELgvQADAEAEERAR------ 1058
|
890 900 910 920
....*....|....*....|....*....|....*....|....*....
gi 1387193866 1706 lietsERVQLLHSQNTSLINQKKKMEADLSQLQTEVEEAVQECRNAEEK 1754
Cdd:COG3096 1059 -----IRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERD 1102
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1725-1927 |
6.77e-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: 50.53 E-value: 6.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1725 NQKKKMEADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQiA 1804
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA-E 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1805 LKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELT----YQTEEDRKNLLRLQDLVDKLQLKVKAYKR 1880
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAparrEQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1387193866 1881 QAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDI 1927
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1539-1920 |
8.08e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.11 E-value: 8.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1539 ELQSALEEAeASLEHEEGKILRAQLEFNQIKAEMERKLA-----EKDEEME-QAKRNHLRVVdslqtsldaetrsrNEAL 1612
Cdd:PRK04863 280 ERRVHLEEA-LELRRELYTSRRQLAAEQYRLVEMARELAelneaESDLEQDyQAASDHLNLV--------------QTAL 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1613 RVKKKME---GDLNEMEIQLSHANRLAAEAQKQVKSLqsllkdtQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELR 1689
Cdd:PRK04863 345 RQQEKIEryqADLEELEERLEEQNEVVEEADEQQEEN-------EARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQ 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1690 AVVEQTERSRKL---AEQELIETSERVQLLHSQNTSLINQKKKMEADLSQLQ---TEVEEAVQECRN---------AEEK 1754
Cdd:PRK04863 418 QAVQALERAKQLcglPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQaahSQFEQAYQLVRKiagevsrseAWDV 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1755 AKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTiKDLQHRLDEAEQIALKG--GKKQLQKLEARVRELENELEAEQKR 1832
Cdd:PRK04863 498 ARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQ-QRAERLLAEFCKRLGKNldDEDELEQLQEELEARLESLSESVSE 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1833 NAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADI 1912
Cdd:PRK04863 577 ARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQA 656
|
....*...
gi 1387193866 1913 AESQVNKL 1920
Cdd:PRK04863 657 LDEEIERL 664
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1485-1920 |
8.35e-06 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 50.60 E-value: 8.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1485 KNAYEEsLEHLETFKRE--NKNLQEEISDLtEQLGSSGKTIHELEKVRKQ----------------LEAEKL-------E 1539
Cdd:PRK04778 25 KRNYKR-IDELEERKQEleNLPVNDELEKV-KKLNLTGQSEEKFEEWRQKwdeivtnslpdieeqlFEAEELndkfrfrK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1540 LQSALEEAEASLEHEEGKILRAQLEFNQIKaEMERKLaekDEEMEQAKRNHlrvvDSLQTSLDAETRSRNEALrvkKKME 1619
Cdd:PRK04778 103 AKHEINEIESLLDLIEEDIEQILEELQELL-ESEEKN---REEVEQLKDLY----RELRKSLLANRFSFGPAL---DELE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1620 GDLNEMEIQLSHANRLAA-----EAQKQVKSLQSLLKDTQIQLDDavranddlkenI-AIVERRNNLLQAELEELRAVVE 1693
Cdd:PRK04778 172 KQLENLEEEFSQFVELTEsgdyvEAREILDQLEEELAALEQIMEE-----------IpELLKELQTELPDQLQELKAGYR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1694 Q-TERSRKLAEQELIETSERVQLLHSQNTSLINQK--KKMEADLSQLQTEVE------EAVQECRNAEEKAKKAITDAAM 1764
Cdd:PRK04778 241 ElVEEGYHLDHLDIEKEIQDLKEQIDENLALLEELdlDEAEEKNEEIQERIDqlydilEREVKARKYVEKNSDTLPDFLE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1765 MAEELKKEqdTSAHLERMKKN-------------MEQTIKDLQHRLDEAEQiALKGGKKQLQKLEARVRELENEL---EA 1828
Cdd:PRK04778 321 HAKEQNKE--LKEEIDRVKQSytlneselesvrqLEKQLESLEKQYDEITE-RIAEQEIAYSELQEELEEILKQLeeiEK 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1829 EQKRNAESVKGMRKSERRIKEltyQTEEDRKNLLRLQDLVDKLQL-----KVKAYKRQAEEAEEQANTNLSKFR----KV 1899
Cdd:PRK04778 398 EQEKLSEMLQGLRKDELEARE---KLERYRNKLHEIKRYLEKSNLpglpeDYLEMFFEVSDEIEALAEELEEKPinmeAV 474
|
490 500
....*....|....*....|.
gi 1387193866 1900 QHELDEAEERADIAESQVNKL 1920
Cdd:PRK04778 475 NRLLEEATEDVETLEEETEEL 495
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1349-1909 |
8.37e-06 |
|
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: 50.88 E-value: 8.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1349 EETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEE------AKKKLAQRLQDAEEAV----EAVNAKCSSLEKTK 1418
Cdd:pfam05483 71 ENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQEnrkiieAQRKAIQELQFENEKVslklEEEIQENKDLIKEN 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1419 HRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTEL-FKLKNAYEEsLEHLET 1497
Cdd:pfam05483 151 NATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMhFKLKEDHEK-IQHLEE 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1498 -FKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQL--EAEKLELQSALEEAEASLEHEEGKILRAQLEfnQIKAEMER 1574
Cdd:pfam05483 230 eYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESrdKANQLEEKTKLQDENLKELIEKKDHLTKELE--DIKMSLQR 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1575 KLAEK---DEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRLAAEAQKQVKSLQSLLK 1651
Cdd:pfam05483 308 SMSTQkalEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQ 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1652 DTQIQLDDAVRAND----DLKENIAIVERRNNLLQAE------LEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNT 1721
Cdd:pfam05483 388 KKSSELEEMTKFKNnkevELEELKKILAEDEKLLDEKkqfekiAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEE 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1722 SLINQKKKMEADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMeqtikdlqhrldeae 1801
Cdd:pfam05483 468 HYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERM--------------- 532
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1802 qialkggKKQLQKLEARVRELENELEA---EQKRNAESVK-GMRKSERRIKELTYQTEEDRKNLLRLQDL---------- 1867
Cdd:pfam05483 533 -------LKQIENLEEKEMNLRDELESvreEFIQKGDEVKcKLDKSEENARSIEYEVLKKEKQMKILENKcnnlkkqien 605
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1387193866 1868 ----VDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEER 1909
Cdd:pfam05483 606 knknIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQK 651
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1251-1409 |
9.89e-06 |
|
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: 48.77 E-value: 9.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1251 TLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVKAK--NA 1328
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1329 LAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEAVEAVN 1408
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIP 173
|
.
gi 1387193866 1409 A 1409
Cdd:COG1579 174 P 174
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1090-1364 |
1.06e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.40 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1090 LNARIEDEQALGSQLQKKLKELQARIeeleeeleaeRTARAKVEKLRS-----DLSRELEEISERLEEAggatsvqiemn 1164
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKEL----------EEAEAALEEFRQknglvDLSEEAKLLLQQLSEL----------- 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1165 kkrEAEFQKMRRDLEEAtlqhEATAAALRKKHADSVAELSEQIDN--LQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAK 1242
Cdd:COG3206 225 ---ESQLAEARAELAEA----EARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTPNHPDVIALR 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1243 ANLEkmcrTLEDQMnehrskAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRgkltYTQQLEDLKRQLEee 1322
Cdd:COG3206 298 AQIA----ALRAQL------QQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPE----LEAELRRLEREVE-- 361
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1387193866 1323 vkaknalahalqsarhdcdLLREQYE------EETEAKAELQ----RVLSKA 1364
Cdd:COG3206 362 -------------------VARELYEsllqrlEEARLAEALTvgnvRVIDPA 394
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
861-1408 |
1.14e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 50.67 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 861 EALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMTERL---EDEEEMNAELT 937
Cdd:PRK01156 162 NSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYnnaMDDYNNLKSAL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 938 AKKRKLEDECSELKRDI----DDLELTLAKVEKEKHATENKVK-----------------NLTEEMAGLDEIIAKLTKEK 996
Cdd:PRK01156 242 NELSSLEDMKNRYESEIktaeSDLSMELEKNNYYKELEERHMKiindpvyknrnyindyfKYKNDIENKKQILSNIDAEI 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 997 KALQEAHQQaLDDLQAEEDKVNTLTKAKVKLEQHVDDLEGSleqekkvRMDLERAKRKLEGDLKLTQESIMDLENDKQQL 1076
Cdd:PRK01156 322 NKYHAIIKK-LSVLQKDYNDYIKKKSRYDDLNNQILELEGY-------EMDYNSYLKSIESLKKKIEEYSKNIERMSAFI 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1077 DERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARA------------------KVEKLRSD 1138
Cdd:PRK01156 394 SEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEmlngqsvcpvcgttlgeeKSNHIINH 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1139 LSRELEEISE---RLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELSEQIDnlqrvkq 1215
Cdd:PRK01156 474 YNEKKSRLEEkirEIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHD------- 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1216 KLEKEKSEFK-LELDDVTSNMEQIIKAKANLEKM-CRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDE 1293
Cdd:PRK01156 547 KYEEIKNRYKsLKLEDLDSKRTSWLNALAVISLIdIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIEN 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1294 KealiSQLTRGKLTYTQQLEDLKRQLEEEVKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRT 1373
Cdd:PRK01156 627 E----ANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLES 702
|
570 580 590
....*....|....*....|....*....|....*
gi 1387193866 1374 KYETDaIQRTEELEEAKKKLAQRLQDAEEAVEAVN 1408
Cdd:PRK01156 703 TIEIL-RTRINELSDRINDINETLESMKKIKKAIG 736
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1236-1884 |
1.33e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 50.57 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1236 EQIIKAKANLEKmcrtLEDQMNEHRSKAEETQRSVND----LTSQRAKLQTENGELSRQ---LDEKEALISQLTRgklty 1308
Cdd:PRK10246 191 EQHKSARTELEK----LQAQASGVALLTPEQVQSLTAslqvLTDEEKQLLTAQQQQQQSlnwLTRLDELQQEASR----- 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1309 TQQLedLKRQLEEEVKAKNALAhALQSARHDCDL--LREQYEEETEAKAELQRVLSKANS---EVAQWRTKYETDAIQRT 1383
Cdd:PRK10246 262 RQQA--LQQALAAEEKAQPQLA-ALSLAQPARQLrpHWERIQEQSAALAHTRQQIEEVNTrlqSTMALRARIRHHAAKQS 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1384 EELEEAKKKLAQRLQDAE------EAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNA------------AAAALDK- 1444
Cdd:PRK10246 339 AELQAQQQSLNTWLAEHDrfrqwnNELAGWRAQFSQQTSDREQLRQWQQQLTHAEQKLNAlpaitltltadeVAAALAQh 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1445 -KQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKnayeeslEHLETFKRENKNLQEEISDLteqlgssgKTI 1523
Cdd:PRK10246 419 aEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRN-------AALNEMRQRYKEKTQQLADV--------KTI 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1524 HELEKVRKQLEAEKLELQSALE------------EAEASLEHEEGKILRAQLE--FNQIKAEMERKLAEKDEEMEQAKRN 1589
Cdd:PRK10246 484 CEQEARIKDLEAQRAQLQAGQPcplcgstshpavEAYQALEPGVNQSRLDALEkeVKKLGEEGAALRGQLDALTKQLQRD 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1590 HLRVVDSLQ--TSLDAETRSRNEALRVKKKMEGDLN-------EMEIQLSHAN-RLA-----AEAQKQVKSLQSLLKDTQ 1654
Cdd:PRK10246 564 ESEAQSLRQeeQALTQQWQAVCASLNITLQPQDDIQpwldaqeEHERQLRLLSqRHElqgqiAAHNQQIIQYQQQIEQRQ 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1655 IQLDDAVRA-----NDDLKENIAIVER------------RNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLH 1717
Cdd:PRK10246 644 QQLLTALAGyaltlPQEDEEASWLATRqqeaqswqqrqnELTALQNRIQQLTPLLETLPQSDDLPHSEETVALDNWRQVH 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1718 SQNTSLINQKKKMEADLSQLQTEVEEAVQECRNAEEK---AKKAITDAAMMAEElkkeqdTSAHLERMKKNMEQTIKDLQ 1794
Cdd:PRK10246 724 EQCLSLHSQLQTLQQQDVLEAQRLQKAQAQFDTALQAsvfDDQQAFLAALLDEE------TLTQLEQLKQNLENQRQQAQ 797
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1795 HRLDEAEQialkggkKQLQKLEARVRELENELEAE--QKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVdklq 1872
Cdd:PRK10246 798 TLVTQTAQ-------ALAQHQQHRPDGLDLTVTVEqiQQELAQLAQQLRENTTRQGEIRQQLKQDADNRQQQQALM---- 866
|
730
....*....|..
gi 1387193866 1873 LKVKAYKRQAEE 1884
Cdd:PRK10246 867 QQIAQATQQVED 878
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1261-1588 |
1.48e-05 |
|
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: 50.01 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1261 SKAEETQRSVNDLTsqRAKLQTENGELSRQLDEKE-----ALISQLTRGKLTYTQQLEDLKRQLEEEV--KAKNALAHAL 1333
Cdd:NF033838 50 SSGNESQKEHAKEV--ESHLEKILSEIQKSLDKRKhtqnvALNKKLSDIKTEYLYELNVLKEKSEAELtsKTKKELDAAF 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1334 QSARHDCDLLREQYEEETEAKAELQRvlsKANSEVAQWRTKYETDAIqRTEELEEAKKKLaqRLQDAEEAVEAVNAKCSS 1413
Cdd:NF033838 128 EQFKKDTLEPGKKVAEATKKVEEAEK---KAKDQKEEDRRNYPTNTY-KTLELEIAESDV--EVKKAELELVKEEAKEPR 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1414 LEKTkhrlqneIEDLMVDVERSNAAAAALDKKQRnfDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLE 1493
Cdd:NF033838 202 DEEK-------IKQAKAKVESKKAEATRLEKIKT--DREKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVLGE 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1494 HLETFKRENKNLQEEISDLTEQLGS----SGKTIHELEKvrKQLEAEK--------------------LELQSA-----L 1544
Cdd:NF033838 273 PATPDKKENDAKSSDSSVGEETLPSpslkPEKKVAEAEK--KVEEAKKkakdqkeedrrnyptntyktLELEIAesdvkV 350
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1387193866 1545 EEAEASLEHEEGKILRAQLEFNQIKAEMERKLAE----------KDEEMEQAKR 1588
Cdd:NF033838 351 KEAELELVKEEAKEPRNEEKIKQAKAKVESKKAEatrlekiktdRKKAEEEAKR 404
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1048-1202 |
1.63e-05 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 50.14 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1048 LERAKRKLEGDLKLTQESIMDLENDKQQLDERLKkkdfELNALNARIEDEQAlgsQLQKKLKELQARieeleeELEAERT 1127
Cdd:COG1193 502 IERARELLGEESIDVEKLIEELERERRELEEERE----EAERLREELEKLRE---ELEEKLEELEEE------KEEILEK 568
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387193866 1128 ARAKVEKLRSDLSRELEEISERLEEAggatsvqiemnKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAE 1202
Cdd:COG1193 569 AREEAEEILREARKEAEELIRELREA-----------QAEEEELKEARKKLEELKQELEEKLEKPKKKAKPAKPP 632
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
835-1200 |
1.74e-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: 50.12 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 835 KIKPLLKSAETEKEIaLMK--EEFGRLKEALEKSE-------------ARRKELEEKMVSLLQEKNDLQLQ----VQAEQ 895
Cdd:pfam15921 462 KVSSLTAQLESTKEM-LRKvvEELTAKKMTLESSErtvsdltaslqekERAIEATNAEITKLRSRVDLKLQelqhLKNEG 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 896 DNLADAEERCDQLI-----KNKIQ--LEAKVKEMTERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEK 968
Cdd:pfam15921 541 DHLRNVQTECEALKlqmaeKDKVIeiLRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKI 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 969 HATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQHVDDLEGSLEQE-KKVRMD 1047
Cdd:pfam15921 621 RELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTtNKLKMQ 700
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1048 LERAKRKLEGdlklTQESIMDLENDkqqlderlkkkdfELNALNARIEDEQALGSQlQKKLKELQARIEELEEELEAERT 1127
Cdd:pfam15921 701 LKSAQSELEQ----TRNTLKSMEGS-------------DGHAMKVAMGMQKQITAK-RGQIDALQSKIQFLEEAMTNANK 762
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387193866 1128 ARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSV 1200
Cdd:pfam15921 763 EKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESV 835
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1686-1935 |
1.75e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.94 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1686 EELRAVVEQT-------ERsRKLAEQELIETSE---RVQLLHSQntslinqkkkMEADLSQLQTEVEEAVqecRNAEEKA 1755
Cdd:COG1196 155 EERRAIIEEAagiskykER-KEEAERKLEATEEnleRLEDILGE----------LERQLEPLERQAEKAE---RYRELKE 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1756 KKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQiALKGGKKQLQKLEARVRELENELEAEQKRNAE 1835
Cdd:COG1196 221 ELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEA-ELEELRLELEELELELEEAQAEEYELLAELAR 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1836 SVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAES 1915
Cdd:COG1196 300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
|
250 260
....*....|....*....|
gi 1387193866 1916 QVNKLRAKSRDIGTKGLNEE 1935
Cdd:COG1196 380 ELEELAEELLEALRAAAELA 399
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
774-1792 |
1.85e-05 |
|
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: 50.05 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 774 EEMRDERLSRIITRIQAQSRGVLSRMEFKKLLE---RRDSLLIIQWNIRAfmgvknwpwmKLYFKIKPLLKSAET----- 845
Cdd:TIGR01612 487 ENSKQDNTVKLILMRMKDFKDIIDFMELYKPDEvpsKNIIGFDIDQNIKA----------KLYKEIEAGLKESYElaknw 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 846 EKEIALMKEEFGRLKEALEKSEARRKELEEKMVSLLQEK---NDLQLQVQAEQDNLADAEERCDQLIKNKIQLE------ 916
Cdd:TIGR01612 557 KKLIHEIKKELEEENEDSIHLEKEIKDLFDKYLEIDDEIiyiNKLKLELKEKIKNISDKNEYIKKAIDLKKIIEnnnayi 636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 917 ---AKVK--EMTERLEDEEEMNAELTAKKRKLEDEcselkrDIDDLELTLAKVEKEkhateNKVKNlTEEMAGLDEIIAK 991
Cdd:TIGR01612 637 delAKISpyQVPEHLKNKDKIYSTIKSELSKIYED------DIDALYNELSSIVKE-----NAIDN-TEDKAKLDDLKSK 704
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 992 LTKEKKALQEAHQQALD-DLQAEEDKVNTLTKAKVKLEQHVddlegsleqEKKVRMDLERAKRKLEGDLKLTQESIMDLE 1070
Cdd:TIGR01612 705 IDKEYDKIQNMETATVElHLSNIENKKNELLDIIVEIKKHI---------HGEINKDLNKILEDFKNKEKELSNKINDYA 775
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1071 NDKQQLDERLKKKDFELNALNAR-----IEDEQAlgSQLQKKLKELQARIEELEEeleaertaraKVEKLRSDLSRELEE 1145
Cdd:TIGR01612 776 KEKDELNKYKSKISEIKNHYNDQinidnIKDEDA--KQNYDKSKEYIKTISIKED----------EIFKIINEMKFMKDD 843
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1146 ISERLEeaggaTSVQIEMNKKreaefqkmrrdlEEATLQHEATAAALRKKHAdsvaELSEqiDNLQRVKQKLEKEKS--- 1222
Cdd:TIGR01612 844 FLNKVD-----KFINFENNCK------------EKIDSEHEQFAELTNKIKA----EISD--DKLNDYEKKFNDSKSlin 900
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1223 EFKLELDDVTSNMEQIIKAKANLeKMCRTLEDQMNEHRSKaeetQRSVNDLTSQRAKLQTENGELSRQLDEK--EALISQ 1300
Cdd:TIGR01612 901 EINKSIEEEYQNINTLKKVDEYI-KICENTKESIEKFHNK----QNILKEILNKNIDTIKESNLIEKSYKDKfdNTLIDK 975
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1301 LTRGKLTYTQ-QLEDLKRQLEEEVKAKNALAHALQSARHDcdLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDA 1379
Cdd:TIGR01612 976 INELDKAFKDaSLNDYEAKNNELIKYFNDLKANLGKNKEN--MLYHQFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSI 1053
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1380 IQRTEELEEAKKKLAQRLQdaEEAVEAVNAKCSSLEKTKHRLqneiedlmvdversnaaaaaldkKQRNFDKILAEWKQK 1459
Cdd:TIGR01612 1054 YNIIDEIEKEIGKNIELLN--KEILEEAEINITNFNEIKEKL-----------------------KHYNFDDFGKEENIK 1108
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1460 YEesqselessqKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISdlteqlgssgKTIHELEKVrkqleAEKLE 1539
Cdd:TIGR01612 1109 YA----------DEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIK----------AQINDLEDV-----ADKAI 1163
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1540 LQSALEEAEASLEHEEGKILRAQLEFNQIKAEM-ERKLAEKDE-EMEQAKRNHLRVVDSLQT----SLDAEtrsrnealr 1613
Cdd:TIGR01612 1164 SNDDPEEIEKKIENIVTKIDKKKNIYDEIKKLLnEIAEIEKDKtSLEEVKGINLSYGKNLGKlfleKIDEE--------- 1234
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1614 vKKKMEGDLNEMEIQLSHANRLAAEAQkQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVE 1693
Cdd:TIGR01612 1235 -KKKSEHMIKAMEAYIEDLDEIKEKSP-EIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHDENISDIREKSLKIIE 1312
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1694 QTERSRKLAEqelIETSERVQLLHSQ-NTSLINQKKKMEADLSQLQT-----EVEEAVQECRNAEEKAKKAITDAAMMAE 1767
Cdd:TIGR01612 1313 DFSEESDIND---IKKELQKNLLDAQkHNSDINLYLNEIANIYNILKlnkikKIIDEVKEYTKEIEENNKNIKDELDKSE 1389
|
1050 1060
....*....|....*....|....*
gi 1387193866 1768 ELKKEQDTSAHLERMKKNMEQTIKD 1792
Cdd:TIGR01612 1390 KLIKKIKDDINLEECKSKIESTLDD 1414
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
833-1451 |
1.98e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.90 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 833 YFKIKPLLKSAETE-KEIALMKEEFGRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQA---EQDNLADAEERCDQL 908
Cdd:PRK01156 168 YDKLKDVIDMLRAEiSNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNamdDYNNLKSALNELSSL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 909 IKNKIQLEAKVKEMTERLEDEEEMNAELTAKKRKLedecselkrdiddLELTLAKVEKEKHATeNKVKNLTEEMAGLDEI 988
Cdd:PRK01156 248 EDMKNRYESEIKTAESDLSMELEKNNYYKELEERH-------------MKIINDPVYKNRNYI-NDYFKYKNDIENKKQI 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 989 IAKLTKEKKALQEAHQQaLDDLQAEEDKVNTLTKAKVKLEQHVDDLEGSleqekkvRMDLERAKRKLEGDLKLTQESIMD 1068
Cdd:PRK01156 314 LSNIDAEINKYHAIIKK-LSVLQKDYNDYIKKKSRYDDLNNQILELEGY-------EMDYNSYLKSIESLKKKIEEYSKN 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1069 LENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARA------------------ 1130
Cdd:PRK01156 386 IERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEmlngqsvcpvcgttlgee 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1131 KVEKLRSDLSRELEEISE---RLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELSEQI 1207
Cdd:PRK01156 466 KSNHIINHYNEKKSRLEEkirEIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKH 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1208 DnlqrvkqKLEKEKSEFK-LELDDVTSNMEQIIKAKANLEKMcrtledQMNEHRSKAEETQRSVNDLTSQraklqtenge 1286
Cdd:PRK01156 546 D-------KYEEIKNRYKsLKLEDLDSKRTSWLNALAVISLI------DIETNRSRSNEIKKQLNDLESR---------- 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1287 lsrqLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANs 1366
Cdd:PRK01156 603 ----LQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRIN- 677
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1367 evaqwrtkyetdaiqrteELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSN---AAAAALD 1443
Cdd:PRK01156 678 ------------------DIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKkikKAIGDLK 739
|
....*...
gi 1387193866 1444 KKQRNFDK 1451
Cdd:PRK01156 740 RLREAFDK 747
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1340-1552 |
2.02e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 49.54 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1340 CDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKH 1419
Cdd:PRK05771 38 EELSNERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1420 RLQNEIEDLM------VDVER----SNAAAAALDKKQRNFDKILAEWKQKYEESQSELESS-------QKEARSLSTELF 1482
Cdd:PRK05771 118 ELEQEIERLEpwgnfdLDLSLllgfKYVSVFVGTVPEDKLEELKLESDVENVEYISTDKGYvyvvvvvLKELSDEVEEEL 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387193866 1483 KlKNAYEE-SLEHLETFKRENKNLQEEISDLTEQLGSsgkTIHELEKVRKQLEAEKL----ELQSALEEAEASLE 1552
Cdd:PRK05771 198 K-KLGFERlELEEEGTPSELIREIKEELEEIEKERES---LLEELKELAKKYLEELLalyeYLEIELERAEALSK 268
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1321-1623 |
2.64e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 49.69 E-value: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1321 EEVKAKNALAHALQSARHDCDLLREQYEEETEAKAE--LQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLaQRLQ 1398
Cdd:COG5022 810 KEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEvlIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQL-QELK 888
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1399 DAEEAVEAVNAKCSSLEKTKHRLQNEIE-DLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKeaRSL 1477
Cdd:COG5022 889 IDVKSISSLKLVNLELESEIIELKKSLSsDLIENLEFKTELIARLKKLLNNIDLEEGPSIEYVKLPELNKLHEVE--SKL 966
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1478 STELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGkTIHELEKVRKQLEAEKLELQSAleEAEASLEHEEGK 1557
Cdd:COG5022 967 KETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYG-ALQESTKQLKELPVEVAELQSA--SKIISSESTELS 1043
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387193866 1558 ILR--AQLEFNQIKAEMErkLAEKDEEMEQAKRNHLRvvDSLQTSLDAETRSRNEALRVKKKMEGDLN 1623
Cdd:COG5022 1044 ILKplQKLKGLLLLENNQ--LQARYKALKLRRENSLL--DDKQLYQLESTENLLKTINVKDLEVTNRN 1107
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
860-1681 |
2.71e-05 |
|
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: 49.66 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 860 KEALEK--SEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLA------------DAEERCDQLIKN----KIQLEAKVKE 921
Cdd:TIGR01612 976 INELDKafKDASLNDYEAKNNELIKYFNDLKANLGKNKENMLyhqfdekekatnDIEQKIEDANKNipniEIAIHTSIYN 1055
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 922 MTERLEDEEEMNAELTAKK--RKLEDECSELKRDIDDLEL----TLAKVEKEKHATE-NKVKNlteEMAGLDEIIAKLTK 994
Cdd:TIGR01612 1056 IIDEIEKEIGKNIELLNKEilEEAEINITNFNEIKEKLKHynfdDFGKEENIKYADEiNKIKD---DIKNLDQKIDHHIK 1132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 995 EKKALQEAHQQALDDLQAEEDKVNTLTKAKVkleqHVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQEsIMDLENDK- 1073
Cdd:TIGR01612 1133 ALEEIKKKSENYIDEIKAQINDLEDVADKAI----SNDDPEEIEKKIENIVTKIDKKKNIYDEIKKLLNE-IAEIEKDKt 1207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1074 ---------------------QQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAeRTARAKV 1132
Cdd:TIGR01612 1208 sleevkginlsygknlgklflEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEMDIKAEMETF-NISHDDD 1286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1133 EKLRSDLSRELEEISERLEEaggatSVQIEMNKKREAEFQKMRRDLEEATLQHEataaalrkKHADSVAELSEQIDNLQR 1212
Cdd:TIGR01612 1287 KDHHIISKKHDENISDIREK-----SLKIIEDFSEESDINDIKKELQKNLLDAQ--------KHNSDINLYLNEIANIYN 1353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1213 VKQ--KLEKEKSEFKLELDDVTSNMEQIIKAKANLEKMCRTLEDQMN--EHRSKAEETQ---------RSVNDLTSQRAK 1279
Cdd:TIGR01612 1354 ILKlnKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDINleECKSKIESTLddkdideciKKIKELKNHILS 1433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1280 LQTENGELSRQLDEKEALISQLTRgkltyTQQLEDLKRQLEEEVKAKNAlahalqSARHDCDL--LREQYEEETEAKAEL 1357
Cdd:TIGR01612 1434 EESNIDTYFKNADENNENVLLLFK-----NIEMADNKSQHILKIKKDNA------TNDHDFNIneLKEHIDKSKGCKDEA 1502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1358 QR----------VLSKANSEVAQWRTKYETDAIQrtEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNE--- 1424
Cdd:TIGR01612 1503 DKnakaieknkeLFEQYKKDVTELLNKYSALAIK--NKFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEkfr 1580
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1425 IEDLMVDVERSNAAAAALDKKQRNFDkilaewkqkyeesqselessqkearslsTELFKLKNAYEESLEHLetfkRENKN 1504
Cdd:TIGR01612 1581 IEDDAAKNDKSNKAAIDIQLSLENFE----------------------------NKFLKISDIKKKINDCL----KETES 1628
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1505 LQEEISDLT-----EQLGSSGKTIHELEKVRKQLEAEKlelqSALEEAEASLEHEEGKILRAQLEFNQIKAEMERKLAEK 1579
Cdd:TIGR01612 1629 IEKKISSFSidsqdTELKENGDNLNSLQEFLESLKDQK----KNIEDKKKELDELDSEIEKIEIDVDQHKKNYEIGIIEK 1704
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1580 DEEMEQAKRNHL------------RVVDSLQTSlDAETRSRNEALRVKKKMEGDLNEMEIQLSH--ANRLAAEAQKQVKS 1645
Cdd:TIGR01612 1705 IKEIAIANKEEIesikelieptieNLISSFNTN-DLEGIDPNEKLEEYNTEIGDIYEEFIELYNiiAGCLETVSKEPITY 1783
|
890 900 910
....*....|....*....|....*....|....*.
gi 1387193866 1646 LQslLKDTQIQlddavrANDDLKENIAIVERRNNLL 1681
Cdd:TIGR01612 1784 DE--IKNTRIN------AQNEFLKIIEIEKKSKSYL 1811
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1595-1807 |
2.77e-05 |
|
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: 48.61 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1595 DSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRLAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIV 1674
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1675 ER------RNNLLQ--------AELEELRAVVEQTERSRKLAEQELIETSERvqlLHSQNTSLINQKKKMEADLSQLQTE 1740
Cdd:COG4942 110 LRalyrlgRQPPLAlllspedfLDAVRRLQYLKYLAPARREQAEELRADLAE---LAALRAELEAERAELEALLAELEEE 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387193866 1741 VEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKG 1807
Cdd:COG4942 187 RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKG 253
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
843-1014 |
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 1387193866 843 AETEKEIALMKEEfgrLKEALEKSEARRKELEEKMVSLLQEKNDLQ-LQVQAEQDNLADAEERCDQLikNKIqleakVKE 921
Cdd:COG3883 61 EALQAEIDKLQAE---IAEAEAEIEERREELGERARALYRSGGSVSyLDVLLGSESFSDFLDRLSAL--SKI-----ADA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 922 MTERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQE 1001
Cdd:COG3883 131 DADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
170
....*....|...
gi 1387193866 1002 AHQQALDDLQAEE 1014
Cdd:COG3883 211 AAAAAAAAAAAAA 223
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1378-1923 |
3.23e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.13 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1378 DAIQRTEELEEAKKKLaqrlqdaEEAVEAVNAKCSSLEKTKHRLQNEIEDlmvdVERSNAAAAALDKKQRNFDKILAEWK 1457
Cdd:PRK01156 156 DEILEINSLERNYDKL-------KDVIDMLRAEISNIDYLEEKLKSSNLE----LENIKKQIADDEKSHSITLKEIERLS 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1458 QKYEESQSELESSQKEARSLSTeLFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLG--------SSGKTIHELEKV 1529
Cdd:PRK01156 225 IEYNNAMDDYNNLKSALNELSS-LEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMkiindpvyKNRNYINDYFKY 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1530 RKQLEAEKLELQSAleEAEASLEHEEGKILRAQLEFNQIKAEMERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRN 1609
Cdd:PRK01156 304 KNDIENKKQILSNI--DAEINKYHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEE 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1610 EALRVKK---KMEGDLNEMEIQLSHANRLAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRN-------- 1678
Cdd:PRK01156 382 YSKNIERmsaFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSvcpvcgtt 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1679 ----------NLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTS-LINQKKKMEADLSQLqTEVEEAVQE 1747
Cdd:PRK01156 462 lgeeksnhiiNHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINkSINEYNKIESARADL-EDIKIKINE 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1748 CRNAEEKAKKAITDAAMMAEELKKEQDTSaHLERMKKNMEQTIKDLQHRLDEAeqialkggKKQLQKLEARVRELENELE 1827
Cdd:PRK01156 541 LKDKHDKYEEIKNRYKSLKLEDLDSKRTS-WLNALAVISLIDIETNRSRSNEI--------KKQLNDLESRLQEIEIGFP 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1828 AEQKRNAESVkgmrkseRRIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQA---EEAEEQANTNLSKFRKVQHELD 1904
Cdd:PRK01156 612 DDKSYIDKSI-------REIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIaeiDSIIPDLKEITSRINDIEDNLK 684
|
570
....*....|....*....
gi 1387193866 1905 EAEERADIAESQVNKLRAK 1923
Cdd:PRK01156 685 KSRKALDDAKANRARLEST 703
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1381-1588 |
3.44e-05 |
|
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: 48.22 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1381 QRTEELEEAKKKLAQ---RLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWK 1457
Cdd:COG4942 24 EAEAELEQLQQEIAElekELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1458 QKYeesQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLgssgktiHELEKVRKQLEAEK 1537
Cdd:COG4942 104 EEL---AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL-------AELAALRAELEAER 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1387193866 1538 LELQSALEEAEASLEHEEGKILRAQLEFNQIKAEMERKLAEKDEEMEQAKR 1588
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1484-1935 |
4.01e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 4.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1484 LKNAYEESLEHLETFK-RENKNLQEEISDLTEQL---GSSGKTIHELEKVRKQLEAEKLELQSALEEAEASLEHEEgkIL 1559
Cdd:COG4717 47 LLERLEKEADELFKPQgRKPELNLKELKELEEELkeaEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE--KL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1560 RAQLEFNQIKAEMERKLAEKDEEMEQAKRNHlrvvdslqtsldaetRSRNEALRVKKKMEGDLNEMEIQLSHANRLAAEA 1639
Cdd:COG4717 125 LQLLPLYQELEALEAELAELPERLEELEERL---------------EELRELEEELEELEAELAELQEELEELLEQLSLA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1640 QKQvkslqsLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQ 1719
Cdd:COG4717 190 TEE------ELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1720 NTSLINQKKKMEADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKK--EQDTSAHLERMKKNMEQTIKDLQHRL 1797
Cdd:COG4717 264 LGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEEleEEELEELLAALGLPPDLSPEELLELL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1798 DEAEQIalkggKKQLQKLEARVRELE-NELEAEQKRNAESVKGmrKSERRIKELTYQTEEDRKNLLRLQDLVDKLQLKVK 1876
Cdd:COG4717 344 DRIEEL-----QELLREAEELEEELQlEELEQEIAALLAEAGV--EDEEELRAALEQAEEYQELKEELEELEEQLEELLG 416
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1387193866 1877 AYKRQAEEAEEQANTnlSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGTKGLNEE 1935
Cdd:COG4717 417 ELEELLEALDEEELE--EELEELEEELEELEEELEELREELAELEAELEQLEEDGELAE 473
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1496-1851 |
4.40e-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: 48.35 E-value: 4.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1496 ETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKLELQsalEEAEASLEHEEGKILRAQLEFNQIKAEMERK 1575
Cdd:pfam07888 69 EQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELS---EEKDALLAQRAAHEARIRELEEDIKTLTQRV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1576 LaEKDEEMEQAKRNHLRVVDSLQtsldaETRSRNEALRVK-KKMEGDLNEMEIQLSHANRLAAEAQKQVKSLQSLLKDTQ 1654
Cdd:pfam07888 146 L-ERETELERMKERAKKAGAQRK-----EEEAERKQLQAKlQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLT 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1655 IQLDDAvranddlkeniaivERRNNLLQAELEELRAVveqtersrklaeQELIETSER-VQLLHSQNTSLINQKKKMEAD 1733
Cdd:pfam07888 220 QKLTTA--------------HRKEAENEALLEELRSL------------QERLNASERkVEGLGEELSSMAAQRDRTQAE 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1734 LSQLQTEVEE----------AVQECRNAEEKAKKAITDAAMMAEElkKEQDTSAHLERMKKNMEQTIKDLQH------RL 1797
Cdd:pfam07888 274 LHQARLQAAQltlqladaslALREGRARWAQERETLQQSAEADKD--RIEKLSAELQRLEERLQEERMEREKlevelgRE 351
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1387193866 1798 DEAEQIALKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELT 1851
Cdd:pfam07888 352 KDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLETVA 405
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1385-1888 |
4.88e-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: 48.43 E-value: 4.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1385 ELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTkhrlQNEIEDLMVDVERSNAAAAALDKKQrnfdkilaEWKQKYEESQ 1464
Cdd:TIGR00618 195 KAELLTLRSQLLTLCTPCMPDTYHERKQVLEKE----LKHLREALQQTQQSHAYLTQKREAQ--------EEQLKKQQLL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1465 SELESSQKEARSLSTELFKLKNAYEES------LEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQ----LE 1534
Cdd:TIGR00618 263 KQLRARIEELRAQEAVLEETQERINRArkaaplAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQqssiEE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1535 AEKLELQSALEEAEASLEHEEGKILRAQLEfnQIKAEMERKLA-----EKDEEMEQAKRNHLRVVDSLQTSLDAETRSRN 1609
Cdd:TIGR00618 343 QRRLLQTLHSQEIHIRDAHEVATSIREISC--QQHTLTQHIHTlqqqkTTLTQKLQSLCKELDILQREQATIDTRTSAFR 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1610 EALRVKKKMEGdlnEMEIQLSHANRLAAEAQKQVKSLqsllKDTQIQLDDAVRANDDLKENIAIVErrnNLLQAELE--- 1686
Cdd:TIGR00618 421 DLQGQLAHAKK---QQELQQRYAELCAAAITCTAQCE----KLEKIHLQESAQSLKEREQQLQTKE---QIHLQETRkka 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1687 -ELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTS-----LINQKKKMEADLSQLQTEVEEAVQECRNAEEKAKKAIT 1760
Cdd:TIGR00618 491 vVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTrrmqrGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQ 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1761 DAAMMAEelkKEQDTSAHLERMKkNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEARVRELENELEAEQKRNAESVKGM 1840
Cdd:TIGR00618 571 SFSILTQ---CDNRSKEDIPNLQ-NITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLT 646
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1387193866 1841 RKsERRIKELTYQTEEDRKNLLRLQDlvdklqlKVKAYKRQAEEAEEQ 1888
Cdd:TIGR00618 647 AL-HALQLTLTQERVREHALSIRVLP-------KELLASRQLALQKMQ 686
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1475-1923 |
5.18e-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: 48.43 E-value: 5.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1475 RSLSTELFKLKNAYEESLEHLEtfkrenKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKLELQSALEEAEASLEHE 1554
Cdd:TIGR00618 179 TQLALMEFAKKKSLHGKAELLT------LRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQ 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1555 EGKILRAQLEFNQIKAEMERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANR 1634
Cdd:TIGR00618 253 EEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAA 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1635 LAAEaQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSE--R 1712
Cdd:TIGR00618 333 HVKQ-QSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREqaT 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1713 VQLLHSQNTSLINQKKKMEAD--LSQLQTEVEEAVQECRNAEEKAKKAitDAAMMAEELKKEQDTSAHLERMKKNMEQTI 1790
Cdd:TIGR00618 412 IDTRTSAFRDLQGQLAHAKKQqeLQQRYAELCAAAITCTAQCEKLEKI--HLQESAQSLKEREQQLQTKEQIHLQETRKK 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1791 KDLQHRLDEaEQIALKGGKKQLQKLEARvRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDK 1870
Cdd:TIGR00618 490 AVVLARLLE-LQEEPCPLCGSCIHPNPA-RQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQE 567
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1387193866 1871 LQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELD-EAEERADIAESQVNKLRAK 1923
Cdd:TIGR00618 568 IQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEkLSEAEDMLACEQHALLRKL 621
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
891-1099 |
5.58e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 5.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 891 VQAEqDNLADAEERCDQLIKNKIQLEAKVKEMTERLEdeeemnaELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHA 970
Cdd:COG3883 12 AFAD-PQIQAKQKELSELQAELEAAQAELDALQAELE-------ELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 971 TENKVKNLTEEM--AGLDEIIAKLTKEKKALQEA--HQQALDDL-QAEEDKVNTLTKAKVKLEQHVDDLEGSLEQEKKVR 1045
Cdd:COG3883 84 RREELGERARALyrSGGSVSYLDVLLGSESFSDFldRLSALSKIaDADADLLEELKADKAELEAKKAELEAKLAELEALK 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1387193866 1046 MDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQA 1099
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1535-1920 |
6.01e-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: 48.41 E-value: 6.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1535 AEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEMERK-LAEKDEEME-QAKRNHLRVVdslqtsldaetrsrNEAL 1612
Cdd:COG3096 278 NERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELsARESDLEQDyQAASDHLNLV--------------QTAL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1613 RVKKKME---GDLNEMEIQLSHANRLAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRN----NLLQAeL 1685
Cdd:COG3096 344 RQQEKIEryqEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAiqyqQAVQA-L 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1686 EELRAVVEQTERSRKLAEQELIETSERVQLLHSqntSLINQKKKMeADLSQLQTEVEEAVQ---------ECRNAEEKAK 1756
Cdd:COG3096 423 EKARALCGLPDLTPENAEDYLAAFRAKEQQATE---EVLELEQKL-SVADAARRQFEKAYElvckiagevERSQAWQTAR 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1757 KAITDAAMMAEELKKEQDTSAHLERMKKNMEQtikdlQHRLDE-AEQIALKGGKK--QLQKLEARVRELENELEAEQKRN 1833
Cdd:COG3096 499 ELLRRYRSQQALAQRLQQLRAQLAELEQRLRQ-----QQNAERlLEEFCQRIGQQldAAEELEELLAELEAQLEELEEQA 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1834 AESVKGMRKSERRIKELTYQTEEDRK---NLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERA 1910
Cdd:COG3096 574 AEAVEQRSELRQQLEQLRARIKELAArapAWLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDELAARK 653
|
410
....*....|
gi 1387193866 1911 DIAESQVNKL 1920
Cdd:COG3096 654 QALESQIERL 663
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
859-1085 |
7.61e-05 |
|
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: 47.84 E-value: 7.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 859 LKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDnladaEERCDQLIKNKIQLEAKVKEMTERLEdeeemnaeltA 938
Cdd:pfam18971 619 LEKSLRKREHLEKEVEKKLESKSGNKNKMEAKAQANSQ-----KDEIFALINKEANRDARAIAYTQNLK----------G 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 939 KKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAkLTKEKKALQEAHQQALDDLQAEEDK-V 1017
Cdd:pfam18971 684 IKRELSDKLEKISKDLKDFSKSFDEFKNGKNKDFSKAEETLKALKGSVKDLG-INPEWISKVENLNAALNEFKNGKNKdF 762
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387193866 1018 NTLTKAKVKLEQHVDDLEGSLEQEKKV-RMDLERAKRKLEGDLKLTQESIMDLEN-DKQQLDERLKK-KDF 1085
Cdd:pfam18971 763 SKVTQAKSDLENSVKDVIINQKVTDKVdNLNQAVSVAKAMGDFSRVEQVLADLKNfSKEQLAQQAQKnEDF 833
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
999-1703 |
7.70e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 47.87 E-value: 7.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 999 LQEAHQQALDD-LQAEEDKVNTLTKAKVKLEQHVDDL--EGSLEQEKKVRMDLERAKRKlegdlkltqesimDLENDKQQ 1075
Cdd:PRK10246 213 LTPEQVQSLTAsLQVLTDEEKQLLTAQQQQQQSLNWLtrLDELQQEASRRQQALQQALA-------------AEEKAQPQ 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1076 LDE-RLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTA----RAKVEKLRSDLSRELEEiSERL 1150
Cdd:PRK10246 280 LAAlSLAQPARQLRPHWERIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHaakqSAELQAQQQSLNTWLAE-HDRF 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1151 ----EEAGGATSVQIEMNKKReAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELSEQIDNLQRVKQKLEKEKSEFKL 1226
Cdd:PRK10246 359 rqwnNELAGWRAQFSQQTSDR-EQLRQWQQQLTHAEQKLNALPAITLTLTADEVAAALAQHAEQRPLRQRLVALHGQIVP 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1227 ELDDVTSNMEQIIKAKANLEKMCRTLEDQMNEHRSKAEETQR---------SVNDLTSQRAKLQTENGELSRQLDEKEAl 1297
Cdd:PRK10246 438 QQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADvkticeqeaRIKDLEAQRAQLQAGQPCPLCGSTSHPA- 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1298 ISQLTRGKLTYTQQLEDlkrQLEEEVKaknALAHALQSARHDCDLLREQYEEETEakaELQRVLSKANSEVAQWRTKYET 1377
Cdd:PRK10246 517 VEAYQALEPGVNQSRLD---ALEKEVK---KLGEEGAALRGQLDALTKQLQRDES---EAQSLRQEEQALTQQWQAVCAS 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1378 DAIQRT------------EELEEAKKKLAQR--LQDAEEAVEAVNAKCSS-LEKTKHRLQNEIEDLMVDVERSNAAAAAL 1442
Cdd:PRK10246 588 LNITLQpqddiqpwldaqEEHERQLRLLSQRheLQGQIAAHNQQIIQYQQqIEQRQQQLLTALAGYALTLPQEDEEASWL 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1443 DKKQRNFdkilAEWKQKyeesqselessqkearslstelfklknayeeslehletfKRENKNLQEEISDLT---EQLGSS 1519
Cdd:PRK10246 668 ATRQQEA----QSWQQR---------------------------------------QNELTALQNRIQQLTpllETLPQS 704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1520 GKTIHELEKVR----KQLEAEKLELQSALEEAEASLEHEEGKILRAQLEFnqikaemERKLAEKDEEMEQAkrnhlrvvd 1595
Cdd:PRK10246 705 DDLPHSEETVAldnwRQVHEQCLSLHSQLQTLQQQDVLEAQRLQKAQAQF-------DTALQASVFDDQQA--------- 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1596 SLQTSLDAETRSRNEALrvKKKMEGDLNEMEIQLSHANR-LAAEAQKQVKSLQSLLKDTQIQLDDAVRAnDDLKENIAIV 1674
Cdd:PRK10246 769 FLAALLDEETLTQLEQL--KQNLENQRQQAQTLVTQTAQaLAQHQQHRPDGLDLTVTVEQIQQELAQLA-QQLRENTTRQ 845
|
730 740 750
....*....|....*....|....*....|..
gi 1387193866 1675 -ERRNNLLQAE--LEELRAVVEQTERSRKLAE 1703
Cdd:PRK10246 846 gEIRQQLKQDAdnRQQQQALMQQIAQATQQVE 877
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1071-1242 |
7.86e-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: 46.07 E-value: 7.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1071 NDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERL 1150
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1151 EEAGG-----ATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELSEQIDNLQRVKQKLEKEKSEFK 1225
Cdd:COG1579 83 GNVRNnkeyeALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
170
....*....|....*..
gi 1387193866 1226 LELDDVTSNMEQIIKAK 1242
Cdd:COG1579 163 AEREELAAKIPPELLAL 179
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1048-1586 |
9.95e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.59 E-value: 9.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1048 LERAKRKLEGDLKLTQESIMDLENdkqqLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERT 1127
Cdd:PRK01156 164 LERNYDKLKDVIDMLRAEISNIDY----LEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKS 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1128 A--------------RAKVEKLRSDLSRELEE---ISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAA 1190
Cdd:PRK01156 240 AlnelssledmknryESEIKTAESDLSMELEKnnyYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDA 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1191 ALRKKHaDSVAELSE-QIDNLQRVKQKleKEKSEFKLELDDVTSNMEQIIKAKANLEKMCRTLEDQMNEHRSKAEETQRS 1269
Cdd:PRK01156 320 EINKYH-AIIKKLSVlQKDYNDYIKKK--SRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEI 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1270 VNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVKAKNALAHALQSARHDCDLLREQYEE 1349
Cdd:PRK01156 397 LKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIINHYNE 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1350 E----TEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQR---LQDAEEAVEAVNAKCSSLEKTKHRLQ 1422
Cdd:PRK01156 477 KksrlEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESAradLEDIKIKINELKDKHDKYEEIKNRYK 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1423 N-EIEDL---------------MVDVE----RSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLS---T 1479
Cdd:PRK01156 557 SlKLEDLdskrtswlnalavisLIDIEtnrsRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNnkyN 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1480 ELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKLELQSALEEAEASLEHEEgkil 1559
Cdd:PRK01156 637 EIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRIN---- 712
|
570 580
....*....|....*....|....*..
gi 1387193866 1560 raqlEFNQIKAEMERKLaEKDEEMEQA 1586
Cdd:PRK01156 713 ----ELSDRINDINETL-ESMKKIKKA 734
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1226-1397 |
1.02e-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: 45.69 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1226 LELDDVTSNMEQIIKAKANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGK 1305
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1306 ltytqQLEDLKRQLEEEVKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEE 1385
Cdd:COG1579 90 -----EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
170
....*....|..
gi 1387193866 1386 LEEAKKKLAQRL 1397
Cdd:COG1579 165 REELAAKIPPEL 176
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1493-1932 |
1.06e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 47.21 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1493 EHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKLELQSAL--------EEAEASLEHEEGKILRAQLE 1564
Cdd:COG5278 76 SFLEPYEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIalrragglEAALALVRSGEGKALMDEIR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1565 FNQIKAEMERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRLAAEAQKQVK 1644
Cdd:COG5278 156 ARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1645 SLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLI 1724
Cdd:COG5278 236 AALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1725 NQKKKMEADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIA 1804
Cdd:COG5278 316 AAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAI 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1805 LKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEE 1884
Cdd:COG5278 396 AAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALA 475
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1387193866 1885 AEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGTKGL 1932
Cdd:COG5278 476 ALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAA 523
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1422-1922 |
1.13e-04 |
|
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: 47.04 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1422 QNEIEDLMVDVERSNAAAAALDKKQRNFDKILAewKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLEtfkRE 1501
Cdd:pfam05557 20 QMELEHKRARIELEKKASALKRQLDRESDRNQE--LQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKL---NE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1502 NKNLQEEISDLTEQLGSsgktihELEKVRKQLEAEKLELQSALEEAEASLEHEEGKILRAQlEFNQIKAEMERKLAEKDE 1581
Cdd:pfam05557 95 KESQLADAREVISCLKN------ELSELRRQIQRAELELQSTNSELEELQERLDLLKAKAS-EAEQLRQNLEKQQSSLAE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1582 EMEQAKRnhLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRLaaeaqkqvKSLQSLLKDTQIQLDDAV 1661
Cdd:pfam05557 168 AEQRIKE--LEFEIQSQEQDSEIVKNSKSELARIPELEKELERLREHNKHLNEN--------IENKLLLKEEVEDLKRKL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1662 RANDDLKENIAIVERRNNLLQAELEELravvEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMEADLSQLQTEV 1741
Cdd:pfam05557 238 EREEKYREEAATLELEKEKLEQELQSW----VKLAQDTGLNLRSPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKAR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1742 EEAVQECRNAEEKakkaITDAAMMAEELK--------------KEQD-TSAHLERMKK--NMEQTIKDLQHRLDEAEQIA 1804
Cdd:pfam05557 314 RELEQELAQYLKK----IEDLNKKLKRHKalvrrlqrrvllltKERDgYRAILESYDKelTMSNYSPQLLERIEEAEDMT 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1805 LKGgKKQLQKLEARVRELENELEAEQKRNA--ESVKGMRKSERRIKELTYQTEED---RKNLLRLQDLVDKLQLKVKAYK 1879
Cdd:pfam05557 390 QKM-QAHNEEMEAQLSVAEEELGGYKQQAQtlERELQALRQQESLADPSYSKEEVdslRRKLETLELERQRLREQKNELE 468
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1387193866 1880 RQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRA 1922
Cdd:pfam05557 469 MELERRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQA 511
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
931-1221 |
1.14e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.93 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 931 EMNAELTAKKRkledecsELKRDIDDLELTLAKVEkEKHATENKvknlteemagldeIIAKLTKEKKALQEAHQQALDDL 1010
Cdd:PHA02562 167 EMDKLNKDKIR-------ELNQQIQTLDMKIDHIQ-QQIKTYNK-------------NIEEQRKKNGENIARKQNKYDEL 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1011 QAE-EDKVNTLTKAKVKLEQHVDDLEGSLEQEKKVRMDLERAKRKLEgdlKLTQESIMDLEND-----KQQLDERlkkkd 1084
Cdd:PHA02562 226 VEEaKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIE---QFQKVIKMYEKGGvcptcTQQISEG----- 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1085 felnalNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAggatsvqiemn 1164
Cdd:PHA02562 298 ------PDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKA----------- 360
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1387193866 1165 KKREAEFQKmrrdleeatlqheatAAALRKKHADSVAELSEQIDNLQRVKQKLEKEK 1221
Cdd:PHA02562 361 KKVKAAIEE---------------LQAEFVDNAEELAKLQDELDKIVKTKSELVKEK 402
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
843-1086 |
1.22e-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: 46.81 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 843 AETEKEIALMKEEFGRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEM 922
Cdd:pfam07888 76 RELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERM 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 923 TER-------LEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAK---L 992
Cdd:pfam07888 156 KERakkagaqRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAEneaL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 993 TKEKKALQE---AHQQA-------LDDLQAEEDKVNT-LTKAKVKLEQHVDDLEGSLEQEKKVRMDLERAKRKLEGDLKL 1061
Cdd:pfam07888 236 LEELRSLQErlnASERKveglgeeLSSMAAQRDRTQAeLHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEA 315
|
250 260
....*....|....*....|....*
gi 1387193866 1062 TQESIMDLENDKQQLDERLKKKDFE 1086
Cdd:pfam07888 316 DKDRIEKLSAELQRLEERLQEERME 340
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
955-1339 |
1.27e-04 |
|
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: 47.14 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 955 DDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDL-------QAEEDKVN-TLTKAKVK 1026
Cdd:pfam12128 600 EELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLrrlfdekQSEKDKKNkALAERKDS 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1027 LEQHVDDLEGSLEQ-EKKVRMDLERAKRKLEGDLKLTQESIMDLENDkqqlderlkkKDFELNALNARIEDEQALGSQLQ 1105
Cdd:pfam12128 680 ANERLNSLEAQLKQlDKKHQAWLEEQKEQKREARTEKQAYWQVVEGA----------LDAQLALLKAAIAARRSGAKAEL 749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1106 KKLKELQARieeleeeleaERTARAKVEKLRSDLSRELEEISERLEEAggatsvqiemnKKREAEFQKMRRDLEEATLQH 1185
Cdd:pfam12128 750 KALETWYKR----------DLASLGVDPDVIAKLKREIRTLERKIERI-----------AVRRQEVLRYFDWYQETWLQR 808
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1186 EataaalrkkhadsvaelseqiDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKMCRTLEDQMNEHRSKAEE 1265
Cdd:pfam12128 809 R---------------------PRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRC 867
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387193866 1266 TQRSVNDLTSQRAKLQTEnGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEevKAKNALAHALQSARHD 1339
Cdd:pfam12128 868 EMSKLATLKEDANSEQAQ-GSIGERLAQLEDLKLKRDYLSESVKKYVEHFKNVIAD--HSGSGLAETWESLREE 938
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1075-1555 |
1.34e-04 |
|
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: 47.04 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1075 QLDERLKKKdfELNALNARIEDEQALGSQLQ------KKLKELQARIeeleeeleaertarakveklrsdlsrelEEISE 1148
Cdd:pfam05557 13 QLQNEKKQM--ELEHKRARIELEKKASALKRqldresDRNQELQKRI----------------------------RLLEK 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1149 RLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQhEATAAALRKKHADSVAELSEQIDNLQRVKQKLEKEKSEFKLEL 1228
Cdd:pfam05557 63 REAEAEEALREQAELNRLKKKYLEALNKKLNEKESQ-LADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1229 DDVTSNMEQIIKAKANLEKMCRTL---EDQMNE---HRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALiSQLT 1302
Cdd:pfam05557 142 DLLKAKASEAEQLRQNLEKQQSSLaeaEQRIKElefEIQSQEQDSEIVKNSKSELARIPELEKELERLREHNKHL-NENI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1303 RGKLTYTQQLEDLKRQLeeevkaknalahalqsarhdcdllrEQYEEETEAKAELQRVLSKANSEVAQWRTKYETDA--I 1380
Cdd:pfam05557 221 ENKLLLKEEVEDLKRKL-------------------------EREEKYREEAATLELEKEKLEQELQSWVKLAQDTGlnL 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1381 QRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNE-------IEDLMVDVERSNAAAAALDK------KQR 1447
Cdd:pfam05557 276 RSPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQElaqylkkIEDLNKKLKRHKALVRRLQRrvllltKER 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1448 NFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEES-------LEHLETFKRENKNLQEEISDLTEQ----- 1515
Cdd:pfam05557 356 DGYRAILESYDKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEMeaqlsvaEEELGGYKQQAQTLERELQALRQQeslad 435
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1387193866 1516 LGSSGKTIHELEKVRKQLEAEKLELQSALEEAEASLEHEE 1555
Cdd:pfam05557 436 PSYSKEEVDSLRRKLETLELERQRLREQKNELEMELERRC 475
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1669-1917 |
1.36e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.30 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1669 ENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMEADLSQLQTEVEEAVQEC 1748
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1749 RNAEEKAKKAITDAAMMAE----ELKKEQDTSAHLERMKKNMEQTIKDLQHRLDE--AEQIALKGGKKQLQKLEARVREL 1822
Cdd:COG4942 100 EAQKEELAELLRALYRLGRqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEElrADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1823 ENELEAEQKRnaesvkgmrkserrikeltyqteedrknllrLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHE 1902
Cdd:COG4942 180 LAELEEERAA-------------------------------LEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
250
....*....|....*
gi 1387193866 1903 LDEAEERADIAESQV 1917
Cdd:COG4942 229 IARLEAEAAAAAERT 243
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
859-1398 |
1.38e-04 |
|
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: 47.05 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 859 LKEALEKSEARRKELEEKMVSLLQE-----KNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAK----VKEMTERLEDE 929
Cdd:pfam07111 120 LRAALAGAEMVRKNLEEGSQRELEEiqrlhQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKrageAKQLAEAQKEA 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 930 EEMNAELTAKKRKLEDECS---ELKRDIDDL---ELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKK------ 997
Cdd:pfam07111 200 ELLRKQLSKTQEELEAQVTlveSLRKYVGEQvppEVHSQTWELERQELLDTMQHLQEDRADLQATVELLQVRVQslthml 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 998 ALQEAHQ----QALDDLQAEEDKvntltKAKVKLEQHVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDK 1073
Cdd:pfam07111 280 ALQEEELtrkiQPSDSLEPEFPK-----KCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQ 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1074 QQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVE-KLRSDLSReLEEISERLEE 1152
Cdd:pfam07111 355 AILQRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQiWLETTMTR-VEQAVARIPS 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1153 AGGATSVQIemnKKREAEFQKMRRDLEEATLQHEATAAALRKKHADsvAELSEQIDNLQRVKQKLEKE-KSEFKLELDDV 1231
Cdd:pfam07111 434 LSNRLSYAV---RKVHTIKGLMARKVALAQLRQESCPPPPPAPPVD--ADLSLELEQLREERNRLDAElQLSAHLIQQEV 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1232 TSNMEQIIKAKANLEKMCRTLEDQMNehrsKAEETQRSVNDLTSQRAKLQTENGE----LSRQLDEKEALISQLTRGKLT 1307
Cdd:pfam07111 509 GRAREQGEAERQQLSEVAQQLEQELQ----RAQESLASVGQQLEVARQGQQESTEeaasLRQELTQQQEIYGQALQEKVA 584
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1308 YT-----QQLEDLKRQLEEevkAKNALAHALQSARHdcdlLREQYEEETEAKAELQRVLSKANSEVAQWRTKyetdaiqR 1382
Cdd:pfam07111 585 EVetrlrEQLSDTKRRLNE---ARREQAKAVVSLRQ----IQHRATQEKERNQELRRLQDEARKEEGQRLAR-------R 650
|
570
....*....|....*.
gi 1387193866 1383 TEELEEAKKKLAQRLQ 1398
Cdd:pfam07111 651 VQELERDKNLMLATLQ 666
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1010-1170 |
1.46e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.69 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1010 LQAEEDKVNTLTKAKVKLEQHVDDLEgsLEQEKKVrmdlERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNA 1089
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKEAL--LEAKEEI----HKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1090 LNARIEDEQALGSQLQKKLKELQARIEELEEEleaertARAKVEKLrSDLSRE------LEEISERLEEAGGATSVQIEM 1163
Cdd:PRK12704 108 REEELEKKEKELEQKQQELEKKEEELEELIEE------QLQELERI-SGLTAEeakeilLEKVEEEARHEAAVLIKEIEE 180
|
....*..
gi 1387193866 1164 NKKREAE 1170
Cdd:PRK12704 181 EAKEEAD 187
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
859-995 |
1.62e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.77 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 859 LKEALEKSEARRKELEEKmvsllqeknDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMTERLEDEEEMNAELTA 938
Cdd:COG2433 378 IEEALEELIEKELPEEEP---------EAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLER 448
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1387193866 939 KKRKL----------EDECSELKRDIDDLELTLAKVEKEKHATENKVKNLtEEMAGLDE--------IIAKLTKE 995
Cdd:COG2433 449 ELSEArseerreirkDREISRLDREIERLERELEEERERIEELKRKLERL-KELWKLEHsgelvpvkVVEKFTKE 522
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1702-1889 |
1.62e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1702 AEQELIETSERVQLLHSQNTSLINQKKKMEADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDT-SAHLE 1780
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1781 RMKKNMEQT-----------IKDLQHRLDEAEQIAlKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKE 1849
Cdd:COG3883 94 ALYRSGGSVsyldvllgsesFSDFLDRLSALSKIA-DADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1387193866 1850 LTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQA 1889
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
885-1536 |
1.73e-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: 46.97 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 885 NDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMTERLEDEEEMnaELTAKKRKLEDECSELKRDIDDLEltlAKV 964
Cdd:TIGR01612 1486 NELKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKYSAL--AIKNKFAKTKKDSEIIIKEIKDAH---KKF 1560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 965 EKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAhQQALDDLqaeEDKVNTLTKAKVKLEQHVDDLEGSLEQEKKV 1044
Cdd:TIGR01612 1561 ILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDI-QLSLENF---ENKFLKISDIKKKINDCLKETESIEKKISSF 1636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1045 RMDLERAKRKLEGDLKLT-QESIMDLENDKQQLDERLKkkdfELNALNARIEDEQALGSQlQKKLKELqarieelEEELE 1123
Cdd:TIGR01612 1637 SIDSQDTELKENGDNLNSlQEFLESLKDQKKNIEDKKK----ELDELDSEIEKIEIDVDQ-HKKNYEI-------GIIEK 1704
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1124 AERTARAKVEKLRSdLSRELEEISERLEEAGGATSVQ-IEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAe 1202
Cdd:TIGR01612 1705 IKEIAIANKEEIES-IKELIEPTIENLISSFNTNDLEgIDPNEKLEEYNTEIGDIYEEFIELYNIIAGCLETVSKEPIT- 1782
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1203 lSEQIDNLQRVKQ----KLEKEKSEFKLELDDVTSN-MEQIIKA-KANLEKMCRTLEDQMNEHRSKAEETQRSVNDLtsq 1276
Cdd:TIGR01612 1783 -YDEIKNTRINAQneflKIIEIEKKSKSYLDDIEAKeFDRIINHfKKKLDHVNDKFTKEYSKINEGFDDISKSIENV--- 1858
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1277 raKLQTENGELSRQLDE-KEALISQLTRGKLTYTQQLEDLKRQLeeeVKAKNALAHALQSARhDCDLLREQYEE-----E 1350
Cdd:TIGR01612 1859 --KNSTDENLLFDILNKtKDAYAGIIGKKYYSYKDEAEKIFINI---SKLANSINIQIQNNS-GIDLFDNINIAilsslD 1932
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1351 TEAKAELQRVLSKAN-SEV-AQWRTKYET-----DAIQRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQN 1423
Cdd:TIGR01612 1933 SEKEDTLKFIPSPEKePEIyTKIRDSYDTlldifKKSQDLHKKEQDTLNIIFENQQLYEKIQASNELKDTLSDLKYKKEK 2012
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1424 EIEDLMVDVERSNAAAAaLDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENK 1503
Cdd:TIGR01612 2013 ILNDVKLLLHKFDELNK-LSCDSQNYDTILELSKQDKIKEKIDNYEKEKEKFGIDFDVKAMEEKFDNDIKDIEKFENNYK 2091
|
650 660 670
....*....|....*....|....*....|...
gi 1387193866 1504 NLQEEISDLTEQLGSSGKTIHELEKVRKQLEAE 1536
Cdd:TIGR01612 2092 HSEKDNHDFSEEKDNIIQSKKKLKELTEAFNTE 2124
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1477-1656 |
1.76e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1477 LSTELFKLKNAYEESLEHLETFKRENKnlqeeISDLTEQLGSSGKTIHELEKVRKQLEAEKLELQSALEEAEASLEHEEG 1556
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKNG-----LVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPD 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1557 KI--LRAQLEFNQIKAEMERKLAEKDEEMEQAKRNHLRVV------DSLQTSLDAETRSRNEALRV--------KKKMEG 1620
Cdd:COG3206 255 ALpeLLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIalraqiAALRAQLQQEAQRILASLEAelealqarEASLQA 334
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1387193866 1621 DLNEMEIQLSHANRLAAE----------AQKQVKSLQSLLKDTQIQ 1656
Cdd:COG3206 335 QLAQLEARLAELPELEAElrrlerevevARELYESLLQRLEEARLA 380
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1384-1919 |
1.92e-04 |
|
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: 46.17 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1384 EELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKhrlqNEIEDLMVDVERsnaaaAALDKKQRNFDKILAEWKQKyees 1463
Cdd:pfam05701 42 LELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTK----RLIEELKLNLER-----AQTEEAQAKQDSELAKLRVE---- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1464 QSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDL----------TEQLGSSGKtihELEKVRKQL 1533
Cdd:pfam05701 109 EMEQGIADEASVAAKAQLEVAKARHAAAVAELKSVKEELESLRKEYASLvserdiaikrAEEAVSASK---EIEKTVEEL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1534 EAEKLELQSALEEAEAS-LEHEEGKIlRAQLEFNQIKAEMERKLAEKDEEMEQAkRNHLRVVDSLQTSLDAetrsrNEAL 1612
Cdd:pfam05701 186 TIELIATKESLESAHAAhLEAEEHRI-GAALAREQDKLNWEKELKQAEEELQRL-NQQLLSAKDLKSKLET-----ASAL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1613 RVKKK------MEGDLNEMEIQLSHANRLAAEAQKQVKSLQSLLKDTQIQLDdavRANDDLKENIAIVERrnnlLQAELE 1686
Cdd:pfam05701 259 LLDLKaelaayMESKLKEEADGEGNEKKTSTSIQAALASAKKELEEVKANIE---KAKDEVNCLRVAAAS----LRSELE 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1687 ELRAVVEQTERSRKLAeqelietservqllhsqntslinqkkkmEADLSQLQTEVEEAVQECRNAEEKAKKAitdAAMMA 1766
Cdd:pfam05701 332 KEKAELASLRQREGMA----------------------------SIAVSSLEAELNRTKSEIALVQAKEKEA---REKMV 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1767 EELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQialkgGKKQLQKLEARVRELENELEA---EQKRNAESVKGMRKS 1843
Cdd:pfam05701 381 ELPKQLQQAAQEAEEAKSLAQAAREELRKAKEEAEQ-----AKAAASTVESRLEAVLKEIEAakaSEKLALAAIKALQES 455
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387193866 1844 ERRiKELTYQTEEDRKNLLRLQDLvdklqlkvKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNK 1919
Cdd:pfam05701 456 ESS-AESTNQEDSPRGVTLSLEEY--------YELSKRAHEAEELANKRVAEAVSQIEEAKESELRSLEKLEEVNR 522
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
981-1159 |
2.01e-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: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 981 EMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQHVDDLEgSLEQEKKVRMDLERAKRKLEGdlk 1060
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVE-ARIKKYEEQLGNVRNNKEYEA--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1061 LTQEsIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTA-RAKVEKLRSDL 1139
Cdd:COG1579 94 LQKE-IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEElEAEREELAAKI 172
|
170 180
....*....|....*....|
gi 1387193866 1140 SRELEEISERLEEAGGATSV 1159
Cdd:COG1579 173 PPELLALYERIRKRKNGLAV 192
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1017-1234 |
2.08e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1017 VNTLTKAKVK--LEQHVDDLEGSL----EQEKKVRMDLERAKRKLEgDLKlTQESIMDLENDKQQLDERLKKKDFELNAL 1090
Cdd:COG3206 154 ANALAEAYLEqnLELRREEARKALefleEQLPELRKELEEAEAALE-EFR-QKNGLVDLSEEAKLLLQQLSELESQLAEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1091 NARIEDEQALGSQLQKKLK----------------ELQARIEELEEELEAERT-----------ARAKVEKLRSDLSREL 1143
Cdd:COG3206 232 RAELAEAEARLAALRAQLGsgpdalpellqspviqQLRAQLAELEAELAELSArytpnhpdviaLRAQIAALRAQLQQEA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1144 EEISERLEeaggatsVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRkkhadsvaELSEQIDNLQRVKQKLEKEKSE 1223
Cdd:COG3206 312 QRILASLE-------AELEALQAREASLQAQLAQLEARLAELPELEAELR--------RLEREVEVARELYESLLQRLEE 376
|
250
....*....|.
gi 1387193866 1224 FKLELDDVTSN 1234
Cdd:COG3206 377 ARLAEALTVGN 387
|
|
| Yuri_gagarin |
pfam15934 |
Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis. |
868-1022 |
2.22e-04 |
|
Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis.
Pssm-ID: 318204 [Multi-domain] Cd Length: 234 Bit Score: 44.95 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 868 ARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQL---------------IKNKI--------QLEAKVKEMTE 924
Cdd:pfam15934 41 ENKNEQEQQLKEFTVQNQRLACQIDNLHETLKDRDHQIKQLqsmitgysdisennrLKEEIhdlkqkncVQARVVRKMGL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 925 RLEDEEEMNAELTAKKRKL----EDECSELK---RDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLdeiiakltKEKK 997
Cdd:pfam15934 121 ELKGQEEQRVELCDKYESLlgsfEEQCQELKranRRVQSLQTRLSQVEKLQEELRTERKILREEVIAL--------KEKD 192
|
170 180
....*....|....*....|....*....
gi 1387193866 998 ALQEAHQQALDD----LQAEEDKVNTLTK 1022
Cdd:pfam15934 193 AKSNGRERALQDqlkcCQTEIEKSRTLIR 221
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1170-1905 |
2.27e-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: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1170 EFQKMRRDLEEATLQHEATAAALRKKhadSVAELSEQIDNLQRVKQKLEKEKSE-FKLELDDVTSNMEQIIKakanlEKM 1248
Cdd:TIGR01612 617 EYIKKAIDLKKIIENNNAYIDELAKI---SPYQVPEHLKNKDKIYSTIKSELSKiYEDDIDALYNELSSIVK-----ENA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1249 CRTLEDqmnehRSKAEETQRSVNDLTSQRAKLQTENGE--LSRQLDEKEALISQLTR-GKLTYTQQLEDLKRQLEEEVKA 1325
Cdd:TIGR01612 689 IDNTED-----KAKLDDLKSKIDKEYDKIQNMETATVElhLSNIENKKNELLDIIVEiKKHIHGEINKDLNKILEDFKNK 763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1326 KNALAHALQSarhdcdllreqYEEETEAkaelqrvLSKANSEVAQWRTKY-ETDAIQRTEElEEAKkklaQRLQDAEEAV 1404
Cdd:TIGR01612 764 EKELSNKIND-----------YAKEKDE-------LNKYKSKISEIKNHYnDQINIDNIKD-EDAK----QNYDKSKEYI 820
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1405 EAVNAKCSSLEKTKHRLQNEIEDLMVDVER----SNAAAAALDKKQRNFDKILAEWKQKYEESQSEL-ESSQKEARSLST 1479
Cdd:TIGR01612 821 KTISIKEDEIFKIINEMKFMKDDFLNKVDKfinfENNCKEKIDSEHEQFAELTNKIKAEISDDKLNDyEKKFNDSKSLIN 900
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1480 ELfklKNAYEESLEHLETFKREN------KNLQEEISD-------LTEQLGSSGKTIHELEKVRK----QLEAEKLELQS 1542
Cdd:TIGR01612 901 EI---NKSIEEEYQNINTLKKVDeyikicENTKESIEKfhnkqniLKEILNKNIDTIKESNLIEKsykdKFDNTLIDKIN 977
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1543 ALEEA--EASLEHEEGKILRAQLEFNQIKAEM----ERKLAEKDEEMEQAKRNHL-RVVDSLQTSLDAETRSRNEALRVK 1615
Cdd:TIGR01612 978 ELDKAfkDASLNDYEAKNNELIKYFNDLKANLgknkENMLYHQFDEKEKATNDIEqKIEDANKNIPNIEIAIHTSIYNII 1057
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1616 KKMEGD------------LNEMEIQLSHANRLaaEAQKQVKSLQSLLKDTQIQLDDAV-RANDDLK-------ENIAIVE 1675
Cdd:TIGR01612 1058 DEIEKEigkniellnkeiLEEAEINITNFNEI--KEKLKHYNFDDFGKEENIKYADEInKIKDDIKnldqkidHHIKALE 1135
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1676 RRNNLLQAELEELRAVVEQTER-SRKLAEQELIETSERVQllhsQN-TSLINQKKKMEADLSQLQTEVEE------AVQE 1747
Cdd:TIGR01612 1136 EIKKKSENYIDEIKAQINDLEDvADKAISNDDPEEIEKKI----ENiVTKIDKKKNIYDEIKKLLNEIAEiekdktSLEE 1211
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1748 CRNAEEKAKKAItdAAMMAEELKKEQDTSAHlerMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEARVRELENELE 1827
Cdd:TIGR01612 1212 VKGINLSYGKNL--GKLFLEKIDEEKKKSEH---MIKAMEAYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDDD 1286
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1828 AE----QKRNAESVKGMRKSERRI--------------KEL-TYQTEEDRKN------LLRLQDLVDKLQL--------K 1874
Cdd:TIGR01612 1287 KDhhiiSKKHDENISDIREKSLKIiedfseesdindikKELqKNLLDAQKHNsdinlyLNEIANIYNILKLnkikkiidE 1366
|
810 820 830
....*....|....*....|....*....|.
gi 1387193866 1875 VKAYKRQAEEAEEQANTNLSKFRKVQHELDE 1905
Cdd:TIGR01612 1367 VKEYTKEIEENNKNIKDELDKSEKLIKKIKD 1397
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
765-1110 |
2.35e-04 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 46.48 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 765 FKAGLLGLLEEMR---------DERLSRIITRIQaqsrgvlsRMEFKKLLERRDSLLIIQWNIRAFMGVKNWPWMKLYF- 834
Cdd:pfam15818 5 FKTSLLEALEELRmrreaetqyEEQIGKIIVETQ--------ELKWQKETLQNQKETLAKQHKEAMAVFKKQLQMKMCAl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 835 ---KIKPLLKSAETEKEIAlmkeefgRLKEALEKSEARRKELEEKmVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKN 911
Cdd:pfam15818 77 eeeKGKYQLATEIKEKEIE-------GLKETLKALQVSKYSLQKK-VSEMEQKLQLHLLAKEDHHKQLNEIEKYYATITG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 912 KIQLeakVKEMTERLE----DEEEMNAELTAKKRKLEDECSELKRDIDDL--ELTLAKVE-KEKHATEN--------KVK 976
Cdd:pfam15818 149 QFGL---VKENHGKLEqnvqEAIQLNKRLSALNKKQESEICSLKKELKKVtsDLIKSKVTcQYKMGEENinltikeqKFQ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 977 NLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEqhvddleGSLEQEKKVRMDLERAKRKLE 1056
Cdd:pfam15818 226 ELQERLNMELELNKKINEEITHIQEEKQDIIISFQHMQQLLQQQTQANTEME-------AELKALKENNQTLERDNELQR 298
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1387193866 1057 GDLKLTQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKE 1110
Cdd:pfam15818 299 EKVKENEEKFLNLQNEHEKALGTWKKHVEELNGEINEIKNELSSLKETHIKLQE 352
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1687-1871 |
2.36e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.16 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1687 ELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMEADLSQLQTEVEEAVQECRNAEEKAKK---AITDAA 1763
Cdd:PHA02562 189 KIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKlntAAAKIK 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1764 MMAEELKKE--------------QDTSAHLERMKKNMEQtIKDLQHRLDEAE--QIALKGGKKQLQKLEARVRELENELE 1827
Cdd:PHA02562 269 SKIEQFQKVikmyekggvcptctQQISEGPDRITKIKDK-LKELQHSLEKLDtaIDELEEIMDEFNEQSKKLLELKNKIS 347
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1387193866 1828 AEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKL 1871
Cdd:PHA02562 348 TNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKI 391
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1534-1763 |
2.46e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 2.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1534 EAEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEMERKLAEKDEEMEQakrnhlrvVDSLQTSLDaetrsrnealr 1613
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAE--------IDKLQAEIA----------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1614 vkkKMEGDLNEMEIQLSHANRLAAEAQKQVKSLQSLLKDTQIqlDDAVRANDDLKeniAIVERRNNLLQaELEELRAVVE 1693
Cdd:COG3883 76 ---EAEAEIEERREELGERARALYRSGGSVSYLDVLLGSESF--SDFLDRLSALS---KIADADADLLE-ELKADKAELE 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1694 QTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMEADLSQLQTEVEEAVQECRNAEEKAKKAITDAA 1763
Cdd:COG3883 147 AKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1381-1582 |
2.61e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1381 QRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAaaaLDKKQRNFDKIL-AEWKQK 1459
Cdd:COG3883 23 KELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAE---IEERREELGERArALYRSG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1460 YEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGssgktihELEKVRKQLEAEKLE 1539
Cdd:COG3883 100 GSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLA-------ELEALKAELEAAKAE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1387193866 1540 LQSALEEAEA---SLEHEEGKILRAQLEFNQIKAEMERKLAEKDEE 1582
Cdd:COG3883 173 LEAQQAEQEAllaQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
911-1180 |
2.71e-04 |
|
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: 45.88 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 911 NKIQLEAKVKEM-TERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDeiI 989
Cdd:pfam17380 285 SERQQQEKFEKMeQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRE--L 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 990 AKLTKEKKALQEAHQQALDDLQAEEDKVN--------TLTKAKVKLEQHVDDLEGSLEQEKKVRMDLERAK----RKLEG 1057
Cdd:pfam17380 363 ERIRQEEIAMEISRMRELERLQMERQQKNervrqeleAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARqrevRRLEE 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1058 DLKLTQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQalgsQLQKKLKELQARIEELEEEleAERTARAKVEKLRS 1137
Cdd:pfam17380 443 ERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEK----RDRKRAEEQRRKILEKELE--ERKQAMIEEERKRK 516
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1387193866 1138 DLSRELEEIS------ERLEEAGGATSVQIEMNKKREAEfQKMRRDLEE 1180
Cdd:pfam17380 517 LLEKEMEERQkaiyeeERRREAEEERRKQQEMEERRRIQ-EQMRKATEE 564
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
934-1158 |
2.78e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 934 AELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQ-- 1011
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYrs 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1012 -AEEDKVNTLTKAK--VKLEQHVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKkkdfeln 1088
Cdd:COG3883 99 gGSVSYLDVLLGSEsfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA------- 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1089 ALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATS 1158
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1325-1459 |
2.94e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1325 AKNALAHALQSARHDCDLLREqyEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEAV 1404
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILE--EAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKL 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1387193866 1405 EAVNAKCSSLEKTKHRLQNEIEDlmvdversnaaaaaLDKKQRNFDKILAEWKQK 1459
Cdd:PRK12704 103 ELLEKREEELEKKEKELEQKQQE--------------LEKKEEELEELIEEQLQE 143
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
833-1326 |
3.12e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.81 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 833 YFKIKPLLKSA--ETEKEIALMKEEFGRLKEALEKSEAR----RKELEEKMVSLLQEKNDL--QLQVQAEQDNLADAEER 904
Cdd:TIGR00606 568 YFPNKKQLEDWlhSKSKEINQTRDRLAKLNKELASLEQNknhiNNELESKEEQLSSYEDKLfdVCGSQDEESDLERLKEE 647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 905 CDQLIKNKIQLEAKV---KEMTERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEE 981
Cdd:TIGR00606 648 IEKSSKQRAMLAGATavySQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDE 727
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 982 MAGLDE----IIAKLTKEKKALQEAHQQALDDLQAEEDKVN---TLTKAKVKLEQHVDDLEGSLEQEKKVRMDLERAKRK 1054
Cdd:TIGR00606 728 MLGLAPgrqsIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEeqeTLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERK 807
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1055 LE----------GDLKLTQ-------------------ESIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQ 1105
Cdd:TIGR00606 808 IAqqaaklqgsdLDRTVQQvnqekqekqheldtvvskiELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFE 887
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1106 KKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATlqh 1185
Cdd:TIGR00606 888 EQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKI--- 964
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1186 EATAAALRKKHADSVAELSEQIDNLQRVKQKLEKeksEFKLELDDVTSNMEQIIKAKANLEKMCRtledqmnehRSKAEE 1265
Cdd:TIGR00606 965 QDGKDDYLKQKETELNTVNAQLEECEKHQEKINE---DMRLMRQDIDTQKIQERWLQDNLTLRKR---------ENELKE 1032
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387193866 1266 TQRSVNDLTSQRAKLQ-TENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVKAK 1326
Cdd:TIGR00606 1033 VEEELKQHLKEMGQMQvLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREP 1094
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1673-1811 |
3.15e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.97 E-value: 3.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1673 IVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMEAdlsQLQTEVEEAVQECRNAE 1752
Cdd:PRK00409 503 IIEEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQE---EEDKLLEEAEKEAQQAI 579
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1387193866 1753 EKAKKAITDAAMMAEELKKEQDTSAHLermkKNMEQTIKDLQHRLDEAEQIALKGGKKQ 1811
Cdd:PRK00409 580 KEAKKEADEIIKELRQLQKGGYASVKA----HELIEARKRLNKANEKKEKKKKKQKEKQ 634
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
839-1083 |
3.25e-04 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 45.05 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 839 LLKSAETEKEIALMKEEFGRLKEALEKSEARRKELEEKMVSLLQ---------EKNDLQLQVQAEQDNLADAEERCDQLI 909
Cdd:pfam15742 99 VLKQAQSIKSQNSLQEKLAQEKSRVADAEEKILELQQKLEHAHKvcltdtcilEKKQLEERIKEASENEAKLKQQYQEEQ 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 910 KNKIQLEAKVKEMTERLEDeeemnaeLTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEemagLDEII 989
Cdd:pfam15742 179 QKRKLLDQNVNELQQQVRS-------LQDKEAQLEMTNSQQQLRIQQQEAQLKQLENEKRKSDEHLKSNQE----LSEKL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 990 AKLTKEKKALQEAHQQALDDLQAEEDKVNtltkakvkleqhvddlegslEQEKKVRMDLERAKRKLEGDLKLTQESIMDL 1069
Cdd:pfam15742 248 SSLQQEKEALQEELQQVLKQLDVHVRKYN--------------------EKHHHHKAKLRRAKDRLVHEVEQRDERIKQL 307
|
250
....*....|....
gi 1387193866 1070 ENDKQQLDERLKKK 1083
Cdd:pfam15742 308 ENEIGILQQQSEKE 321
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1578-1922 |
3.38e-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: 45.27 E-value: 3.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1578 EKDEEMEQAKRNHLRVVDS---LQTSLDAETRSRNEALR----VKKKMEGDLNEMEIQLSHANRLAAEAQKQVKSLQSLL 1650
Cdd:pfam07888 10 EEESHGEEGGTDMLLVVPRaelLQNRLEECLQERAELLQaqeaANRQREKEKERYKRDREQWERQRRELESRVAELKEEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1651 KDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKM 1730
Cdd:pfam07888 90 RQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1731 EADLSQLQTEVEEAVQECRNaeekakkaitdaamMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQ--IALKGG 1808
Cdd:pfam07888 170 EAERKQLQAKLQQTEEELRS--------------LSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRkeAENEAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1809 KKQLQKLEARVRELENELEAeQKRNAESVKGMRksERRIKELTYQTEEDRKNLLRLQDLvdKLQLKVKAYKRQAEEAEEQ 1888
Cdd:pfam07888 236 LEELRSLQERLNASERKVEG-LGEELSSMAAQR--DRTQAELHQARLQAAQLTLQLADA--SLALREGRARWAQERETLQ 310
|
330 340 350
....*....|....*....|....*....|....*.
gi 1387193866 1889 ANTNLSKFR--KVQHELDEAEERADIAESQVNKLRA 1922
Cdd:pfam07888 311 QSAEADKDRieKLSAELQRLEERLQEERMEREKLEV 346
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
846-1036 |
3.43e-04 |
|
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: 45.98 E-value: 3.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 846 EKEIALMKEEF-GRLKEALEKSEARRKELEE----KMVSLLQEKNDLQLQVQAEQDNLAdaEERCDQLIK------NKIQ 914
Cdd:pfam12128 695 DKKHQAWLEEQkEQKREARTEKQAYWQVVEGaldaQLALLKAAIAARRSGAKAELKALE--TWYKRDLASlgvdpdVIAK 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 915 LEAKVKEMTERLEDEEEMNAE------------------LTAKKRKLEDECSELK----RDIDDLELTLAKVEKEKHATE 972
Cdd:pfam12128 773 LKREIRTLERKIERIAVRRQEvlryfdwyqetwlqrrprLATQLSNIERAISELQqqlaRLIADTKLRRAKLEMERKASE 852
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387193866 973 NKVKNLTEEMAGLDEIIAKLT--KEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQHVDDLEG 1036
Cdd:pfam12128 853 KQQVRLSENLRGLRCEMSKLAtlKEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHFKN 918
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1203-1447 |
3.49e-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: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1203 LSEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEqiikAKANLEKMcRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQT 1282
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKNGLVDLSEE----AKLLLQQL-SELESQLAEARAELAEAEARLAALRAQLGSGPD 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1283 ENGELSRQldekeALISQLTrgkltytQQLEDLKRQLEEEvkaknalahalqSARhdcdlLREQYEEETEAKAELQRVLS 1362
Cdd:COG3206 255 ALPELLQS-----PVIQQLR-------AQLAELEAELAEL------------SAR-----YTPNHPDVIALRAQIAALRA 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1363 KANSEVAQWRTKYETDAiqrtEELEEAKKKLAQRLQDAEEAVEAVNAKcsslektkhrlQNEIEDLMVDVERSNAAAAAL 1442
Cdd:COG3206 306 QLQQEAQRILASLEAEL----EALQAREASLQAQLAQLEARLAELPEL-----------EAELRRLEREVEVARELYESL 370
|
....*
gi 1387193866 1443 DKKQR 1447
Cdd:COG3206 371 LQRLE 375
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
871-1223 |
3.53e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.28 E-value: 3.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 871 KELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMTERLEDEEEMNAELTAKKRKLEDECSEL 950
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 951 KRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQH 1030
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1031 VDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKE 1110
Cdd:COG4372 166 LAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1111 LQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAA 1190
Cdd:COG4372 246 EDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
330 340 350
....*....|....*....|....*....|...
gi 1387193866 1191 ALRKKHADSVAELSEQIDNLQRVKQKLEKEKSE 1223
Cdd:COG4372 326 KKLELALAILLAELADLLQLLLVGLLDNDVLEL 358
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
873-1177 |
3.56e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 45.69 E-value: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 873 LEEKMVSLLQEKNDLQLqVQAEQDNLADAEERcdqlIKNKIQLEAKVKEMTERLEDEeeMNAELTAKKRKLEDECSELKR 952
Cdd:PRK05771 14 LKSYKDEVLEALHELGV-VHIEDLKEELSNER----LRKLRSLLTKLSEALDKLRSY--LPKLNPLREEKKKVSVKSLEE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 953 DIDDLELTLAKVEKEkhatenkVKNLTEEMAGLDEIIAKLTKEKKALQEAHqqALD-DLQAEEDKVNTLTKAKVKLEQHV 1031
Cdd:PRK05771 87 LIKDVEEELEKIEKE-------IKELEEEISELENEIKELEQEIERLEPWG--NFDlDLSLLLGFKYVSVFVGTVPEDKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1032 DDLEGSLEQEKkvrmdLERAKRKLEGDLKLtqesIMDLENDKQQLDERLKKKDFELNALNARIEDEQALgSQLQKKLKEL 1111
Cdd:PRK05771 158 EELKLESDVEN-----VEYISTDKGYVYVV----VVVLKELSDEVEEELKKLGFERLELEEEGTPSELI-REIKEELEEI 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387193866 1112 qarieeleeeleaertarakvEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRD 1177
Cdd:PRK05771 228 ---------------------EKERESLLEELKELAKKYLEELLALYEYLEIELERAEALSKFLKT 272
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1141-1410 |
4.09e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 45.32 E-value: 4.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1141 RELEEISERLEEAggatsvqiemnKKR-EAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELseqidnLQRVKQKLEK 1219
Cdd:PRK05035 439 RAIEQEKKKAEEA-----------KARfEARQARLEREKAAREARHKKAAEARAAKDKDAVAAA------LARVKAKKAA 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1220 EKSEFKLELDDVTSNMEQIIKAKAnlekmcrtledqmnehrSKAEETQRSVNDLTSQRAklqtengelsrqlDEKEALIS 1299
Cdd:PRK05035 502 ATQPIVIKAGARPDNSAVIAAREA-----------------RKAQARARQAEKQAAAAA-------------DPKKAAVA 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1300 Q-LTRGKLTYTQQLEDLKRQLEEEVKAKNALAHALqsARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETD 1378
Cdd:PRK05035 552 AaIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAI--ARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKA 629
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1387193866 1379 AIQRTEELEE---------------AKKKLAQRLQDAEEAVEAVNAK 1410
Cdd:PRK05035 630 EQQANAEPEEpvdprkaavaaaiarAKARKAAQQQANAEPEEAEDPK 676
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1622-1763 |
4.18e-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: 44.15 E-value: 4.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1622 LNEMEIQLSHANRLAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQA---------ELEELRAVV 1692
Cdd:COG1579 19 LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvrnnkEYEALQKEI 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387193866 1693 EQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMEADLSQLQTEVEEAVQECRNAEEKAKKAITDAA 1763
Cdd:COG1579 99 ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELA 169
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
969-1358 |
4.63e-04 |
|
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: 45.00 E-value: 4.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 969 HATENKVKNLTEEMAGLDEIiakLTKEKKALQEAHQQALDDLQAEEDK---------VNTLTKAKVKLEQHVDDLEGSLE 1039
Cdd:NF033838 36 HAEEVRGGNNPTVTSSGNES---QKEHAKEVESHLEKILSEIQKSLDKrkhtqnvalNKKLSDIKTEYLYELNVLKEKSE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1040 QE--KKVRMDLERAKRKLEGDLkltqesimdLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLkELQariee 1117
Cdd:NF033838 113 AEltSKTKKELDAAFEQFKKDT---------LEPGKKVAEATKKVEEAEKKAKDQKEEDRRNYPTNTYKTL-ELE----- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1118 leeeleaerTARAKVEKLRSDLSRELEEISE-RLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKH 1196
Cdd:NF033838 178 ---------IAESDVEVKKAELELVKEEAKEpRDEEKIKQAKAKVESKKAEATRLEKIKTDREKAEEEAKRRADAKLKEA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1197 ADSVAELSEQIDNLQRVKQKLEKE-----KSEFKLELDDVTSNMEQIIKAKANLEKMCRTLEDQMNEHRSKA----EETQ 1267
Cdd:NF033838 249 VEKNVATSEQDKPKRRAKRGVLGEpatpdKKENDAKSSDSSVGEETLPSPSLKPEKKVAEAEKKVEEAKKKAkdqkEEDR 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1268 RsvNDLTSQRAKLQTENGELSRQLDEKEA-LISQLTRGKltytqQLEDLKRQLEEEVKAKNALAHALQSARHDcdllREQ 1346
Cdd:NF033838 329 R--NYPTNTYKTLELEIAESDVKVKEAELeLVKEEAKEP-----RNEEKIKQAKAKVESKKAEATRLEKIKTD----RKK 397
|
410
....*....|..
gi 1387193866 1347 YEEETEAKAELQ 1358
Cdd:NF033838 398 AEEEAKRKAAEE 409
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1024-1573 |
6.22e-04 |
|
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: 44.73 E-value: 6.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1024 KVKLEQHVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDfelNALNARIEDEQALGSQ 1103
Cdd:pfam05557 8 KARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAE---EALREQAELNRLKKKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1104 LQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSvQIEMNKKREAEFQKMRRDLEEAtl 1183
Cdd:pfam05557 85 LEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQE-RLDLLKAKASEAEQLRQNLEKQ-- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1184 QHEATAAALRKKhadsvaELSEQIDNLQRVKQKLEKEKSEFkLELDDVTSNMEQIIKAKANLEKMCRT---LEDQMNEHR 1260
Cdd:pfam05557 162 QSSLAEAEQRIK------ELEFEIQSQEQDSEIVKNSKSEL-ARIPELEKELERLREHNKHLNENIENkllLKEEVEDLK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1261 SKAEETQRSVNDLtsqrAKLQTENGELSRQLDEKEAL-----------------ISQLTRGKLTYTQQLEDLKRQLEEEV 1323
Cdd:pfam05557 235 RKLEREEKYREEA----ATLELEKEKLEQELQSWVKLaqdtglnlrspedlsrrIEQLQQREIVLKEENSSLTSSARQLE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1324 KAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEelEEAKKKLAQRLQDAEEA 1403
Cdd:pfam05557 311 KARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILESYDKELTM--SNYSPQLLERIEEAEDM 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1404 VEAVNAKCSSLEktkHRLQNEIEDLMVDVERSNAAAAALDKKQRNfdkilaewkqkyeesqseleSSQKEARSLSTELFK 1483
Cdd:pfam05557 389 TQKMQAHNEEME---AQLSVAEEELGGYKQQAQTLERELQALRQQ--------------------ESLADPSYSKEEVDS 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1484 LKNAYEESLEHLETFKRENKNLQEEISDLTEQLG---SSGKTIH---------------ELEKVRKQLEAEKLELQSALE 1545
Cdd:pfam05557 446 LRRKLETLELERQRLREQKNELEMELERRCLQGDydpKKTKVLHlsmnpaaeayqqrknQLEKLQAEIERLKRLLKKLED 525
|
570 580
....*....|....*....|....*...
gi 1387193866 1546 EAEASLEHEEGKILRAQLEFNQIKAEME 1573
Cdd:pfam05557 526 DLEQVLRLPETTSTMNFKEVLDLRKELE 553
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
849-1321 |
6.36e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 44.79 E-value: 6.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 849 IALMKEEFGRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQliknkiqleakvkemTERLED 928
Cdd:PRK10246 428 LVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADVKTICEQ---------------EARIKD 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 929 EEEMNAELTAKK----------------RKLEDECSELKRdiDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKL 992
Cdd:PRK10246 493 LEAQRAQLQAGQpcplcgstshpaveayQALEPGVNQSRL--DALEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSL 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 993 TKEKKALQEAHQQALDDL---QAEEDKVNTLTKAKVKLEQHVDDLEGSLEQEKKVRmDLERAKRKLEGDLKLTQESimdL 1069
Cdd:PRK10246 571 RQEEQALTQQWQAVCASLnitLQPQDDIQPWLDAQEEHERQLRLLSQRHELQGQIA-AHNQQIIQYQQQIEQRQQQ---L 646
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1070 ENDKQQLDERLKKKDFELNALNARiEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISER 1149
Cdd:PRK10246 647 LTALAGYALTLPQEDEEASWLATR-QQEAQSWQQRQNELTALQNRIQQLTPLLETLPQSDDLPHSEETVALDNWRQVHEQ 725
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1150 leeaggATSVQIEMNKKREAEFQKMRRdLEEATLQHEATAAALRkkHADSVAELS-----EQIDNLQRVKQKLEKeksef 1224
Cdd:PRK10246 726 ------CLSLHSQLQTLQQQDVLEAQR-LQKAQAQFDTALQASV--FDDQQAFLAalldeETLTQLEQLKQNLEN----- 791
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1225 klelddvtsnmeQIIKAKANLEKMCRTLEDQMN------EHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALI 1298
Cdd:PRK10246 792 ------------QRQQAQTLVTQTAQALAQHQQhrpdglDLTVTVEQIQQELAQLAQQLRENTTRQGEIRQQLKQDADNR 859
|
490 500
....*....|....*....|...
gi 1387193866 1299 SQLtrgkLTYTQQLEDLKRQLEE 1321
Cdd:PRK10246 860 QQQ----QALMQQIAQATQQVED 878
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1049-1850 |
6.57e-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: 44.94 E-value: 6.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1049 ERAKRKLEGDLKLTQEsimdLENDKQQLDE---RLKKKDFELNALNARIED-EQALGS------------QLQKKLKELQ 1112
Cdd:COG3096 278 NERRELSERALELRRE----LFGARRQLAEeqyRLVEMARELEELSARESDlEQDYQAasdhlnlvqtalRQQEKIERYQ 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1113 ARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEA-GGATSVQ--IEMNKKREAEFQKMRRDLEEATLQHEA-- 1187
Cdd:COG3096 354 EDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLkSQLADYQqaLDVQQTRAIQYQQAVQALEKARALCGLpd 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1188 -TAAALRKKHADSVAELSEQIDNLQRVKQKlekeksefkleLDDVTSNMEQIIKAKANLEKMCRTLEdqmnehRSKAEET 1266
Cdd:COG3096 434 lTPENAEDYLAAFRAKEQQATEEVLELEQK-----------LSVADAARRQFEKAYELVCKIAGEVE------RSQAWQT 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1267 QRSV-NDLTSQRAKLQTENGeLSRQLDEKEALISQLTRGKltytQQLEDLKRQLEEEVKAKNALAHALQSARHDCDLLRE 1345
Cdd:COG3096 497 ARELlRRYRSQQALAQRLQQ-LRAQLAELEQRLRQQQNAE----RLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEE 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1346 QYEEETEAKAELQRVLSKANSEVAQ-------WRT---KYETDAIQRTEELEEAKKKLAQRLQDAEEAVEAVNAKcSSLE 1415
Cdd:COG3096 572 QAAEAVEQRSELRQQLEQLRARIKElaarapaWLAaqdALERLREQSGEALADSQEVTAAMQQLLEREREATVER-DELA 650
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1416 KTKHRLQNEIEDLmvdversNAAAAALDKKQRNfdkiLAEwkqkyeesqselessqKEARSLSTELFK---LKNA-YEES 1491
Cdd:COG3096 651 ARKQALESQIERL-------SQPGGAEDPRLLA----LAE----------------RLGGVLLSEIYDdvtLEDApYFSA 703
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1492 L----------EHLETFKRENKNLQEEISDL-----TEQLGS-SGKTIHELEK---VR---------------------- 1530
Cdd:COG3096 704 LygparhaivvPDLSAVKEQLAGLEDCPEDLyliegDPDSFDdSVFDAEELEDavvVKlsdrqwrysrfpevplfgraar 783
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1531 -KQLEAEKLELQsALEEAEASLEHEEGKILRAQLEFNQIKAEMERKLAEKDEEME-QAKRNHLRVVDSLQTSLDAETRSR 1608
Cdd:COG3096 784 eKRLEELRAERD-ELAEQYAKASFDVQKLQRLHQAFSQFVGGHLAVAFAPDPEAElAALRQRRSELERELAQHRAQEQQL 862
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1609 NEALRVKKKMEGDLNEMeiqLSHANRLAAEaqkqvkSLQSLLKDTQIQLDDAVRANDDLKEN---IAIVERRNNLLQ--- 1682
Cdd:COG3096 863 RQQLDQLKEQLQLLNKL---LPQANLLADE------TLADRLEELREELDAAQEAQAFIQQHgkaLAQLEPLVAVLQsdp 933
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1683 AELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMEADLS-QLQTEVEEAVQECRNAEEKAKKA--- 1758
Cdd:COG3096 934 EQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHFSYEDAVGLLGENSDLNeKLRARLEQAEEARREAREQLRQAqaq 1013
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1759 ITDAAMMAEELKKEQDTSAhleRMKKNMEQTIKDLQHRLD-EAEQIAlkggkkqlqklEARVRELENELEAEQKRNAESV 1837
Cdd:COG3096 1014 YSQYNQVLASLKSSRDAKQ---QTLQELEQELEELGVQADaEAEERA-----------RIRRDELHEELSQNRSRRSQLE 1079
|
890
....*....|...
gi 1387193866 1838 KGMRKSERRIKEL 1850
Cdd:COG3096 1080 KQLTRCEAEMDSL 1092
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1312-1887 |
8.32e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.51 E-value: 8.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1312 LEDLKRQLEEEVKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYE--TDAIQRTEELEEA 1389
Cdd:PRK01156 171 LKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNnlKSALNELSSLEDM 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1390 KKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLqNEIEDLMVDVERSNAAAAALDKKQ-RNFDKILAEWK---QKYeesqs 1465
Cdd:PRK01156 251 KNRYESEIKTAESDLSMELEKNNYYKELEERH-MKIINDPVYKNRNYINDYFKYKNDiENKKQILSNIDaeiNKY----- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1466 elessqKEARSLSTELFKLKNAYEESlehletfKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKLELQSALE 1545
Cdd:PRK01156 325 ------HAIIKKLSVLQKDYNDYIKK-------KSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSA 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1546 EAEASLEHEEGKilraQLEFNQIKAEMERKLAEKDEEmeqakrnhlrvVDSLQTSLDAETRSRNEALRVKKKMEG----- 1620
Cdd:PRK01156 392 FISEILKIQEID----PDAIKKELNEINVKLQDISSK-----------VSSLNQRIRALRENLDELSRNMEMLNGqsvcp 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1621 ----DLNEMEIqlshaNRLAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKEniaiveRRNNLLQAELEELRAVVEQTE 1696
Cdd:PRK01156 457 vcgtTLGEEKS-----NHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKK------RKEYLESEEINKSINEYNKIE 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1697 RSRklAEQELIETSE-RVQLLHSQNTSLINQKKKME-ADLSQLQTEVEEA--------VQECRNAEEKAKKAITDAAMMA 1766
Cdd:PRK01156 526 SAR--ADLEDIKIKInELKDKHDKYEEIKNRYKSLKlEDLDSKRTSWLNAlavislidIETNRSRSNEIKKQLNDLESRL 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1767 EELKKE-QDTSAHLERMKKNMEQTIKDLQHRLDEAEqiALKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSER 1845
Cdd:PRK01156 604 QEIEIGfPDDKSYIDKSIREIENEANNLNNKYNEIQ--ENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIED 681
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1387193866 1846 RIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEE 1887
Cdd:PRK01156 682 NLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINE 723
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
898-1013 |
8.50e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 8.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 898 LADAEERCDQLIKN----------KIQLEAK--VKEMTERLEDE-EEMNAELTAKKRKLEDECSELKRDIDDLELTLAKV 964
Cdd:PRK12704 33 IKEAEEEAKRILEEakkeaeaikkEALLEAKeeIHKLRNEFEKElRERRNELQKLEKRLLQKEENLDRKLELLEKREEEL 112
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1387193866 965 EKEKHATENKVKNLTEEMAGLDEIIAK----------LTKEkkalqEAHQQALDDLQAE 1013
Cdd:PRK12704 113 EKKEKELEQKQQELEKKEEELEELIEEqlqelerisgLTAE-----EAKEILLEKVEEE 166
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
849-1173 |
9.41e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 9.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 849 IALMKEEFGRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMTERLED 928
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 929 EEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAH-QQAL 1007
Cdd:COG4372 106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEaEQAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1008 DDLQAEEDKVNTLTKAKVKLEQHVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFEL 1087
Cdd:COG4372 186 DELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELEL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1088 NALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKR 1167
Cdd:COG4372 266 AILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQL 345
|
....*.
gi 1387193866 1168 EAEFQK 1173
Cdd:COG4372 346 LLVGLL 351
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
855-1321 |
1.01e-03 |
|
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: 43.96 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 855 EFGRLKEALEKSEARRKELEEKMVSLLQEkndLQLQVQ-------------------AEQDNLADAEERCDQLIKNKIQL 915
Cdd:pfam05557 150 EAEQLRQNLEKQQSSLAEAEQRIKELEFE---IQSQEQdseivknskselaripeleKELERLREHNKHLNENIENKLLL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 916 EAKVKEMTERLEDEEEMNAELTA---KKRKLEDECSELKRDIDDLELTLAKVEkekhATENKVKNLTEEMAGLDEIIAKL 992
Cdd:pfam05557 227 KEEVEDLKRKLEREEKYREEAATlelEKEKLEQELQSWVKLAQDTGLNLRSPE----DLSRRIEQLQQREIVLKEENSSL 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 993 TKEKKALQEAHQQalddlqaeedkvntltkakvkLEQHVDDLEGSLEQEKKVRMDLERAKRKLegdlkltQESIMDLEND 1072
Cdd:pfam05557 303 TSSARQLEKARRE---------------------LEQELAQYLKKIEDLNKKLKRHKALVRRL-------QRRVLLLTKE 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1073 KQQLDERLKKKDFELNALNAriedeqalGSQLQKKLKELqarieeleeeleaertarakvEKLRSDLSRELEEISERLEE 1152
Cdd:pfam05557 355 RDGYRAILESYDKELTMSNY--------SPQLLERIEEA---------------------EDMTQKMQAHNEEMEAQLSV 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1153 AGGATSVQIEMNKKREAEFQKMRRDleeatlqheaTAAALRKKHADSVAELSEQIDNLQRVKQKLEKEKSEFKLELddvt 1232
Cdd:pfam05557 406 AEEELGGYKQQAQTLERELQALRQQ----------ESLADPSYSKEEVDSLRRKLETLELERQRLREQKNELEMEL---- 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1233 snMEQIIKAKANLEKmCRTLEDQMNehrSKAEETQRSVNDLTsqraKLQTENGELSRQL----DEKEALISQLTRGKLTY 1308
Cdd:pfam05557 472 --ERRCLQGDYDPKK-TKVLHLSMN---PAAEAYQQRKNQLE----KLQAEIERLKRLLkkleDDLEQVLRLPETTSTMN 541
|
490
....*....|...
gi 1387193866 1309 TQQLEDLKRQLEE 1321
Cdd:pfam05557 542 FKEVLDLRKELES 554
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1562-1836 |
1.03e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 44.27 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1562 QLEFNQIKAEMERklAEKDEEMEQAKrnhlrVVDSLQTSLDAetrsrnealrvkkkmegdLNEMEIQLSHANrlaaEAQK 1641
Cdd:PRK10929 22 APDEKQITQELEQ--AKAAKTPAQAE-----IVEALQSALNW------------------LEERKGSLERAK----QYQQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1642 QVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAE---LEELRAVVEQTERSRKLAE-------------QE 1705
Cdd:PRK10929 73 VIDNFPKLSAELRQQLNNERDEPRSVPPNMSTDALEQEILQVSsqlLEKSRQAQQEQDRAREISDslsqlpqqqtearRQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1706 LIETSERVQLLHSQNTSLinqkkkMEADLSQLQteveeavqecrnAEEKAKKAITDaammaeELKkeqdtsahLERMKKN 1785
Cdd:PRK10929 153 LNEIERRLQTLGTPNTPL------AQAQLTALQ------------AESAALKALVD------ELE--------LAQLSAN 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1387193866 1786 MEQTIKDLQHRLdeaeqialkgGKKQLQKLEARVRELENELEAEQKRNAES 1836
Cdd:PRK10929 201 NRQELARLRSEL----------AKKRSQQLDAYLQALRNQLNSQRQREAER 241
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1489-1628 |
1.03e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.08 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1489 EESLEHLeTFKRENKNLQEEISDLTEQ---LGSSGKTIHELEKVRKQLEAEKLELQSALEEAEASLEHEEGKILRAQLEf 1565
Cdd:COG2433 379 EEALEEL-IEKELPEEEPEAEREKEHEereLTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSE- 456
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387193866 1566 nqikaemERKLAEKDEEMEQAKrnhlRVVDSLQTSLDaETRSRNEALRVKKKMEGDLNEMEIQ 1628
Cdd:COG2433 457 -------ERREIRKDREISRLD----REIERLERELE-EERERIEELKRKLERLKELWKLEHS 507
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1253-1447 |
1.03e-03 |
|
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: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1253 EDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVKAKNALAHA 1332
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1333 LQSARHDCDLLrEQYEEETEAKAELQRV-----LSKANSEVAQwrtkyetDAIQRTEELEEAKKKLAQRLQDAEEAVEAV 1407
Cdd:COG3883 95 LYRSGGSVSYL-DVLLGSESFSDFLDRLsalskIADADADLLE-------ELKADKAELEAKKAELEAKLAELEALKAEL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1387193866 1408 NAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQR 1447
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1275-1795 |
1.13e-03 |
|
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: 44.17 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1275 SQRAKLQTENGELSRQLDEKEALI--SQLTRGKLTYTQQLEDLKRQLEEEvkAKNALAHALQSARHDCDLLREQyeeETE 1352
Cdd:COG3096 215 SLRDYLLPENSGVRKAFQDMEAALreNRMTLEAIRVTQSDRDLFKHLITE--ATNYVAADYMRHANERRELSER---ALE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1353 AKAELQRVLSKANSEvaQWRTKYETDAIqrtEELEEAKKKLAQRLQDAEEAVEAVnakcssleKTKHRLQNEIEDLMVDV 1432
Cdd:COG3096 290 LRRELFGARRQLAEE--QYRLVEMAREL---EELSARESDLEQDYQAASDHLNLV--------QTALRQQEKIERYQEDL 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1433 ErsnAAAAALDKKQrnfdKILAEWKQKYEESQSELESSQKEARSLSTELFKlknaYEESLEHLETfkrenKNLQEEisdl 1512
Cdd:COG3096 357 E---ELTERLEEQE----EVVEEAAEQLAEAEARLEAAEEEVDSLKSQLAD----YQQALDVQQT-----RAIQYQ---- 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1513 teqlgssgKTIHELEKVRKQLEAEKLELQSALEEAEASLEHEEgkilraqlEFNQIKAEMERKLAEKDEemeqAKRNHLR 1592
Cdd:COG3096 417 --------QAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQ--------QATEEVLELEQKLSVADA----ARRQFEK 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1593 VVDSLQTSLDAETRSR-----NEALRV---KKKMEGDLNEMEIQLSHANRLAAEAQKQVKSLQSLLKDTQIQLDDAvran 1664
Cdd:COG3096 477 AYELVCKIAGEVERSQawqtaRELLRRyrsQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAA---- 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1665 DDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHsqntslinqkkKMEADLSQLQTEVEEA 1744
Cdd:COG3096 553 EELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWL-----------AAQDALERLREQSGEA 621
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1387193866 1745 VQECRnaeekakkAITDAamMAEELKKEQDTSA---HLERMKKNMEQTIKDLQH 1795
Cdd:COG3096 622 LADSQ--------EVTAA--MQQLLEREREATVerdELAARKQALESQIERLSQ 665
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
840-1810 |
1.13e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 44.05 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 840 LKSAET--EKEIALMKEEFGRL-KEALEKSEARRKELEEKMVSLLQEKNDLQLQVqAEQDNLADAEERCDQLIK------ 910
Cdd:NF041483 296 LASAESanEQRTRTAKEEIARLvGEATKEAEALKAEAEQALADARAEAEKLVAEA-AEKARTVAAEDTAAQLAKaartae 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 911 ---NKIQLEAK-----VKEMTERLEDEEEMNAE-LTAKKRKLEDECS-ELKRDIDDLELTLAKVEKEKHATENKVKNLTE 980
Cdd:NF041483 375 evlTKASEDAKattraAAEEAERIRREAEAEADrLRGEAADQAEQLKgAAKDDTKEYRAKTVELQEEARRLRGEAEQLRA 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 981 EMAGLDEIIakltkEKKALQEAHQQALDDLQAEEDkvnTLTKAKVKleqhVDDLEGSLEQE-KKVRMD-LERA---KRKL 1055
Cdd:NF041483 455 EAVAEGERI-----RGEARREAVQQIEEAARTAEE---LLTKAKAD----ADELRSTATAEsERVRTEaIERAttlRRQA 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1056 EGDLKLTQESIMDLENDKQQLDERLKKkDFELNALNARIEDEQALGSQLQKKLKELqARIEELEEE-----LEAERTARA 1130
Cdd:NF041483 523 EETLERTRAEAERLRAEAEEQAEEVRA-AAERAARELREETERAIAARQAEAAEEL-TRLHTEAEErltaaEEALADARA 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1131 KVEKLRSDLSRELEEIseRLEEAGGATSVQiemnKKREAEFQKMRR----DLEEATLQHEATAAALRKKHADSVAEL-SE 1205
Cdd:NF041483 601 EAERIRREAAEETERL--RTEAAERIRTLQ----AQAEQEAERLRTeaaaDASAARAEGENVAVRLRSEAAAEAERLkSE 674
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1206 QIDNLQRVK-------QKLEKEKSEfkleldDVTSNMEQIIKAKANLEKMCRTLEDQMNEHRSKAEEtqRSVNDLTSQRA 1278
Cdd:NF041483 675 AQESADRVRaeaaaaaERVGTEAAE------ALAAAQEEAARRRREAEETLGSARAEADQERERARE--QSEELLASARK 746
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1279 KLQTENGELSRQLDEKEALISQLTRGKLTYTQQLED----LKRQLEEEVKA-KNALAHALQSARhdcdllreqyeeeTEA 1353
Cdd:NF041483 747 RVEEAQAEAQRLVEEADRRATELVSAAEQTAQQVRDsvagLQEQAEEEIAGlRSAAEHAAERTR-------------TEA 813
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1354 KAELQRVLSKANSEvaqwRTKYETDAI---QRTEELEEAKKKLAQR-LQDAEEAVEAVNAKCSSLEKtkhRLQNEIEDLM 1429
Cdd:NF041483 814 QEEADRVRSDAYAE----RERASEDANrlrREAQEETEAAKALAERtVSEAIAEAERLRSDASEYAQ---RVRTEASDTL 886
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1430 VDVERSNAAAAALDKKQRNfdKILAEwkqkyeeSQSELESSQKEARSLSTELFKLKNAYEESLehLETFKRENKNLQEEI 1509
Cdd:NF041483 887 ASAEQDAARTRADAREDAN--RIRSD-------AAAQADRLIGEATSEAERLTAEARAEAERL--RDEARAEAERVRADA 955
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1510 SDLTEQLGSsgKTIHELEKVRK---------QLEAEKLELQSALEEAEASLEHEEgkiLRAQlefnqIKAEMERKLAEKD 1580
Cdd:NF041483 956 AAQAEQLIA--EATGEAERLRAeaaetvgsaQQHAERIRTEAERVKAEAAAEAER---LRTE-----AREEADRTLDEAR 1025
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1581 EEMEQAKRNHLRVVDSLQTSLDAE-----TRSRNEALRVKKKMEGDLNEM-EIQLSHANRLAAEAQKQVKSLQSLLKDTQ 1654
Cdd:NF041483 1026 KDANKRRSEAAEQADTLITEAAAEadqltAKAQEEALRTTTEAEAQADTMvGAARKEAERIVAEATVEGNSLVEKARTDA 1105
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1655 IQLDDAVRanddlKENIAIVERRNNL---LQAELEEL--RAVVEQTERSR----------KLAEQELIETSERVQLLHSQ 1719
Cdd:NF041483 1106 DELLVGAR-----RDATAIRERAEELrdrITGEIEELheRARRESAEQMKsagercdalvKAAEEQLAEAEAKAKELVSD 1180
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1720 NTS-----LINQKKKMEADLSQLQTEVEEAVQEcrnAEEKAKKAITDAAMMAEELKKEQDTsahLERMKKNMEQTIKDLQ 1794
Cdd:NF041483 1181 ANSeaskvRIAAVKKAEGLLKEAEQKKAELVRE---AEKIKAEAEAEAKRTVEEGKRELDV---LVRRREDINAEISRVQ 1254
|
1050
....*....|....*.
gi 1387193866 1795 HRLDEAEQIALKGGKK 1810
Cdd:NF041483 1255 DVLEALESFEAPSGGG 1270
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1766-1917 |
1.24e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.69 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1766 AEELKKEQDTSAHLERMKKNMEQTIKDLQhrldeaeqialkggkKQLQKLEARVRELENELEAEQKRNAES---VKGMRK 1842
Cdd:COG2433 391 PEEEPEAEREKEHEERELTEEEEEIRRLE---------------EQVERLEAEVEELEAELEEKDERIERLereLSEARS 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1843 SERR-------IKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRqAEEAEEQANT----NLSKFRKvqHELDEAEERAD 1911
Cdd:COG2433 456 EERReirkdreISRLDREIERLERELEEERERIEELKRKLERLKE-LWKLEHSGELvpvkVVEKFTK--EAIRRLEEEYG 532
|
....*.
gi 1387193866 1912 IAESQV 1917
Cdd:COG2433 533 LKEGDV 538
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
1682-1923 |
1.49e-03 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 43.77 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1682 QAELEELRAVVEQTERSRKLAE-QELietseRVQLLHSQNTSLINQKKK---------MEADLSQLQTEVEEAVQECrnA 1751
Cdd:PLN03188 973 QDELEHYRNFYDMGEREVLLEEiQDL-----RSQLQYYIDSSLPSARKRnsllkltysCEPSQAPPLNTIPESTDES--P 1045
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1752 EEKAKK-------AITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQK---------- 1814
Cdd:PLN03188 1046 EKKLEQerlrwteAESKWISLAEELRTELDASRALAEKQKHELDTEKRCAEELKEAMQMAMEGHARMLEQyadleekhiq 1125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1815 LEARVRELENELEAEQKrnAESVKGMRKSERR--------IKELTYQTEEDRKnllRLQDLVDKLQLKVkaykRQAEEAE 1886
Cdd:PLN03188 1126 LLARHRRIQEGIDDVKK--AAARAGVRGAESKfinalaaeISALKVEREKERR---YLRDENKSLQAQL----RDTAEAV 1196
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1387193866 1887 EQANTNLSKFRKVQHELDEAEERADIAE-------SQVNKLRAK 1923
Cdd:PLN03188 1197 QAAGELLVRLKEAEEALTVAQKRAMDAEqeaaeayKQIDKLKRK 1240
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1628-1833 |
1.52e-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: 42.32 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1628 QLSHANRLAAEAQKQVKSLQSLLKDTQIQLDdavRANDDLKENiaiverrnnllQAELEELRAVVEQTERSRKLAEQELI 1707
Cdd:pfam00261 23 KLEEAEKRAEKAEAEVAALNRRIQLLEEELE---RTEERLAEA-----------LEKLEEAEKAADESERGRKVLENRAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1708 ETSERVQLLHSQNTSLINQKKKMEADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLE------- 1780
Cdd:pfam00261 89 KDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSLEaseekas 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1387193866 1781 RMKKNMEQTIKDLQHRLDEAEQIALKGgKKQLQKLEARVRELENELEAEQKRN 1833
Cdd:pfam00261 169 EREDKYEEQIRFLTEKLKEAETRAEFA-ERSVQKLEKEVDRLEDELEAEKEKY 220
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
843-998 |
1.71e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 843 AETEKEIALMKEEfgRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLadaEERCDQLIKNKIQLEAKVKEM 922
Cdd:PRK12704 45 EEAKKEAEAIKKE--ALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENL---DRKLELLEKREEELEKKEKEL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 923 TERLEDEEEMNAELTAKKRKLEDE---CSELKRDiDDLELTLAKVEKE-KHATENKVKNLTEEmagldeiiAKLTKEKKA 998
Cdd:PRK12704 120 EQKQQELEKKEEELEELIEEQLQElerISGLTAE-EAKEILLEKVEEEaRHEAAVLIKEIEEE--------AKEEADKKA 190
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1605-1861 |
1.81e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 42.49 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1605 TRSRNEALRVKKKMEGDLNEM------EIQLSHANRLAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRN 1678
Cdd:pfam15905 52 TARKVKSLELKKKSQKNLKESkdqkelEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1679 NLLQAELEELRAVVEQTERSRKLA--EQELIETSERvqlLHSQNTSLINQKKKMEADLSQLQTEVEEAVQECRNAEEKAK 1756
Cdd:pfam15905 132 LELTRVNELLKAKFSEDGTQKKMSslSMELMKLRNK---LEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLV 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1757 -----------------KAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIAlkggKKQLQKLEARV 1819
Cdd:pfam15905 209 stekekieeksetekllEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQEL----SKQIKDLNEKC 284
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1387193866 1820 RELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKNL 1861
Cdd:pfam15905 285 KLLESEKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKL 326
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
863-1075 |
2.03e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 863 LEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEErcdqliknkiQLEAKVKEMTERLEDEEEMNAELTAKKRK 942
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQA----------ELEALQAEIDKLQAEIAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 943 LEDECSELKR---DIDDLELTLAkvekekhATE-----NKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEE 1014
Cdd:COG3883 88 LGERARALYRsggSVSYLDVLLG-------SESfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387193866 1015 DKVNTLTKAKVKLEQHVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQ 1075
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| PRK15374 |
PRK15374 |
type III secretion system needle tip complex protein SipB; |
914-1115 |
2.16e-03 |
|
type III secretion system needle tip complex protein SipB;
Pssm-ID: 185272 [Multi-domain] Cd Length: 593 Bit Score: 43.03 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 914 QLEAKVKEMTERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLT 993
Cdd:PRK15374 103 QLESRLAVWQAMIESQKEMGIQVSKEFQTALGEAQEATDLYEASIKKTDTAKSVYDAAEKKLTQAQNKLQSLDPADPGYA 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 994 KEKKALQEAHQQALDDLQAEEDK----VNTLTKAKVKLEQhVDDLEGSLEQEKKVRMDLERAK---RKLEGDLKLTQESI 1066
Cdd:PRK15374 183 QAEAAVEQAGKEATEAKEALDKAtdatVKAGTDAKAKAEK-ADNILTKFQGTANAASQNQVSQgeqDNLSNVARLTMLMA 261
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1387193866 1067 MDLENDKQQLDERLKKkdfELNALNARIEDEQAlgsQLQKKLKELQARI 1115
Cdd:PRK15374 262 MFIEIVGKNTEESLQN---DLALFNALQEGRQA---EMEKKSAEFQEET 304
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
960-1191 |
2.16e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 960 TLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQHVDDLEGSLE 1039
Cdd:COG3883 10 TPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1040 qekkvrmdlERAKRKLEG-------DLKLTQESIMDL-----------ENDKQQLDERLKKKDfELNALNARIEDEQAlg 1101
Cdd:COG3883 90 ---------ERARALYRSggsvsylDVLLGSESFSDFldrlsalskiaDADADLLEELKADKA-ELEAKKAELEAKLA-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1102 sQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEA 1181
Cdd:COG3883 158 -ELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
250
....*....|
gi 1387193866 1182 TLQHEATAAA 1191
Cdd:COG3883 237 AAAAAAAASA 246
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
835-1056 |
2.31e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 835 KIKPLLKSAETEKEIALMKEEFGRLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQ 914
Cdd:PRK02224 497 RLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAE 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 915 LEAKVKEMTERLEDEEEMnAELTAKKRKLEDECSELKRDIDDleltLAKVEKEKHATenkvknLTEEMAGLDEIIAKLTK 994
Cdd:PRK02224 577 LNSKLAELKERIESLERI-RTLLAAIADAEDEIERLREKREA----LAELNDERRER------LAEKRERKRELEAEFDE 645
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1387193866 995 EK-KALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQHVDDLEGSLEQEKKVRMDLERAKRKLE 1056
Cdd:PRK02224 646 ARiEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREALENRVE 708
|
|
| F-BAR_PSTPIP2 |
cd07672 |
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ... |
1232-1424 |
2.33e-03 |
|
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine Phosphatase-Interacting Protein 2; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Proline-Serine-Threonine Phosphatase-Interacting Protein 2 (PSTPIP2), also known as Macrophage Actin-associated tYrosine Phosphorylated protein (MAYP), is mostly expressed in hematopoietic cells but is also expressed in the brain. It is involved in regulating cell adhesion and motility. Mutations in the gene encoding murine PSTPIP2 can cause autoinflammatory disorders such as chronic multifocal osteomyelitis and macrophage autoinflammatory disease. PSTPIP2 contains an N-terminal F-BAR domain and lacks the PEST motifs and SH3 domain that are found in PSTPIP1. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.
Pssm-ID: 153356 [Multi-domain] Cd Length: 240 Bit Score: 41.86 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1232 TSNMEQIIKAKANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQ 1311
Cdd:cd07672 4 TGGYDCIIQHLNDGRKNCKEFEDFLKERASIEEKYGKELLNLSKKKPCGQTEINTLKRSLDVFKQQIDNVGQSHIQLAQT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1312 LEDLKRQLE---EEVKAKNALAHALQSARHDCDLLreQYEEETEAKAEL-QRVLSKANSEVAQWRTKYETDAIQRteelE 1387
Cdd:cd07672 84 LRDEAKKMEdfrERQKLARKKIELIMDAIHKQRAM--QFKKTMESKKNYeQKCRDKDEAEQAVNRNANLVNVKQQ----E 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 1387193866 1388 EAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNE 1424
Cdd:cd07672 158 KLFAKLAQSKQNAEDADRLYMQNISVLDKIREDWQKE 194
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1172-1388 |
2.36e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 43.12 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1172 QKMRRDLEEA-------------TLQHEATAAALRKKHADSVAELSEQIDNLQRVKQKLEKEKSEFKLELDDVTSNM--- 1235
Cdd:PRK10929 26 KQITQELEQAkaaktpaqaeiveALQSALNWLEERKGSLERAKQYQQVIDNFPKLSAELRQQLNNERDEPRSVPPNMstd 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1236 ---EQIIKAKANLEKMCRtledQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQL 1312
Cdd:PRK10929 106 aleQEILQVSSQLLEKSR----QAQQEQDRAREISDSLSQLPQQQTEARRQLNEIERRLQTLGTPNTPLAQAQLTALQAE 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387193866 1313 EDLKRQLEEEVKAKNALAHALQS-ARHDCDLLREQYEeetEAKAELQRVLSKANSEvaqwRTKYETDAIQRTEELEE 1388
Cdd:PRK10929 182 SAALKALVDELELAQLSANNRQElARLRSELAKKRSQ---QLDAYLQALRNQLNSQ----RQREAERALESTELLAE 251
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1571-1886 |
2.38e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 42.55 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1571 EMERKLAEKDEEMEQAKRNHLRVVDSLQTsldAETRSRNEALRVKKKMEGDLNEMEIQLSHANRLAAEAQKQVKSLQsll 1650
Cdd:pfam02029 10 ERRRRAREERRRQKEEEEPSGQVTESVEP---NEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQKRLQEAL--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1651 kDTQIQLDDAvraNDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHsQNTSLINQKKKM 1730
Cdd:pfam02029 84 -ERQKEFDPT---IADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWS-TEVRQAEEEGEE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1731 EADLSQLQTEVE------EAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDL----QHRLDEA 1800
Cdd:pfam02029 159 EEDKSEEAEEVPtenfakEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQgglsQSQEREE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1801 EQIALKGGKKQLQKLEARVRELENElEAEQKRNA--------ESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQ 1872
Cdd:pfam02029 239 EAEVFLEAEQKLEELRRRRQEKESE-EFEKLRQKqqeaelelEELKKKREERRKLLEEEEQRRKQEEAERKLREEEEKRR 317
|
330
....*....|....
gi 1387193866 1873 LKVKAYKRQAEEAE 1886
Cdd:pfam02029 318 MKEEIERRRAEAAE 331
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1254-1447 |
2.57e-03 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 42.90 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1254 DQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEkealISQlTRGKLTYTQQledlkrqleeevkakNALAHAL 1333
Cdd:NF012221 1545 DAVSKHAKQDDAAQNALADKERAEADRQRLEQEKQQQLAA----ISG-SQSQLESTDQ---------------NALETNG 1604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1334 QSARhdcDLLREQYEEETEAKAELQRVLSKANSEVA-------QWRTKYET---DAIQR---------TEELEEAKKKLA 1394
Cdd:NF012221 1605 QAQR---DAILEESRAVTKELTTLAQGLDALDSQATyagesgdQWRNPFAGgllDRVQEqlddakkisGKQLADAKQRHV 1681
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1387193866 1395 QRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNaaAAALDKKQR 1447
Cdd:NF012221 1682 DNQQKVKDAVAKSEAGVAQGEQNQANAEQDIDDAKADAEKRK--DDALAKQNE 1732
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
859-1034 |
2.71e-03 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 43.00 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 859 LKEALEKSEARRKELEEKMVSLLQEkndLQLQVQA------EQDNLADAEERCDQLIKNKIQLEAK-VKEMTERLEDEEE 931
Cdd:PLN03188 1045 PEKKLEQERLRWTEAESKWISLAEE---LRTELDAsralaeKQKHELDTEKRCAEELKEAMQMAMEgHARMLEQYADLEE 1121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 932 MNAELTAKKRKLEDECSELK-------------RDIDDL--ELTLAKVEKEKHAT----ENK-----VKNLTEEMAGLDE 987
Cdd:PLN03188 1122 KHIQLLARHRRIQEGIDDVKkaaaragvrgaesKFINALaaEISALKVEREKERRylrdENKslqaqLRDTAEAVQAAGE 1201
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1387193866 988 IIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQHVDDL 1034
Cdd:PLN03188 1202 LLVRLKEAEEALTVAQKRAMDAEQEAAEAYKQIDKLKRKHENEISTL 1248
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1165-1320 |
2.73e-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: 42.74 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1165 KKREAEFQKMRRDLEEATLQheATAAALRKKHADS-VAELSEQIDNLqrvkqkleKEKSEFKLElddvtsnmEQIIKAKA 1243
Cdd:pfam05911 20 EKAEAEALALKQQLESVTLQ--KLTAEERAAHLDGaLKECMQQLRNV--------KEEQEQKIH--------DVVLKKTK 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387193866 1244 NLEKMCRTLEDQMNEhrskaeetqrsvndlTSQR-AKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLE 1320
Cdd:pfam05911 82 EWEKIKAELEAKLVE---------------TEQElLRAAAENDALSRSLQERENLLMKLSEEKSQAEAEIEALKSRLE 144
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1642-1926 |
2.91e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 42.58 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1642 QVKSLQSLLKDTQ---IQLDDA-VRANDDLKEniaiVERRNNLLQAELEELRAVVEQTERSRKLAEQELIetseRVQLLH 1717
Cdd:PLN02939 129 QLEDLVGMIQNAEkniLLLNQArLQALEDLEK----ILTEKEALQGKINILEMRLSETDARIKLAAQEKI----HVEILE 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1718 SQntsLINQKKKMEADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTS---AHLERMKKNMEQTIKDLQ 1794
Cdd:PLN02939 201 EQ---LEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEervFKLEKERSLLDASLRELE 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1795 HRLDEAEQIALKGGKKQLQKLEARVRELENELEAEQKRNAESV---KGMRKSERRIKELTYQTEEDRKNLLRLQdLVDKL 1871
Cdd:PLN02939 278 SKFIVAQEDVSKLSPLQYDCWWEKVENLQDLLDRATNQVEKAAlvlDQNQDLRDKVDKLEASLKEANVSKFSSY-KVELL 356
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1387193866 1872 QLKVKAYKRQAEEAEEQANTnlskfrKVQHELDEAEERADIAESQVNKLRAKSRD 1926
Cdd:PLN02939 357 QQKLKLLEERLQASDHEIHS------YIQLYQESIKEFQDTLSKLKEESKKRSLE 405
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
845-1106 |
2.91e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 42.53 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 845 TEKEIAL-MKEEFGRLKEALEKSEARRK----ELEEKMVSLLQEKN------------DLQLQVQAEQDNLADAEERCDQ 907
Cdd:PLN03229 476 TEAVIAMgLQERLENLREEFSKANSQDQlmhpVLMEKIEKLKDEFNkrlsrapnylslKYKLDMLNEFSRAKALSEKKSK 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 908 LIKNKIQLEAKVKEMTERLEDEEEMNAeltakkRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMaGLDE 987
Cdd:PLN03229 556 AEKLKAEINKKFKEVMDRPEIKEKMEA------LKAEVASSGASSGDELDDDLKEKVEKMKKEIELELAGVLKSM-GLEV 628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 988 IIAKltkeKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQHVDDLEGSLEQEKkvrmdLERAKRKLEGDLKlTQESIM 1067
Cdd:PLN03229 629 IGVT----KKNKDTAEQTPPPNLQEKIESLNEEINKKIERVIRSSDLKSKIELLK-----LEVAKASKTPDVT-EKEKIE 698
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1387193866 1068 DLEND-KQQLDE-----RLKKKDFELNA-LNARIEDEQALGSQLQK 1106
Cdd:PLN03229 699 ALEQQiKQKIAEalnssELKEKFEELEAeLAAARETAAESNGSLKN 744
|
|
| PRK10361 |
PRK10361 |
DNA recombination protein RmuC; Provisional |
1762-1931 |
2.98e-03 |
|
DNA recombination protein RmuC; Provisional
Pssm-ID: 182409 [Multi-domain] Cd Length: 475 Bit Score: 42.28 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1762 AAMMAEELKKEQDTSAHLERMKKNMEQTikdlQHRLDEAEQI--ALKGGKKQLQKLEARVRELENELEAEQKRNAESVKG 1839
Cdd:PRK10361 28 AQQKAEQLAEREEMVAELSAAKQQITQS----EHWRAECELLnnEVRSLQSINTSLEADLREVTTRMEAAQQHADDKIRQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1840 MRKSERRIKE----LTYQTEE------DRKNLLRLQDLVDKLQLKVKAYKRQAEEA---EEQANTNLSkfrkvqHELDEA 1906
Cdd:PRK10361 104 MINSEQRLSEqfenLANRIFEhsnrrvDEQNRQSLNSLLSPLREQLDGFRRQVQDSfgkEAQERHTLA------HEIRNL 177
|
170 180
....*....|....*....|....*.
gi 1387193866 1907 EE-RADIAESQVNKLRAKSRDIGTKG 1931
Cdd:PRK10361 178 QQlNAQMAQEAINLTRALKGDNKTQG 203
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1128-1361 |
3.11e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.83 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1128 ARAKVEKLRSDLSRELEEISERLEEaggatsvqiEMNKKR--EAEFQKMRRDLEEATLQH---EATA-------AALRKK 1195
Cdd:pfam00038 69 ERARLQLELDNLRLAAEDFRQKYED---------ELNLRTsaENDLVGLRKDLDEATLARvdlEAKIeslkeelAFLKKN 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1196 HADSVAELSEQIDNLQRVkqklekeksefkLELDDVTS-NMEQIIK-AKANLEKMC-RTLEDQMNEHRSKAEETQRSVND 1272
Cdd:pfam00038 140 HEEEVRELQAQVSDTQVN------------VEMDAARKlDLTSALAeIRAQYEEIAaKNREEAEEWYQSKLEELQQAAAR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1273 LTSQRAKLQTENGELSRQLDEKEALISQLTRgkltytqQLEDLKRQLEEevkAKNALAHALQSARhdcDLLREQYEEETE 1352
Cdd:pfam00038 208 NGDALRSAKEEITELRRTIQSLEIELQSLKK-------QKASLERQLAE---TEERYELQLADYQ---ELISELEAELQE 274
|
....*....
gi 1387193866 1353 AKAELQRVL 1361
Cdd:pfam00038 275 TRQEMARQL 283
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1131-1856 |
3.11e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.51 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1131 KVEKLRSDLSRELEEISERLEEAGGATSVQIEmNKKREAEFQ--KMRRDLEEATLQHEATAAALRKKHADSVAEL----- 1203
Cdd:NF041483 44 QVEVLRAKLHEARRSLASRPAYDGADIGYQAE-QLLRNAQIQadQLRADAERELRDARAQTQRILQEHAEHQARLqaelh 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1204 SEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIikaKANLEKMCRTLedqMNEHRSKAE--------ETQRsVNDLTS 1275
Cdd:NF041483 123 TEAVQRRQQLDQELAERRQTVESHVNENVAWAEQL---RARTESQARRL---LDESRAEAEqalaaaraEAER-LAEEAR 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1276 QRAKLQTEN--GELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVKAKN--ALAHALQSARHDCDLLREQYEEET 1351
Cdd:NF041483 196 QRLGSEAESarAEAEAILRRARKDAERLLNAASTQAQEATDHAEQLRSSTAAESdqARRQAAELSRAAEQRMQEAEEALR 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1352 EAKAELQRVLSKANSEVAQWRTKYETDAIQRTeelEEAKKKLAQRLQDAEEAVEAVNAKCsslEKTKHRLQNEIEDLMVD 1431
Cdd:NF041483 276 EARAEAEKVVAEAKEAAAKQLASAESANEQRT---RTAKEEIARLVGEATKEAEALKAEA---EQALADARAEAEKLVAE 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1432 VE---RSNAA---AAALDKKQRNFDKILAEwkqkyeesqselesSQKEARSLStelfklKNAYEESLEHLETFKRENKNL 1505
Cdd:NF041483 350 AAekaRTVAAedtAAQLAKAARTAEEVLTK--------------ASEDAKATT------RAAAEEAERIRREAEAEADRL 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1506 QEEISDLTEQLGSSGKtiheleKVRKQLEAEKLELQSaleeaEASLEHEEGKILRAQL--EFNQIKAEMERKLAEKDEEM 1583
Cdd:NF041483 410 RGEAADQAEQLKGAAK------DDTKEYRAKTVELQE-----EARRLRGEAEQLRAEAvaEGERIRGEARREAVQQIEEA 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1584 EQAKRNHLRVV----DSLQTSLDAET-RSRNEALRVKKKMEGDLNE-MEIQLSHANRLAAEAQKQVKSLQSLLKDTQIQL 1657
Cdd:NF041483 479 ARTAEELLTKAkadaDELRSTATAESeRVRTEAIERATTLRRQAEEtLERTRAEAERLRAEAEEQAEEVRAAAERAAREL 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1658 -DDAVRANDDLKENIAIVERRnnlLQAELEELRAVVEQT--------ERSRKLAEQEL----IETSERVQLLHSQntsli 1724
Cdd:NF041483 559 rEETERAIAARQAEAAEELTR---LHTEAEERLTAAEEAladaraeaERIRREAAEETerlrTEAAERIRTLQAQ----- 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1725 nqkkkMEADLSQLQTE-VEEAVQECRNAEEKAKKAITDAAMMAEELKKE-QDTS--------AHLERMKKNMEQTIKDLQ 1794
Cdd:NF041483 631 -----AEQEAERLRTEaAADASAARAEGENVAVRLRSEAAAEAERLKSEaQESAdrvraeaaAAAERVGTEAAEALAAAQ 705
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1387193866 1795 H----RLDEAEQIaLKGGKKQLQKLEARVRELENELEAEQKR-----NAESVKGMRKSERRIKELTYQTEE 1856
Cdd:NF041483 706 EeaarRRREAEET-LGSARAEADQERERAREQSEELLASARKrveeaQAEAQRLVEEADRRATELVSAAEQ 775
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
911-1862 |
3.20e-03 |
|
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: 42.63 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 911 NKIQLEAkVKEmTERLEDE-----EEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAgl 985
Cdd:COG3096 241 NRMTLEA-IRV-TQSDRDLfkhliTEATNYVAADYMRHANERRELSERALELRRELFGARRQLAEEQYRLVEMARELE-- 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 986 deiiaKLTKEKKALQEAHQQALDDLQaeedKVNTLTKAKVKLEQHVDDLEG---SLEQEKKVRMDLERAKRKLEGDLKLT 1062
Cdd:COG3096 317 -----ELSARESDLEQDYQAASDHLN----LVQTALRQQEKIERYQEDLEElteRLEEQEEVVEEAAEQLAEAEARLEAA 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1063 QESIMDLEN---DKQQ-LDERLKKKDFELNALNARIEDEQALG------SQLQKKLKELQARieeLEEELEAERTARAKV 1132
Cdd:COG3096 388 EEEVDSLKSqlaDYQQaLDVQQTRAIQYQQAVQALEKARALCGlpdltpENAEDYLAAFRAK---EQQATEEVLELEQKL 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1133 EkLRSDLSRELEEISERLEEAGGATSvqiemnkkREAEFQKMRRDLEEA-TLQHEA-TAAALRKKHADSVAELSEQidnl 1210
Cdd:COG3096 465 S-VADAARRQFEKAYELVCKIAGEVE--------RSQAWQTARELLRRYrSQQALAqRLQQLRAQLAELEQRLRQQ---- 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1211 qrvkQKLEKEKSEFKLELDDVTSNMEQiikakanlekmcrtLEDQMNEHRSKAEETQRSVNDLTSQRAklqtengELSRQ 1290
Cdd:COG3096 532 ----QNAERLLEEFCQRIGQQLDAAEE--------------LEELLAELEAQLEELEEQAAEAVEQRS-------ELRQQ 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1291 LDEKEALISQLTRGK---LTYTQQLEDLKRQLEEEVKAKNALAHALQsarhdcdllrEQYEEETEAKAELQRVLskanse 1367
Cdd:COG3096 587 LEQLRARIKELAARApawLAAQDALERLREQSGEALADSQEVTAAMQ----------QLLEREREATVERDELA------ 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1368 vaqwrtkyetdaiQRTEELEEAKKKLAQ-------RLQDAEEAVEAVnakcsslektkhrLQNEI-EDLMVD-------- 1431
Cdd:COG3096 651 -------------ARKQALESQIERLSQpggaedpRLLALAERLGGV-------------LLSEIyDDVTLEdapyfsal 704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1432 ---------VERSNAAAAALDKK----------QRN---FDKILAEWKQkyEESQSELESSQKEAR-SLSTELFKLKNAY 1488
Cdd:COG3096 705 ygparhaivVPDLSAVKEQLAGLedcpedlyliEGDpdsFDDSVFDAEE--LEDAVVVKLSDRQWRySRFPEVPLFGRAA 782
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1489 EEslEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEK-VRKQL--------EAEKLELQSALEEAEASLEHEEGKIL 1559
Cdd:COG3096 783 RE--KRLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQfVGGHLavafapdpEAELAALRQRRSELERELAQHRAQEQ 860
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1560 RAQLEFNQIKAEME--RKLAE-----KDEEMEQakrnhlRVVDslqtsLDAETRSRNEALRVKKKMEGDLNEMEIQLShA 1632
Cdd:COG3096 861 QLRQQLDQLKEQLQllNKLLPqanllADETLAD------RLEE-----LREELDAAQEAQAFIQQHGKALAQLEPLVA-V 928
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1633 NRLAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLkeniaiVERRNNLLQAE----LEELRAVVEQTERSRKLAEQELIE 1708
Cdd:COG3096 929 LQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEV------VQRRPHFSYEDavglLGENSDLNEKLRARLEQAEEARRE 1002
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1709 TSERVQLLHSQNTSLiNQKkkmeadLSQLQTEVEEAVQECRNAEEKAK----KAITDAAMMAEELKKEQDTSAHLERMKK 1784
Cdd:COG3096 1003 AREQLRQAQAQYSQY-NQV------LASLKSSRDAKQQTLQELEQELEelgvQADAEAEERARIRRDELHEELSQNRSRR 1075
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1785 NmeQTIKDLQHRldEAEQIALkggKKQLQKLEARVRELENELEAEQKRNAESVKGMRKS--ERRI--KELTYQTEEDRKN 1860
Cdd:COG3096 1076 S--QLEKQLTRC--EAEMDSL---QKRLRKAERDYKQEREQVVQAKAGWCAVLRLARDNdvERRLhrRELAYLSADELRS 1148
|
..
gi 1387193866 1861 LL 1862
Cdd:COG3096 1149 MS 1150
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1681-1775 |
3.32e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.63 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1681 LQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMEADLSQLQTEVEEAVQEcrnaEEKAKKAIT 1760
Cdd:PRK11448 147 LQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQE----RKQKRKEIT 222
|
90
....*....|....*
gi 1387193866 1761 DAAMMAEELkKEQDT 1775
Cdd:PRK11448 223 DQAAKRLEL-SEEET 236
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1433-1826 |
3.49e-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: 42.36 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1433 ERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFK--LKNAYEESLEHLETFKRENKNLQEEIS 1510
Cdd:pfam13166 89 EESIEIQEKIAKLKKEIKDHEEKLDAAEANLQKLDKEKEKLEADFLDECWKkiKRKKNSALSEALNGFKYEANFKSRLLR 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1511 DLteqlgssgktihelekVRKQLEAEKLELQSALEEAEASLEhEEGKILRAQLEFNQIkaemERKLAEKDEEMEQAKRNH 1590
Cdd:pfam13166 169 EI----------------EKDNFNAGVLLSDEDRKAALATVF-SDNKPEIAPLTFNVI----DFDALEKAEILIQKVIGK 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1591 LRVVDSLQTSLDAETRSRnEALRVKKKMEGD--LNEMEIQLSHANRLAA----EAQKQVKSLQSLLKD---------TQI 1655
Cdd:pfam13166 228 SSAIEELIKNPDLADWVE-QGLELHKAHLDTcpFCGQPLPAERKAALEAhfddEFTEFQNRLQKLIEKvesaissllAQL 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1656 Q-LDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQterSRKlaeqeliETSERVQLlhsqnTSLINQKKKMEADL 1734
Cdd:pfam13166 307 PaVSDLASLLSAFELDVEDIESEAEVLNSQLDGLRRALEA---KRK-------DPFKSIEL-----DSVDAKIESINDLV 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1735 SQLQTEVEEAVQECRNAEEKAKKAITD-AAMMAEELKKEQDTsahLERMKKNMEQTIKDLQHRLDEAEqialkggkKQLQ 1813
Cdd:pfam13166 372 ASINELIAKHNEITDNFEEEKNKAKKKlRLHLVEEFKSEIDE---YKDKYAGLEKAINSLEKEIKNLE--------AEIK 440
|
410
....*....|...
gi 1387193866 1814 KLEARVRELENEL 1826
Cdd:pfam13166 441 KLREEIKELEAQL 453
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
873-1151 |
3.74e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.44 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 873 LEEKMVSLLQEKNDLQLQVQAEQDN--------LADAEERCDQLIKNKIQLEAKVKEMTERLEDEEEMNAELTAKKRKLE 944
Cdd:pfam00038 23 LEQQNKLLETKISELRQKKGAEPSRlyslyekeIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 945 DECSELKRDIDdlELTLAKVEkekhaTENKVKNLTEEMAGLDEIiakLTKEKKALQEAHQQalDDLQAEEDKVntltkAK 1024
Cdd:pfam00038 103 NDLVGLRKDLD--EATLARVD-----LEAKIESLKEELAFLKKN---HEEEVRELQAQVSD--TQVNVEMDAA-----RK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1025 VKLEQHVDDLEGSLE-QEKKVRMDLERA-KRKLEgdlKLTQESIMDLEnDKQQLDERLKKKDFELNALNARIEDEQALGS 1102
Cdd:pfam00038 166 LDLTSALAEIRAQYEeIAAKNREEAEEWyQSKLE---ELQQAAARNGD-ALRSAKEEITELRRTIQSLEIELQSLKKQKA 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1387193866 1103 QLQKKLKELQARIEEleeeleaertARAKVEKLRSDLSRELEEISERLE 1151
Cdd:pfam00038 242 SLERQLAETEERYEL----------QLADYQELISELEAELQETRQEMA 280
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1749-1914 |
3.85e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1749 RNAEEKAKKAITDAAMMAEELKKEqdtsahLERMKKNMEQTIKDLQHRLdeaeqialkggkkqLQKLEARVRELENELEA 1828
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKKE------AEAIKKEALLEAKEEIHKL--------------RNEFEKELRERRNELQK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1829 EQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQAnTNLSKFRKVQHELDEAEE 1908
Cdd:PRK12704 87 LEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERI-SGLTAEEAKEILLEKVEE 165
|
....*...
gi 1387193866 1909 --RADIAE 1914
Cdd:PRK12704 166 eaRHEAAV 173
|
|
| PRK09303 |
PRK09303 |
histidine kinase; |
1505-1658 |
3.93e-03 |
|
histidine kinase;
Pssm-ID: 236462 [Multi-domain] Cd Length: 380 Bit Score: 41.86 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1505 LQEEISDLTEQLGSSGKTI----HELekvRKQLEAEKLELQSaleeaeasleheegkilraqLEFNQIKAEMERKLAEKD 1580
Cdd:PRK09303 137 LRQENETLLEQLKFKDRVLamlaHDL---RTPLTAASLALET--------------------LELGQIDEDTELKPALIE 193
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1387193866 1581 EEMEQAkRNHLRVVDSLQTSLDAETRSRNEALRVkkkmegdlNEMEIQLShanRLAAEAQKQvksLQSLLKDTQIQLD 1658
Cdd:PRK09303 194 QLQDQA-RRQLEEIERLITDLLEVGRTRWEALRF--------NPQKLDLG---SLCQEVILE---LEKRWLAKSLEIQ 256
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1076-1238 |
4.01e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.49 E-value: 4.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1076 LDERLKKKDFELNALNARIED-------EQALGSQLQKKLKELQARIEELEEEleaertaRAKVEKLRSDLSRELEEISE 1148
Cdd:PRK09039 44 LSREISGKDSALDRLNSQIAEladllslERQGNQDLQDSVANLRASLSAAEAE-------RSRLQALLAELAGAGAAAEG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1149 RLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSvAELSEQIDNL---------QRVKQkLEK 1219
Cdd:PRK09039 117 RAGELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALDASEKRD-RESQAKIADLgrrlnvalaQRVQE-LNR 194
|
170
....*....|....*....
gi 1387193866 1220 EKSEFKLELDDVTSNMEQI 1238
Cdd:PRK09039 195 YRSEFFGRLREILGDREGI 213
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1069-1263 |
4.63e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 41.98 E-value: 4.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1069 LENDKQQLDERLKKKDF------ELNALNARIEDEQALGSQLQK-----KLKELQARIEELEEELEAE-----RTARAKV 1132
Cdd:COG0497 174 LEELRADEAERARELDLlrfqleELEAAALQPGEEEELEEERRRlsnaeKLREALQEALEALSGGEGGaldllGQALRAL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1133 EKLrSDLSRELEEISERLEEAggatSVQIEmnkkrEA--EFQKMRRDLE------EATLQHEATAAALRKKHADSVAELs 1204
Cdd:COG0497 254 ERL-AEYDPSLAELAERLESA----LIELE-----EAasELRRYLDSLEfdperlEEVEERLALLRRLARKYGVTVEEL- 322
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1387193866 1205 eqIDNLQRVKQKLEkeksefklELDDVTSNMEQIIKAKANLEKMCRTLEDQMNEHRSKA 1263
Cdd:COG0497 323 --LAYAEELRAELA--------ELENSDERLEELEAELAEAEAELLEAAEKLSAARKKA 371
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1771-1923 |
4.94e-03 |
|
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: 41.65 E-value: 4.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1771 KEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKGGK------KQLQKLEARVRELENELEAEQKRNAESVKGMRKSE 1844
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRqldresDRNQELQKRIRLLEKREAEAEEALREQAELNRLKK 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387193866 1845 RRIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAK 1923
Cdd:pfam05557 83 KYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQ 161
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1525-1796 |
4.98e-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: 42.03 E-value: 4.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1525 ELEKVRkqLEAEKLELQSALEEaEASLEHEEGKIL-RAQLEFNQ----IKAEMERKLAEKDEEMEQAKRNHLRVVDSLQT 1599
Cdd:pfam17380 349 ELERIR--QEERKRELERIRQE-EIAMEISRMRELeRLQMERQQknerVRQELEAARKVKILEEERQRKIQQQKVEMEQI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1600 SLDAETRSRNEALRVKKKMEgdlNEMEiqlshanRLAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNN 1679
Cdd:pfam17380 426 RAEQEEARQREVRRLEEERA---REME-------RVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRK 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1680 LLQAELEELRAVVEQTERSRKLAEQELIEtservqllhSQNTSLINQKKKMEADLSQLQTEVEEavqecrnaeekaKKAI 1759
Cdd:pfam17380 496 ILEKELEERKQAMIEEERKRKLLEKEMEE---------RQKAIYEEERRREAEEERRKQQEMEE------------RRRI 554
|
250 260 270
....*....|....*....|....*....|....*..
gi 1387193866 1760 TDAAMMAEELKKEQDTsahLERMKKNMEQTIKDLQHR 1796
Cdd:pfam17380 555 QEQMRKATEERSRLEA---MEREREMMRQIVESEKAR 588
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1168-1390 |
5.03e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 5.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1168 EAEFQKMRRDLEEATLQHEATAAALRKKHADsVAELSEQIDNLQRVKQKLEKEKSEFKLELDDVTsnmEQIIKAKANLEK 1247
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAE-LEELNEEYNELQAELEALQAEIDKLQAEIAEAE---AEIEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1248 MCRTLedQMNEHRSKAEET-------------QRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLED 1314
Cdd:COG3883 91 RARAL--YRSGGSVSYLDVllgsesfsdfldrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387193866 1315 LKRQLEEEVKAKNALAHALQSARhdcDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAK 1390
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEE---AAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1788-1927 |
5.54e-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: 5.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1788 QTIKDLQHRLDEAEQIA--LKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQ 1865
Cdd:COG1579 7 RALLDLQELDSELDRLEhrLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1387193866 1866 DL--VDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDI 1927
Cdd:COG1579 87 NNkeYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE 150
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1525-1788 |
5.57e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.96 E-value: 5.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1525 ELEKVRKQLEAEKLELQSALEEAEASLEHEEGKILRAQL------EFNQIKAEMERKLAEKDEEMEQAKRNhlRVVDSL- 1597
Cdd:PRK10929 31 ELEQAKAAKTPAQAEIVEALQSALNWLEERKGSLERAKQyqqvidNFPKLSAELRQQLNNERDEPRSVPPN--MSTDALe 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1598 ----QTS--LDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRLAAEAQKQVKSLQSllkdtqiqlddavranddlkENI 1671
Cdd:PRK10929 109 qeilQVSsqLLEKSRQAQQEQDRAREISDSLSQLPQQQTEARRQLNEIERRLQTLGT--------------------PNT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1672 AIVERRNNLLQAELEELRAVVEQTERSRKLA--EQELIETseRVQLLHSQNTSLINQKKKMEADL-SQLQTEVEEAVQec 1748
Cdd:PRK10929 169 PLAQAQLTALQAESAALKALVDELELAQLSAnnRQELARL--RSELAKKRSQQLDAYLQALRNQLnSQRQREAERALE-- 244
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1387193866 1749 rNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQ 1788
Cdd:PRK10929 245 -STELLAEQSGDLPKSIVAQFKINRELSQALNQQAQRMDL 283
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
950-1111 |
5.64e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 40.27 E-value: 5.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 950 LKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKAlQEAHQQALDDLQAeedKVNTLTKAKVKLEQ 1029
Cdd:pfam13851 31 LKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLEN-YEKDKQSLKNLKA---RLKVLEKELKDLKW 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1030 HVDDLEgslEQEKKVRMDLERAKRKLEGDLKLTQESI----MDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQ 1105
Cdd:pfam13851 107 EHEVLE---QRFEKVERERDELYDKFEAAIQDVQQKTglknLLLEKKLQALGETLEKKEAQLNEVLAAANLDPDALQAVT 183
|
....*.
gi 1387193866 1106 KKLKEL 1111
Cdd:pfam13851 184 EKLEDV 189
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1432-1705 |
6.28e-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: 41.48 E-value: 6.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1432 VERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARslstelFKLKNAYEESLEHLETfkrENKNLQEEISD 1511
Cdd:COG5185 277 SKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAA------AEAEQELEESKRETET---GIQNLTAEIEQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1512 LTEQLGSSGKTIHElekvrkqlEAEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEMERKLAEKDEEMEQAKRNHL 1591
Cdd:COG5185 348 GQESLTENLEAIKE--------EIENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAAD 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1592 RVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEM--EIQLSHANRLAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKE 1669
Cdd:COG5185 420 RQIEELQRQIEQATSSNEEVSKLLNELISELNKVmrEADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKA 499
|
250 260 270
....*....|....*....|....*....|....*.
gi 1387193866 1670 NiaiVERRNNLLQAELEELRAVVEQTERSRKLAEQE 1705
Cdd:COG5185 500 T---LEKLRAKLERQLEGVRSKLDQVAESLKDFMRA 532
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1734-1920 |
6.36e-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: 40.40 E-value: 6.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1734 LSQLQTEVEEAVQECRNAEEK---AKKAITDAAMMAEELKKE-QDTSAHLERMKKNMEQTikdlQHRLDEAEQIA----- 1804
Cdd:pfam00261 3 MQQIKEELDEAEERLKEAMKKleeAEKRAEKAEAEVAALNRRiQLLEEELERTEERLAEA----LEKLEEAEKAAdeser 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1805 -LKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTE--EDRKNLL--RLQDLVDKLQL---KVK 1876
Cdd:pfam00261 79 gRKVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLEraEERAELAesKIVELEEELKVvgnNLK 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1387193866 1877 AYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKL 1920
Cdd:pfam00261 159 SLEASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKL 202
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1100-1429 |
6.48e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.42 E-value: 6.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1100 LGSQLQKKLKEL-------QARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQ 1172
Cdd:pfam07888 32 LQNRLEECLQERaellqaqEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1173 KMRRDLEEATLQHEATAAALRKKHADSVAELSEQID---NLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKMC 1249
Cdd:pfam07888 112 ELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLEretELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLS 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1250 RTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENgelsRQLDEKEALISQL--TRGKLTYTQQ-LEDLKRQLEEEVKAK 1326
Cdd:pfam07888 192 KEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAH----RKEAENEALLEELrsLQERLNASERkVEGLGEELSSMAAQR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1327 NALAHALQSARHDCDLLREQYEE------ETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTE-------------ELE 1387
Cdd:pfam07888 268 DRTQAELHQARLQAAQLTLQLADaslalrEGRARWAQERETLQQSAEADKDRIEKLSAELQRLEerlqeermereklEVE 347
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1387193866 1388 EAKKKLAQRLQDAEEAVEAVNAKCS--SLEKTKHRLQNEIEDLM 1429
Cdd:pfam07888 348 LGREKDCNRVQLSESRRELQELKASlrVAQKEKEQLQAEKQELL 391
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1523-1744 |
7.08e-03 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 40.36 E-value: 7.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1523 IHELEKvRKQLEAEKLELQSALEEAEASLEHEEgkilraqlEFNQIKAEMERKLAEKDEEMEQAKRNhlrvVDSLQTSLD 1602
Cdd:pfam12795 2 LDELEK-AKLDEAAKKKLLQDLQQALSLLDKID--------ASKQRAAAYQKALDDAPAELRELRQE----LAALQAKAE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1603 AETRSRNEALRVK------KKMEGDLNEMEIQLSHANRLAAEAQKQVKSLQSLLKDTQIQLDDA-VRANDDLKENIAIVE 1675
Cdd:pfam12795 69 AAPKEILASLSLEeleqrlLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIrNRLNGPAPPGEPLSE 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1387193866 1676 RRNNLLQAELEELRAVVEQTERS-------RKLAEQELIETSERVQLLHSQNT---SLINQKKKMEADLSQLQTEVEEA 1744
Cdd:pfam12795 149 AQRWALQAELAALKAQIDMLEQEllsnnnrQDLLKARRDLLTLRIQRLEQQLQalqELLNEKRLQEAEQAVAQTEQLAE 227
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
860-1182 |
7.19e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 41.43 E-value: 7.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 860 KEALEKSEARRKELE---EKMVSLLQ--EKNDLQLQvQAEqdnlADAEERCDQLIKNKIQLEAKVKEMterledeeEMNA 934
Cdd:PLN02939 113 NEQQTNSKDGEQLSDfqlEDLVGMIQnaEKNILLLN-QAR----LQALEDLEKILTEKEALQGKINIL--------EMRL 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 935 ELTAKKRKLedeCSELKRDIDDLELTLAKVEKEkhatenkvknLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEE 1014
Cdd:PLN02939 180 SETDARIKL---AAQEKIHVEILEEQLEKLRNE----------LLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLK 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1015 DKVNtltkakvkleqHVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQ-LDERLKKKDFELNALNAR 1093
Cdd:PLN02939 247 AELI-----------EVAETEERVFKLEKERSLLDASLRELESKFIVAQEDVSKLSPLQYDcWWEKVENLQDLLDRATNQ 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1094 IEDEQALGSQ---LQKKLKELQARIeeleeeleaertARAKVEKLRSD----LSRELEEISERLEEAGGATSVQIEMNKK 1166
Cdd:PLN02939 316 VEKAALVLDQnqdLRDKVDKLEASL------------KEANVSKFSSYkvelLQQKLKLLEERLQASDHEIHSYIQLYQE 383
|
330
....*....|....*.
gi 1387193866 1167 REAEFQKMRRDLEEAT 1182
Cdd:PLN02939 384 SIKEFQDTLSKLKEES 399
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
854-1059 |
7.39e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 40.95 E-value: 7.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 854 EEFGRLKEalEKSEARRKELEEKMVSLLQEKnDLQLQVQAEQDNL-ADAEERCDQLIKNKIQLEAKVKEMTERLEDEEEM 932
Cdd:PRK09510 62 EQYNRQQQ--QQKSAKRAEEQRKKKEQQQAE-ELQQKQAAEQERLkQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 933 NAELTAKKRKLEDE---CSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKltkeKKALQEAHQQAldd 1009
Cdd:PRK09510 139 AKAAAAAKAKAEAEakrAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAK----KKAEAEAKKKA--- 211
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1010 lqAEEDKVNTLTKAKVKLEQHVDDLEGSLEQEKKVRMDLERAKRKLEGDL 1059
Cdd:PRK09510 212 --AAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1195-1418 |
7.40e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.07 E-value: 7.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1195 KHADSVAELSEQIDNLQRVKQKLEKEKSEFKLElddvtsnmEQIIKAKANLEKmcRTLEDQMNEHRSKAEETQRSVNDLT 1274
Cdd:PRK05771 37 KEELSNERLRKLRSLLTKLSEALDKLRSYLPKL--------NPLREEKKKVSV--KSLEELIKDVEEELEKIEKEIKELE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1275 SQRAKLQTENGELSRQLDEKEAL------ISQLTRGKLTY------------TQQLEDLKRQLEEEVKAKN-----ALAH 1331
Cdd:PRK05771 107 EEISELENEIKELEQEIERLEPWgnfdldLSLLLGFKYVSvfvgtvpedkleELKLESDVENVEYISTDKGyvyvvVVVL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1332 ALQSARHDCDLLREQYEE-ETEAKAELQRVLSKANSEVAQWRTKYEtdaiQRTEELEEAKKKLAQRLQDAEEAVEAVNAK 1410
Cdd:PRK05771 187 KELSDEVEEELKKLGFERlELEEEGTPSELIREIKEELEEIEKERE----SLLEELKELAKKYLEELLALYEYLEIELER 262
|
....*...
gi 1387193866 1411 CSSLEKTK 1418
Cdd:PRK05771 263 AEALSKFL 270
|
|
| ATG14 |
pfam10186 |
Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are ... |
858-998 |
7.42e-03 |
|
Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are hydrophilic proteins with a predicted molecular mass of 40.5 kDa, and have a coiled-coil motif at the N terminus region. Yeast cells with mutant Atg14 are defective not only in autophagy but also in sorting of carboxypeptidase Y (CPY), a vacuolar-soluble hydrolase, to the vacuole. Subcellular fractionation indicate that Apg14p and Apg6p are peripherally associated with a membrane structure(s). Apg14p was co-immunoprecipitated with Apg6p, suggesting that they form a stable protein complex. These results imply that Apg6/Vps30p has two distinct functions: in the autophagic process and in the vacuolar protein sorting pathway. Apg14p may be a component specifically required for the function of Apg6/Vps30p through the autophagic pathway. There are 17 auto-phagosomal component proteins which are categorized into six functional units, one of which is the AS-PI3K complex (Vps30/Atg6 and Atg14). The AS-PI3K complex and the Atg2-Atg18 complex are essential for nucleation, and the specific function of the AS-PI3K apparently is to produce phosphatidylinositol 3-phosphate (PtdIns(3)P) at the pre-autophagosomal structure (PAS). The localization of this complex at the PAS is controlled by Atg14. Autophagy mediates the cellular response to nutrient deprivation, protein aggregation, and pathogen invasion in humans, and malfunction of autophagy has been implicated in multiple human diseases including cancer. This effect seems to be mediated through direct interaction of the human Atg14 with Beclin 1 in the human phosphatidylinositol 3-kinase class III complex.
Pssm-ID: 462986 [Multi-domain] Cd Length: 347 Bit Score: 40.90 E-value: 7.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 858 RLKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAeercdQLIKNKI-QLEAKVKEMTERLEdeeEMNAEL 936
Cdd:pfam10186 23 ELRVDLARLLSEKDSLKKKVEEALEGKEEGEQLEDNIGNKKLKL-----RLLKSEVaISNERLNEIKDKLD---QLRREI 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1387193866 937 TAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKA 998
Cdd:pfam10186 95 AEKKKKIEKLRSSLKQRRSDLESASYQLEERRASQLAKLQNSIKRIKQKWTALHSKTAESRS 156
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
929-1319 |
7.99e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.44 E-value: 7.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 929 EEEMNAEL-TAKKRKLEDEcsELKRDIDDLELTL---AKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQ 1004
Cdd:PRK11281 38 EADVQAQLdALNKQKLLEA--EDKLVQQDLEQTLallDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1005 QALDDLQAEEdkvntltkakvkLEQHVDDLEGSLEQekkVRMDL--------------ERAKRKLEGDLKLTQE----SI 1066
Cdd:PRK11281 116 ETLSTLSLRQ------------LESRLAQTLDQLQN---AQNDLaeynsqlvslqtqpERAQAALYANSQRLQQirnlLK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1067 MDLENDKQQLDERLKKKDFELNALNARIEDEQAL---GSQLQ----KKLKELQARIEELEEELEAERTArakVEKLRSDL 1139
Cdd:PRK11281 181 GGKVGGKALRPSQRVLLQAEQALLNAQNDLQRKSlegNTQLQdllqKQRDYLTARIQRLEHQLQLLQEA---INSKRLTL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1140 SRELEEISERLEEAGgatsvQIEMNK--KREAEF-QKMRRDLEEATLQ-HEATAAALRKKHA-DSVAE----LSEQIDNL 1210
Cdd:PRK11281 258 SEKTVQEAQSQDEAA-----RIQANPlvAQELEInLQLSQRLLKATEKlNTLTQQNLRVKNWlDRLTQsernIKEQISVL 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1211 Q------RV--KQKLekeksefKLELDDVTSNM-EQIikakANLekmcRTLEDQMNEHRSKAEETQRSVNDLtsqrakLQ 1281
Cdd:PRK11281 333 KgslllsRIlyQQQQ-------ALPSADLIEGLaDRI----ADL----RLEQFEINQQRDALFQPDAYIDKL------EA 391
|
410 420 430
....*....|....*....|....*....|....*....
gi 1387193866 1282 TENGELSRQldEKEALISQL-TRGKLtytqqLEDLKRQL 1319
Cdd:PRK11281 392 GHKSEVTDE--VRDALLQLLdERREL-----LDQLNKQL 423
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
938-1220 |
8.26e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 40.99 E-value: 8.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 938 AKKRKLEDECSELKRDIDDLELTLAK---------VEKEKHATENKVKN------LTEEMAGLDEIIAKLTKEKKALQEA 1002
Cdd:PLN03229 429 TPVRELEGEVEKLKEQILKAKESSSKpselalnemIEKLKKEIDLEYTEaviamgLQERLENLREEFSKANSQDQLMHPV 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1003 HQQALDDLQAE-----------------EDKVNTLTKAKVKLEQHVDDLEGSLEQEKKVR--MDLERAKRKLEGDLKLTQ 1063
Cdd:PLN03229 509 LMEKIEKLKDEfnkrlsrapnylslkykLDMLNEFSRAKALSEKKSKAEKLKAEINKKFKevMDRPEIKEKMEALKAEVA 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1064 ESIMDLENDkqqLDERLKKKdfelnALNARIEDEQALGSQLqkKLKELQARIEELEEELEAERTA----RAKVEKLRSDL 1139
Cdd:PLN03229 589 SSGASSGDE---LDDDLKEK-----VEKMKKEIELELAGVL--KSMGLEVIGVTKKNKDTAEQTPppnlQEKIESLNEEI 658
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1140 SRELEEISE-----------RLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATlqheaTAAALRKKHADSVAELSEQID 1208
Cdd:PLN03229 659 NKKIERVIRssdlkskiellKLEVAKASKTPDVTEKEKIEALEQQIKQKIAEAL-----NSSELKEKFEELEAELAAARE 733
|
330
....*....|..
gi 1387193866 1209 NLQRVKQKLEKE 1220
Cdd:PLN03229 734 TAAESNGSLKND 745
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1500-1798 |
8.73e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 40.29 E-value: 8.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1500 RENKNLQEEISDLTEQLGSsgktihELEKVRKQLEAEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEMERKLAEK 1579
Cdd:pfam00038 25 QQNKLLETKISELRQKKGA------EPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1580 dEEMEQAKRNHLRVVDSL---QTSLDAETRSRNEALR-VKKKMEGDLNEMEIQLSHANRLAAEAQKQVKSLQSLLKDTQI 1655
Cdd:pfam00038 99 -TSAENDLVGLRKDLDEAtlaRVDLEAKIESLKEELAfLKKNHEEEVRELQAQVSDTQVNVEMDAARKLDLTSALAEIRA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1656 QLDDAVRANDDLKENiaiverrnnLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMEADLS 1735
Cdd:pfam00038 178 QYEEIAAKNREEAEE---------WYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLA 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1387193866 1736 QLQteveeavqecrnaeekakkaitdaAMMAEELKKEQDTSAHLER----MKKNMEQTIKDLQHRLD 1798
Cdd:pfam00038 249 ETE------------------------ERYELQLADYQELISELEAelqeTRQEMARQLREYQELLN 291
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1531-1652 |
8.75e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 8.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1531 KQLEAEKlELQSALEEAEASLE-HEEGKILRAQLEFNQIKAEMERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRN 1609
Cdd:PRK12704 32 KIKEAEE-EAKRILEEAKKEAEaIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREE 110
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1387193866 1610 EALRVKKKMEGDLNEMEIQLSHANRLAAEAQKQVKSLQSLLKD 1652
Cdd:PRK12704 111 ELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAE 153
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1440-1617 |
9.34e-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: 9.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1440 AALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAY---EESLEHLETFKRENKNLQEEISDlTEQL 1516
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIkrlELEIEEVEARIKKYEEQLGNVRN-NKEY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1517 GSSGKTIHELEKVRKQLEAEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEMERKLAEKDEEMEQAKRNhlrvVDS 1596
Cdd:COG1579 92 EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE----REE 167
|
170 180
....*....|....*....|.
gi 1387193866 1597 LQTSLDAETRSRNEALRVKKK 1617
Cdd:COG1579 168 LAAKIPPELLALYERIRKRKN 188
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1664-1919 |
9.49e-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: 40.88 E-value: 9.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1664 NDDLKENIAIVERRNNLLQAELEELRAVVEQtERSRKLAEQELIETSERVQLLHSQNT--SLINQKKKMEADLSQLQTEV 1741
Cdd:pfam17380 268 NEFLNQLLHIVQHQKAVSERQQQEKFEKMEQ-ERLRQEKEEKAREVERRRKLEEAEKArqAEMDRQAAIYAEQERMAMER 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1742 EEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSA-HLERMKKNmEQTIKDL-----QHRLDEAEQIALKGGKKQLQKL 1815
Cdd:pfam17380 347 ERELERIRQEERKRELERIRQEEIAMEISRMRELERlQMERQQKN-ERVRQELeaarkVKILEEERQRKIQQQKVEMEQI 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387193866 1816 -----EARVRELEnELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQAN 1890
Cdd:pfam17380 426 raeqeEARQREVR-RLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEER 504
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1387193866 1891 TNL-----SKFRKVQHELDE------AEERADIAESQVNK 1919
Cdd:pfam17380 505 KQAmieeeRKRKLLEKEMEErqkaiyEEERRREAEEERRK 544
|
|
| |
